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Information on EC 3.1.26.13 - retroviral ribonuclease H
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3.1.26.13 retroviral ribonuclease HSpecify your search results
Word Map
- 3.1.26.13
-
integrase
- hiv-rt
- rna-dna
-
template-primer
-
moloney
-
polypurine
- transcriptases
-
minus-strand
- 3'-azido-3'-deoxythymidine
-
nnrti
-
primer-template
-
nonnucleoside
- drug development
- medicine
- analysis
- pharmacology
The enzyme appears in viruses and cellular organisms
Reaction Schemes
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
Synonyms
human immunodeficiency virus reverse transcriptase, hiv-1 rnase h, rt-rnase h, reverse transcriptase-associated rnase h, hiv-1 rt-associated rnase h, retroviral ribonuclease h, hiv rt-associated rnase h, hiv-1 reverse transcriptase ribonuclease h, reverse-transcriptase-associated ribonuclease h, hiv-1 reverse transcriptase rnase h, 
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SYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
HIV reverse transcriptase ribonuclease H
HIV reverse transcriptase-associated RNase H
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HIV RT RNaseH
HIV RT-associated RNase H
HIV-1 reverse transcriptase RNase H
HIV-1 RH
HIV-1 ribonuclease H
HIV-1 ribonuclease H domain
HIV-1 RNase H
human immunodeficiency virus reverse transcriptase-associated ribonuclease H
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human immunodeficiency virus reverse transcriptase-associated RNase H
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human immunodeficiency virus RT-associated RNase H
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reverse transcriptase
reverse transcriptase-associated ribonuclease H
reverse transcriptase-associated RNase H
ribonuclease H
RNase H
RNaseH
RNH
RT RNase H
RT-RNase H
HIV-1 ribonuclease H domain
Human immunodeficiency virus type 1 group M subtype B BH10
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reverse transcriptase
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bifunctional enzyme with DNA polymerase and ribonuclease H activities
reverse transcriptase
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the large subunit of reverse transcriptase contains separated DNA polymerase and RNase H domains at its N- and C-terminal regions, respectively
reverse transcriptase
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the multifunctional enzyme contains a ribonuclease H domain
reverse transcriptase
-
the multifunctional enzyme has RNA and DNA dependent polymerase activity, along with ribonuclease H activity
reverse transcriptase-associated ribonuclease H
Human immunodeficiency virus type 1 group M subtype B
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reverse transcriptase-associated ribonuclease H
Human immunodeficiency virus type 1 group M subtype B BH10
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reverse transcriptase-associated RNase H
Human immunodeficiency virus type 1 group M subtype B
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reverse transcriptase-associated RNase H
Human immunodeficiency virus type 1 group M subtype B BH10
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ribonuclease H
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RNase H
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RNase H
Human immunodeficiency virus type 1 group O subtype B ESP49
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RNH
Human immunodeficiency virus type 1 group M subtype B BH10
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RT RNase H
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reverse transcriptase contains a C-terminal ribonuclease H domain on its p66 subunit
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REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
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Endohydrolysis of RNA in RNA/DNA hybrids. Three different cleavage modes: 1. sequence-specific internal cleavage of RNA. Human immunodeficiency virus type 1 and Moloney murine leukemia virus enzymes prefer to cleave the RNA strand one nucleotide away from the RNA-DNA junction. 2. RNA 5'-end directed cleavage 13-19 nucleotides from the RNA end. 3. DNA 3'-end directed cleavage 15-20 nucleotides away from the primer terminus.
cleavage reaction mechanism and substrate specificity of HIV-1 RNase H, overview
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CAS REGISTRY NUMBER
COMMENTARY
9050-76-4
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SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
5'-end-labeled 267 nt-long RNA annealed to 20 nt-long synthetic DNA + H2O
?
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?
5'-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3'/3'-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O
5'-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC/dGdGdGdGdAdTdCdCdTdCdTdAdG-3' + 3'-dTdCdGdAdGdCdCdAdTdGdGdG/dCdCdCdCdTdAdGdGdAdGdTdC-5'
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model substrate, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication, contains sequences from the HIV genome and sequences unrelated to the HIV viral genome
hydrolysis of the phosphodiester bond at the DNA-RNA junction
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?
5'-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3'/3'-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5' + H2O
5'-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA/dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3' + 3'-dGdAdCdAdAdGdCdCdCdGdCdGdGdT/dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5'
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model substrate containing sequences from the HIV genome, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication. The DNA-extended RNA was a template and was annealed to a DNA oligonucleotide that primed reverse transcription of the RNA in the template
hydrolysis of the phosphodiester bond at the DNA-RNA junction
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?
5-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3 + 3-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O
?
5-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3 + 3-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5 + H2O
?
HTS-1 + H2O
?
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RNA/DNA duplex substrate HTS-1 (RNA 5'-gaucugagccuggagcu-3'-fluorescein annealed to DNA 3'-CTAGACTCGGACCCTCGA-5'-dabsyl) is a high sensitivity duplex that assesses non-specific internal cleavage
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?
HTS-2 + H2O
?
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HTS-2 (RNA 5'-cugguuagaccagaucugagccugggagcu-3'-fluorescein annealed to DNA 3'-GGTCTAGACTCGGACCCTCGA-5'-dabsyl) provides a duplex with a recessed DNA 3'-terminus and measures 3'-DNA directed or polymerase directed RNase H cleavage
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?
HTS-3 + H2O
?
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HTS-3 (RNA 5'-accagaucugagccugggagcu-3'-fluorescein annealed to DNA 3'-GACCAATCTGGTCTAGACTCGGACCCTCGA-5'-dabsyl) measures 5'-RNA-directed RNase H cleavage
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?
poly(A)+ mRNA primed with oligo(dT) + H2O
double-stranded DNA copies between 1.3 and 9.9 kilobases in length + ?
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multifunctional enzyme containing RNase H and reverse transcriptase activity
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?
poly(dT)-poly(rA) + H2O
?
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substrate poly(dC)-poly(rG) is markedly preferred over substrate poly(dT)-poly(rA)
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?
RNA-DNA hybrid containing the polypurine tract + H2O
?
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extension of the polypurine tract primer by at least 2 nucleotides is sufficient for recognition and correct cleavage by RNase H at the RNA-DNA junction to remove the primer. Primer removal occurs by cleavage one nucleotide away from the RNA-DNA junction. The same polypurine tract specificity determinants responsible for generation of the polypurine tract primer also direct polypurine tract primer removal. Once the primer has been extended and removed from the nascent plus-strand DNA, reinitiation at the resulting plus-strand primer terminus does not occur
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?
5-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3 + 3-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O
?
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model substrate, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication, contains sequences from the HIV genome and sequences unrelated to the HIV viral genome
hydrolysis of the substrate to leave a single ribonucleotide 5-phosphate at the 5-terminus of the model DNA genome
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?
5-rGrGrGrCrGrArArUrUrCrGrArGrCrUrCrGrGrUrArCrCrC-dGdGdGdGdAdTdCdCdTdCdTdAdG-3 + 3-dTdCdGdAdGdCdCdAdTdGdGdG-dCdCdCdCdTdAdGdGdAdGdTdC-5' + H2O
?
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model substrate, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication, contains sequences from the HIV genome and sequences unrelated to the HIV viral genome
hydrolysis of the substrate to leave a single ribonucleotide 5-phosphate at the 5-terminus of the model DNA genome
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?
5-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3 + 3-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5 + H2O
?
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model substrate containing sequences from the HIV genome, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication. The DNA-extended RNA was a template and was annealed to a DNA oligonucleotide that primed reverse transcription of the RNA in the template
hydrolysis of the substrate to leave a single ribonucleotide 5'-phosphate at the 5'-terminus of the model DNA genome
-
?
5-rGrGrGrUrCrCrCrUrGrUrUrCrGrGrGrCrGrCrCrA-dCdTdGdCdTdAdGdAdGdAdTdTdTdTdT-3 + 3-dGdAdCdAdAdGdCdCdCdGdCdGdGdT-dGdAdCdGdAdTdCdTdCdTdAdAdAdAdA-5 + H2O
?
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model substrate containing sequences from the HIV genome, designed to be structurally similar to the DNA-extended tRNA created by initiation of minus-strand DNA synthesis during retroviral replication. The DNA-extended RNA is a template and is annealed to a DNA oligonucleotide that primed reverse transcription of the RNA in the template
hydrolysis of the substrate to leave a single ribonucleotide 5-phosphate at the 5-terminus of the model DNA genome
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?
RNA-DNA hybrid + H2O
?
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5'-GTTTTCTTTTCCCCCCTGAC-3'-fluorescein/5'-CAAAAGAAAAGGGGGGACUG-3'-dabcyl
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?
additional information
?
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evaluation of activity by enzyme's ability to select and extend the 3' polypurine tract primers into (+) strand DNA. Evaluation via concerted and two-step reactions for (+) strand priming, the latter of which allows discrimination between selection end extension events
3' polypurine tract primer selection appears to represent a specialized form of RNase H activity that is more sensitive to minor structural alterations within this domain
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?
additional information
?
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no substrate: single-stranded RNA or the DNA component of DNA-RNA hybrids. Products consist primarily of monomers, dimers, and trimers with 3'-OH groups
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?
additional information
?
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the HIV polymerase and RNase H active sites are separated by a distance equivalent to the length of a 15-nucleotide RNA-DNA heteroduplex
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?
additional information
?
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a nick separating an upstream RNA and a downstream RNA annealed to DNA is essentially ignored by RNase H, indicating that the RNA 5' end at a nick is not sufficient to position 5' end-directed cleavages. Cleavage sites that are located close to the 5' end of the downstream RNA are not recognized in the absence of the upstream RNA, and the 5' ends of the shorter upstream RNAs enhance cleavage at these sites. The recognition of an internal cleavage site depends on local sequence features found both upstream and downstream of the cleavage site, designated as the -1/+1 position. Preferred nucleotides have been identified in the flanking sequences spanning positions -14 to +1
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?
additional information
?
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interdependence of the polymerase and RNase H activities of HIV-1 reverse transcription during viral DNA synthesis
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?
additional information
?
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RNase H acts at or about 14 to 18 nucleotides from the 5' end of the template, the cleavage site for the RNase H is therefore held at around this distance behind the DNA polymerase activity. For the intact protein, the RNase H and reverse transcriptase activities may work in a coupled or coordinate manner. More than 80% of the residual 5' oligonucleotides remain base paired to the RNA-directed DNA product. Under certain conditions, these short RNAs can act as efficient primers for an associated DNA-directed DNA synthesis in the reverse direction
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?
additional information
?
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study on specificity of RNase H cleavage by use of synthetic DNA-RNA hybrids based on the same 81-base RNA template. First series of RNase H substrates is prepared with complementary DNA oligonucleotides of different lengths, ranging from 6 to 20 nucleotides, all of which share a common 5' end and are successively shorter at their 3' ends. The second series of oligonucleotides has a common 3' end but shorter 5' ends. The DNA oligonucleotides in the third series are all 20 bases long but have non-complementary stretches at either the 5' end, 3' end, or both ends. Enzyme cleaves fairly efficiently if the duplex region is at least eight bases long, but not if it is shorter. Although enzyme requires the substrate to have a region of RNA-DNA duplex, Moloney murine leukemia virus RT can cleave RNA outside the region that is part of the RNA-DNA duplex. The polymerase domain of HIV-1 RT uses certain mismatched segments of RNA-DNA to position the enzyme for RNase H cleavage. A mismatched region near the RNase H domain can interfere with RNase H cleavage, cleavage is usually but not always more efficient if the mismatched segment is deleted
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?
additional information
?
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substrate heteropolymeric 90-nt 5' end-labeled RNA template-annealed to a 36-nt DNA primer is cleaved by wild-type p66/p51 RT precisely at the RNA/DNA junction to liberate a 20-nt (+) strand DNA
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?
additional information
?
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substrates consist of SP6 runoff transcripts from a portion of the gag region of the HIV-1 genome hybridized to complementary single-stranded DNA from either an M 13 subclone or a phagemid transcription vector subclone. The corresponding hybrids are fully base-paired
products formed from the fully complementary hybrid consist of a nonuniform distribution of oligonucleotides ranging in size from 4 to 15 nt
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?
additional information
?
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substrates consist of SP6 runoff transcripts from a portion of the gag region of the HIV-1 genome hybridized to complementary single-stranded DNA from either an M 13 subclone or a phagemid transcription vector subclone. The corresponding hybrids carry a 5'-mismatch of seven nucleotides
products are a few prominent intermediates of 24-42 nt in size with relatively little accumulation of larger products
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?
additional information
?
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the recognition and precise cleavage of the polypurine tract of the human immunodeficiency virus type 1 is an essential step in HIV-1 reverse transcription. Mutations at positions 2 and 5 of the 3'-end of the polypurine tract do significantly alter the cleavage specificity at the polypurine tract/U3 junction. The structure of the polypurine tract primer, rather than the base-specific contacts between the polypurine tract and HIV-1 RT, are the primary determinants of RNase H cleavage specificity at the polypurine tract/U3 junction
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?
additional information
?
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the selection of 5' end-directed cleavage sites by retroviral RNases H results from a combination of nucleotide sequence, permissible distance, and accessibility to the RNA 5' end. Enzyme strongly prefers A or U at the +1 position and C or G at the -2 position, and A is disfavored at the -4 position. 5' End-directed cleavages occur when sites are positioned between the 13th and 20th nucleotides from the RNA 5' end. The extent of 5' end-directed cleavages observed in substrates containing a free recessed RNA 5' end is most comparable to substrates with a gap of 2 or 3 bases between the upstream and downstream RNAs
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?
additional information
?
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5'end-directed RNase H of reverse transcriptase
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?
additional information
?
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HIV-1 reverse transcriptase has two enzymatic functions, DNA polymerase and RNase H activities
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?
additional information
?
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RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview
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?
additional information
?
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cleavage of DNA-RNA and RNA-DNA primer templates
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?
additional information
?
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RNA-DNA duplex substrate from a 41-mer 5'-labeled 32P-heteropolymeric RNA template kim40R annealed to complementary 32-mer DNA oligomer kim32D
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?
additional information
?
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RNA-DNA substrate in a tRNA removal assay, the cleavage patterns for the recombinant HIV-1 reverse transcriptase and mutant p51-G-TCR construct correspond to the release of the 11mer RNA, corresponding with the authentic cleavage identified in vivo. The relative activity of the isolated HIV-1 RNaseH(p51-G-TCR) is comparable to that of the full-length HIV reverse transcriptase
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?
additional information
?
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RNA/DNA hybrid duplex substrate
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?
additional information
?
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substrate is 18-nucleotide 3'-fluourescein-labeled RNA annealed to a complementary 18-nucleotide 5'-dabsyl-labeled DNA
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?
additional information
?
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the tC5U-p12 hybrid is used as reaction substrate the RNase H activity
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?
additional information
?
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conserved residues in the connection subdomain and C-terminal ribonuclease H, RNase H, domain of HIV-1 RT contact the nascent DNA primer and modulate the trajectory of the template relative to the RNase H catalytic center. Within the RNase H domain, these residues include Thr473, Glu475, Lys476, Tyr501, and Ile505, while His539 and Asn474 interact with the scissile phosphate of the RNA template,m substrate recognition and binding, overview
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?
additional information
?
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a 5'-32P-labeled AZT-MP chain-terminated RNA/DNA template/primer substrate
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?
additional information
?
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a DNA/RNA hybrid can simultaneously engage both active sites. Of the tested interconverting reverse transcriptase-DNA/RNA species, 43% are active for both sites simultaneously, 27% show only polymerase activity, and the remaining 30% are nonproductive. A string of at least 4-6 nucleotides downstream of the cleaving site is required for efficient RNA cleavage. During processive nucleotide incorporation, sequential rounds of RNA cleavage occur each time after about 6 nucleotides are incorporated, during processive primer extension, diphosphate release is rate-limiting. Although polymerization is efficient and processive, RNase H is inefficient and periodic. This combination allows the two catalytic centers of HIVRT to work simultaneously at similar speeds without being tightly coupled
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?
additional information
?
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HIV RNase H cleaves viral RNA at multiple stages of reverse transcription with at least three distinct modes: random internal cleavages, DNA 3' end-directed and polymerase dependent cleavages, and RNA 5' end-directed cleavages. A biochemical assay uses the HTS-1 RNA/DNA substrate to specifically probe random internal cleavage, which is believed to be the dominant mode of RNA cutting
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?
additional information
?
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a 18-nucleotide 3'-fluorescein-labeled RNA is annealed to a complementary 18-nucleotide 5'-dabsyl-labeled DNA. Cleavage of the HIV-1 polypurine tract (PPT) primer is performed with a 29 nt Cy5-labeled RNA (5'-Cy5-UUU UAA AAG AAA AGGGGG G*AC UGG AAG GG-3', where * represents the PPT 3' terminus) hybridized to a 40 nt DNA (5'-ATT AGCCCT TCC AGT CCC CCC TTT TCT TTT AAA AAG TGG C-3'). For cytopathicity assays, HIV-1 virus strain RF is used to infect CEM-SS cells
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?
additional information
?
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a 18-nucleotide 3'-fluorescein-labeled RNA is annealed to a complementary 18-nucleotide 5'-dabsyl-labeled DNA. Cleavage of the HIV-1 polypurine tract (PPT) primer is performed with a 29 nt Cy5-labeled RNA (5'-Cy5-UUU UAA AAG AAA AGGGGG G*AC UGG AAG GG-3', where * represents the PPT 3' terminus) hybridized to a 40 nt DNA (5'-ATT AGCCCT TCC AGT CCC CCC TTT TCT TTT AAA AAG TGG C-3'). For cytopathicity assays, HIV-1 virus strain RF is used to infect CEM-SS cells
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?
additional information
?
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RNA/DNA duplex substrate HTS-1 (RNA 5'-gaucugagccuggagcu-3'-fluorescein annealed to DNA 3'-CTAGACTCGGACCCTCGA-5'-dabsyl) is a high sensitivity duplex that assesses non-specific internal cleavage
-
-
?
additional information
?
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RNA/DNA duplex substrate HTS-1 (RNA 5'-gaucugagccuggagcu-3'-fluorescein annealed to DNA 3'-CTAGACTCGGACCCTCGA-5'-dabsyl) is a high sensitivity duplex that assesses non-specific internal cleavage
-
-
?
additional information
?
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RNA/DNA duplex substrate HTS-1 (RNA 5'-gaucugagccugggagcu-3'-fluorescein annealed to DNA 3'-CTAGACTCGGACCCTCGA-5'-dabsyl) is a high sensitivity duplex assessing non-specific internal cleavage
-
-
?
additional information
?
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RNA/DNA duplex substrate HTS-1 (RNA 5'-gaucugagccugggagcu-3'-fluorescein annealed to DNA 3'-CTAGACTCGGACCCTCGA-5'-dabsyl) is a high sensitivity duplex assessing non-specific internal cleavage
-
-
?
additional information
?
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RNase H activity is determined using oligomeric substrates. 5'-Fluorescein-labeled 29 bp RNA/DNA hybrid (R29/D29), 12 bp RNA/RNA duplex (R12/R12), and 12 bp DNA/DNA duplex (D12/D12) are prepared by hybridizing 5'-fluorescein-labeled 29 b RNA (5'-aauagagaaaaagaaaaaagauggcaaag-3'), 12 b RNA (5'-cggagaugacgg-3'), and 12 b DNA (5'-CGGAGAUGACGG-3') with a 1.5 molar equivalent of the complementary DNA
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?
additional information
?
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usage of DNA/RNA hybrid substrates for enzyme activity assay. The majority of species represent the active form of RTx02DNA/RNA complexes that can perform both activities simultaneously. Efficient RNase H cleavage required at least four ribonucleotides downstream of the cutting site
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?
additional information
?
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when the RNA/DNA hybrid is immobilized at the polymerase active site, RNase H cleavage occurs, experimentally verifying that the substrate can simultaneously interact with both active sites, analysis of the mechanism of the coordination of the two activities. Cross-linking of HIV-1 RT with RNA/DNA hybrids, inhibition of complex formation by salt and heparin. Purified HIV-1 RT D186C, M184C and Q258C variants are tethered to appropriately modified CL3 substrates, and RNase H activity within the cross-linked complexes is determined, overview
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?
additional information
?
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cleavage of DNA-RNA and RNA-DNA primer templates
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?
additional information
?
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RNA-DNA duplex substrate from a 41-mer 5'-labeled 32P-heteropolymeric RNA template kim40R annealed to complementary 32-mer DNA oligomer kim32D
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?
additional information
?
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RNA/DNA hybrid duplex substrate
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?
additional information
?
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a 18-nucleotide 3'-fluorescein-labeled RNA is annealed to a complementary 18-nucleotide 5'-dabsyl-labeled DNA. Cleavage of the HIV-1 polypurine tract (PPT) primer is performed with a 29 nt Cy5-labeled RNA (5'-Cy5-UUU UAA AAG AAA AGGGGG G*AC UGG AAG GG-3', where * represents the PPT 3' terminus) hybridized to a 40 nt DNA (5'-ATT AGCCCT TCC AGT CCC CCC TTT TCT TTT AAA AAG TGG C-3'). For cytopathicity assays, HIV-1 virus strain RF is used to infect CEM-SS cells
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-
?
additional information
?
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RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview
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?
additional information
?
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Human immunodeficiency virus type 1 group M subtype B
5' end labeled RNA-DNA heteroduplexe substrates aligned from commercial RNA and DNA oligonucleotides are used
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?
additional information
?
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Human immunodeficiency virus type 1 group M subtype B
activity of wild-type enzyme is determined with the RNA/DNA template-primer R33B/20A, comparison of HIV-1 group O subtype B ESP49 and HIV-1 group M subtype B BH10
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?
additional information
?
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Human immunodeficiency virus type 1 group M subtype B
hybrid RNA/DNA 5'-GAUCUGAGCCUGGGAGCU-fluorescin-3' and 5'-dabsyl-AGCTCCCAGGCTCAGATC-3' are used for RNase H activity assays
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?
additional information
?
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Human immunodeficiency virus type 1 group M subtype B
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usage of DNA/RNA hybrid substrates for enzyme activity assay. The isolated RNH domain of reverse transcriptase (RT), folded by itself, is not catalytically active, due to lack of the substrate handle region, but exhibits a native-like protein fold
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?
additional information
?
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Human immunodeficiency virus type 1 group M subtype B BH10
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usage of DNA/RNA hybrid substrates for enzyme activity assay. The isolated RNH domain of reverse transcriptase (RT), folded by itself, is not catalytically active, due to lack of the substrate handle region, but exhibits a native-like protein fold
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?
additional information
?
-
Human immunodeficiency virus type 1 group M subtype B BH10
hybrid RNA/DNA 5'-GAUCUGAGCCUGGGAGCU-fluorescin-3' and 5'-dabsyl-AGCTCCCAGGCTCAGATC-3' are used for RNase H activity assays
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?
additional information
?
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Human immunodeficiency virus type 1 group M subtype B BH10
activity of wild-type enzyme is determined with the RNA/DNA template-primer R33B/20A, comparison of HIV-1 group O subtype B ESP49 and HIV-1 group M subtype B BH10
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?
additional information
?
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Human immunodeficiency virus type 1 group M subtype B BH10
5' end labeled RNA-DNA heteroduplexe substrates aligned from commercial RNA and DNA oligonucleotides are used
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?
additional information
?
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Human immunodeficiency virus type 1 group O subtype B
-
activities of wild-type and mutant enzymes are determined with the RNA/DNA template-primer R33B/20A, comparison of HIV-1 group O subtype B ESP49 and HIV-1 group M subtype B BH10
-
-
?
additional information
?
-
Human immunodeficiency virus type 1 group O subtype B ESP49
-
activities of wild-type and mutant enzymes are determined with the RNA/DNA template-primer R33B/20A, comparison of HIV-1 group O subtype B ESP49 and HIV-1 group M subtype B BH10
-
-
?
additional information
?
-
-
a nick separating an upstream RNA and a downstream RNA annealed to DNA is essentially ignored by RNase H, indicating that the RNA 5' end at a nick is not sufficient to position 5' end-directed cleavages. Cleavage sites that are located close to the 5' end of the downstream RNA are not recognized in the absence of the upstream RNA, and the 5' ends of the shorter upstream RNAs enhance cleavage at these sites. The recognition of an internal cleavage site depends on local sequence features found both upstream and downstream of the cleavage site, designated as the -1/+1 position. Preferred nucleotides have been identified in the flanking sequences spanning positions -11 to +1
-
-
?
additional information
?
-
-
study on specificity of RNase H cleavage by use of synthetic DNA-RNA hybrids based on the same 81-base RNA template. First series of RNase H substrates is prepared with complementary DNA oligonucleotides of different lengths, ranging from 6 to 20 nucleotides, all of which share a common 5' end and are successively shorter at their 3' ends. The second series of oligonucleotides has a common 3' end but shorter 5' ends. The DNA oligonucleotides in the third series are all 20 bases long but have non-complementary stretches at either the 5' end, 3' end, or both ends. Enzyme cleaves fairly efficiently if the duplex region is at least eight bases long, but not if it is shorter. Although enzyme requires the substrate to have a region of RNA-DNA duplex, Moloney murine leukemia virus RT can cleave RNA outside the region that is part of the RNA-DNA duplex. The polymerase domain of Moloney murine leukemia virus RT does not use the same mismatched segments to define the position for RNase H cleavage
-
-
?
additional information
?
-
-
the selection of 5' end-directed cleavage sites by retroviral RNases H results from a combination of nucleotide sequence, permissible distance, and accessibility to the RNA 5' end. Enzyme strongly prefers A or U at the +1 position and C or G at the -2 position. 5' End-directed cleavages occurr when sites are positioned between the 13th and 20th nucleotides from the RNA 5' end. The extent of 5' end-directed cleavages observed in substrates containing a free recessed RNA 5' end is most comparable to substrates with a gap of 2 or 3 bases between the upstream and downstream RNAs
-
-
?
additional information
?
-
-
Moloney murine leukemia virus reverse transcriptase, M-MuLV RT, is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules
-
-
?
additional information
?
-
-
Moloney murine leukemia virus reverse transcriptase, MMLV RT, shows DNA polymerization activity and RNase H activity. Stabilization of the reverse transcriptase activity by eliminating the RNase H activity, overview
-
-
?
additional information
?
-
-
retroviral reverse transcriptase also possesses a ribonuclease H activity, an enzyme which cleaves the RNA strand of RNA/DNA hetroduplex
-
-
?
additional information
?
-
-
DNA binding by M-MuLV RT assay using 5'-end labeled 48/36 bp RNA-DNA oligonucleotide duplex, method, overview. RNA-DNA hybrid binding and 5'-end labeled 48/36 bp RNA-DNA oligonucleotide duplex by M-MuLV RT derivatives, overview
-
-
?
additional information
?
-
-
substrate is a 3H-UTP-labeled RNA: RNA-DNA hybrid, synthesis, overview
-
-
?
additional information
?
-
-
the active site of the RNase H function contains four acidic residues, D443, E478, D498, and D549, that likely coordinate two divalent metal ions that are essential for catalysis
-
-
?
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NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
5'end-directed RNase H of reverse transcriptase
-
-
?
additional information
?
-
-
HIV-1 reverse transcriptase has two enzymatic functions, DNA polymerase and RNase H activities
-
-
?
additional information
?
-
-
RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview
-
-
?
additional information
?
-
-
conserved residues in the connection subdomain and C-terminal ribonuclease H, RNase H, domain of HIV-1 RT contact the nascent DNA primer and modulate the trajectory of the template relative to the RNase H catalytic center. Within the RNase H domain, these residues include Thr473, Glu475, Lys476, Tyr501, and Ile505, while His539 and Asn474 interact with the scissile phosphate of the RNA template,m substrate recognition and binding, overview
-
-
?
additional information
?
-
-
a DNA/RNA hybrid can simultaneously engage both active sites. Of the tested interconverting reverse transcriptase-DNA/RNA species, 43% are active for both sites simultaneously, 27% show only polymerase activity, and the remaining 30% are nonproductive. A string of at least 4-6 nucleotides downstream of the cleaving site is required for efficient RNA cleavage. During processive nucleotide incorporation, sequential rounds of RNA cleavage occur each time after about 6 nucleotides are incorporated, during processive primer extension, diphosphate release is rate-limiting. Although polymerization is efficient and processive, RNase H is inefficient and periodic. This combination allows the two catalytic centers of HIVRT to work simultaneously at similar speeds without being tightly coupled
-
-
?
additional information
?
-
-
HIV RNase H cleaves viral RNA at multiple stages of reverse transcription with at least three distinct modes: random internal cleavages, DNA 3' end-directed and polymerase dependent cleavages, and RNA 5' end-directed cleavages. A biochemical assay uses the HTS-1 RNA/DNA substrate to specifically probe random internal cleavage, which is believed to be the dominant mode of RNA cutting
-
-
?
additional information
?
-
-
RNase H functions as an endonuclease that specifically cleaves the RNA moiety of RNA/DNA hybrids, substrate binding and reaction mechanism, overview
-
-
?
additional information
?
-
-
Moloney murine leukemia virus reverse transcriptase, M-MuLV RT, is a domain structured enzyme that has the N-terminally located DNA polymerization activity and C-terminally located RNase H activity, which interferes with the efficient synthesis of long cDNA molecules
-
-
?
additional information
?
-
-
Moloney murine leukemia virus reverse transcriptase, MMLV RT, shows DNA polymerization activity and RNase H activity. Stabilization of the reverse transcriptase activity by eliminating the RNase H activity, overview
-
-
?
additional information
?
-
-
retroviral reverse transcriptase also possesses a ribonuclease H activity, an enzyme which cleaves the RNA strand of RNA/DNA hetroduplex
-
-
?
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METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Mg2+
Mn2+
Zn2+
additional information
Mg2+
-
required, with more than 90% of maximum activity between 4 and 12 mM
Mg2+
-
required
Mg2+
-
two Mg2+ ions as essential in formation of the active catalytic complex
Mg2+
Human immunodeficiency virus type 1 group M subtype B
-
binding thermodynamics of Mg2+ to RNH, Mg2+ binding has little effect on the thermal stability of enzyme domain RNH
Mg2+
-
Mn2+ is preferred over Mg2+. One-metal catalytic mechanism for the Mn2+/Mg2+-dependent activities
Mn2+
-
solid state structure, two Mn2+ ions bound to the RNase H active site
Mn2+
-
modeling of the HIV-1 RNase H domain in complex with an inhibitor and two Mn2+ cations from crystal structure of manicol-bound enzyme
Mn2+
Human immunodeficiency virus type 1 group M subtype B
-
Mn2+ binding increased the stability of the enzyme domain RNH
Mn2+
-
activation at 0.01-1 mM, inhibitory above. Mn2+ is preferred over Mg2+. One-metal catalytic mechanism for the Mn2+/Mg2+-dependent activities
Zn2+
Human immunodeficiency virus type 1 group M subtype B
-
Zn2+ binding increased the stability of the enzyme domain RNH
additional information
-
in the crystal structure, two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues
additional information
metal coordination, structure, overview
additional information
Human immunodeficiency virus type 1 group M subtype B
-
structural effect of divalent metal ions, i.e. Mn2+, Zn2+, and Mg2+, to the isolated ribonuclease H (RNH) of human immunodeficiency virus (HIV) using isothermal titration calorimetry and circular dichroism, overview. The binding affinity of Mg2+ is about 40 and 400 times lower than those of Mn2+ and of Zn2+, respectively. The structural analysis shows that Mg2+ binding has little effect on the thermal stability of RNH, while Zn2+ and Mn2+ binding increased the stability
additional information
-
the active site of the RNase H function contains four acidic residues, D443, E478, D498, and D549, that likely coordinate two divalent metal ions that are essential for catalysis
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INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(2S)-5,7-dihydroxy-2-(2-hydroxy-1-(phenylsulfonyl)propan-2-yl)-9-methyl-3,4-dihydro-1H-benzo[7]annulen-6(2H)-one
-
-
(2Z)-4-[1-(4-fluorobenzyl)-4-oxo-7-(pyrrolidin-1-yl)-1,4-dihydroquinolin-3-yl]-2-hydroxy-4-oxobut-2-enoic acid
-
-
(4-N,N-dimethylaminobenzoyl)-2-hydroxy-1-naphthyl hydrazone
-
specific
(5E)-6-[1-(2,4-dimethylbenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
-
-
(5E)-6-[1-(2-chlorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
-
-
(5E)-6-[1-(3-methoxybenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
-
-
(5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
-
-
(5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoic acid
-
-
(5E)-6-[1-(4-fluorobenzyl)-4-phenyl-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoic acid
-
-
(6,6,12,12,18,18,18-heptaoxido-5,7,11,13,17-pentaoxa-6l5,12l5,18l5-triphosphaoctadec-1-yl)phosphonate
-
-
1,2-bis[(3-oxobutan-2-yl)oxy]anthracene-9,10-dione
-
20% inhibition
1,2-dihydroxyanthracene-9,10-dione
-
i.e. alizarine, 8% inhibition
1,6-bis[(4-fluorophenyl)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
1,6-dibenzyl-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
1-(3-[[(4-benzyl-5-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]methyl]-4-methoxyphenyl)ethanone
-
-
1-(ethoxymethyl)-3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)pyrimidine-2,4(1H,3H)-dione
-
-
1-(ethoxymethyl)-6-[(4-fluorophenyl)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
1-benzyl-6-[(4-fluorophenyl)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
1-hydroxy-4-((4-(morpholinomethyl)phenyl)amino)pyrido[2,3-d]pyrimidin-2(1H)-one
-
-
1-hydroxy-4-((4-(pyridin-4-yl)phenyl)amino)pyrido[2,3-d]pyrimidin-2(1H)-one
-
-
1-hydroxy-4-([[3-(4-morpholinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
-
-
1-hydroxy-4-([[3-(4-morpholinylmethyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
-
-
1-hydroxy-4-([[4-(4-morpholinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
-
-
1-hydroxy-4-([[4-(4-pyridinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
-
-
1-hydroxy-4-[4-(quinolin-3-yl)anilino]pyrido[2,3-d]pyrimidin-2(1H)-one
-
-
1-hydroxy-4-[[4-(4-morpholinyl)phenyl]amino]pyrido[2,3-d]pyrimidin-2(1H)-one
-
-
1-hydroxy-4-[[4-(quinolin-3-yl)phenyl]amino]pyrido[2,3-d]pyrimidin-2(1H)-one
-
GSK5724, exceptional RNase H inhibitory potency
1-[([1,1'-biphenyl]-4-yl)methyl]-5-hydroxy-4-oxo-1,4-dihydropyridine-3-carboxylic acid
-
-
1-[[(4-fluorophenyl)methoxy]methyl]-6-[(4-fluorophenyl)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-2-phenyl-6,7-dihydrotetraceno[1,2-g]phthalazine-1,9,14(2H)-trione
-
-
2',3'-dideoxy-3'-triaz-2-en-2-ium-3-id-1-yl-3,4-dihydrothymidine
-
-
2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-guanosine
-
40% inhibition of RNase H at 0.05 microM
2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-[2-(4-nitrophenyl)ethyl]guanosine
-
69% inhibition of RNase H at 0.05 microM
2'-deoxy-P-thioguanylyl-(3'->5')-guanosine
-
65% inhibition of RNase H at 0.05 microM
-
2,3,7-trihydroxy-6-(3-nitrobenzyl)cyclohepta-2,4,6-trien-1-one
-
-
2,6-dimethoxy-N-(3-(pyridin-2-ylcarbamoyl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophen-2-yl)nicotinamide
Human immunodeficiency virus type 1 group M subtype B
-
2,7-dihydroxy-4-isopropyl-cyclohepta-2,4,6-triene
-
i.e. beta-thujaplicinol
2,7-dihydroxy-4-methyl-5-(2-methylbutanoyl)cyclohepta-2,4,6-trien-1-one
-
2,7-dihydroxy-4-methyl-5-(4-nitrophenyl)cyclohepta-2,4,6-trien-1-one
-
2,7-dihydroxy-4-methyl-5-(naphthalen-1-yl)cyclohepta-2,4,6-trien-1-one
-
2,7-dihydroxy-4-methyl-5-(naphthalen-2-yl)cyclohepta-2,4,6-trien-1-one
-
2,7-dihydroxy-4-methyl-5-phenylcyclohepta-2,4,6-trien-1-one
-
2,7-dihydroxy-4-methyl-5-[4-(trifluoromethyl)phenyl]cyclohepta-2,4,6-trien-1-one
-
2-(1,2-dihydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
2-(1-benzylamino-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
2-(2,3-dihydro-1H-inden-1-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-(2,3-dihydro-1H-inden-2-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-(2,4-dichlorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-(2-fluorophenyl)acetamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-aminobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-benzylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
2-(2-bromobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-chloro-4-fluorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-chlorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-cyclohexylacetamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-diethylamino-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
2-(2-ethanesulfonyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
2-(2-ethylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
2-(2-fluorobenzamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-fluorobenzamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylic acid
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-fluorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-methoxybenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-methylbenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(2-nitrobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(3,4-dihydroxybenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(3,4-dihydroxyphenyl)-3,5,6,7,8,9-hexahydro-4H-cyclohepta[4,5]thieno[2,3-d]pyrimidin-4-one
Human immunodeficiency virus type 1 group M subtype B
-
2-(3,4-dimethoxybenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(3,5-dimethylphenyl)-2-(3-(ethoxymethyl)-1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)acetonitrile
-
-
2-(3-bromo-4-methoxybenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
-
inhibition of enzymatic activity, but no antiviral effect
2-(3-fluorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(3-phenylpropanamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(4-aminobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(4-chlorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(4-fluorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-(4-nitrobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-([1,1'-biphenyl]-4-yl)-2-(3-(ethoxymethyl)-1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydro pyrimidin-4-yl)acetonitrile
-
-
2-acetamido-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
-
-
2-amino-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-benzamido-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-hydroxy-(4H)-isoquinoline-1,3-dione
-
inhibits RNase H in vitro with submicromolar potency
2-hydroxy-4-(2-phenyl)ethylisoquinoline-1,3(2H,4H)-dione
-
enol-form
2-hydroxy-4-(3-phenyl)propylisoquinoline-1,3(2H,4H)-dione
-
mixture of th mixed ketoenol forms or keto-form
2-hydroxy-4-(4-methylbenzyl)isoquinoline-1,3(2H,4H)-dione
-
mixture of th mixed ketoenol forms or keto-form
2-hydroxy-4-(4-trifluoromethylbenzyl)isoquinoline-1,3(2H-4H)-dione
-
keto-form
2-hydroxy-4-butylisoquinoline-1,3(2H,4H)-dione
-
mixture of th mixed ketoenol forms or keto-form
2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H, 4H)-dione
-
inhibits RNase H in vitro with nanomolar potency
2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H,4H)-dione
-
shows antiviral activity
2-hydroxy-6-methoxy-N-(3-(pyridin-2-ylcarbamoyl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophen-2-yl)nicotinamide
Human immunodeficiency virus type 1 group M subtype B
-
2-oxo-2-(1,2,3,4-tetrahydronaphthalen-1-ylamino)ethyl 5-nitrofuran-2-carboxylate
-
-
2-oxo-2-(tetrahydrofuran-2-ylamino)ethyl 5-nitrofuran-2-carboxylate
-
-
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl benzyl(phenyl)carbamodithioate
-
-
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl dibenzylcarbamodithioate
-
-
2-oxo-2-[(2-phenylpropan-2-yl)amino]ethyl 5-nitrofuran-2-carboxylate
-
-
2-[(2,3,4-trichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
-
inhibitor indentified by FRET-based high-throughput screening assay
2-[(2,4-dichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
-
-
2-[(2,4-dimethylphenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
-
inhibitor indentified by FRET-based high-throughput screening assay
2-[(2-bromo-5-chloro-1-benzothiophen-3-yl)methyl]-5,6-dihydroxypyrimidine-4-carboxylic acid
-
-
2-[(2-methoxy-5-methylphenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioate
-
-
2-[(2-methyl-1-phenylpropan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[(2-methylbutan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[(3,4-dichlorophenyl)methyl]-5,6-dihydroxypyrimidine-4-carboxylic acid
-
-
2-[(3-cyanophenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioate
-
-
2-[(3-cyanophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
-
-
2-[(4-hydroxybenzyl)(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[(cyclohexanecarbonyl)amino]-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
2-[2-(2-fluoro-benzylamino)-1-hydroxy-1-methyl-ethyl]-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
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2-[2-(4-bromophenyl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
-
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2-[2-(biphenyl-4-yl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
-
-
2-[3-(4-chlorophenyl)propanamido]-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
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2-[3-(4-fluorophenyl)propanamido]-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
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2-[4-benzyl-5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]pyridine
-
inhibitor indentified by FRET-based high-throughput screening assay
2-[4-benzyl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridine
-
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2-[benzyl(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
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2-[bis(4-methoxyphenyl)(phenyl)methoxy]ethyl 2-cyanoethyl dipropan-2-ylphosphoramidoite
-
-
2-[tert-butyl(2-phenylethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(3-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(3-oxo-3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(4-fluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(4-methoxybenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(4-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(pentafluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl(phenyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl[2-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl[3-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[tert-butyl[4-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[[2-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[[4-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
2-[[4-(benzyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
-
-
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
-
-
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
-
-
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
-
-
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
-
-
3'-[(E)-[2-(3,4,5-trihydroxybenzoyl)hydrazinylidene]methyl]biphenyl-4-carboxylic acid
-
-
3,4-dihydroxy-N'-[(E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
-
-
3,9,11,14,15-pentahydroxy-7-methoxy-10-methyl-5,6-dihydrobenzo[9,10]tetrapheno[2,3-c]furan-1,8,13(3H)-trione
-
-
3-(benzyloxy)-6-((2'-methoxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-(furan-2-yl)-4-(4-methoxybenzyl)-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazole
-
-
3-(furan-2-yl)-4-phenyl-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazole
-
-
3-cyclopentyl-1,4-dihydroxy-1,8-naphthyridin-2(1H)-one
-
3-hydroxy-1,5,6,7-tetrahydro-2H-cyclopenta[4,5]thieno[2,3-d]pyrimidine-2,4(3H)-dione
-
-
3-hydroxy-1-methyl-6-((3-(pyrimidin-5-yl)phenyl)amino)-pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-1-methyl-6-((3-(tetrahydrofuran-3-yl)phenyl)amino)-pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-1-methyl-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-2-yl)-oxy)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-1-methyl-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)-amino)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-1-methyl-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)-oxy)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-1-methyl-6-(4-(pyridin-4-yl)phenoxy)pyrimidine-2,4-(1H,3H)-dione
-
-
3-hydroxy-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-5,6,7,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-2,4(1H,3H)-dione hydrobromide
-
-
3-hydroxy-5,6-dimethylthieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-5-methyl-2,4-dioxo-1,2,3,4-tetrahydrothieno[2,3-d]pyrimidine-6-carboxylic acid
-
-
3-hydroxy-5-methylthieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-5-phenylthieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((2'-hydroxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((2'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((2-(trifluoromethyl)phenyl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((2-methoxyphenyl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-(trifluoromethyl)-[1,1'-biphenyl]-3-yl)methyl)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-(trifluoromethyl)-[1,1'-biphenyl]-3-yl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3-(trifluoromethyl)phenyl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((3-methoxyphenyl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-2-yl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-3-yl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4-(trifluoromethyl)phenyl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4-hydroxyphenyl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4-methoxyphenyl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((4-nitrophenyl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-((40-methyl-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-(4'-(trifluoromethyl)-[1,10-biphenyl]-4-carbonyl)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-(4'-methoxy-[1,10-biphenyl]-4-carbonyl)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-(4-(trifluoromethyl)benzoyl)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-(40-methyl-[1,10-biphenyl]-4-carbonyl)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-(naphthalen-1-ylthio)pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-phenylthieno [3,2-d]pyrimidine-2,4(1H,3H)-dione
-
-
3-hydroxy-6-phenylthieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
-
3-[2-(4-bromophenyl)-2-oxoethoxy]-1,8-dihydroxy-6-methylanthracene-9,10-dione
-
-
3-[4-(2-methyl-imidazo[4,5-c]pyridin-1-yl)-benzyl]-3H-benzothiazol-2-one
-
-
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
-
-
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
-
-
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
-
-
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
-
-
4'-((3-(ethoxymethyl)-1-hydroxy-5-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)methyl)-[1,1'-biphenyl]-4-carbonitrile
-
-
4'-(1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carbonyl)-[1,1'-biphenyl]-4-carbonitrile
-
-
4-((4'-amino-[1,1'-biphenyl]-4-yl)amino)-1-hydroxy-1,8-naphthyridin-2(1H)-one
Human immunodeficiency virus type 1 group M subtype B
-
4-((cyclopropylmethyl)amino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-(([1,1'-biphenyl]-4-ylmethyl)amino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-(3-bromophenyl)-2,7-dihydroxy-5-methylcyclohepta-2,4,6-trien-1-one
-
4-(4,4-difluoropiperidin-1-yl)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-(4-bromophenyl)-2,7-dihydroxy-5-methylcyclohepta-2,4,6-trien-1-one
-
4-(4-chlorophenyl)-2,7-dihydroxy-5-methylcyclohepta-2,4,6-trien-1-one
-
4-(cyclohexanecarbonyl)-2,7-dihydroxy-5-methylcyclohepta-2,4,6-trien-1-one
-
4-(cyclohexylacetyl)-2,7-dihydroxy-5-methylcyclohepta-2,4,6-trien-1-one
-
4-([1,1'-biphenyl]-4-carbonyl)-2,7-dihydroxy-5-methylcyclohepta-2,4,6-trien-1-one
-
4-([1,1'-biphenyl]-4-yl)-2,7-dihydroxy-5-methylcyclohepta-2,4,6-trien-1-one
-
4-([1,1'-biphenyl]-4-ylamino)-1-hydroxy-1,8-naphthyridin-2(1H)-one
Human immunodeficiency virus type 1 group M subtype B
-
4-([1,1'-biphenyl]-4-ylamino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-([[4-benzyl-5-(furan-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
-
-
4-acetyl-2,7-dihydroxy-5-methylcyclohepta-2,4,6-trien-1-one
-
4-benzoyl-2,7-dihydroxy-5-methylcyclohepta-2,4,6-trien-1-one
-
4-benzyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
-
keto-form; mixture of th mixed ketoenol forms
4-benzyl-3-(benzylsulfanyl)-5-(furan-2-yl)-4H-1,2,4-triazole
-
inhibitor indentified by FRET-based high-throughput screening assay
4-benzyl-3-(benzylsulfanyl)-5-(thiophen-2-yl)-4H-1,2,4-triazole
-
inhibitor indentified by FRET-based high-throughput screening assay
4-benzyl-3-(benzylsulfanyl)-5-phenyl-4H-1,2,4-triazole
-
inhibitor indentified by FRET-based high-throughput screening assay
4-benzyl-3-(furan-2-yl)-5-[(4-methoxybenzyl)sulfanyl]-4H-1,2,4-triazole
-
-
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(furan-2-yl)-4H-1,2,4-triazole
-
-
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
-
inhibitor indentified by FRET-based high-throughput screening assay
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazole
-
-
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
-
-
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazole
-
inhibitor indentified by FRET-based high-throughput screening assay
4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
-
keto-form; mixture of th mixed ketoenol forms
4-tert-butyl-N'-[(E)-(2-hydroxynaphthalen-1-yl)methylidene]benzohydrazide
-
-
4-[1-4-[(4-fluorophenyl)methyl]-7-[N-(3-chloroprop-1-yl)-piperazin-1-yl]-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
35% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(dimethylamino)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
72% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(dimethylamino)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
26% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(morpholin-4-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
0.7% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-acetylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
22% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-acetylpiperazin-1-yl)-4-(1h)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
30% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-ethylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
34% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-ethylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
63% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-methylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
44% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(N-methylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
41% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
44% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
-
18% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-(thiomorpholin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
74% inhibition at 0.01 mM
4-[1-[(4-fluorophenyl)methyl]-7-[N-(3-chloroprop-1-yl)piperazin-1-yl]-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
-
78% inhibition at 0.01 mM
4-[[(4-fluorophenyl)methyl]amino]-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
-
-
4-[[4'-(aminomethyl)biphenyl-4-yl]methyl]-1-hydroxy-1,8-naphthyridin-2(1H)-one
-
-
4-[[4'-(aminomethyl)[1,1'-biphenyl]-4-yl]methyl]-1-hydroxy-1,8-naphthyridin-2(1H)-one
-
-
4-[[4-([4-[(E)-2-cyanovinyl]-2,6-dimethylphenyl]amino)pyrimidin-2-yl]amino]benzonitrile
-
i.e. TMC278 or rilpivirine, enzyme-bound structure, overview
5,6-dimethyl-2-(4-nitrophenyl)thieno[2,3-d]pyrimidin-4(3H)-one
Human immunodeficiency virus type 1 group M subtype B
-
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylaminoethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylsulfanylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-piperidin-1-ylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-(1-hydroxy-2-imadazol-1-yl-1-methyl ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-(1-hydroxy-ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
-
5,7-dihydroxy-2-isopropenyl-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
i.e. manicol, the alpha-hydroxytroplone potently and specifically inhibits HIV RT ribonuclease H, enzyme-bound structure, overview
5-(1,1-dioxido-1,2-thiazinan-2-yl)-N-(4-fluorobenzyl)-8-hydroxy-1,6-naphthyridine-7-carboxamide
-
-
5-(4-chlorophenyl)-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
-
5-benzyl-6-ethyl-1-(((4-fluorobenzyl)oxy)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
5-bromo-6-((4-bromophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
5-ethyl-1-(((4-fluorobenzyl)oxy)methyl)-6-(4-fluorophenyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
6-( (3'- fluoro-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((2',4'-bis(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((2',4'-dichloro-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((2',4'-difluoro-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((2',4'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((2-(3,5-dimethylisoxazol-4-yl)phenyl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((2-bromophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((2-ethylphenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((2-fluorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((3',4'-dimethoxy-[1,10-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3',5'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)methyl)-1-(ethoxymethyl)-3-hydroxy-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-chloro-4'-fluoro-[1,1'-biphenyl]-3-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-chloro-5'-(trifluoromethyl)-[1,1'-biphenyl]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-chloro-5'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-chloro-[1,1'-biphenyl ] - 4 -yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-chloro-[1,1'-biphenyl ]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-fluoro-4'-methoxy-[1,1'-biphenyl]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-fluoro-4'-methoxy-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-fluoro-4'-methoxy-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-fluoro-[1,1'-biphenyl]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-fluoro-[1,1'-biphenyl]-3-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3'-fluoro-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3-bromophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3-chlorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((3-fluorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-chloro-3'-fluoro-[1,1'-biphenyl]-4-yl)methyl)-1-(ethoxymethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-chloro-3'-fluoro-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-chloro-[1,1'-biphenyl ]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-chloro-[1,1'-biphenyl]-2-yl)oxy)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-chloro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-chloro-[1,1'-biphenyl]-3-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-chloro-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-chloro-[1,1'-biphenyl]-4-yl)oxy)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-chloro-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-fluoro-3'-methyl-[1,1'-biphenyl]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-fluoro-3'-methyl-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-fluoro-3'-methyl-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-fluoro-[1,1'-biphenyl]-2-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-fluoro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-fluoro-[1,1'-biphenyl]-3-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4'-fluoro-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4-(3,5-dimethylisoxazol-4-yl)phenyl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-((4-bromophenyl)thio)-3-hydroxy-5-iodopyrimidine-2,4(1H,3H)-dione
-
-
6-((4-bromophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4-chlorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4-ethylphenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-((4-fluorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-(3',4'-dimethoxy-[1,10-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-(3',5'-dimethyl-[1,10-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-(3,5-dimethylbenzoyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-(4'-chloro-3'-fluoro-[1,10-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-(4'-fluoro-3'-methyl-[1,10-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-(4'-fluoro-[1,1'-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-(4-chlorophenyl)-3-hydroxythieno[3,2-d]pyrimidine-2,4(1H,3H)-dione
-
-
6-(4-fluorophenyl)-3-hydroxythieno[3,2-d]pyrimidine-2,4(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-2-yloxy)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-3-carbonyl)-1-(ethoxymethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-3-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-3-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-3-ylmethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-3-yloxy)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-4-carbonyl)-1-(ethoxymethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-4-yl)-1-(ethoxymethyl)-3-hydroxy-5-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-4-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-4-ylmethyl)-1-(ethoxymethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-4-ylmethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-4-yloxy)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
-
-
6-([1,1'-biphenyl]-4-ylthio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-(((4-fluorobenzyl)oxy)methyl)-5-isopropyl-3-methoxypyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-(((4-fluorobenzyl)oxy)methyl)-5-isopropyl-3-methylpyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-(ethoxymethyl)-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-[(benzyloxy)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-[2-(4-fluorophenyl)ethyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-[3-(4-fluorophenyl)propyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-[4-(4-fluorophenyl)butyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-[[(2,4-difluorophenyl)methoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-[[(3-chloro-2-fluorophenyl)methoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-[[(4-fluorophenyl)methoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-[[3-(4-fluorophenyl)propoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-1-[[4-(4-fluorophenyl)butoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
-
-
6-benzyl-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
-
6-[(4'-chloro[1,1'-biphenyl]-3-yl)amino]-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-[([1,1'-biphenyl]-4-yl)amino]-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-[([1,1'-biphenyl]-4-yl)methyl]-2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
-
6-[([1,1'-biphenyl]-4-yl)methyl]-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-[([1,1'-biphenyl]-4-yl)oxy]-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-[([1,1'-biphenyl]-4-yl)sulfanyl]-3-hydroxypyrimidine-2,4(1H,3H)-dione
-
-
6-[1-(4-fluorophenyl)methyl-1H-pyrrol-2-yl)]-2,4-dioxo-5-hexenoic acid ethyl ester
-
i.e. RDS1643, RNase H inhibitor
6-[1-(4-fluorophenyl)methyl-1H-pyrrol-2-yl]-2,4-dioxo-5-hexenoic acid ethyl ester
-
i.e. RDS-1643, shows relatively weak but selective inhibitory activity against RNase H
6-[4-(diethylamino)phenoxy]-3-[ethoxy(hydroxy)methyl]-1,4-dihydroxy-1,8-naphthyridin-2(1H)-one
-
7-benzyl-3-hydroxy-5,6,7,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-2,4(1H,3H)-dione hydrochloride
-
-
7-benzyl-3-hydroxyhexahydropyrido[3,4-d]pyrimidine-2,4(1H,3H)-dione hydrochloride
-
-
7-ethyl-3-hydroxy-5,6,7,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-2,4(1H,3H)-dione hydrochloride
-
-
9,10-dioxo-2-(2-oxo-2-phenylethoxy)-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-(2-oxopropoxy)-9,10-dihydroanthracen-1-yl acetate
-
10% inhibition
9,10-dioxo-2-(prop-2-en-1-yloxy)-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-(prop-2-yn-1-yloxy)-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-2-[(2-oxopentan-3-yl)oxy]-9,10-dihydroanthracen-1-yl acetate
-
inhibits the RNase H function and is inactive on the DNA polymerase function
9,10-dioxo-2-[(3-oxobutan-2-yl)oxy]-9,10-dihydroanthracen-1-yl acetate
-
-
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl diacetate
-
12% inhibition
actinomycin D
-
limits the enzyme to the first strand synthesis
delaviridine
-
a nonnucleoside reverse transcriptase inhibitor
Dextran sulfate
-
more potent inhibitor of RNase H than of reverse transcriptase. 50% infective dose corresponds to 0.1 nM
-
dimethyl 3-(chloromethyl)-5,7-dihydroxy-6-oxocyclohepta-2,4,7-triene-1,2-dicarboxylate
-
dimethyl 5,7-dihydroxy-3-(methoxymethyl)-6-oxocyclohepta-2,4,7-triene-1,2-dicarboxylate
-
dimethyl 5,7-dihydroxy-3-methyl-6-oxocyclohepta-2,4,7-triene-1,2-dicarboxylate
-
ethyl (2Z)-4-[1-(4-fluorobenzyl)-4-oxo-7-(pyrrolidin-1-yl)-1,4-dihydroquinolin-3-yl]-2-hydroxy-4-oxobut-2-enoate
-
-
ethyl (5E)-6-[1-(2,4-dimethylbenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
-
ethyl (5E)-6-[1-(2-chlorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
selectively inhibits RNase H activity in the low micromolar range
ethyl (5E)-6-[1-(3-methoxybenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
-
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
-
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoate
-
-
ethyl (5E)-6-[1-(4-fluorobenzyl)-4-phenyl-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoate
-
-
ethyl 2-(2-fluorobenzamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
Human immunodeficiency virus type 1 group M subtype B
-
ethyl 2-(4-chlorobenzamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
Human immunodeficiency virus type 1 group M subtype B
-
ethyl 4,6-dihydroxy-2,7-dimethyl-5-oxocyclohepta-1,3,6-triene-1-carboxylate
-
ethyl 4,6-dihydroxy-2-methyl-5-oxocyclohepta-1,3,6-triene-1-carboxylate
-
F3284-8495
-
specific inhibitor with low micromolar potency in vitro
guanylyl-(3'->5')-guanosine
-
89% inhibition of RNase H at 0.05 microM
manicol
source of manicol is the root bark of a rare Guyanan tree, Dulacia guianeinsis
methyl 2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinoline-4-carboxylate
-
-
methyl 4'-(1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carbonyl)-[1,10-biphenyl]-4-carboxylate
-
-
methyl 4,6-dihydroxy-2-methyl-5-oxocyclohepta-1,3,6-triene-1-carboxylate
-
methyl 4-((4'-amino-[1,1'-biphenyl]-4-yl)amino)-1-hydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylate
Human immunodeficiency virus type 1 group M subtype B
-
methyl 4-(1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carbonyl)benzoate
-
-
methyl 4-amino-1-hydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylate
Human immunodeficiency virus type 1 group M subtype B
-
methyl 7-bromo-4,6-dihydroxy-2-methyl-5-oxocyclohepta-1,3,6-triene-1-carboxylate
-
N-(3-((2-fluorophenyl)carbamoyl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophen-2-yl)picolinamide
Human immunodeficiency virus type 1 group M subtype B
-
N-(4-chlorobenzyl)-8-hydroxy-1,6-naphthyridine-7-carboxamide
-
-
N-(pyridin-2-yl)-2-(thiophene-2-carboxamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
N-(pyridin-2-yl)-2-[2-(quinolin-6-yl)acetamido]-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
-
NaCl
-
inhibits substrate binding by the enzyme, in the samples that are pretreated with DTT, the addition of salt strongly inhibits the reaction and completely eliminates off-register cleavage
P-thioguanylyl-(3'->5')-guanosine
-
50% inhibition of RNase H at 0.05 microM
-
tenofovir disoproxil
-
a nucleoside reverse transcriptase inhibitor
xylan polysulfate
-
more potent inhibitor of RNase H than of reverse transcriptase. 50% infective dose corresponds to 8 nM
-
2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosine
-
61% inhibition of RNase H at 0.05 microM
2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosine
-
11% inhibition of RNase H at 0.05 microM
2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one
-
inhibition of enzymatic activity, but no antiviral effect
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
-
inhibition of enzymatic activity, but no antiviral effect
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
-
-
2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
inhibition of enzymatic activity, but no antiviral effect
2-hydroxyisoquinoline-1,3(2H,4H)-dione
an active site directed inhibitor, stabilizes RH domain helix E
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
-
inhibitor indentified by FRET-based high-throughput screening assay
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
-
-
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
-
inhibitor has little effect on bacterial RNase H activity in vitro
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
-
-
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
-
additionally inhibits HIV-1 replication effectively. Inhibitor has little effect on bacterial RNase H activity in vitro
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
-
-
beta-thujaplicinol
slow-binding RNase H inhibitor with noncompetitive kinetics that forms a tropylium ion that interacts favorably with reverse transcriptase and the RNA:DNA substrate
beta-thujaplicinol
-
shows submicromolar inhibitory activity against RNase H
beta-thujaplicinol
a non-competitive inhibitor of RNase H
efavirenz
-
second generation non-nucleoside reverse transcriptase inhibitor, shows the effect of simultaneously reorienting domain motions and obstructing the p66 thumb fluctuations
efavirenz
-
stronger effect of mutation N348I on RNase H susceptibility to nevirapine as compared with efavirenz
ethyl 1,4-dihydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylate
interactions between MK1 and two Mn2+ ions, which are coordinated by the RNase H active site residues D443, E478, D498, and D549, binding structure, overview. In addition, G444, S499, A538, H539, V552, and S553 contribute to the binding site
ethyl 1,4-dihydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylate
-
-
heparin
-
more potent inhibitor of RNase H than of reverse transcriptase. 50% infective dose corresponds to 0.5-1.5 nM
heparin
-
inhibits substrate binding by the enzyme, in the samples that are pretreated with DTT, the addition of heparin strongly inhibits the reaction and completely eliminates off-register cleavage
nevirapine
-
non-nucleoside RT inhibitors such as nevirapine interfere directly with the global hinge-bending mechanism that controls the cooperative motions of the p66 fingers and thumb subdomains. The net effect of nevirapine binding is to change the direction of domain movements rather than suppress their mobilities
nevirapine
-
a non-nucleoside RT inhibitor, NNRTI, stronger effect of mutation N348I on RNase H susceptibility to nevirapine as compared with efavirenz
nevirapine
a nonnucleoside reverse transcriptase inhibitor, NNRTI
NSC727447
-
mutation T473C increases sensitivity of the enzyme for NSC727447 by 50fold
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid
-
additionally inhibits DNA strand transfer and DNA polymerase activity of the retroviral reverse transcriptase
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid
-
inhibits RNase H activity, does not significantly affect DNA polymerase activity of reverse transcriptase. In the absence of DNA synthesis, [2-(4-chlorophenyl)hydrazinylidene]propanedioic acid interferes with the translocation, or repositioning, of the enzyme on the RNA-DNA template duplex. Inhibitor is highly specific for human immunodeficiency virus. The dicarboxylic acid moiety is essential for activity, and Mg2+ chelates directly with a Kd value of 2.4 mM
additional information
-
synthesis of 2-hydroxyisoquinoline-1,3(2H,4H)-dione derivatives as inhibitors of the RNase H activity of the reverse transcriptase of HIV-1, docking, study, overview. No inhibition by keto-5i and 5l
-
additional information
-
antiretroviral drugs inhibit the reverse-transcriptase (RT) of HIV. The differences between HIV-1 and HIV-2 RTs explain why some of the anti-HIV-1 drugs are not effective against HIV-2. One major difference between the two HIV RTs is the low ribonuclease H (RNase H) activity of HIV-2 RT relative to HIV-1 RT
-
additional information
-
identification and evaluation of thiocarbamate and triazole inhibitors targeting RNase H activity of HIV reverse transcriptase, overview
-
additional information
-
design, synthesis, and screening of derivatives of 5-nitro-furan-2-carboxylic acid as inhibitors of the RNAse H activity of HIV-1 reverse transcriptase, overview. Modulation of the 5-nitro-furan-2-carboxylic moiety results in a drastic decrease in inhibitory potency. Binding mode of active derivatives, in which three oxygen atoms aligned in a straight form at the nitro-furan moiety are coordinated to two divalent metal ions located at RNase H reaction site. The nitro-furan-carboxylic moiety is one of the critical scaffolds for RNase H inhibition. Cytotoxicity of the synthesized compounds, overview
-
additional information
-
non-nucleoside RT inhibitors, NNRTIs, bind to an allosteric site that is 10 A from the polymerase active site and 60 A from the RNase H active site
-
additional information
-
no inhibition by 5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-piperidin-1-ylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one, 5,7-dihydroxy-2-(1-hydroxy-2-imadazol-1-yl-1-methyl ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one, 2-(2-diethylamino-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one, and 2-(1-benzylamino-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
-
additional information
structures of naphthyridinone-containing inhibitors bound to the RNase H active site, overview. This class of compounds binds to the active site via two metal ions that are coordinated by catalytic site residues, D443, E478, D498, and D549. The directionality of the naphthyridinone pharmacophore is restricted by the ordering of D549 and H539 in the RNase H domain
-
additional information
-
C-terminal domain mutations reduce RNase H activity either directly by affecting the RNase H cleavage activity of the enzyme, or indirectly by affecting the overall positioning of the template/primer strand, which in turn affects RNase H activity, template switching, polymerization and/or nucleotide excision. Effects of enzyme mutations on treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors, detailed overview. Nucleoside reverse transcriptase inhibitors are nucleoside analogues that lack the 3' OH on the sugar ring and competitively block reverse transcription by causing chain termination during DNA polymerization. Nucleoside reverse transcriptase inhibitors are prodrugs that require intracellular phosphorylation to the 5'-triphosphate formed by host cell kinases in order to become active. Nonnucleoside reverse transcriptase inhibitors in general are non-competitive inhibitors of RT that bind to a hydrophobic pocket near the polymerase active site, inducing conformational changes that inhibit RT enzymatic activity. Inhibition mechanisms of the two inhibitor classes, overview
-
additional information
-
mechanisms of catalysis and drug inhibition of polymerase and RNase H functions of RT by nucleos(t)ide reverse transcriptase inhibitor and non-nucleoside reverse transcriptase inhibitor drugs, and molecular mechanisms of drug resistance, detailed overview
-
additional information
-
discovery and development of bona fide RNase H inhibitors, overview
-
additional information
-
design, synthesis and biological evaluations of N-hydroxy thienopyrimidine-2,4-diones as inhibitors of HIV reverse transcriptase-associated RNase H, antiviral activity, overview. The compounds potently and selectively inhibit RNase H with considerable potency against HIV-1 in cell culture. They also show inhibition of integrase strand transfer (INST) activity. Structure-activity-relationship analysis. Molecular modeling of analogues 3-hydroxy-6-phenylthieno[2,3-d]pyrimidine-2,4(1H,3H)-dione and 5-(4-chlorophenyl)-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione at the RNase H active site. Analysis of the enzyme's crystal structure in complex with inhibitor 6-benzyl-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
-
additional information
-
major chemotypes reported as HIV RNase H active site inhibitors, overview. Design, synthesis, biochemical and antiviral evaluations of a 6-arylthio subtype of the 3-hydroxypyrimidine-2,4-dione (HPD) chemotype as inhibitors of the enzyme. The analogues inhibit RT RNase H in single-digit nanomolar range without inhibiting RT polymerase (pol) at concentrations up to 0.01 mM showing high inhibitory selectivity. Many of the analogues also inhibit integrase strand transfer (INST) activity in low to sub micromolar range. Most analogues inhibit HIV progression in low micromolar range without cytotoxicity. Molecular docking and modelling
-
additional information
-
6-biphenylmethyl-3-hydroxypyrimidine-2,4-diones potently and selectively inhibit HIV reverse transcriptase-associated RNase H, overview. Design, synthesis, biochemical and antiviral evaluations of a 6-biphenylmethyl subtype of the 3-hydroxypyrimidine-2,4-dione (HPD) chemotype. The subtype potently inhibits RT RNase H in low nanomolar range without inhibiting RT polymerase (pol) or integrase strand transfer (INST) at the highest concentrations tested. A few analogues inhibit HIV in low micromolar range without cytotoxicity at concentrations up to 0.1 mM in cell-based assays. EC50 values and antiviral activity of the compounds, overview
-
additional information
-
pharmacophore-based design and sythesis of 3-hydroxypyrimidine-2,4-dione subtypes as inhibitors of HIV reverse transcriptase-associated RNase H, enzyme inhibition shows tolerance of a nonflexible linker, overview. 3-Hydroxypyrimidine-2,4-dione (HPD) subtypes with a nonflexible C-6 carbonyl linkage exhibit potent and selective biochemical inhibitory profiles with strong RNase H inhibition at low nM, weak to moderate integrase strand transfer (INST) inhibition at low micromolecular range, and no to marginal RT polymerase (pol) inhibition up to 0.010 mM. A few analogues also demonstrate significant antiviral activity without cytotoxicity. EC50 values of the compounds, overview
-
additional information
-
3-hydroxypyrimidine-2,4-diones act as selective active site inhibitors of HIV reverse transcriptase-associated RNase H, design, synthesis, and biochemical evaluations, overview. No inhibition by 9z. The activity and selectivity profiles of subtype 11 are manifested with a few selected analogues demonstrating exceptional potency in inhibiting RNase H. Although they also inhibit RT pol, the micromolar activity reflects a sizable selectivity (14-49 fold) strongly favoring RNase H inhibition. The compounds also show inhibition of integrase strand transfer (INST) activity. Molecular modelling
-
additional information
library screening of alpha-hydroxytropolones synthesized through a convenient oxidopyrylium cycloaddition/ring-opening sequence, synthetic alpha-hydroxytropolones act as inhibitors of HIV reverse transcriptase ribonuclease H activity, structure-function analysis, overview. Homology model of substrate- and inhibitor-bound HIV-1 RNase H, molecular docking. beta-Thujaplicinol and manicol share a rare alpha-hydroxytropolone moiety that crystal-structure analysis reveals to be a key for the potent inhibition of the enzyme. Unfortunately, both of these natural products display cytotoxicity in cell-based antiviral assays that precludes cellular antiviral activity. The slight steric change from a methyl to chloromethylene to methoxymethylene decreases the inhibitory potency by close to a full order of magnitude. Enzyme residue Tyr501, which is predicted computationally to be involved in interactions with the side chain, is blocked by the substrate. HIV-1 cytopathicity assays are performed, cytotoxicity of synthetic alpha-hydroxytropolones and beta-thujaplicinol against CEM-SS cells
-
additional information
-
library screening of alpha-hydroxytropolones synthesized through a convenient oxidopyrylium cycloaddition/ring-opening sequence, synthetic alpha-hydroxytropolones act as inhibitors of HIV reverse transcriptase ribonuclease H activity, structure-function analysis, overview. Homology model of substrate- and inhibitor-bound HIV-1 RNase H, molecular docking. beta-Thujaplicinol and manicol share a rare alpha-hydroxytropolone moiety that crystal-structure analysis reveals to be a key for the potent inhibition of the enzyme. Unfortunately, both of these natural products display cytotoxicity in cell-based antiviral assays that precludes cellular antiviral activity. The slight steric change from a methyl to chloromethylene to methoxymethylene decreases the inhibitory potency by close to a full order of magnitude. Enzyme residue Tyr501, which is predicted computationally to be involved in interactions with the side chain, is blocked by the substrate. HIV-1 cytopathicity assays are performed, cytotoxicity of synthetic alpha-hydroxytropolones and beta-thujaplicinol against CEM-SS cells
-
additional information
-
extracts of Uvaria angolensis from tropical zone of Cameroon (Mount Kalla in Yaounde City) are a promising source of inhibitors of HIV-1 reverse transcriptase-associated RNA-dependent DNA polymerase (RDDP) and HIV-1 RNase H functions. Usage of stem bark methanol extract that inhibits both HIV-1 RNase H function and RDDP activity with IC50 values of 0.001 mg/ml and 0.00062 mg/ml, respectively, and, after been fractionated with different solvents, its solid residue shows an IC50 of 0.00010 mg/ml and of 0.00023 mg/ml against RNase H and RDDP, respectively. Methanol and water extracts from leaves and twigs, are also effective but much less than stem bark extracts. Determination of cytotoxicity
-
additional information
-
binding mode and resistance profile for a dual-target pyrrolyl diketo acid scaffold against HIV-1 integrase and reverse-transcriptase-associated ribonuclease H (RNase H), using wild-type and mutant enzymes, and detail energy components contribution of calculated binding free energies of studied inhibitors binding to HIV-1 IN and RNase H wild-types and mutants, overview
-
additional information
Human immunodeficiency virus type 1 group M subtype B
inhibitor library screening, identification and synthesis of cycloheptathiophene-3-carboxamide derivatives as allosteric HIV-1 ribonuclease H inhibitors, binding mode of compounds 2-(3,4-dihydroxyphenyl)-3,5,6,7,8,9-hexahydro-4H-cyclohepta[4,5]thieno[2,3-d]pyrimidin-4-one, 2-(3,4-dimethoxybenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide, and 2-(3,4-dihydroxybenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide, overview
-
additional information
Human immunodeficiency virus type 1 group M subtype B
development and evaluation of inhibitors against the RNase H active site of HIV-1 reverse transcriptase. The RNase H active site of HIV-1 RT is sufficiently different from the active sites of the two cellular human enzymes, RNase H1 and RNase H2, that compounds can be developed as selective inhibitors of viral RH. Antiviral activities of compounds XZ456, XZ460, XZ462, and MK463 against wild-type enzyme and against HIV-1 vectors that carry well-known INSTI, NNRTI, and NRTI resistance mutations, overview. XZ456 and XZ460 both inhibit these NRTI mutants with efficacies similar to their antiviral activities against wild-type HIV-1. Conversely, the NRTI-resistant mutants cause a 3 to 4fold reduction in susceptibility to XZ462 and MK463. Compounds are tested in viral replication and cytotoxicity assays. For enzyme-inhibitor structural modelling, coordinates of the following retroviral RT-RT inhibitor structures are used: HIV RT-MK1 (PDB ID 3LP0) and HIV RT-MK2 (PDB ID 3LP1). The compounds target the catalytic magnesium ions in the HIV-1 RNase H
-
additional information
-
inhibitory potency and binding of dumbbell oligonucleotides to MoMuL virus RNase H, overview. The best dumbbell oligonucleotide, inhibitor contained phosphorothioate residues in both the loops
-
additional information
-
magnesium chelating 2-hydroxyisoquinoline-1,3(2H,4H)-diones, as inhibitors of HIV-1 integrase and/or the HIV-1 reverse transcriptase ribonuclease H domain, overview. 2-Hydroxyisoquinoline-1,3(2H,4H)-dione forms a 1:1 complex with Mg2+, but a 1:2 complex with Mn2+,
-
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ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
efavirenz
-
stimulates reverse transcriptase RNase H activity. Efavirenz stimulates DNA 3'-directed and RNA 5'-directed RNase H activity
nucleocapsid protein NCp7
-
enhances ribonuclease H activity and changes the specificity of hydrolysis. As a model, the NCp7 binds to the DNA strand and through interaction with HIV-1 RT facilitates the delivery of the DNA-RNA duplex into the RNase H site for cleavage, thereby altering the rate and location of RNase H cleavage
-
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DISEASE
TITLE OF PUBLICATION
LINK TO PUBMED
Acquired Immunodeficiency Syndrome
Evaluation of natural products as inhibitors of human immunodeficiency virus type 1 (HIV-1) reverse transcriptase.
Acquired Immunodeficiency Syndrome
Recent Advances in the Research of HIV-1 RNase H Inhibitors.
Acquired Immunodeficiency Syndrome
Recombinant polypeptides from the human immunodeficiency virus reverse transcriptase define three epitopes recognized by antibodies in sera from patients with acquired immunodeficiency syndrome.
Acquired Immunodeficiency Syndrome
Species differences in nucleotide pool levels of 2',3'-dideoxycytidine: a possible explanation for species-specific toxicity.
Acquired Immunodeficiency Syndrome
Ultrastructure of peripheral neuropathy induced in rabbits by 2',3'-dideoxycytidine.
Anemia
Purification and characterization of recombinant equine infectious anemia virus reverse transcriptase.
Anemia
Substituting a conserved residue of the ribonuclease H domain alters substrate hydrolysis by retroviral reverse transcriptase.
Equine Infectious Anemia
Purification and characterization of recombinant equine infectious anemia virus reverse transcriptase.
Equine Infectious Anemia
Substituting a conserved residue of the ribonuclease H domain alters substrate hydrolysis by retroviral reverse transcriptase.
Hepatitis B
HBV genotypic resistance to lamivudine in kidney recipients and hemodialyzed patients.
Infections
A Single Dose of a MIV-150/Zinc Acetate Gel Provides 24?h of Protection Against Vaginal Simian Human Immunodeficiency Virus Reverse Transcriptase Infection, with More Limited Protection Rectally 8-24?h After Gel Use.
Infections
Short communication: a repeated simian human immunodeficiency virus reverse transcriptase/herpes simplex virus type 2 cochallenge macaque model for the evaluation of microbicides.
Leukemia
Abortive reverse transcription by mutants of Moloney murine leukemia virus deficient in the reverse transcriptase-associated RNase H function.
Leukemia
Human immunodeficiency virus reverse transcriptase ribonuclease H: specificity of tRNA(Lys3)-primer excision.
Leukemia
Inhibition of human immunodeficiency virus-associated reverse transcriptase by 14-O-acyladriamycins.
Leukemia
Mechanisms of the inhibition of reverse transcription by antisense oligonucleotides.
Leukemia
RNase H domain of Moloney murine leukemia virus reverse transcriptase retains activity but requires the polymerase domain for specificity.
Leukemia
Sequence requirements for removal of tRNA by an isolated human immunodeficiency virus type 1 RNase H domain.
Leukemia
Specificity of human immunodeficiency virus-1 reverse transcriptase-associated ribonuclease H in removal of the minus-strand primer, tRNA(Lys3).
Leukemia, T-Cell
Human T-cell leukemia virus type 1 reverse transcriptase (RT) originates from the pro and pol open reading frames and requires the presence of RT-RNase H (RH) and RT-RH-integrase proteins for its activity.
Neoplasms
Role of altered metabolism in dideoxynucleoside pharmacokinetics. Studies of 2'-beta-fluoro-2',3'-dideoxyinosine and 2'-beta-fluoro-2',3'-dideoxyadenosine in rats.
Neoplasms
Selective inhibition of HIV-1 reverse transcriptase-associated ribonuclease H activity by hydroxylated tropolones.
Visna
Treatment of visna virus infection in lambs with the acyclic nucleoside phosphonate analogue 9-(2-phosphonylmethoxyethyl)adenine (PMEA).
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KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.000029
RNA-DNA hybrid
-
mutant enzyme Y501A, at pH 7.8 and 37°C
-
0.00003
RNA-DNA hybrid
-
mutant enzyme N474A, at pH 7.8 and 37°C
-
0.000041
RNA-DNA hybrid
-
mutant enzyme R557A, at pH 7.8 and 37°C
-
0.000085
RNA-DNA hybrid
-
mutant enzyme R448A, at pH 7.8 and 37°C
-
0.0001
RNA-DNA hybrid
-
mutant enzyme Q475A, at pH 7.8 and 37°C
-
0.000126
RNA-DNA hybrid
-
wild type enzyme, at pH 7.8 and 37°C
-
additional information
additional information
-
pre-steady-state kinetics, overview
-
additional information
additional information
-
presteady-state kinetic analyses, overview
-
additional information
additional information
Human immunodeficiency virus type 1 group M subtype B
-
analysis of the binding thermodynamics and structural effect of divalent metal ions, i.e. Mn2+, Zn2+, and Mg2+, to the isolated ribonuclease H (RNH) of human immunodeficiency virus (HIV) using isothermal titration calorimetry and circular dichroism, overview
-
additional information
additional information
Human immunodeficiency virus type 1 group O subtype B
-
kinetics of wild-type and mutant enzymes are determined with the RNA/DNA template-primer R33B/20A
-
additional information
additional information
Human immunodeficiency virus type 1 group M subtype B
kinetics of wild-type enzyme are determined with the RNA/DNA template-primer R33B/20A
-
additional information
additional information
-
RNase H activity is analysed using presteady-state kinetics using global data
-
additional information
poly(rA)/oligo(dT)
-
apparent binding constant 3500 per mM
-
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TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.004
RNA-DNA hybrid
-
mutant enzyme Y501A, at pH 7.8 and 37°C
-
0.04
RNA-DNA hybrid
-
mutant enzyme N474A, at pH 7.8 and 37°C
-
0.18
RNA-DNA hybrid
-
mutant enzyme Q475A, at pH 7.8 and 37°C
-
0.42
RNA-DNA hybrid
-
mutant enzyme R557A, at pH 7.8 and 37°C
-
0.73
RNA-DNA hybrid
-
mutant enzyme R448A, at pH 7.8 and 37°C
-
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kcat/KM VALUE [1/mMs-1]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
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Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0115
2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-[2-(4-nitrophenyl)ethyl]guanosine
-
-
0.00014
beta-thujaplicinol
presence of Mg2+ and DNA:RNA hybrid, pH 8.0
additional information
additional information
-
non competitive inhibition kinetics of alizarine derivatives, overview
-
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IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.00051
(2S)-5,7-dihydroxy-2-(2-hydroxy-1-(phenylsulfonyl)propan-2-yl)-9-methyl-3,4-dihydro-1H-benzo[7]annulen-6(2H)-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0193
(5E)-6-[1-(2,4-dimethylbenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0192
(5E)-6-[1-(2-chlorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.087
(5E)-6-[1-(3-methoxybenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0161
(5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.028
(5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0077
(5E)-6-[1-(4-fluorobenzyl)-4-phenyl-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoic acid
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.013
1,6-bis[(4-fluorophenyl)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.015
1,6-dibenzyl-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0008
1-(3-[[(4-benzyl-5-methyl-4H-1,2,4-triazol-3-yl)sulfanyl]methyl]-4-methoxyphenyl)ethanone
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0021
1-(ethoxymethyl)-3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.025
1-(ethoxymethyl)-6-[(4-fluorophenyl)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
above, pH and temperature not specified in the publication
0.01
1-benzyl-6-[(4-fluorophenyl)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0002
1-hydroxy-4-((4-(morpholinomethyl)phenyl)amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000079
1-hydroxy-4-((4-(pyridin-4-yl)phenyl)amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.0002
1-hydroxy-4-([[3-(4-morpholinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000398
1-hydroxy-4-([[3-(4-morpholinylmethyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.0001
1-hydroxy-4-([[4-(4-morpholinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000016
1-hydroxy-4-([[4-(4-pyridinyl)phenyl]methyl]amino)pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.00005
1-hydroxy-4-[[4-(4-morpholinyl)phenyl]amino]pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000003
1-hydroxy-4-[[4-(quinolin-3-yl)phenyl]amino]pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0062
1-[[(4-fluorophenyl)methoxy]methyl]-6-[(4-fluorophenyl)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.04
2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-naphthalen-1-ylguanosine
Human immunodeficiency virus 1
-
-
0.04
2'-deoxy-2'-fluoro-P-thioadenylyl-(3'->5')-N-[2-(4-nitrophenyl)ethyl]guanosine
Human immunodeficiency virus 1
-
-
0.0215
2,6-dimethoxy-N-(3-(pyridin-2-ylcarbamoyl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophen-2-yl)nicotinamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0006
2,7-dihydroxy-4-(propan-2-yl)cyclohepta-2,4,6-trien-1-one
Human immunodeficiency virus 1
-
-
0.0019
2-(1,2-dihydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00096
2-(1-benzylamino-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0061
2-(2,3-dihydro-1H-inden-1-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0055
2-(2,3-dihydro-1H-inden-2-ylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.01224
2-(2,4-dichlorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0099
2-(2-(2-fluorophenyl)acetamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.01488
2-(2-aminobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0013
2-(2-benzylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00457
2-(2-bromobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0075
2-(2-chloro-4-fluorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0239
2-(2-chlorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0671
2-(2-cyclohexylacetamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0005
2-(2-diethylamino-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00024
2-(2-ethanesulfonyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00038
2-(2-ethylsulfanyl-1-hydroxy-1-methyl-ethyl)-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.01373
2-(2-fluorobenzamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.1
2-(2-fluorobenzamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylic acid
Human immunodeficiency virus type 1 group M subtype B
above, pH 7.8, 37°C
0.02189
2-(2-fluorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.01425
2-(2-methoxybenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0183
2-(2-methylbenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.05348
2-(2-nitrobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0012
2-(3,4-dichlorobenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
Human immunodeficiency virus 1
-
-
0.00084
2-(3,4-dihydroxybenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.00401
2-(3,4-dimethoxybenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0037
2-(3,5-dimethylphenyl)-2-(3-(ethoxymethyl)-1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)acetonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0009
2-(3-bromo-4-methoxybenzyl)-5,6-dihydroxypyrimidine-4-carboxylic acid
Human immunodeficiency virus 1
-
-
0.02047
2-(3-fluorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0146
2-(3-phenylpropanamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.02143
2-(4-aminobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.01778
2-(4-chlorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.00472
2-(4-fluorobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.02047
2-(4-nitrobenzamido)-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.018
2-(tert-butylamino)-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.00076
2-([1,1'-biphenyl]-4-yl)-2-(3-(ethoxymethyl)-1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydro pyrimidin-4-yl)acetonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.1
2-acetamido-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
above, pH 7.8, 37°C
0.0071
2-amino-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.002
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0201
2-amino-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0148
2-benzamido-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0668
2-hydroxy-4-(3-phenyl)propylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.08
2-hydroxy-4-(4-methylbenzyl)isoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0427
2-hydroxy-4-(4-trifluoromethylbenzyl)isoquinoline-1,3(2H-4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0132
2-hydroxy-4-butylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0388
2-hydroxy-4-ethylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0185
2-hydroxy-4-isopropylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.000061
2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H, 4H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000061
2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H,4H)-dione
Moloney murine leukemia virus
-
pH 8.0, 37°C
0.0336
2-hydroxy-4-pentylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0468
2-hydroxy-4-propylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.001507
2-hydroxy-6-methoxy-N-(3-(pyridin-2-ylcarbamoyl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophen-2-yl)nicotinamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0013
2-hydroxy-6-phenylisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0301
2-hydroxyisoquinoline-1,3(2H,4H)-dione magnesium complex
Moloney murine leukemia virus
-
pH 8.0, 37°C
0.0043
2-oxo-2-(1,2,3,4-tetrahydronaphthalen-1-ylamino)ethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0019
2-oxo-2-(phenylamino)ethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0132
2-oxo-2-(propan-2-yloxy)ethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0042
2-oxo-2-(tetrahydrofuran-2-ylamino)ethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0266
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl benzyl(phenyl)carbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0033
2-oxo-2-[(2,3,4-trichlorophenyl)amino]ethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0082
2-oxo-2-[(2-phenylpropan-2-yl)amino]ethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0033
2-[(2,3,4-trichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.0058
2-[(2,4-dichlorophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.00017
2-[(2-bromo-5-chloro-1-benzothiophen-3-yl)methyl]-5,6-dihydroxypyrimidine-4-carboxylic acid
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0083
2-[(2-methoxy-5-methylphenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0043
2-[(2-methyl-1-phenylpropan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0058
2-[(2-methylbutan-2-yl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0114
2-[(3-cyanophenyl)amino]-2-oxoethyl benzyl(phenyl)carbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0047
2-[(3-cyanophenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.005
2-[(4-hydroxybenzyl)(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0166
2-[(cyclohexanecarbonyl)amino]-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0012
2-[2-(2-fluoro-benzylamino)-1-hydroxy-1-methyl-ethyl]-5,7-dihydroxy-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.021
2-[2-(4-bromophenyl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.1
2-[2-(biphenyl-4-yl)-2-oxoethoxy]-9,10-dioxo-9,10-dihydroanthracen-1-yl acetate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0099
2-[3-(4-chlorophenyl)propanamido]-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0145
2-[3-(4-fluorophenyl)propanamido]-N-(pyridin-2-yl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.0026
2-[4-benzyl-5-[(pyridin-4-ylmethyl)sulfanyl]-4H-1,2,4-triazol-3-yl]pyridine
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0077
2-[benzyl(tetrahydrofuran-2-ylmethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0142
2-[tert-butyl(2-phenylethyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0098
2-[tert-butyl(3-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.05
2-[tert-butyl(3-oxo-3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.05
2-[tert-butyl(3-phenylpropyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0085
2-[tert-butyl(4-fluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0075
2-[tert-butyl(4-methoxybenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0069
2-[tert-butyl(4-nitrobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0068
2-[tert-butyl(pentafluorobenzyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0009
2-[tert-butyl(phenyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.009
2-[tert-butyl[2-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0085
2-[tert-butyl[3-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.008
2-[tert-butyl[4-(trifluoromethyl)benzyl]amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0128
2-[[2-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0087
2-[[4-(acetyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.05
2-[[4-(benzyloxy)benzyl](tert-butyl)amino]-2-oxoethyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0011 - 0.0041
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
0.0007 - 0.0034
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
0.0009 - 0.0067
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
0.0012 - 0.0069
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
0.0001
3'-[(E)-[2-(3,4,5-trihydroxybenzoyl)hydrazinylidene]methyl]biphenyl-4-carboxylic acid
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0219
3,3-dimethyl-2-oxobutyl 5-nitrofuran-2-carboxylate
Human immunodeficiency virus 1
-
pH 7.5, 37°C
0.0081
3-(benzyloxy)-6-((2'-methoxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0065
3-(furan-2-yl)-4-(4-methoxybenzyl)-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0047
3-(furan-2-yl)-4-phenyl-5-[[4-(trifluoromethyl)benzyl]sulfanyl]-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0001
3-hydroxy-1,5,6,7-tetrahydro-2H-cyclopenta[4,5]thieno[2,3-d]pyrimidine-2,4(3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0014 - 0.0041
3-hydroxy-1-methyl-6-((3-(pyrimidin-5-yl)phenyl)amino)-pyrimidine-2,4(1H,3H)-dione
0.0095
3-hydroxy-1-methyl-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-2-yl)-oxy)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0036 - 0.0089
3-hydroxy-1-methyl-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)-amino)pyrimidine-2,4(1H,3H)-dione
0.0062
3-hydroxy-1-methyl-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)-oxy)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0017 - 0.0072
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
0.0027 - 0.0066
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
0.0001
3-hydroxy-5,6,7,8-tetrahydrobenzo[4,5]thieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0003
3-hydroxy-5,6,7,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-2,4(1H,3H)-dione hydrobromide
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0001
3-hydroxy-5,6-dimethylthieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0001
3-hydroxy-5-methyl-2,4-dioxo-1,2,3,4-tetrahydrothieno[2,3-d]pyrimidine-6-carboxylic acid
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0001
3-hydroxy-5-methylthieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0001
3-hydroxy-5-phenylthieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.011
3-hydroxy-6-((2'-hydroxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00024 - 0.00049
3-hydroxy-6-((2'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
0.0012 - 0.0038
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
0.0025 - 0.013
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
0.0028 - 0.0093
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
0.0028 - 0.022
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
0.000012
3-hydroxy-6-((2-(trifluoromethyl)phenyl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000017
3-hydroxy-6-((2-methoxyphenyl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000037
3-hydroxy-6-((3'-(trifluoromethyl)-[1,1'-biphenyl]-3-yl)methyl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000007
3-hydroxy-6-((3'-(trifluoromethyl)-[1,1'-biphenyl]-3-yl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000025
3-hydroxy-6-((3'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000008
3-hydroxy-6-((3'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0009 - 0.015
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
0.00022 - 0.00043
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
0.0057
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0006 - 0.0043
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
0.001 - 0.017
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
0.0008 - 0.0051
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
0.00015 - 0.00025
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
0.002 - 0.016
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
0.000005
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000013
3-hydroxy-6-((3-(trifluoromethyl)phenyl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000013
3-hydroxy-6-((3-methoxyphenyl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000013
3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-2-yl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000007
3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-3-yl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000047
3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000039
3-hydroxy-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00038 - 0.0038
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
0.00018 - 0.00045
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
0.0039 - 0.021
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
0.000004
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0023 - 0.022
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
0.0005 - 0.0031
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
0.0002 - 0.0004
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
0.0004 - 0.0047
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
0.0013 - 0.0066
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
0.0016 - 0.012
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
0.000006
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0004 - 0.0007
3-hydroxy-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
0.000031
3-hydroxy-6-((4-(trifluoromethyl)phenyl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000011
3-hydroxy-6-((4-hydroxyphenyl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000012
3-hydroxy-6-((4-methoxyphenyl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000012
3-hydroxy-6-((4-nitrophenyl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000006
3-hydroxy-6-((40-methyl-[1,1'-biphenyl]-4-yl)thio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000026
3-hydroxy-6-(4'-(trifluoromethyl)-[1,10-biphenyl]-4-carbonyl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00053
3-hydroxy-6-(4'-methoxy-[1,10-biphenyl]-4-carbonyl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000081
3-hydroxy-6-(4-(trifluoromethyl)benzoyl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000093
3-hydroxy-6-(4-methylbenzoyl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000021
3-hydroxy-6-(40-methyl-[1,10-biphenyl]-4-carbonyl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000007
3-hydroxy-6-(naphthalen-1-ylthio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000033
3-hydroxy-6-(p-tolylthio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000016
3-hydroxy-6-(phenylthio)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0001
3-hydroxy-6-phenylthieno [3,2-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000084
3-hydroxy-6-phenylthieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0002
3-hydroxy-7-phenylquinazoline-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0002
3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.029
3-[2-(4-bromophenyl)-2-oxoethoxy]-1,8-dihydroxy-6-methylanthracene-9,10-dione
Human immunodeficiency virus 1
-
-
0.0012 - 0.0037
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
0.0011 - 0.0037
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
0.0019 - 0.013
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
0.0025 - 0.011
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
0.0052
4'-((3-(ethoxymethyl)-1-hydroxy-5-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)methyl)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000024
4'-(1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carbonyl)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000398
4-((cyclopropylmethyl)amino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.00001
4-(([1,1'-biphenyl]-4-ylmethyl)amino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000501
4-(4,4-difluoropiperidin-1-yl)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000032
4-([1,1'-biphenyl]-4-ylamino)-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.004
4-([[4-benzyl-5-(furan-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0002 - 0.2
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
0.0149
4-benzyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0038
4-benzyl-3-(furan-2-yl)-5-[(4-methoxybenzyl)sulfanyl]-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0028
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(furan-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.006
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.001
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-phenyl-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.045
4-heptyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0035
4-tert-butyl-N'-[(E)-(2-hydroxynaphthalen-1-yl)methylidene]benzohydrazide
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0066
4-[1-[(4-fluorophenyl)methyl]-7-(dimethylamino)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0068
4-[1-[(4-fluorophenyl)methyl]-7-(morpholin-4-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0033
4-[1-[(4-fluorophenyl)methyl]-7-(N-acetylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0262
4-[1-[(4-fluorophenyl)methyl]-7-(N-ethylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0185
4-[1-[(4-fluorophenyl)methyl]-7-(N-methylpiperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid ethyl ester
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0287
4-[1-[(4-fluorophenyl)methyl]-7-(piperazin-1-yl)-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0057
4-[1-[(4-fluorophenyl)methyl]-7-[N-(3-chloroprop-1-yl)piperazin-1-yl]-4-(1H)-quinolinon-3-yl]-2-hydroxy-4-oxo-2-butenoic acid
Human immunodeficiency virus 1
-
in 50 mM Tris-HCl, pH 8.0, at 37°C
0.0032
4-[5-(benzoylamino)thiophen-2-yl]-2,4-dioxobutanoic acid
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000158
4-[[(4-fluorophenyl)methyl]amino]-1-hydroxypyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
in 50 mM Tris, pH 8.0, 80 mM KCl, 10 mM MgCl2, at 22°C
0.000045
4-[[4'-(aminomethyl)biphenyl-4-yl]methyl]-1-hydroxy-1,8-naphthyridin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0012
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylaminoethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00093
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-phenylsulfanylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00082
5,7-dihydroxy-2-(1-hydroxy-1-methyl-2-piperidin-1-ylethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00911
5,7-dihydroxy-2-(1-hydroxy-2-imadazol-1-yl-1-methyl ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00068
5,7-dihydroxy-2-(1-hydroxy-ethyl)-9-methyl-1,2,3,4-tetrahydrobenzocyclohepten-6-one
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00004
5-(4-chlorophenyl)-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.015
5-benzyl-6-ethyl-1-(((4-fluorobenzyl)oxy)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00007
5-bromo-6-((4-bromophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.017
5-ethyl-1-(((4-fluorobenzyl)oxy)methyl)-6-(4-fluorophenyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0026 - 0.0322
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
0.000028
6-( (3'- fluoro-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000085
6-((2',4'-bis(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0000092
6-((2',4'-dichloro-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000015
6-((2',4'-difluoro-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.001 - 0.0042
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
0.00031 - 0.0024
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
0.0015 - 0.0053
6-((2',4'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
0.0019 - 0.0069
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
0.00047 - 0.0007
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
0.0066
6-((2-(3,5-dimethylisoxazol-4-yl)phenyl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.000008
6-((2-bromophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00001
6-((2-ethylphenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000015
6-((2-fluorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0005 - 0.003
6-((3',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
0.000004
6-((3',4'-dimethoxy-[1,10-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0006 - 0.004
6-((3',5'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
0.0016 - 0.0092
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
0.00019 - 0.00032
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
0.0067
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)methyl)-1-(ethoxymethyl)-3-hydroxy-5-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000006
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000005
6-((3'-chloro-4'-fluoro-[1,1'-biphenyl]-3-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000038
6-((3'-chloro-5'-(trifluoromethyl)-[1,1'-biphenyl]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000015
6-((3'-chloro-5'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000016
6-((3'-chloro-[1,1'-biphenyl ] - 4 -yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00002
6-((3'-chloro-[1,1'-biphenyl ]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0000077
6-((3'-fluoro-4'-methoxy-[1,1'-biphenyl]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0000076
6-((3'-fluoro-4'-methoxy-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000004
6-((3'-fluoro-4'-methoxy-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000018
6-((3'-fluoro-[1,1'-biphenyl]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000006
6-((3'-fluoro-[1,1'-biphenyl]-3-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000005
6-((3'-fluoro-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000011
6-((3-bromophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000011
6-((3-chlorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000014
6-((3-fluorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00043
6-((4'-chloro-3'-fluoro-[1,1'-biphenyl]-4-yl)methyl)-1-(ethoxymethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0000094
6-((4'-chloro-3'-fluoro-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000012
6-((4'-chloro-[1,1'-biphenyl ]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0033 - 0.013
6-((4'-chloro-[1,1'-biphenyl]-2-yl)oxy)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
0.00022 - 0.00045
6-((4'-chloro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
0.000005
6-((4'-chloro-[1,1'-biphenyl]-3-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00047 - 0.00066
6-((4'-chloro-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
0.0024 - 0.011
6-((4'-chloro-[1,1'-biphenyl]-4-yl)oxy)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
0.000007
6-((4'-chloro-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0000088
6-((4'-fluoro-3'-methyl-[1,1'-biphenyl]-3-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000011
6-((4'-fluoro-3'-methyl-[1,1'-biphenyl]-4-yl)methyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000005
6-((4'-fluoro-3'-methyl-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000012
6-((4'-fluoro-[1,1'-biphenyl]-2-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0002 - 0.0003
6-((4'-fluoro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
0.000005
6-((4'-fluoro-[1,1'-biphenyl]-3-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000006
6-((4'-fluoro-[1,1'-biphenyl]-4-yl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0016 - 0.0044
6-((4-(3,5-dimethylisoxazol-4-yl)phenyl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
0.00012
6-((4-bromophenyl)thio)-3-hydroxy-5-iodopyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00001
6-((4-bromophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000012
6-((4-chlorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00001
6-((4-ethylphenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000037
6-((4-fluorophenyl)thio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000074
6-(3',4'-dimethoxy-[1,10-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000063
6-(3',5'-dimethyl-[1,10-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00009
6-(3,5-dimethylbenzoyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000013
6-(3-bromobenzyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000023
6-(4'-chloro-3'-fluoro-[1,10-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000019
6-(4'-fluoro-3'-methyl-[1,10-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000027
6-(4'-fluoro-[1,1'-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000011
6-(4-bromobenzyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00007
6-(4-chlorophenyl)-3-hydroxythieno[3,2-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000085
6-(4-fluorobenzoyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0002
6-(4-fluorophenyl)-3-hydroxythieno[3,2-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0047
6-([1,1'-biphenyl]-2-yloxy)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0011
6-([1,1'-biphenyl]-3-carbonyl)-1-(ethoxymethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000017
6-([1,1'-biphenyl]-3-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00085 - 0.0035
6-([1,1'-biphenyl]-3-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
0.000016
6-([1,1'-biphenyl]-3-ylmethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.001
6-([1,1'-biphenyl]-3-yloxy)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00042
6-([1,1'-biphenyl]-4-carbonyl)-1-(ethoxymethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000022
6-([1,1'-biphenyl]-4-carbonyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0062
6-([1,1'-biphenyl]-4-yl)-1-(ethoxymethyl)-3-hydroxy-5-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0008 - 0.0051
6-([1,1'-biphenyl]-4-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
0.005
6-([1,1'-biphenyl]-4-ylmethyl)-1-(ethoxymethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000016
6-([1,1'-biphenyl]-4-ylmethyl)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00009
6-([1,1'-biphenyl]-4-ylthio)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.011
6-benzyl-1-(((4-fluorobenzyl)oxy)methyl)-5-isopropyl-3-methoxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.007
6-benzyl-1-(((4-fluorobenzyl)oxy)methyl)-5-isopropyl-3-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0068
6-benzyl-1-(ethoxymethyl)-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0025
6-benzyl-1-[(benzyloxy)methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0066
6-benzyl-1-[2-(4-fluorophenyl)ethyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0038
6-benzyl-1-[3-(4-fluorophenyl)propyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0009
6-benzyl-1-[4-(4-fluorophenyl)butyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0018
6-benzyl-1-[[(2,4-difluorophenyl)methoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0009
6-benzyl-1-[[(3-chloro-2-fluorophenyl)methoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0021
6-benzyl-1-[[(4-fluorophenyl)methoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0028
6-benzyl-1-[[3-(4-fluorophenyl)propoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0018
6-benzyl-1-[[4-(4-fluorophenyl)butoxy]methyl]-3-hydroxy-5-(propan-2-yl)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000043
6-benzyl-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00022
6-[(4'-chloro[1,1'-biphenyl]-3-yl)amino]-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00025
6-[([1,1'-biphenyl]-4-yl)amino]-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00013
6-[1-(4-fluorophenyl)methyl-1H-pyrrol-2-yl]-2,4-dioxo-5-hexenoic acid ethyl ester
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0002
7-(4-chlorophenyl)-3-hydroxyquinazoline-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0001
7-benzyl-3-hydroxy-5,6,7,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-2,4(1H,3H)-dione hydrochloride
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.00033
7-benzyl-3-hydroxyhexahydropyrido[3,4-d]pyrimidine-2,4(1H,3H)-dione hydrochloride
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0002
7-ethyl-3-hydroxy-5,6,7,8-tetrahydropyrido[4',3':4,5]thieno[2,3-d]pyrimidine-2,4(1H,3H)-dione hydrochloride
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.039
9,10-dioxo-2-(2-oxo-2-phenylethoxy)-9,10-dihydroanthracen-1-yl acetate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.013
9,10-dioxo-9,10-dihydroanthracene-1,2-diyl dibenzoate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.01
dolutegravir
Human immunodeficiency virus 1
-
above, pH and temperature not specified in the publication
0.0082
ethyl (5E)-6-[1-(2,4-dimethylbenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0073
ethyl (5E)-6-[1-(2-chlorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0063
ethyl (5E)-6-[1-(3-methoxybenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0086
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.0112
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.008
ethyl (5E)-6-[1-(4-fluorobenzyl)-4-phenyl-1H-pyrrol-3-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
at pH 7.8 and 37°C
0.00011
ethyl 1,4-dihydroxy-2-oxo-1,2-dihydro-1,8-naphthyridine-3-carboxylate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0252
ethyl 2-(2-fluorobenzamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.07258
ethyl 2-(4-chlorobenzamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxylate
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.000015
methyl 4'-(1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carbonyl)-[1,10-biphenyl]-4-carboxylate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.000031
methyl 4-(1-hydroxy-2,6-dioxo-1,2,3,6-tetrahydropyrimidine-4-carbonyl)benzoate
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0137
N-(3-((2-fluorophenyl)carbamoyl)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophen-2-yl)picolinamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.01036
N-(pyridin-2-yl)-2-(thiophene-2-carboxamido)-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.01644
N-(pyridin-2-yl)-2-[2-(quinolin-6-yl)acetamido]-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus type 1 group M subtype B
pH 7.8, 37°C
0.01
raltegravir
Human immunodeficiency virus 1
-
above, pH and temperature not specified in the publication
0.0007
1-hydroxy-4-[4-(quinolin-3-yl)anilino]pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.0007
1-hydroxy-4-[4-(quinolin-3-yl)anilino]pyrido[2,3-d]pyrimidin-2(1H)-one
Human immunodeficiency virus 1
-
enzyme activity reaction with substrates HTS-1-3, pH and temperature not specified in the publication
0.0388
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dione
Moloney murine leukemia virus
-
pH 8.0, 37°C
0.07
2-hydroxy-4-methylisoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0019
2-[(2,4-dimethylphenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.0019
2-[(2,4-dimethylphenyl)amino]-2-oxoethyl dibenzylcarbamodithioate
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0017
2-[4-benzyl-5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]pyridine
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.0017
2-[4-benzyl-5-(benzylsulfanyl)-4H-1,2,4-triazol-3-yl]pyridine
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0011
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0032
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0041
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0007
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0023
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0034
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0009
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0046
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0067
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0012
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0039
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0069
3'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0014
3-hydroxy-1-methyl-6-((3-(pyrimidin-5-yl)phenyl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0039
3-hydroxy-1-methyl-6-((3-(pyrimidin-5-yl)phenyl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0041
3-hydroxy-1-methyl-6-((3-(pyrimidin-5-yl)phenyl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0036
3-hydroxy-1-methyl-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)-amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0066
3-hydroxy-1-methyl-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)-amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0089
3-hydroxy-1-methyl-6-((4'-(trifluoromethyl)-[1,1'-biphenyl]-4-yl)-amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0017
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0062
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0072
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0027
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0035
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0066
3-hydroxy-1-methyl-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0037
3-hydroxy-1-methyl-6-(4-(pyridin-4-yl)phenoxy)pyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.01
3-hydroxy-1-methyl-6-(4-(pyridin-4-yl)phenoxy)pyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00024
3-hydroxy-6-((2'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00046
3-hydroxy-6-((2'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00049
3-hydroxy-6-((2'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0012
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0021
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0038
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0025
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.013
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0028
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0089
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0093
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0028
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.022
3-hydroxy-6-((2'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0009
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0022
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0043
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.011
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.012
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.015
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.00022
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0004
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00043
3-hydroxy-6-((3'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0006
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0035
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0043
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.001
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0094
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.017
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0008
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0035
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0051
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00015
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00025
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.00025
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.002
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.016
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.016
3-hydroxy-6-((3'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00038
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00044
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00045
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.00075
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0027
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0038
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.00018
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00037
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00045
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0039
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.021
3-hydroxy-6-((4'-hydroxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0023
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.022
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-2-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0005
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0026
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0031
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0002
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00025
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0003
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0003
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0004
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)amino)-pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0004
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.004
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0047
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-3-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0013
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.005
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0066
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)amino)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0016
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.011
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.012
3-hydroxy-6-((4'-methoxy-[1,1'-biphenyl]-4-yl)oxy)-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0004
3-hydroxy-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0005
3-hydroxy-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0007
3-hydroxy-6-((4'-methyl-[1,1'-biphenyl]-4-yl)amino)pyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0012
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0033
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0037
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0011
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0026
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0037
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)amino)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0019
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.011
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.013
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-3-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0025
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0047
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.011
4'-((1-hydroxy-3-methyl-2,6-dioxo-1,2,3,6-tetrahydropyrimidin-4-yl)oxy)-[1,1'-biphenyl]-4-carbonitrile
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0002
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.0002
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
Human immunodeficiency virus 1
-
pH and temperature not specified in the publication
0.2
4-([[4-benzyl-5-(thiophen-2-yl)-4H-1,2,4-triazol-3-yl]sulfanyl]methyl)pyridine
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0012
4-benzyl-3-(benzylsulfanyl)-5-(furan-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.0012
4-benzyl-3-(benzylsulfanyl)-5-(furan-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.00021
4-benzyl-3-(benzylsulfanyl)-5-(thiophen-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.00021
4-benzyl-3-(benzylsulfanyl)-5-(thiophen-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.001
4-benzyl-3-(benzylsulfanyl)-5-phenyl-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.001
4-benzyl-3-(benzylsulfanyl)-5-phenyl-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.001
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH 8.0, 25°C
0.001
4-benzyl-3-[(4-chlorobenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.001
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0059
4-benzyl-3-[(4-methoxybenzyl)sulfanyl]-5-(thiophen-2-yl)-4H-1,2,4-triazole
Human immunodeficiency virus 1
-
pH not specified in the publication, temperature not specified in the publication
0.0078
4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.038
4-hexyl-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
Human Immunodeficiency Virus
-
pH 8.0, 37°C
0.0038
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Human immunodeficiency virus 1
-
-
0.0084
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Moloney murine leukemia virus
-
-
0.0265
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Human immunodeficiency virus 1
-
-
0.0296
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Human immunodeficiency virus 1
-
-
0.0026
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
Human immunodeficiency virus 1
-
-
0.0086
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
Moloney murine leukemia virus
-
-
0.0267
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
Human immunodeficiency virus 1
-
-
0.0322
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
Human immunodeficiency virus 1
-
-
0.001
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0021
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0042
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00031
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00054
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0024
6-((2',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0015
6-((2',4'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0043
6-((2',4'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0053
6-((2',4'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0019
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0045
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0069
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.00047
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00051
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0007
6-((2',6'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0005
6-((3',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0022
6-((3',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.003
6-((3',4'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0006
6-((3',5'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0028
6-((3',5'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.004
6-((3',5'-dimethoxy-[1,1'-biphenyl]-3-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0016
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0072
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0092
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00019
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00025
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00032
6-((3',5'-dimethoxy-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0033
6-((4'-chloro-[1,1'-biphenyl]-2-yl)oxy)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.013
6-((4'-chloro-[1,1'-biphenyl]-2-yl)oxy)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00022
6-((4'-chloro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.00037
6-((4'-chloro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00045
6-((4'-chloro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.00047
6-((4'-chloro-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0006
6-((4'-chloro-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.00066
6-((4'-chloro-[1,1'-biphenyl]-4-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0024
6-((4'-chloro-[1,1'-biphenyl]-4-yl)oxy)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.011
6-((4'-chloro-[1,1'-biphenyl]-4-yl)oxy)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0002
6-((4'-fluoro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0003
6-((4'-fluoro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0003
6-((4'-fluoro-[1,1'-biphenyl]-3-yl)amino)-3-hydroxypyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0016
6-((4-(3,5-dimethylisoxazol-4-yl)phenyl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0038
6-((4-(3,5-dimethylisoxazol-4-yl)phenyl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0044
6-((4-(3,5-dimethylisoxazol-4-yl)phenyl)amino)-3-hydroxy-1-methylpyrimidine-2,4(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.00085
6-([1,1'-biphenyl]-3-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0034
6-([1,1'-biphenyl]-3-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0035
6-([1,1'-biphenyl]-3-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0008
6-([1,1'-biphenyl]-4-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0035
6-([1,1'-biphenyl]-4-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.0051
6-([1,1'-biphenyl]-4-ylamino)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.0019
6-([1,1'-biphenyl]-4-yloxy)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-1, pH and temperature not specified in the publication
0.0053
6-([1,1'-biphenyl]-4-yloxy)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-2, pH and temperature not specified in the publication
0.006
6-([1,1'-biphenyl]-4-yloxy)-3-hydroxy-1-methylpyrimidine-2,4-(1H,3H)-dione
Human immunodeficiency virus 1
-
enzyme activity reaction with substrate HTS-3, pH and temperature not specified in the publication
0.000186
ARK-2452
Human immunodeficiency virus 1
-
pH 8.0, 37°C, purified recombinant mutant p51-G-TCR construct
-
0.00047
ARK-2452
Human immunodeficiency virus 1
-
pH 8.0, 37°C, purified recombinant wild-type HIV-1 reverse transcriptase RNase H
-
0.00007
beta-thujaplicinol
Human immunodeficiency virus 1
-
mutant enzyme Y501A, at pH 7.8 and 37°C
0.00009
beta-thujaplicinol
Human immunodeficiency virus 1
-
mutant enzyme N474A, at pH 7.8 and 37°C
0.00015
beta-thujaplicinol
Human immunodeficiency virus 1
-
mutant enzyme R448A, at pH 7.8 and 37°C
0.000176
beta-thujaplicinol
Human immunodeficiency virus 1
-
pH 8.0, 37°C, purified recombinant mutant p51-G-TCR construct
0.00019
beta-thujaplicinol
Human immunodeficiency virus 1
-
mutant enzyme Q475A, at pH 7.8 and 37°C
0.00022
beta-thujaplicinol
Human immunodeficiency virus 1
-
mutant enzyme R557A, at pH 7.8 and 37°C
0.000257
beta-thujaplicinol
Human immunodeficiency virus 1
-
pH 8.0, 37°C, purified recombinant wild-type HIV-1 reverse transcriptase RNase H
0.0022
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid
Human immunodeficiency virus 1
-
pH 7.6, 37°C
0.003
[2-(4-chlorophenyl)hydrazinylidene]propanedioic acid
Human immunodeficiency virus 1
-
pH 7.6, 37°C
Please wait a moment until the data is sorted. This message will disappear when the data is sorted.
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
level of RNase H activity is low in HIV-2 isolates
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pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
7.5
7.8
8 - 8.5
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TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
25
37
37
-
assay at
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ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
Human immunodeficiency virus type 1 group M subtype B
Human immunodeficiency virus type 1 group M subtype B BH10
Human immunodeficiency virus type 1 group O subtype B
Human immunodeficiency virus type 1 group O subtype B ESP49
-
652865, 652907, 665720, 666034, 695644, 695645, 696181, 696183, 696189, 696192, 696194, 698692, 698694, 698701, 699509, 699893, 699894, 700927, 701025, 701113, 701116, 701216, 701386
-
-
brenda
-
-
-
brenda
HIV-1
-
-
brenda
HIV-1
-
-
brenda
Human immunodeficiency virus type 1 group M subtype B BH10
HIV-1
UniProt
brenda
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SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
additional information
-
virus passage in human 293 cells
brenda
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GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
evolution
malfunction
physiological function
additional information
evolution
-
RNase H acts as gene modifier, driver of evolution and antiviral defense, overview
evolution
-
the N-terminal amino acid residue of HIV-1 RNase H is highly conserved
malfunction
-
antiviral activity of 2-hydroxy-4-methoxycarbonylisoquinoline-1,3(2H,4H)-dione is probably due to the RNase H inhibition
malfunction
-
patients treated with nucleoside reverse transcriptase inhibitors develop classical patterns of resistance-associated mutations in the pol domain. Thymidine analogue mutations, TAMs, arise with zidovudine and stavudine treatment, which encompass M41L, D67N, K70R, L210W, T215F/Y, and K219Q/E/N. Different patterns of thymidine analogue mutations accumulate in patients, which segregate into two distinct pathways named TAM-1 and TAM-2. The TAM-1 pathway includes M41L, L210W and T215Y, whereas the TAM-2 pathway includes D67N, K70R, T215F and K219Q/E/N
malfunction
-
PEGylation as a tool for engineering the M-MuLV RT derivative deficient in RNase H activity, overview
malfunction
-
severe defects in RNase H activity alone, exemplified by the P236L mutant, appear sufficient to cause a substantial reduction in fitness. Reductions in reverse transcriptase content decrease both polymerization and RNase H activity in virions
malfunction
-
RNase H-deficient HIV-1 reverse transcriptase shows altered error specificity during DNA-dependent DNA synthesis
malfunction
-
an HIV-1 mutant can tolerate an about 10fold higher RNase H activity
malfunction
effect of N-terminal deletion on monomer-dimer interconversion kinetics, overview
malfunction
Human immunodeficiency virus type 1 subtype C
-
identification of nucleoside reverse transcriptase inhibitor (NRTI) treatment-related mutations in RNase H of HIV-1 subtype C, overview
malfunction
-
RNase H N-terminal mutations impact intravirion protein levels and viral infectivity. Reverse transcriptase (RT) with an RNaseHN-terminal mutation is still degraded in the absence of active viral protease
malfunction
-
the Q294P mutant of HIV-2 RT has about 10fold higher RNase H activity than the wild-type. Infectious HIV-2 cannot bear the replacement of the RT's Gln294 by the HIV-1 RT Pro counterpart, as it results in substantially reduced HIV-2 replication and fast reversions to the wild-type Gln294 virus. Critical role of maintaining low RT-associated RNase H activity in HIV-2
malfunction
Human immunodeficiency virus type 1 group O subtype B
-
the substitution of Pro for Leu-92 renders an HIV-1 reverse transcriptase without strand transfer activity but retaining wild-type DNA polymerase and RNase H activities. Introduction of L92P produces a 3-4fold increase in the dissociation equilibrium constant (Kd) for DNA/DNA template-primers, suggesting that the strand transfer defect is a consequence of impaired nucleic acid binding
malfunction
-
two mutations in HIV-1 RNase H, Y501R and Y501W, result in a reduction of inhibitor potency, thus indicating their potential role in providing resistance to the inhibitor
malfunction
-
patients treated with nucleoside reverse transcriptase inhibitors develop classical patterns of resistance-associated mutations in the pol domain. Thymidine analogue mutations, TAMs, arise with zidovudine and stavudine treatment, which encompass M41L, D67N, K70R, L210W, T215F/Y, and K219Q/E/N. Different patterns of thymidine analogue mutations accumulate in patients, which segregate into two distinct pathways named TAM-1 and TAM-2. The TAM-1 pathway includes M41L, L210W and T215Y, whereas the TAM-2 pathway includes D67N, K70R, T215F and K219Q/E/N
-
malfunction
Human immunodeficiency virus type 1 group O subtype B ESP49
-
the substitution of Pro for Leu-92 renders an HIV-1 reverse transcriptase without strand transfer activity but retaining wild-type DNA polymerase and RNase H activities. Introduction of L92P produces a 3-4fold increase in the dissociation equilibrium constant (Kd) for DNA/DNA template-primers, suggesting that the strand transfer defect is a consequence of impaired nucleic acid binding
-
physiological function
-
increasing the stoichiometry of RNase H relative to the amount of functional DNA polymerase by virions engineered to contain phenotypic mixtures of wild-type and RNase H catalytic site point mutant D524N reverse transcriptase, has minimal effects on direct repeat deletion frequency. DNA synthesis is error prone when directed principally by RNase H mutant reverse transcriptase, suggesting a role for RNase H catalytic integrity in the fidelity of intracellular reverse transcription
physiological function
-
the process of reverse transcription involves the copying of the single-stranded RNA of the viral genome into double-stranded DNA. This requires that reverse transcriptase is able to act at times as a RNA-dependent DNA polymerase, a DNA-dependent DNA polymerase, and as an RNase H that cleaves the RNA of RNA/DNA hybrids. These activities are coordinated temporally and spatially. As all three of these processes are absolutely required for the successful completion of reverse transcription, role of RNase H in (+)-strand priming and in strand transfer and (-)-strand primer removal, overview
physiological function
-
the process of reverse transcription involves the copying of the single-stranded RNA of the viral genome into double-stranded DNA. This requires that reverse transcriptase is able to act at times as a RNA-dependent DNA polymerase, a DNA-dependent DNA polymerase, and as an RNase H that cleaves the RNA of RNA/DNA hybrids. These activities are coordinated temporally and spatially. As all three of these processes are absolutely required for the successful completion of reverse transcription, role of RNase H in (+)-strand priming and in strand transfer and (-)-strand primer removal, overview
physiological function
-
the retroviral RNase H degrades the RNA template following first strand synthesis, generates primers for second strand synthesis, and eliminates the t-RNA primer
physiological function
-
the reverse transcriptase generates an RNA/DNA hybrid that is a substrate for RNase H. The RNA/DNA hybrid is degraded to generate a nascent minus-strand single-stranded DNA. As DNA synthesis proceeds, RNase H degrades the RNA strand
physiological function
the enzyme activity and substrate specificity is controlled by the RNase H primer grip, and the width of the minor groove and the trajectroy of the RNA:DNA, both in a sequence-dependent manner
physiological function
-
RNase H activity is essential for virus infectivity
physiological function
-
HIV reverse transcriptase plays a central role in viral replication and requires coordination of both polymerase and RNaseH activities. HIV-1 reverse transcriptase polymerase and RNase H (ribonuclease H) active sites work simultaneously and independently
physiological function
-
HIV-1 reverse trancriptase (RT) is a key multifunctional enzyme which combines an RNA-dependent DNA polymerase activity (RDDP) and a ribonuclease H (RNase H) function, both essential for the viral genome replication
physiological function
-
low ribonuclease H (RNase H) activity of HIV-2 reverse transcriptase (RT) relative to HIV-1 RT. Residue Gln294 in HIV-2 RT accounts for this RNase H reduction (the comparable residue in HIV-1 RT is Pro294), as the Q294P mutant of HIV-2 RT has about 10fold higher RNase H activity
physiological function
-
replication of human immunodeficiency virus 1 (HIV-1) involves conversion of its single-stranded RNA genome to double-stranded DNA, which is integrated into the genome of the host. This conversion is catalyzed by reverse transcriptase (RT), which possesses DNA polymerase and RNase H domains. When the RNA/DNA hybrid is immobilized at the polymerase active site, RNase H cleavage occurs, experimentally verifying that the substrate can simultaneously interact with both active sites
physiological function
-
reverse transcriptase (RT) acts in concert with the RNase H catalyzing retroviral replication, the retroviral ribonuclease H (RNase H) in retrovirus particles is essential component for the replication of viral RNA via an RNA/DNA hybrid intermediate to double-stranded DNA. RNase H is a part of the reverse transcriptase (RT) in retroviruses. But the enzyme has its proper role, impact on evolution and importance for the degradation of nucleic acids in various biological processes
physiological function
-
ribonuclease H (RNase H) is an enzyme that cleaves RNA strand of RNA/DNA hybrid to produce 5'-phosphate and 3'-hydroxyl termini with a two-metal-ion catalysis mechanism. HIV-1 reverse transcriptase (RT) is a heterodimer consisting of a P66 subunit and a P51 subunit. The P66 subunit contains a C-terminal RNase H domain, which exhibits RNase H activity either in the presence of Mg2+ or Mn2+ ions
physiological function
Human immunodeficiency virus type 1 group M subtype B
template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase
physiological function
Human immunodeficiency virus type 1 group O subtype B
-
template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase
physiological function
-
the nature of the N-terminal amino acid residue of HIV-1 RNase H is critical for the stability of reverse transcriptase (RT) in viral particles. Degradation of reverse transcriptase (RT) in RNase H N-terminal mutants occurs in the absence of active viral protease in the virion. Importance of the RNase H N-terminal residue in the dimerization of RT subunits. RNase H is an HIV-1 protein that has the potential to be a substrate for the N-end rule pathway, which is an ubiquitin-dependent proteolytic system in which the identity of the N-terminal amino acid determines the half-life of a protein. HIV-1 proteins are initially made as part of a polyprotein that is cleaved by the viral protease into the proteins that form the virus particle, RT is subject to an internal cleavage event leading to the formation of two subunits in the virion: a p66 subunit and a p51 subunit that lacks the RNase H domain. Importance of the N-terminal amino acid residue of RNase H in the early life cycle of HIV-1
physiological function
Human immunodeficiency virus type 1 group O subtype B ESP49
-
template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase
-
physiological function
Human immunodeficiency virus type 1 group M subtype B BH10
-
template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase
-
additional information
-
catalytically important residues of the RNase H activity are Asp524 and Asp583
additional information
-
HIV-1 reverse transcriptase has two associated activities, DNA polymerase and RNase H, both essential for viral replication and validated drug targets
additional information
-
Q294 is highly conserved in HIV-2 isolates
additional information
-
role of RNase H activity in drug resistance, the RNase H domains can affect the susceptibility of RT to non-nucleoside reverse transcriptase inhibitors and nucleos(t)ide reverse transcriptase inhibitors. Furthermore, RNase H activity itself is implicated in the mechanism of resistance to nucleoside reverse transcriptase inhibitors such as 3'-azidodeoxythymidine, and also to non-nucleoside reverse transcriptase inhibitors such as nevirapine. RNase H exists as a domain in the larger enzyme HIV-1 reverse transcriptase, structure and function of HIV-1 RNase H, overview
additional information
-
RT is a unique viral protein containing two enzymatic properties, i.e. RNase H cleavage activity and RNA- and DNA-dependent DNA polymerase activity
additional information
-
the active site of RNase H consists of four highly conserved carboxylate residues, D443, E478, D498, and D549, and requires Mg2+ or Mn2+ for its catalytic activity
additional information
-
the RNase H activity, which degrades RNA from RNA/DNA hybrids endonucleolytically, is part of the HIV reverse transcriptase
additional information
the polypurine tract, PPT, a purine-rich segment from the HIV-1 genome, is resistant to RNase H cleavage and is used as a primer for second DNA strand synthesis. PPT-enzyme complex structure, detailed overview
additional information
Human immunodeficiency virus type 1 group M subtype B
-
enzyme domain RNH structure-function relationship analysis, overview
additional information
Human immunodeficiency virus type 1 group M subtype B
for enzyme-inhibitor structural modelling, coordinates of the following retroviral RT-RT inhibitor structures are used: HIV RT-MK1 (PDB ID 3LP0) and HIV RT-MK2 (PDB ID 3LP1)
additional information
homology model of substrate- and inhibitor-bound HIV-1 RNase H, molecular docking, overview
additional information
-
homology model of substrate- and inhibitor-bound HIV-1 RNase H, molecular docking, overview
additional information
-
molecular dynamics simulations and determination of the conformation of the complex in which the unwound RNA/DNA substrate simultaneously interacts with the polymerase and RNase H active sites. Existence of a transient conformation of the HIV-1 by reverse transcriptase (RT) substrate complex, which is important for modulating and coordinating the enzymatic activities of HIV-1 RT
additional information
Human immunodeficiency virus type 1 group M subtype B
nucleotide analogues can enhance strand transfer by slowing DNA polymerization kinetics. Contribution of dissociation rate constants (koff) to the strand transfer efficiency of HIV-1 RTs, overview
additional information
Human immunodeficiency virus type 1 group O subtype B
-
nucleotide analogues can enhance strand transfer by slowing DNA polymerization kinetics. Contribution of dissociation rate constants (koff) to the strand transfer efficiency of HIV-1 RTs, overview
additional information
predictions of sequence tolerance suggest that phenylalanine and tyrosine are structurally preferred at residues 440 and 441, respectively, which are the P1 and P1' substrate residues known to require bulky side chains for substrate specificity. The processing site residues, which are critical for protease substrate specificity and must be exposed to the solvent for efficient processing, also function to maintain proper RNH folding in the p66/p51 heterodimer. Molecular dynamics simulations of wild-type and mutant RNH enzyme domains
additional information
-
the isolated RNase H domain of HIV-1 RT (RNHHIV) is inactive, possibly due to the lack of a substrate binding ability, disorder of a loop containing His539, and increased flexibility. The N-terminal substrate binding domain, termed hybrid binding domain (TmaHBD), from Thermotoga maritima RNase H1 and the N-terminal domain (BstNTD) from Bacillus stearothermophilus RNase H2 both function as an RNA/DNA hybrid binding tag, and greatly increase the substrate binding affinity and Mn2+-dependent activity of RNHHIV but do not restore the Mg2+-dependent activity of RNHHIV
additional information
-
RT is a unique viral protein containing two enzymatic properties, i.e. RNase H cleavage activity and RNA- and DNA-dependent DNA polymerase activity
-
additional information
Human immunodeficiency virus type 1 group O subtype B ESP49
-
nucleotide analogues can enhance strand transfer by slowing DNA polymerization kinetics. Contribution of dissociation rate constants (koff) to the strand transfer efficiency of HIV-1 RTs, overview
-
additional information
Human immunodeficiency virus type 1 group M subtype B BH10
-
enzyme domain RNH structure-function relationship analysis, overview
-
additional information
Human immunodeficiency virus type 1 group M subtype B BH10
-
nucleotide analogues can enhance strand transfer by slowing DNA polymerization kinetics. Contribution of dissociation rate constants (koff) to the strand transfer efficiency of HIV-1 RTs, overview
-
additional information
Human immunodeficiency virus type 1 group M subtype B BH10
-
for enzyme-inhibitor structural modelling, coordinates of the following retroviral RT-RT inhibitor structures are used: HIV RT-MK1 (PDB ID 3LP0) and HIV RT-MK2 (PDB ID 3LP1)
-
additional information
-
homology model of substrate- and inhibitor-bound HIV-1 RNase H, molecular docking, overview
-
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UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). POL_SIVVG
Simian immunodeficiency virus agm.vervet (isolate AGM3)
1465
0
166071
Swiss-Prot
other Location (Reliability: 5)
POL_SIVVT
Simian immunodeficiency virus agm.vervet (isolate AGM TYO-1)
1467
0
166058
Swiss-Prot
other Location (Reliability: 5)
POL_JEMBR
1432
0
163421
Swiss-Prot
other Location (Reliability: 3)
POL_OMVVS
Ovine maedi visna related virus (strain South Africa)
1086
0
124515
Swiss-Prot
other Location (Reliability: 3)
POL_BIV29
Bovine immunodeficiency virus (strain R29)
1475
0
168063
Swiss-Prot
other Location (Reliability: 4)
POL_SIVCZ
1384
0
156085
Swiss-Prot
Mitochondrion (Reliability: 5)
POL_SIVEK
Simian immunodeficiency virus (isolate EK505)
1448
0
163246
Swiss-Prot
other Location (Reliability: 2)
POL_SIVG1
Simian immunodeficiency virus agm.grivet (isolate AGM gr-1)
1472
0
166897
Swiss-Prot
other Location (Reliability: 3)
POL_SIVGB
1441
0
163400
Swiss-Prot
other Location (Reliability: 2)
POL_SIVM1
Simian immunodeficiency virus (isolate Mm142-83)
1448
0
163372
Swiss-Prot
other Location (Reliability: 3)
POL_SIVMB
Simian immunodeficiency virus (isolate MB66)
1438
0
162293
Swiss-Prot
other Location (Reliability: 3)
POL_SIVMK
Simian immunodeficiency virus (isolate K6W)
1446
0
163593
Swiss-Prot
other Location (Reliability: 3)
POL_SIVS4
Simian immunodeficiency virus (isolate F236/smH4)
1449
0
163463
Swiss-Prot
other Location (Reliability: 2)
POL_SIVSP
Simian immunodeficiency virus (isolate PBj14/BCL-3)
1449
0
163326
Swiss-Prot
other Location (Reliability: 3)
POL_SIVTN
Simian immunodeficiency virus (isolate TAN1)
1462
0
164427
Swiss-Prot
other Location (Reliability: 4)
POL_SIVV1
Simian immunodeficiency virus agm.vervet (isolate AGM155)
1470
0
165744
Swiss-Prot
other Location (Reliability: 5)
POL_HV190
Human immunodeficiency virus type 1 group M subtype H (isolate 90CF056)
1435
0
162120
Swiss-Prot
other Location (Reliability: 4)
POL_HV192
Human immunodeficiency virus type 1 group M subtype C (isolate 92BR025)
1431
0
161671
Swiss-Prot
other Location (Reliability: 3)
POL_HV193
Human immunodeficiency virus type 1 group M subtype F1 (isolate 93BR020)
1430
0
161004
Swiss-Prot
other Location (Reliability: 4)
POL_HV196
Human immunodeficiency virus type 1 group M subtype K (isolate 96CM-MP535)
1430
0
161487
Swiss-Prot
other Location (Reliability: 4)
POL_HV197
Human immunodeficiency virus type 1 group M subtype K (isolate 97ZR-EQTB11)
1429
0
161685
Swiss-Prot
other Location (Reliability: 3)
POL_HV19N
Human immunodeficiency virus type 1 group M subtype G (isolate 92NG083)
1435
0
161214
Swiss-Prot
other Location (Reliability: 5)
POL_HV1A2
Human immunodeficiency virus type 1 group M subtype B (isolate ARV2/SF2)
1437
0
162015
Swiss-Prot
other Location (Reliability: 3)
POL_HV1AN
Human immunodeficiency virus type 1 group O (isolate ANT70)
1435
0
161671
Swiss-Prot
other Location (Reliability: 2)
POL_HV1B1
Human immunodeficiency virus type 1 group M subtype B (isolate BH10)
1447
0
163288
Swiss-Prot
other Location (Reliability: 4)
POL_HV1B5
Human immunodeficiency virus type 1 group M subtype B (isolate BH5)
1447
0
163265
Swiss-Prot
other Location (Reliability: 4)
POL_HV1B9
Human immunodeficiency virus type 1 group M subtype B (strain 89.6)
1435
0
161526
Swiss-Prot
other Location (Reliability: 4)
POL_HV1BR
Human immunodeficiency virus type 1 group M subtype B (isolate BRU/LAI)
1447
0
163279
Swiss-Prot
other Location (Reliability: 4)
POL_HV1EL
Human immunodeficiency virus type 1 group M subtype D (isolate ELI)
1435
0
162168
Swiss-Prot
other Location (Reliability: 4)
POL_HV1ET
Human immunodeficiency virus type 1 group M subtype C (isolate ETH2220)
1439
0
162166
Swiss-Prot
other Location (Reliability: 2)
POL_HV1H2
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
1435
0
162042
Swiss-Prot
other Location (Reliability: 4)
POL_HV1JR
Human immunodeficiency virus type 1 group M subtype B (isolate JRCSF)
1439
0
162333
Swiss-Prot
other Location (Reliability: 4)
POL_HV1LW
Human immunodeficiency virus type 1 group M subtype B (isolate LW123)
1435
0
162076
Swiss-Prot
other Location (Reliability: 5)
POL_HV1M2
Human immunodeficiency virus type 1 group M subtype F2 (isolate MP257)
1434
0
161594
Swiss-Prot
other Location (Reliability: 4)
POL_HV1MA
Human immunodeficiency virus type 1 group M subtype A (isolate MAL)
1440
0
162122
Swiss-Prot
other Location (Reliability: 4)
POL_HV1MN
Human immunodeficiency virus type 1 group M subtype B (isolate MN)
1441
0
162328
Swiss-Prot
other Location (Reliability: 3)
POL_HV1MP
Human immunodeficiency virus type 1 group M subtype F2 (isolate MP255)
1430
0
161574
Swiss-Prot
other Location (Reliability: 4)
POL_HV1MV
Human immunodeficiency virus type 1 group O (isolate MVP5180)
1446
0
162770
Swiss-Prot
Mitochondrion (Reliability: 5)
POL_HV1N5
Human immunodeficiency virus type 1 group M subtype B (isolate NY5)
1435
0
161789
Swiss-Prot
other Location (Reliability: 3)
POL_HV1ND
Human immunodeficiency virus type 1 group M subtype D (isolate NDK)
1432
0
161441
Swiss-Prot
other Location (Reliability: 5)
POL_HV1OY
Human immunodeficiency virus type 1 group M subtype B (isolate OYI)
1434
0
161772
Swiss-Prot
other Location (Reliability: 3)
POL_HV1RH
Human immunodeficiency virus type 1 group M subtype B (isolate RF/HAT3)
1436
0
162118
Swiss-Prot
other Location (Reliability: 4)
POL_HV1S2
Human immunodeficiency virus type 1 group M subtype J (isolate SE9280)
1432
0
162130
Swiss-Prot
other Location (Reliability: 3)
POL_HV1S9
Human immunodeficiency virus type 1 group M subtype J (isolate SE9173)
1432
0
162096
Swiss-Prot
other Location (Reliability: 3)
POL_HV1SE
Human immunodeficiency virus type 1 group M subtype G (isolate SE6165)
1433
0
161650
Swiss-Prot
other Location (Reliability: 4)
POL_HV1U4
Human immunodeficiency virus type 1 group M subtype A (isolate U455)
1428
0
161103
Swiss-Prot
other Location (Reliability: 4)
POL_HV1V9
Human immunodeficiency virus type 1 group M subtype H (isolate VI991)
1436
0
162057
Swiss-Prot
other Location (Reliability: 5)
POL_HV1VI
Human immunodeficiency virus type 1 group M subtype F1 (isolate VI850)
1430
0
161064
Swiss-Prot
other Location (Reliability: 2)
POL_HV1Y2
Human immunodeficiency virus type 1 group M subtype B (isolate YU-2)
1435
0
161980
Swiss-Prot
other Location (Reliability: 3)
POL_HV1YB
Human immunodeficiency virus type 1 group N (isolate YBF106)
1449
0
162613
Swiss-Prot
other Location (Reliability: 2)
POL_HV1YF
Human immunodeficiency virus type 1 group N (isolate YBF30)
1449
0
163294
Swiss-Prot
other Location (Reliability: 3)
POL_HV1Z2
Human immunodeficiency virus type 1 group M subtype D (isolate Z2/CDC-Z34)
1436
0
161899
Swiss-Prot
other Location (Reliability: 4)
POL_HV2BE
Human immunodeficiency virus type 2 subtype A (isolate BEN)
1550
0
174508
Swiss-Prot
other Location (Reliability: 3)
POL_HV2CA
Human immunodeficiency virus type 2 subtype A (isolate CAM2)
1462
0
164677
Swiss-Prot
other Location (Reliability: 3)
POL_HV2D1
Human immunodeficiency virus type 2 subtype A (isolate D194)
1462
0
164256
Swiss-Prot
other Location (Reliability: 4)
POL_HV2D2
Human immunodeficiency virus type 2 subtype B (isolate D205)
1465
0
164792
Swiss-Prot
other Location (Reliability: 2)
POL_HV2EH
Human immunodeficiency virus type 2 subtype B (isolate EHO)
1464
0
164877
Swiss-Prot
other Location (Reliability: 3)
POL_HV2G1
Human immunodeficiency virus type 2 subtype A (isolate Ghana-1)
1464
0
164882
Swiss-Prot
other Location (Reliability: 3)
POL_HV2KR
Human immunodeficiency virus type 2 subtype A (isolate KR)
1463
0
164851
Swiss-Prot
other Location (Reliability: 4)
POL_HV2NZ
Human immunodeficiency virus type 2 subtype A (isolate NIH-Z)
1461
0
164478
Swiss-Prot
other Location (Reliability: 3)
POL_HV2RO
Human immunodeficiency virus type 2 subtype A (isolate ROD)
1464
0
164645
Swiss-Prot
other Location (Reliability: 5)
POL_HV2SB
Human immunodeficiency virus type 2 subtype A (isolate SBLISY)
1462
0
165014
Swiss-Prot
other Location (Reliability: 3)
POL_HV2ST
Human immunodeficiency virus type 2 subtype A (isolate ST)
1463
0
164856
Swiss-Prot
other Location (Reliability: 3)
POL_HV2UC
Human immunodeficiency virus type 2 subtype B (isolate UC1)
1471
0
165188
Swiss-Prot
other Location (Reliability: 3)
POL_CAEVC
1109
0
127678
Swiss-Prot
other Location (Reliability: 4)
POL_EIAV9
Equine infectious anemia virus (isolate 1369)
1146
0
129510
Swiss-Prot
other Location (Reliability: 5)
POL_EIAVC
Equine infectious anemia virus (isolate CL22)
1146
0
129509
Swiss-Prot
other Location (Reliability: 5)
POL_EIAVY
Equine infectious anemia virus (strain Wyoming)
1145
0
129520
Swiss-Prot
other Location (Reliability: 5)
POL_FIVPE
1124
0
127494
Swiss-Prot
other Location (Reliability: 1)
POL_FIVSD
Feline immunodeficiency virus (strain San Diego)
1124
0
127605
Swiss-Prot
other Location (Reliability: 2)
POL_FIVT2
1124
0
128101
Swiss-Prot
other Location (Reliability: 3)
L7JYM3_TRAHO
155
0
18395
TrEMBL
other Location (Reliability: 2)
RNH_ECOLI
Escherichia coli (strain K12)
155
0
17597
Swiss-Prot
Secretory Pathway (Reliability: 1)
A0A059PIR4_9HIV1
300
0
34169
TrEMBL
-
GAG_HV1H2
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
500
0
55930
Swiss-Prot
-
A0A076Q3N8_9HIV1
1015
0
115049
TrEMBL
-
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PDB
SCOP
CATH
UNIPROT
ORGANISM
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MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
51000
-
1 * 51000, p51 subunit, + 1 * 66000, p66 subunit, of HIV reverse transcriptase, SDS-PAGE
66000
-
1 * 51000, p51 subunit, + 1 * 66000, p66 subunit, of HIV reverse transcriptase, SDS-PAGE
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SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
dimer
monomer
-
1 * 71000, SDS-PAGE of recombinant enzyme with deletion of 204 nucleotides at the 3'-terminus
additional information
dimer
-
1 * 51000, p51 subunit, + 1 * 66000, p66 subunit, of HIV reverse transcriptase, SDS-PAGE
dimer
the mature form of reverse transcriptase (RT) is a heterodimer comprising the intact 66-kDa subunit (p66) and a smaller 51-kDa subunit (p51) that is generated by removal of most of the RNase H (RNH) domain from a p66 subunit by proteolytic cleavage between residues 440 and 441
additional information
-
RNase H activity is associated with the p66 component of reverse transcriptase
additional information
-
the folded structure of the HIV-1 RNase H domain takes the form of a 5-stranded mixed beta-sheet flanked by four alpha helices in an asymmetric distribution, structure comparisons, overview. The p66 subunit is subdivided into three domains: the N-terminal polymerase domain, the C-terminal ribonuclease RNase H domain, and connection domain that links the two functional regions
additional information
enzyme domain organization, overview
additional information
monomer/dimer structural variations of helix B-helix D, overview
additional information
-
monomer/dimer structural variations of helix B-helix D, overview
additional information
-
reverse transcriptase RT-RNase H domain structure compare to other RNases H (EC 3.1.13.2), overview
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POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
formation of the mature HIV-1 reverse transcriptase (RT) p66/p51 heterodimer requires subunit-specific processing of the p66/p66' homodimer precursor, the ribonuclease H (RH) domain contains an occult cleavage site located near its center. NMR spectroscopic determination of a slow, subunit-specific RH domain unfolding process proposed to result from a residue tug-of-war between the polymerase and RH domains on the functionally inactive, p66' subunit. Structural comparison of the isolated RH domain with a domain swapped RH dimer reveals several intrinsically destabilizing characteristics of the isolated domain that facilitate excursions of Tyr427 from its binding pocket and separation of helices B and D. The enzyme shows a subunit-selective RH domain unfolding pathway in which instability of the Tyr427 binding pocket facilitates its release followed by domain transfer, acting as a trigger for further RH domain destabilization and subsequent unfolding
proteolytic modification
the mature form of reverse transcriptase (RT) is a heterodimer comprising the intact 66-kDa subunit (p66) and a smaller 51-kDa subunit (p51) that is generated by removal of most of the RNase H (RNH) domain from a p66 subunit by proteolytic cleavage between residues 440 and 441
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CRYSTALLIZATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
2.80 A and 2.04 A resolution crystal structures of inhibitor, beta-thujaplicinol, bound at the RNase H active site of both HIV-1 RT and an isolated RNase H domain. beta-Thujaplicinol chelates two divalent metal ions at the RNase H active site
crystal structure analysis, overview. The pyrimidinol carboxylic acids is successful crystallized with Mn2+ and the isolated HIV RNase H domain
-
determination and analysis of crystal structure of enzyme mutant C280S in complex with inhibitor 6-benzyl-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione, PDB ID 6AOC, hanging drop vapor diffusion method, mixing of 11 mg/ml protein in 10 mM MnCl2, 5 mM tris(2-carboxyethyl)phosphine (TCEP) HCl, 0.5% beta-octylglucoside, and 1 mM 6-benzyl-3-hydroxythieno[2,3-d]pyrimidine-2,4(1H,3H)-dione in a 1:1 ratio with crystallization solution containing 15% PEG 3500, 0.1 M sodium potassium phosphate, 5% ethylene glycol, and 0.1 M Tris, pH 6.5, large, blocky crystals grow at 18°C in 2-3 days, molecular replacement using structure PDB ID 4KFB as the initial search model
-
docking simulation studies. Residue His 539 and two metal ions in the RNase H catalytic center are involved in inhibition by compounds 5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester and 5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl]-methyl ester
-
in complex with substrate, hanging drop vapor diffusion method, using 50 mM Bis-Tris propane-HCl pH 7.0, 10% PEG 8000 (w/v), 100 mM ammonium sulfate, 5% glycerol (v/v), 5% sucrose (w/v) and 20 mM MgCl2
isolated recombinant RNase H domain, to 2.4 A resolution. The protein folds into a five-stranded mixed beta sheet flanked by an asymmetric distribution of four alpha helices. Two divalent metal cations bind in the active site surrounded by a cluster of four conserved acidic amino acid residues. The peptide bond cleaved by HIV-1 protease near the polymerase-RNase H junction of polypeptide p66 is completely inaccessible to solvent in the structure reported here, suggesting that the homodimeric p66-p66 precursor of mature RT is asymmetric with one of the two RNase H domains at least partially unfolded
-
modeling of the kinetic refolding intermediate using a C-terminal deletion fragment lacking helix E. Like the kinetic intermediate, this variant folds rapidly and shows a decrease in stability
-
purified p66/p51 HIV-1 reverse transcriptase 52A variant in complex with inhibitors manicol and TMC278, 0.0012 ml of 20 mg/mL protein in 9.2 mM Tris, pH 8.0, 68.7 mM NaCl, 3.6 mM manganese sulfate, 0.7 mM tris(2-carboxyethyl) phosphine, 0.27% w/v, beta-ocytl glucopyranoside, 7% v/v DMSO, 0.9 mM manicol, and 0.7 mM TMC278, mixed with 0.0012 ml of reservoir solution containing 50 mM HEPES pH 7.5, 100 mM ammonium sulfate, 15 mM manganese sulfate, 10 mM spermine, 5 mM TCEP, and 11% w/w PEG 8000, X-ray diffraction structure determination and analysis at 2.7 A resolution, modeling
-
purified recombinant detagged enzyme, mixing of 8-10 mg/ml protein in 20 mM potassium phosphate, pH 7.0, and 1 mM inhibitor nevirapine, with reservoir buffer containing 100 mM sodium cacodylate, pH 6.8, and 800 mM sodium citrate, in a 1:1 ratio, X-ray diffraction structure determination and analysis. Isolated RNase H domain is crystallized in a buffer containing 100 mM sodium citrate, pH 5.0, and 15 to 20% PEG-8000. Crystals are harvested for inhibitor soaking in the reservoir solution with the addition of 50 mM MnCl2, and 1 mM inhibitor nevirapine, at 4°C. Mn2+ is used as a surrogate for Mg2+ since soaking experiments with Mg2+ cannot reproducibly yield structures with inhibitor bound
purified wild-type enzyme in complex with polypurine tract RNA:DNA oligonucleotide, hanging drop vapour diffusion method, mixing of equal volumes of protein and precipitant solution, the latter contains 100 mM cacodylate, pH 5.6, 29-31% saturated ammonium sulfate, 4°C, X-ray diffraction structure determination and analysis at 3.0 A resolution, molecular replacement
solution structural dynamics. Enzyme is an asymmetric heterodimer of two subunits, p66 and p51. The two subunits have the same N-terminal sequence, with the p51 subunit lacking the C-terminal RNase H domain. The p66 subunit contains the polymerase and RNase H catalytic sites. H/D exchange indicates that the RNase H domain of p66 is very flexible
study on dynamics of RT in unliganded and inhibitor-bound forms by structure-based approach. Non-nucleoside RT inhibitors such as nevirapine interfere directly with the global hinge-bending mechanism that controls the cooperative motions of the p66 fingers and thumb subdomains. The net effect of nevirapine binding is to change the direction of domain movements rather than suppress their mobilities. The second generation non-nucleoside reverse transcriptase inhibitor, efavirenz, on the other hand, shows the stronger effect of simultaneously reorienting domain motions and obstructing the p66 thumb fluctuations. A second hinge site controlling the global rotational reorientations of the RNase H domain is identified
-
HIV-1 reverse transcriptase mutant form RT52A in complex with rilpivirine and an RNase H inhibitor XZ462, hanging drop vapor diffusion method, the crystallization solution contains 10% PEG 8000, 50 mM imidazole, pH 6.8, 10 mM spermine, 15 mM MgSO4, and 100 mM (NH4)2SO4, crystals of the RT-rilpivirine (RPV) complex are soaked for 30 min with 2 mM compound XZ462 in the crystallization solution in presence of 15 mM MgSO4, X-ray diffraction structure determination and analysis at 1.51-2.2 A resolution, molecular replacement using the 1.51 A resolution structure of the HIV-1 RT-rilpivirine complex (PDB ID 4G1Q) as template
Human immunodeficiency virus type 1 group M subtype B
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PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D549A
-
mutation in polypeptide p66, decrease in RNase H activity
D549N
-
mutation in polypeptide p66, decrease in RNase H activity
E478Q
Q294P
-
site-directed mutagenesis, the Q294P mutant of HIV-2 RT has about 10fold higher RNase H activity than the wild-type. Infectious HIV-2 cannot bear the replacement of the RT's Gln294 by the HIV-1 RT Pro counterpart, as it results in substantially reduced HIV-2 replication and fast reversions to the wild-type Gln294 virus
A360I
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
A360I/V
-
site-directed mutagenesis, a connection/RNase H domain mutant
A360K
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
A360V
A371V
A376S
A554K
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
A554L
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
A554T
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
C280P
-
significant reduction in RNase H activity. A heterodimer p66C280p/p51C280P shows about 8% of wild-type RNaseH activity, 6% of strand transfer activity, and 105% of DNA polymerase activity. A heterodimer p66C280P/p51 shows about 60% of wild-type RNaseH activity, 80% of strand transfer activity, and 100% of DNA polymerase activity. A heterodimer p66/p51C280W shows about 30% of wild-type RNaseH activity, 6% of strand transfer activity, and 99% of DNA polymerase activity
C280S
C280S/K172A/K173A
-
p66/p51 HIV-1 reverse transcriptase 52A mutant variant, the mutation C208S resides in both subunits, the p66 subunit also contains the mutations K172A and K173A
C280W
-
significant reduction in RNase H activity. A heterodimer p66C280W/p51C280W shows about 11% of wild-type RNaseH activity, 6% of strand transfer activity, and 100% of DNA polymerase activity. A heterodimer p66C280W/p51 shows about 44% of wild-type RNaseH activity, 80% of strand transfer activity, and 98% of DNA polymerase activity. A heterodimer p66/p51C280W shows about 29% of wild-type RNaseH activity, 7% of strand transfer activity, and 100% of DNA polymerase activity
C282S
-
site-directed mutagenesis, the mutation avoids non-specific cross-linking in both subunits, p66 and p51 subunits of HIV-1
D443A
-
site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme
D549A
-
site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme
D549N
-
mutation increases the 3'-azido-3'-deoxythymidine concentration needed to inhibit viral replication by 50% 12fold by increasing the time available for excision of incorporated nucleoside reverse transcriptase inhibitors from terminated primers and results in 5- to 10fold reduction in viral titers in a single-replication cycle assay
D67N
E312Q
E396A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
E438N
site-directed mutagenesis, the mutation disrupts RNH folding, viral infectivity is eliminated by the mutation
E438N/T477A
site-directed mutagenesis, addition of the T477A mutation restores correct folding of the RNH domain despite the presence of the E438N mutation
E475A
-
site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
E478A
-
site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme
E478Q
E478Q/N348I
-
mutation of RNase H active site and connection domain
E706Q
F227L
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
F440A
site-directed mutagenesis, the mutation disrupts RNH folding, viral infectivity is eliminated by the mutation. Molecular dynamics simulations suggest that the T477A mutation affects the processing site by altering relative orientations of secondary structure elements
F440A/T477A
site-directed mutagenesis, addition of the T477A mutation restores correct folding of the RNH domain despite the presence of the F440A mutation
G190A
G190S
-
site-directed mutagenesis, the mutant virus shows moderately reduced fitness compared to that of the wild-type virus
G333E
G335C
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
G335D
G359A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
G509L
-
Glu to Leu substitution at residue 509 in the ribonuclease H domain of HIV-1 reverse transcriptase confers zidovudine resistance, mechanism, overview. Q509L increases zidovudine monophosphate excision activity of RT on RNA/DNA template/primers, but not DNA/DNA template/primers, due to Q509L decreasing a secondary RNase H cleavage event that reduces the RNA/DNA duplex length to 10 nucleotides and significantly impairs the enzyme's ability to excise the chain-terminating nucleotide. Mutation Q509L does not affect initial rates of the polymerase-directed RNase H activity but only polymerase-independent cleavages that occur after a template/primer dissociation event. Q509L decreases the affinity of the enzyme to bind template/primers with duplex lengths less than 18 nucleotides in the polymerase-independent RNase H cleavage mode, while not affecting the enzyme's affinity to bind the same template/primers in an zidovudine monophosphate excision competent mode
G544Stop
-
C-terminal truncation of p66 polypeptide. Loss of RNase H activity, while dimerization with polypepitde p51 and DNA polymerase activity are not significantly affected
H539F
-
mutation in isolated RNase H domain, mutant fails to bind RNA/DNA hybrids. Structure of mutant is similar to wild-type
H539N
-
increases the 3'-azido-3'-deoxythymidine concentration needed to inhibit viral replication by 50% 180fold relative to wild-type by increasing the time available for excision of incorporated nucleoside reverse transcriptase inhibitors from terminated primers
I505A
I505G
-
site-directed mutagenesis, the mutant exhibits a dimerization defect. The efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
K103N
K219E
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
K219N
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
K219Q
K390A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
K395A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
K451R
-
mutation present in viral isolates of 11% of antiviral treatment-experienced patients but remaining 100% conserved among treatment-naive patients
K476A
K540A
-
site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme
K558E
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, associated with an increase in thymidine analogue mutations, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
K558G
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, associated with an increase in thymidine analogue mutations, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
K558R
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, associated with an increase in thymidine analogue mutations, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
K65R
K65R/Q151M/A62V/V75I/F77L/F116Y
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
K70R
L100I
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
L210W
L429M/E514L
N-terminal truncated constructs include RHDELTANT, corresponding to p66 residues 429-560 with an N-terminal Leu429Met mutation, an extended linker construct, RHDELTANT-EL, in which an additional Pro-Asp-Gln sequence is introduced into RHDELTANT immediately following Gln512, and RHDELTANT(E514L) in which RHDELTANT contains an E514L substitution in the alphaB-alphaD linker
L469H
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
L469I
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
L469M
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
L469T
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
L74V
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
M184V
-
naturally occuring mutation in HIV infection patients, arises with abacavir, emtricitabine, or lamivudine treatment
M230L
-
the naturally occuring mutation leads to reduced RNase H activity of the HIV reverse transcriptase
M41L
N348I
N474A
N474A/Q475A
-
mutation reduces the viral titer 5- to 10fold, , reduction in the efficiency of DNA synthesis. Mutant is less efficient than the wild-type enzyme in its ability to remove a polypurine tract primer from a model substrate and has an altered RNase H cleavage specificity
N494D
-
mutant closely resembles the wild-type RNase H, exhibits an endonuclease activity and a processive RNase H activity, gives rise to small RNA hydrolysis products, and acts in concert with the reverse transcriptase
P236L
-
site-directed mutagenesis, the mutant virus shows substantially reduced fitness compared to that of the wild-type virus
P537Stop
-
C-terminal truncation of p66 polypeptide. Loss of RNase H activity, while dimerization with polypepitde p51 and DNA polymerase activity are not significantly affected
Q151M
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
Q151M/A62V/V75I/F77L/F116Y
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
Q475A
Q475E
-
mutant exhibits a retarded endonuclease activity and an impaired 3'-5' processive RNA cleavage activity, gives rise to predominantly larger RNA hydrolysis products, is less processive in the presence of competitor substrate, and is defective in its ability to hydrolyze the polypurine tract and homopolymeric hybrids
Q509L
R448A
R557A
-
the mutant shows about 5fold reduced kcat value compared to the wild type enzyme
R72A
-
site-directed mutagenesis, the mutant shows reduced activity compared to wild-type. The R72A mutation might impair the nucleotide-induced conformational change but does not affect the RNase H activity directly, kinetic parameters governing TTP binding and incorporation by the HIVRT mutant, overview. The mutation causes impaired TTP induced conformational change on RNase H activity
T215F
T215Y
T470E
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
T470K
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
T470P
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
T470S
-
naturally occuring mutation in HIV infection patients, the mutation renders the patient more prevalent amongst treatment-experienced patients, treatment with nucleoside reverse transcriptase inhibitors and nonnucleoside reverse transcriptase inhibitors
T473A
T473C
-
the mutation increases the sensitivity of the enzyme for inhibitor NSC727447 by 50fold
T473M
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
T477A
site-directed mutagenesis, addition of the T477A mutation restores correct folding of the RNH domain despite the presence of the F440A or E438N mutations
V106A
V365I
V552Stop
-
C-terminal truncation of p66 polypeptide. Mutant retains endonuclease activity but lacks the directional processing feature of wild-type and barely supports transfer of nascent (-)-stranded DNA between RNA templates
W229F
-
mutation in primer grip residue, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
W229F/Y232W
-
mutation in primer grip residues, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
W229Y
-
mutation in primer grip residue, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
W535A
-
site-directed mutagenesis, altered inhibitor binding compared to wild-type enzyme
W71A
-
site-directed mutagenesis, the mutant is probably less rigidly locked on the substrate DNA/RNA hybrid, parameters governing TTP binding and incorporation by the HIVRT mutant, overview. The mutation causes impaired TTP induced conformational change on RNase H activity
W71D
-
site-directed mutagenesis, the mutant is probably less rigidly locked on the substrate DNA/RNA hybrid, parameters governing TTP binding and incorporation by the HIVRT mutant, overview. The mutation causes impaired TTP induced conformational change on RNase H activity
Y181C
Y188C
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
Y188L
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
Y229F/Y232F
-
mutation in primer grip residues, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
Y232W
-
mutation in primer grip residue, specificity of cleavage is not compromised, efficiency is reduced to 33-44% of wild-type
Y501A
E478Q/N348I
-
mutation of RNase H active site and connection domain
-
N348I
-
connection domain mutant, altered RNase H cleavage pattern compared to the wild-type HIV-1 RT
-
E396A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
-
K390A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
-
K395A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
-
K65R
-
naturally occuring mutation in HIV infection patients, arises with abacavir, didanosine, emtricitabine, lamivudine, or tenofovir disoproxil fumarate treatment
-
M230L
-
the naturally occuring mutation leads to reduced RNase H activity of the HIV reverse transcriptase
-
Y501A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
-
Q294P
-
site-directed mutagenesis of a residue in the catalytically inactive p54 subunit resulting in an increase in RNase H activity comparable with that of HIV-1 reverse transcriptase
D443N
Human immunodeficiency virus type 1 group M subtype B
RNase H inactivating mutation, the mutant is devoid of strand transfer activity
E478Q
Human immunodeficiency virus type 1 group M subtype B
RNase H inactivating mutation, the mutant is devoid of strand transfer activity
G140S/Q148H
Human immunodeficiency virus type 1 group M subtype B
site-directed mutagenesis, mutant INSTI
K70R
Human immunodeficiency virus type 1 group M subtype B
site-directed mutagenesis, mutant NRTI
L100I/K103N
Human immunodeficiency virus type 1 group M subtype B
site-directed mutagenesis, mutant NNRTI
M184V
Human immunodeficiency virus type 1 group M subtype B
site-directed mutagenesis, mutant NRTI
V106A
Human immunodeficiency virus type 1 group M subtype B
site-directed mutagenesis, mutant NNRTI
Y181C
Human immunodeficiency virus type 1 group M subtype B
site-directed mutagenesis, mutant NNRTI
Y188L
Human immunodeficiency virus type 1 group M subtype B
site-directed mutagenesis, mutant NNRTI
D443N
Human immunodeficiency virus type 1 group M subtype B BH10
-
RNase H inactivating mutation, the mutant is devoid of strand transfer activity
-
E478Q
Human immunodeficiency virus type 1 group M subtype B BH10
-
RNase H inactivating mutation, the mutant is devoid of strand transfer activity
-
K70R
Human immunodeficiency virus type 1 group M subtype B BH10
-
site-directed mutagenesis, mutant NRTI
-
M184V
Human immunodeficiency virus type 1 group M subtype B BH10
-
site-directed mutagenesis, mutant NRTI
-
V106A
Human immunodeficiency virus type 1 group M subtype B BH10
-
site-directed mutagenesis, mutant NNRTI
-
Y181C
Human immunodeficiency virus type 1 group M subtype B BH10
-
site-directed mutagenesis, mutant NNRTI
-
Y188L
Human immunodeficiency virus type 1 group M subtype B BH10
-
site-directed mutagenesis, mutant NNRTI
-
D443N
Human immunodeficiency virus type 1 group O subtype B
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
E478Q
Human immunodeficiency virus type 1 group O subtype B
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
F61A
Human immunodeficiency virus type 1 group O subtype B
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
K358R/A359G/S360A
Human immunodeficiency virus type 1 group O subtype B
-
the mutant shows highly increased strand transfer efficiency compared to wild-type
K65R/E478Q
Human immunodeficiency virus type 1 group O subtype B
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
L92P
Human immunodeficiency virus type 1 group O subtype B
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
L92P/D443N
Human immunodeficiency virus type 1 group O subtype B
-
site-directed mutagenesis, the mutant shows decreased dissociation rate constant (koff) compared to wild-type
L92P/E478Q
Human immunodeficiency virus type 1 group O subtype B
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
T355A/Q357M
Human immunodeficiency virus type 1 group O subtype B
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
T355A/Q357MK358R/A359G/S360A
Human immunodeficiency virus type 1 group O subtype B
-
the mutant shows highly increased strand transfer efficiency compared to wild-type
V148I
Human immunodeficiency virus type 1 group O subtype B
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
V148I/K358R/A359G/S360A
Human immunodeficiency virus type 1 group O subtype B
-
the mutant shows highly increased strand transfer efficiency compared to wild-type
D443N
Human immunodeficiency virus type 1 group O subtype B ESP49
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
-
E478Q
Human immunodeficiency virus type 1 group O subtype B ESP49
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
-
L92P
Human immunodeficiency virus type 1 group O subtype B ESP49
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
-
V148I
Human immunodeficiency virus type 1 group O subtype B ESP49
-
site-directed mutagenesis, the mutant shows increased dissociation rate constant (koff) compared to wild-type
-
A554S
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
D460N
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
D488E
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
D549N
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
E529D
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
H539N
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
I505A
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
I506L
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
K451R
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
K476A
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
K476N
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
K512Q
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
K527N
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
K530R
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
K558E
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
K558R
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
L469F
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
L491S
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
N474A
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
Q475A
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
Q500A
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
Q509L
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
Q547K
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
T470N
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
T473A
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
V518I
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
Y501A
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
Y501F
Human immunodeficiency virus type 1 subtype C
-
naturally occurring mutation in the RNase H region of HIV-1 subtype C infected individual
A128T
-
the mutant strain is resistant to 2-hydroxyisoquinoline-1,3(2H,4H)-dione inhibitors in contrast to the wild-type
C635V
-
site-directed mutagenesis, the mutant shows slightly reduced reverse transcriptase and RNAse H activities compared the wild-type enzyme
D524A
D524N
D583A
-
site-directed mutagenesis, RNase H-inactive mutant, that shows increased intrinsic thermal stability compared to the wild-type enzyme. The mutant loses RNase H activity through abolishing of Mg2+ binding to the RNase H domain
D583N
-
less than 0.5% of wild-type activity, no binding of Mn2+
E562Q
-
less than 0.5% of wild-type activity, no binding of Mn2+
G140S/Q148H
-
the mutant strain is resistant to 2-hydroxyisoquinoline-1,3(2H,4H)-dione inhibitors in contrast to the wild-type
D358N
-
mutation eliminates Mg2+- and Mn2+-dependent RNase H function
D426N
-
mutation eliminates Mg2+- and Mn2+-dependent RNase H function
D469N
-
reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA
E401Q
-
mutation eliminates Mg2+- and Mn2+-dependent RNase H function
H427A
-
reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA
Y459A
-
reduced RNase H activity in presence of Mg2+, decrease of turnover rate in presence of Mn2+. Mutant fails to support DNA strand transfer and release of the (+)-strand polypurine tract primer from (+)-RNA
additional information
E478Q
-
the efficiency with which mutant RT catalyzes transfer of nascent DNA between RNA templates is severely reduced
A360V
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
A360V
-
naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity
A371V
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively
A371V
-
site-directed mutagenesis, a connection/RNase H domain mutant
A376S
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B. Mutations N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations
A376S
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
D67N
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
E312Q
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B
E312Q
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
E478Q
-
mutation in isolated RNase H domain, mutant fails to bind RNA/DNA hybrids. Structure of mutant is similar to wild-type
E706Q
-
site-directed mutagenesis of HIV-1 reverse transcriptase, inactive mutant
E706Q
-
site-directed mutagenesis of the recombinant mutant construct G, E706 in construct G corresponds to E478 in HIV-1 reverse transcriptase, inactive mutant
G190A
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
G190A
-
site-directed mutagenesis, the mutant virus shows moderately reduced fitness compared to that of the wild-type virus
G333E
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B
G335D
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively
G335D
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
I505A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
K103N
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
K103N
-
site-directed mutagenesis, the mutant virus shows fitness similar to that of the wild-type virus
K103N
-
site-directed mutagenesis, the mutation does not affect RNase H function
K219Q
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
K476A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
K476A
-
site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
K65R
-
mutation involved in nucleos(t)ide reverse transcriptase inhibitor resistance
K65R
-
naturally occuring mutation in HIV infection patients, arises with abacavir, didanosine, emtricitabine, lamivudine, or tenofovir disoproxil fumarate treatment
K70R
-
naturally occuring mutation in HIV infection patients, is common to stavudine, tenofovir disoproxil fumarate, and zidovudine therapy
K70R
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
L210W
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-1 pathway
M41L
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-1 pathway
N348I
mutations N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations
N348I
-
connection domain mutant, altered RNase H cleavage pattern compared to the wild-type HIV-1 RT
N348I
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
N348I
-
naturally occuring mutant from clinical isolates, a connection/RNase H domain mutant that shows reduced RNase H activity
N474A
-
the mutant shows about 40fold reduced kcat value compared to the wild type enzyme
Q475A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
Q475A
-
the mutant shows about 10fold reduced kcat value compared to the wild type enzyme
Q509L
mutations N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations
Q509L
-
mutation in the RNase H domain, the mutation significantly contributes to zidovudine resistance
Q509L
-
site-directed mutagenesis, a connection/RNase H domain mutant
R448A
-
the mutant shows about 3fold reduced kcat value compared to the wild type enzyme
T215F
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-2 pathway
T215Y
-
thymidine analogue mutation, TAMs, arising with zidovudine and stavudine treatment, take the TAM-1 pathway
T473A
-
site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
V106A
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
V106A
-
site-directed mutagenesis, the mutant virus shows moderately reduced fitness compared to that of the wild-type virus
V365I
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B
V365I
-
mutation in the connection domain, the mutation significantly contributes to zidovudine resistance
Y181C
-
mutation involved in non-nucleoside reverse transcriptase inhibitor resistance
Y181C
-
site-directed mutagenesis, the mutant shows resistance to non-nucleoside reverse transcriptase inhibitors
Y181C
-
site-directed mutagenesis, the mutant virus shows fitness similar to that of the wild-type virus
Y181C
-
site-directed mutagenesis, the mutation does not affect RNase H function
Y501A
-
mutation reduces the viral titer 5- to 10fold, reduction in the efficiency of DNA synthesis. Mutant is less efficient than the wild-type enzyme in its ability to remove a polypurine tract primer from a model substrate and has an altered RNase H cleavage specificity
Y501A
-
naturally occuring mutation in HIV infection patients, the mutation increases zidovudine resistance and decreased reverse trancriptase template switching
Y501A
-
site-directed mutagenesis, the mutant shows only minimally altered substrate specificity or enzyme activity compared to the wild-type enzyme. But the efficiency with which most mutants catalyzed polymerization-independent RNase H cleavage is sharply reduced. This deficiency is more pronounced when the mutant enzyme is challenged to process the (+) strand polypurine tract (PPT) primer from either (+) RNA or a PPT/(+) DNA RNA/DNA chimera
Y501A
-
the mutant shows about 400fold reduced kcat valuecompared to the wild type enzyme
D524A
-
mutant lacks RNase H activity, but retains reverse transcriptase activity. Elimination of RNase H activity enhances the intrinsic thermal stability of the protein rather than its affinity to template-primer
D524A
-
site-directed mutagenesis, RNase H-inactive mutant, that shows increased intrinsic thermal stability compared to the wild-type enzyme. The mutant loses RNase H activity through abolishing of Mg2+ binding to the RNase H domain
D524N
-
less than 0.5% of wild-type activity, no binding of Mn2+
D524N
-
loss of catalytic activity. Construction of vectors encapsidated in virions engineered to contain phenotypic mixtures of wild-type and RNase H catalytic site point mutant D524N reverse transcriptase. There is a steady decline in direct repeat deletion frequency that correlates with decreases in functional RNase H, with greater than fourfold decreases in repeat deletion frequency observed when 95% of virion reverse transcriptase is RNase H defective
additional information
-
an HIV-1 mutant can tolerate an about 10fold higher RNase H activity
additional information
-
naturally occurring polymophisms at position 294 in HIV-2 are Q, E, L, H, and K
additional information
-
chemical modifications by thiol-specific reagents of cysteine 280, located in a helix I in the thumb subdomain of the polymerase domain, affect substantially only the RNase H activity
additional information
-
construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity
additional information
-
construction of two chimeric enzymes by swapping the RNase H domains between HIV-1 RT and Moloney murine leukemia virus MuLV RT. Chimeric HIV-1 RT, having the RNase H domain of MuLV RT, inherits the divalent cation preference characteristic of MuLV RT on the DNA template with no significant change on the RNA template. Chimeric MuLV RT, likewise partially inherits the metal ion preference of HIV-1 RT. Unlike the wild-type MuLV RT, chimeric MuLV RT is able to use both Mn-dNTP and Mg-dNTP on the RNA template with similar efficiency, while a 30-fold higher preference for Mn.dNTP was seen on the DNA template. The metal preferences for the RNase H activity of chimeric HIV-1 RT and chimeric MuLV RT are, respectively, Mn2+ and Mg2+, a property acquired through their swapped RNase H domains. Chimeric HIV-1 RT displays higher fidelity and discrimination against rNTPs than against dNTPs substrates, a property inherited from MuLV RT. The overall fidelity of the chimeric MuLV RT is decreased in comparison to the parental MuLV RT, suggesting that the RNase H domain profoundly influences the function of the polymerase domain
additional information
-
construction of an N-terminally His-tagged mutant p51-G-TCR construct designed to encode the p51 subunit joined by a linker to the thumb (T), connection (C), and RNase H (R) domains of p66, the p51-G-TCR RNase H construct displays Mg2+-dependent activity using a fluorescent nonspecific assay and shows the same cleavage pattern as HIV-1 reverse transcriptase on substrates that mimic the tRNA removal required for second-strand transfer reactions. The RNase H of the p51-G-TCR RNase H construct and wild-type HIV-1 reverse transcriptase have similar Kms for an RNA-DNA hybrid substrate and show similar inhibition kinetics to two known inhibitors of the HIV-1 reverse transcriptase RNase H, molecular modeling
additional information
-
RNase H primer grip mutations suppress polymerization-independent RNase H cleavage. Alteration of RNase H primer grip residues Thr473, Asn474, and Gln475 has little influence on cleavage specificity. Altering the RNase H domain of HIV-1 RT can impact significantly on the ability of mutant enzymes to catalyze DNA synthesis, but all RNase H primer grip mutants show little difference in their DNA-dependent DNA polymerase activity
additional information
effect of N-terminal deletion on monomer-dimer interconversion kinetics, overview. The mutant exhibits large perturbations of the Ile522 and Ile526 resonances corresponding to residues located near the Tyr427 binding pocket, as well as smaller but significant perturbations for several other Ile resonances, consistent with a more subtle, global structural perturbation. As a result of the faster monomer-dimer interconversion rate, even the initial spectrum obtained for the purified dimer sample exhibits significant monomer resonances
additional information
-
effect of N-terminal deletion on monomer-dimer interconversion kinetics, overview. The mutant exhibits large perturbations of the Ile522 and Ile526 resonances corresponding to residues located near the Tyr427 binding pocket, as well as smaller but significant perturbations for several other Ile resonances, consistent with a more subtle, global structural perturbation. As a result of the faster monomer-dimer interconversion rate, even the initial spectrum obtained for the purified dimer sample exhibits significant monomer resonances
additional information
-
mutation of the N-terminal residue of RNase H which is important in the life cycle of HIV-1, change of this residue to several different amino acids. Selection of mutants is based on the N-end rule designation or the structure of the specific amino acid compared to that of the wild-type residue of tyrosine. Compared to wild-type AETF/YVD, the mutants show the following cleavage sites: AETF/MVD, AETF/FVD, AETF/WVD, AETF/TVD, AETF/LVD, AETF/KVD, AETF/AVD, AETF/PVD, AETF/GVD, AETF/SVD, and AETF/VVD, being stabilizing or destabilizing for the N-end rule, packaging and processing of viral polyproteins with RNaseH N-terminal mutations, overview. Reverse transcriptase with an RNase H N-terminal mutation is still degraded in the absence of active viral protease
additional information
-
the isolated RNase H domain of HIV-1 RT (RNHHIV) is inactive, possibly due to the lack of a substrate binding ability, disorder of a loop containing His539, and increased flexibility. To examine whether the activity of RNHHIV is restored by the attachment of TmaHBD or BstNTD to its N-terminus, two chimeric proteins, TmaHBD-RNHHIV and BstNTD-RNHHIV, are constructed and characterized. Both chimeric proteins bind to RNA/DNA hybrid more strongly than RNHHIV and exhibit enzymatic activity in the presence of Mn2+ ions. They do not exhibit activity or exhibited very weak activity in the presence of Mg2+ ions
additional information
-
construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity
additional information
-
construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity
-
additional information
-
construction of chimeric HIV-1/HIV-2 reverse transcriptases, in which protein segments and/or subunits are exchanged. The RNase H specific activity of the chimeric enzymes is either high like HIV-1 reverse transcriptase or low like HIV-2 reverse transcriptase. The origin of the thumb subdomain in the small subunit of the chimeric reverse transcriptases, residues 244-322 determines the level of the RNase H activity
-
additional information
Human immunodeficiency virus type 1 group O subtype B
-
the kinetics of wild-type and mutant enzymes are determined with the RNA/DNA template-primer R33B/20A. Rates of nontemplated nucleotide addition of wild-type and mutant HIV-1 RTs using blunt-ended DNA/DNA substrates, overview. Non-templated nucleotide addition and strand transfer are mechanistically independent
additional information
Human immunodeficiency virus type 1 group O subtype B ESP49
-
the kinetics of wild-type and mutant enzymes are determined with the RNA/DNA template-primer R33B/20A. Rates of nontemplated nucleotide addition of wild-type and mutant HIV-1 RTs using blunt-ended DNA/DNA substrates, overview. Non-templated nucleotide addition and strand transfer are mechanistically independent
-
additional information
Human immunodeficiency virus type 1 subtype C
-
characterization of nucleoside reverse transcriptase inhibitor (NRTI)-associated mutations in the RNase H region of HIV-1 subtype C infected individuals, overview. Mutations are identified by comparing with NRTI-associated RNase H mutations previously identified from subtype B drug-resistance studies
additional information
-
deletion of 204 nucleotides at the 3'-terminus results in 4fold increase in activity level upon recombinant expression and allows for high-level production of the protein
additional information
-
construction of two chimeric enzymes by swapping the RNase H domains between HIV-1 RT and Moloney murine leukemia virus MuLV RT. Chimeric HIV-1 RT, having the RNase H domain of MuLV RT, inherits the divalent cation preference characteristic of MuLV RT on the DNA template with no significant change on the RNA template. Chimeric MuLV RT, likewise partially inherits the metal ion preference of HIV-1 RT. Unlike the wild-type MuLV RT, chimeric MuLV RT is able to use both Mn-dNTP and Mg-dNTP on the RNA template with similar efficiency, while a 30-fold higher preference for Mn.dNTP was seen on the DNA template. The metal preferences for the RNase H activity of chimeric HIV-1 RT and chimeric MuLV RT are, respectively, Mn2+ and Mg2+, a property acquired through their swapped RNase H domains. Chimeric HIV-1 RT displays higher fidelity and discrimination against rNTPs than against dNTPs substrates, a property inherited from MuLV RT. The overall fidelity of the chimeric MuLV RT is decreased in comparison to the parental MuLV RT, suggesting that the RNase H domain profoundly influences the function of the polymerase domain
additional information
-
site-directed chemical modification of the RNase H domain by selectively PEGylating Cys635, one of the eight cysteine residues present in the reverse transcriptase, specifically inactivates its ribonucleolytic activity, PEGylation as a tool for engineering the M-MuLV RT derivative deficient in RNase H activity, overview
additional information
-
construction of a chimeric enzyme containing the first 425 amino acid residues from the N-terminal domain of HIV-1 reverse transcriptase, i.e. the polymerase domain, and 200 amino acid residues from the C-terminal domain of murine leukemia virus reverse transcriptase, i.e. RNase H-domain. The chimeric enzyme exists as a monomer with intact DNA polymerase and RNase-H functions. It is able to catalyze both endonucleolytic and processive RNase-H functions in a manner similar to the wild type HIV-1 reverse transcriptase and murineleukemia virus reverse transcriptase
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TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
29.7
43.5
-
melting temperature, mutant H638G, presence of 1 mM Mn2+
43.6
-
wild-type, 50% residual activity after a 10 min incubation
46.2
-
wild-type, 50% residual activity after a 10 min incubation, presence of primer-template
46.3
-
melting temperature, mutant D524N, presence of 1 mM Mn2+
46.9
-
melting temperature, mutant D653N, presence of 1 mM Mn2+
47.3
-
mutant D524A, 50% residual activity after a 10 min incubation
48.4
-
melting temperature, mutant D583N, presence of 1 mM Mn2+
48.8
-
melting temperature, mutant E562Q, presence of 1 mM Mn2+
49.7
-
mutant D524A, 50% residual activity after a 10 min incubation, presence of primer-template
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PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
a HIV-1 RNase H specific inhibitor from the hydroxyimide class, that contains a primary amine with a long nonfunctional linker, is conjugated to NHS-activated HiTrap HP resins for use in affinity chromatographic HIV reverse transcriptase purifcation. Purification of untagged HIV-1 RT using an avidin affinity column in presence of Mg2+, method evaluations, overview
-
HiTrap column chromatography and Superdex 200 gel filtration
-
Ni-NTA column chromatography and heparin column chromatography
recombinant His-tagged enzyme by nickel affinity chromatography, the His6 tag is removed by proteolysis with thrombin, followed by gel filtration
recombinant His-tagged enzyme from Escherichia coli strain M15 by nickel and heparin affinity chromatography
Human immunodeficiency virus type 1 group M subtype B
recombinant His-tagged p66 or p51 HIV-1 RT DNA fragment from Escherichia coli strain BL21(DE3)pLys by nickel affinity chromatography, expression of a heterodimer of wild-type or F160S and C280S mutant p66 and p51 using plasmid vector RT69A in Escherichia coli strain Rosetta
-
recombinant His6-tagged p66/p51 HIV-1 reverse transcriptase 52A variant C280S by nickel affinity chromatography, the tag is cleaved by HRV14 3C protease
-
recombinant N-terminally His-tagged p66 and p51 subunit mutants C282S from Escherichia coli strain BL21 Rosetta by nickel affinity chromatography, dialysis, heparin affinity chromatography, and gel filtration
-
recombinant N-terminally His6-SUMO-fused wild-type and mutant RNase H RNH domains (residues 427-560) from Escherichia coli strain Rosetta 2 (DE3) by nickel affinity chromatography and gel filtration, the N-terminal His6-SUMO fusion is removed by digestion with histidine tagged ubiquitin-like-protein specific protease (ULP1)
recombinant wild-type enzyme and chimeric mutants from Escherichia coli strain MIC2067 (DE3) by dialysis of cell-free enzyme extract, anion and cation exchange chromatography, dialysis, and gel filtration
-
soluble recombinant RNase H, in an N-terminally His-tagged construct, p51-G-TCR construct, designed to encode the p51 subunit joined by a linker to the thumb (T), connection (C), and RNase H (R) domains of p66, from Escherichia coli strain MIC2067(DE3) by nickel affinity chromatography
-
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CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
cloning a His-tagged p66 or p51 HIV-1 RT DNA fragment into the pQE-9 vector and expression in Escherichia coli strain BL21(DE3)pLys
-
expression in Escherichia coli
expression of His6-tagged p66/p51 HIV-1 reverse transcriptase p51/p66 52A variant C280S, the p66 subunit also contains the mutations K172A and K173A
-
expression of RNase H domain from residue Y427 to L560 as fusion protein in Escherichia coli
-
expression of RNase H, in an N-terminally His-tagged construct designed to encode the p51 subunit joined by a linker to the thumb (T), connection (C), and RNase H (R) domains of p66, in Escherichia coli strain MIC2067(DE3) lacking endogenous RNase HI and HII as soluble protein. The construct G provides sufficient RNase H activity to complement Escherichia coli growth at 42°C
-
expression of the isolated RNase H domain in Escherichia coli
-
isolated 125-residue RNase H domain consisiting of residues G436-L560 of polypepitde p6
-
recombinant expression of both enzyme subunits, N-terminally His-tagged p66 and p51 subunit mutants C282S of HIV-1, in Escherichia coli strain BL21 Rosetta
-
recombinant expression of His-tagged enzyme in Escherichia coli strain M15
Human immunodeficiency virus type 1 group M subtype B
recombinant expression of wild-type and mutant RNase H RNH domains (residues 427-560) in Escherichia coli strain Rosetta 2 (DE3) as N-terminally His6-SUMO-fused proteins
recombinant overexpression of wild-type enzyme and chimeric mutants in Escherichia coli strain MIC2067 (DE3)
-
the entire RNase H region of reverse transcriptase RT is encoded in codons 431-560, DNA and amino acid sequence determination and analysis, genotyping
Human immunodeficiency virus type 1 subtype C
-
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RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
Refolding of the isolated HIV RNase H domain shows a kinetic intermediate detectable by stopped-flow far UV circular dichroism and pulse-labeling H/D exchange. In this intermediate, strands 1, 4, and 5 as well as helices A and D appear to be structured. Compared to its homolog from Escherichia coli, the rate limiting step in refolding of HIV RNase H appears closer to the native state. This kinetic intermediate has been modeled using a C-terminal deletion fragment lacking helix E. Like the kinetic intermediate, this variant folds rapidly and shows a decrease in stability
-
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APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
analysis
drug development
medicine
pharmacology
-
mutations in RNase H can significantly contribute to drug resistance either alone or in combination with nucleoside reverse transcriptase inhibitor-resistance mutations in reverse transcriptase. There exists an equilibrium between nucleoside reverse transcriptase inhibitor incorporation, nucleoside reverse transcriptase inhibitor excision, and resumption of DNA synthesis and degradation of the RNA template by RNase H activity, leading to dissociation of the template-primer and abrogation of HIV-1 replication
analysis
-
use of 6-phenylpyrrolocytidine as a sensitive fluorescent reporter group being non-disruptive to structure and the enzymatic activity of RNase H. A RNA/DNA hybrid possessing a single 6-phenylpyrrolocytidine insert is an excellent substrate for HIV-1 RT Ribonuclease H and rapidly reports cleavage of the RNA strand with a 14-fold increase in fluorescence intensity. The 6-phenylpyrrolocytidine-based assay for RNase H is superior to the traditional molecular beacon approach in terms of responsiveness, rapidity and ease. The assay is amenable to high-throughput microplate assay format
analysis
-
use of a commercially available computed radiography system for dental radiography to produce images from radiolabeled polyacrylamide gel electrophoresis assays and its application for quantitative analyses of the human immunodeficiency virus type 1 reverse transcriptase polymerase-independent ribonuclease H activity monitored by PAGE analysis. The methodology allows quantifying effectively the RNase H catalyses and the obtained data are in good agreement with previous reference works
drug development
-
RNase H activity is an attractive target for a new class of antiviral drugs
drug development
-
the enzyme is a target for the development of effective dual HIV-1 IN and RNase H inhibitors
drug development
-
the HIV RT-associated RNase H is avaluable drug target
medicine
-
genotypical and statistical analyzes in HIV-1 reverse transcriptase from antiretroviral treatment-naive and antiretroviral treatment-experienced patients. Within the RNase H domain, change K451 is present in 11% of treatment-experienced patients, but not in treatment-naive patients
medicine
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively. A significant decline is observed in the viral loads of patients that are infected with HIV-1 carrying these substitutions and are subsequently treated with triple drug regimens, even in the case where zidovudine is included in such regimens. Generally, such single substitutions at the connection subdomain or RNase H domain have no influence on drug susceptibility in vitro by themselves. Instead, they generally enhance zidovudine resistance in the presence of excision-enhancing mutations. However, N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations
medicine
-
within the RNase domain, mutation K451R is present in viral isolates of 11% of antiviral treatment-experienced patients but remaining 100% conserved among treatment-naive patients
medicine
-
activating the RNase H prematurely inside the virus particles destroys the viral genome and abrogates viral infectivity
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Avian myeloblastosis virus, Human Immunodeficiency Virus, Moloney murine leukemia virus
brenda
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Human Immunodeficiency Virus
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Kharlamova, T.
Synthesis of phenacyl derivatives of frangula-emodin and their HIV-1 RNase H activity
Chem. Nat. Compd.
45
500-502
2009
Human immunodeficiency virus 1
-
brenda
Kirschberg, T.A.; Balakrishnan, M.; Squires, N.H.; Barnes, T.; Brendza, K.M.; Chen, X.; Eisenberg, E.J.; Jin, W.; Kutty, N.; Leavitt, S.; Liclican, A.; Liu, Q.; Liu, X.; Mak, J.; Perry, J.K.; Wang, M.; Watkins, W.J.; Lansdon, E.B.
RNase H active site inhibitors of human immunodeficiency virus type 1 reverse transcriptase: design, biochemical activity, and structural information
J. Med. Chem.
52
5781-5784
2009
Human immunodeficiency virus 1
brenda
Esposito, F.; Fanti, V.; Marzeddu, R.; Randaccio, P.; Tramontano, E.; Zinzula, L.
Validation of a computed radiography device to monitor the HIV-1 RNase H activity
Nucl. Instrum. Meth. Phys. Res. A
607
226-228
2009
Human immunodeficiency virus 1
-
brenda
Wahba, A.S.; Esmaeili, A.; Damha, M.J.; Hudson, R.H.
A single-label phenylpyrrolocytidine provides a molecular beacon-like response reporting HIV-1 RT RNase H activity
Nucleic Acids Res.
38
1048-1056
2010
Human immunodeficiency virus 1
brenda
Himmel, D.M.; Maegley, K.A.; Pauly, T.A.; Bauman, J.D.; Das, K.; Dharia, C.; Clark, A.D.; Ryan, K.; Hickey, M.J.; Love, R.A.; Hughes, S.H.; Bergqvist, S.; Arnold, E.
Structure of HIV-1 reverse transcriptase with the inhibitor beta-thujaplicinol bound at the RNase H active site
Structure
17
1625-1635
2009
Human immunodeficiency virus 1 (P03366)
brenda
Talele, T.; Upadhyay, A.; Pandey, V.
Influence of the RNase H domain of retroviral reverse transcriptases on the metal specificity and substrate selection of their polymerase domains
Virol. J.
6
159-170
2009
Human immunodeficiency virus 1, Moloney murine leukemia virus
brenda
Xu, H.; Quan, Y.; Schader, S.; Oliveira, M.; Bar-Magen, T.; Wainberg, M.
The M230L nonnucleoside reverse transcriptase inhibitor resistance mutation in HIV-1 reverse transcriptase impairs enzymatic function and viral replicative capacity
Antimicrob. Agents Chemother.
54
2401-2408
2010
Human immunodeficiency virus 1, Human immunodeficiency virus 1 HXB2
brenda
Farias, R.V.; Vargas, D.A.; Castillo, A.E.; Valenzuela, B.; Cote, M.L.; Roth, M.J.; Leon, O.
Expression of an Mg2+-dependent HIV-1 RNase H construct for drug screening
Antimicrob. Agents Chemother.
55
4735-4741
2011
Human immunodeficiency virus 1
brenda
Yanagita, H.; Urano, E.; Matsumoto, K.; Ichikawa, R.; Takaesu, Y.; Ogata, M.; Murakami, T.; Wu, H.; Chiba, J.; Komano, J.; Hoshino, T.
Structural and biochemical study on the inhibitory activity of derivatives of 5-nitro-furan-2-carboxylic acid for RNase H function of HIV-1 reverse transcriptase
Bioorg. Med. Chem.
19
816-825
2011
Human immunodeficiency virus 1
brenda
Kumar, A.
Binding of dumbbell oligonucleotides to MoMuLV reverse transcriptase: inhibitory properties of RNase H activity
E-J. Chem.
7
701-708
2010
Moloney murine leukemia virus
-
brenda
Billamboz, M.; Bailly, F.; Lion, C.; Calmels, C.; Andreola, M.L.; Witvrouw, M.; Christ, F.; Debyser, Z.; De Luca, L.; Chimirri, A.; Cotelle, P.
2-hydroxyisoquinoline-1,3(2H,4H)-diones as inhibitors of HIV-1 integrase and reverse transcriptase RNase H domain: influence of the alkylation of position 4
Eur. J. Med. Chem.
46
535-546
2011
Human Immunodeficiency Virus
brenda
Esposito, F.; Kharlamova, T.; Distinto, S.; Zinzula, L.; Cheng, Y.C.; Dutschman, G.; Floris, G.; Markt, P.; Corona, A.; Tramontano, E.
Alizarine derivatives as new dual inhibitors of the HIV-1 reverse transcriptase-associated DNA polymerase and RNase H activities effective also on the RNase H activity of non-nucleoside resistant reverse transcriptases
FEBS J.
278
1444-1457
2011
Human immunodeficiency virus 1
brenda
Biondi, M.J.; Beilhartz, G.L.; McCormick, S.; Goette, M.
N348I in HIV-1 reverse transcriptase can counteract the nevirapine-mediated bias toward RNase H cleavage during plus-strand initiation
J. Biol. Chem.
285
26966-26975
2010
Human immunodeficiency virus 1, Human immunodeficiency virus 1 HXB-2
brenda
Billamboz, M.; Bailly, F.; Lion, C.; Touati, N.; Vezin, H.; Calmels, C.; Andreola, M.; Christ, F.; Debyser, Z.; Cotelle, P.
Magnesium chelating 2-hydroxyisoquinoline-1,3(2H, 4H)-diones, as inhibitors of HIV-1 integrase and/or the HIV-1 reverse transcriptase ribonuclease H domain: Discovery of a novel selective inhibitor of the ribonuclease H function
J. Med. Chem.
54
1812-1824
2011
Moloney murine leukemia virus
brenda
Chung, S.; Himmel, D.; Jiang, J.; Wojtak, K.; Bauman, J.; Rausch, J.; Wilson, J.; Beutler, J.; Thomas, C.; Arnold, E.; Le Grice, S.
Synthesis, activity, and structural analysis of novel alpha-hydroxytropolone inhibitors of human immunodeficiency virus reverse transcriptase-associated ribonuclease H
J. Med. Chem.
54
4462-4473
2011
Human immunodeficiency virus 1
brenda
Su, H.P.; Yan, Y.; Prasad, G.S.; Smith, R.F.; Daniels, C.L.; Abeywickrema, P.D.; Reid, J.C.; Loughran, H.M.; Kornienko, M.; Sharma, S.; Grobler, J.A.; Xu, B.; Sardana, V.; Allison, T.J.; Williams, P.D.; Darke, P.L.; Hazuda, D.J.; Munshi, S.
Structural basis for the inhibition of RNase H activity of HIV-1 reverse transcriptase by RNase H active site-directed inhibitors
J. Virol.
84
7625-7633
2010
Human immunodeficiency virus 1 (P0C6F2), Human immunodeficiency virus 1 HXB2 (P0C6F2)
brenda
Wang, J.; Bambara, R.A.; Demeter, L.M.; Dykes, C.
Reduced fitness in cell culture of HIV-1 with nonnucleoside reverse transcriptase inhibitor-resistant mutations correlates with relative levels of reverse transcriptase content and RNase H activity in virions
J. Virol.
84
9377-9389
2010
Human immunodeficiency virus 1
brenda
Radzvilavicius, T.; Lagunavicius, A.
Selective inactivation of M-MuLV RT RNase H activity by site-directed PEGylation: an improved ability to synthesize long cDNA molecules
New Biotechnol.
29
285-292
2012
Moloney murine leukemia virus
brenda
Lu, M.; Ngo, W.; Mei, Y.; Munshi, V.; Burlein, C.; Loughran, M.; Williams, P.; Hazuda, D.; Miller, M.; Grobler, J.; Diamond, T.; Lai, M.
Purification of untagged HIV-1 reverse transcriptase by affinity chromatography
Protein Expr. Purif.
71
231-239
2010
Human immunodeficiency virus 1
brenda
Delviks-Frankenberry, K.A.; Nikolenko, G.N.; Pathak, V.K.
The connection between HIV drug resistance and RNase H
Viruses
2
1476-1503
2010
Human immunodeficiency virus 1, Human immunodeficiency virus 1 HXB2
brenda
Singh, K.; Marchand, B.; Kirby, K.; Michailidis, E.; Sarafianos, S.
Structural aspects of drug resistance and inhibition of HIV-1 reverse transcriptase
Viruses
2
606-638
2010
Human immunodeficiency virus 1
brenda
Beilhartz, G.; Goette, M.
HIV-1 ribonuclease H: structure, catalytic mechanism and inhibitors
Viruses
2
900-926
2010
Human immunodeficiency virus 1, Human immunodeficiency virus 2
brenda
Sarafianos, S.G.; Das, K.; Tantillo, C.; Clark, A.D., Jr.; Ding, J.; Whitcomb, J.M.; Boyer, P.L.; Hughes, S.H.; Arnold, E.
Crystal structure of HIV-1 reverse transcriptase in complex with a polypurine tract RNA:DNA
EMBO J.
20
1449-1461
2001
Human immunodeficiency virus 1 (P03366)
brenda
Broecker, F.; Andrae, K.; Moelling, K.
Premature activation of the HIV RNase H drives the virus into suicide: a novel microbicide?
AIDS Res. Hum. Retroviruses
28
1397-1403
2012
Human Immunodeficiency Virus
brenda
Corona, A.; Di Leva, F.S.; Thierry, S.; Pescatori, L.; Cuzzucoli Crucitti, G.; Subra, F.; Delelis, O.; Esposito, F.; Rigogliuso, G.; Costi, R.; Cosconati, S.; Novellino, E.; Di Santo, R.; Tramontano, E.
Identification of highly conserved residues involved in inhibition of HIV-1 RNase H function by diketo acid derivatives
Antimicrob. Agents Chemother.
58
6101-6110
2014
Human immunodeficiency virus 1
brenda
Muchiri, J.M.; Li, D.; Dykes, C.; Bambara, R.A.
Efavirenz stimulates HIV-1 reverse transcriptase RNase H activity by a mechanism involving increased substrate binding and secondary cleavage activity
Biochemistry
52
4981-4990
2013
Human immunodeficiency virus 1
brenda
Ilina, T.; Labarge, K.; Sarafianos, S.G.; Ishima, R.; Parniak, M.A.
Inhibitors of HIV-1 reverse transcriptase-associated ribonuclease H activity
Biology
1
521-541
2012
Human immunodeficiency virus 1
brenda
Velthuisen, E.J.; Johns, B.A.; Gerondelis, P.; Chen, Y.; Li, M.; Mou, K.; Zhang, W.; Seal, J.W.; Hightower, K.E.; Miranda, S.R.; Brown, K.; Leesnitzer, L.
Pyridopyrimidinone inhibitors of HIV-1 RNase H
Eur. J. Med. Chem.
83
609-616
2014
Human immunodeficiency virus 1
brenda
Corona, A.; Masaoka, T.; Tocco, G.; Tramontano, E.; Le Grice, S.F.
Active site and allosteric inhibitors of the ribonuclease H activity of HIV reverse transcriptase
Future Med. Chem.
5
2127-2139
2013
Human immunodeficiency virus 1
brenda
Beilhartz, G.L.; Ngure, M.; Johns, B.A.; DeAnda, F.; Gerondelis, P.; Goette, M.
Inhibition of the ribonuclease H activity of HIV-1 reverse transcriptase by GSK5750 correlates with slow enzyme-inhibitor dissociation
J. Biol. Chem.
289
16270-16277
2014
Human immunodeficiency virus 1
brenda
Costi, R.; Metifiot, M.; Chung, S.; Cuzzucoli Crucitti, G.; Maddali, K.; Pescatori, L.; Messore, A.; Madia, V.N.; Pupo, G.; Scipione, L.; Tortorella, S.; Di Leva, F.S.; Cosconati, S.; Marinelli, L.; Novellino, E.; Le Grice, S.F.; Corona, A.; Pommier, Y.; Marchand, C.; Di Santo, R.
Basic quinolinonyl diketo acid derivatives as inhibitors of HIV integrase and their activity against RNase H function of reverse transcriptase
J. Med. Chem.
57
3223-3234
2014
Human immunodeficiency virus 1
brenda
Himmel, D.M.; Myshakina, N.S.; Ilina, T.; Van Ry, A.; Ho, W.C.; Parniak, M.A.; Arnold, E.
Structure of a dihydroxycoumarin active-site inhibitor in complex with the RNase H domain of HIV-1 reverse transcriptase and structure-activity analysis of inhibitor analogs
J. Mol. Biol.
426
2617-2631
2014
Human immunodeficiency virus 1
brenda
Zheng, X.; Mueller, G.A.; DeRose, E.F.; London, R.E.
Metal and ligand binding to the HIV-RNase H active site are remotely monitored by Ile556
Nucleic Acids Res.
40
10543-10553
2012
Human immunodeficiency virus 1
brenda
Alvarez, M.; Barrioluengo, V.; Afonso-Lehmann, R.N.; Menendez-Arias, L.
Altered error specificity of RNase H-deficient HIV-1 reverse transcriptases during DNA-dependent DNA synthesis
Nucleic Acids Res.
41
4601-4612
2013
Human immunodeficiency virus 1
brenda
Zheng, X.; Pedersen, L.C.; Gabel, S.A.; Mueller, G.A.; Cuneo, M.J.; DeRose, E.F.; Krahn, J.M.; London, R.E.
Selective unfolding of one ribonuclease H domain of HIV reverse transcriptase is linked to homodimer formation
Nucleic Acids Res.
42
5361-5377
2014
Human immunodeficiency virus 1
brenda
Das, K.; Martinez, S.E.; Bandwar, R.P.; Arnold, E.
Structures of HIV-1 RT-RNA/DNA ternary complexes with dATP and nevirapine reveal conformational flexibility of RNA/DNA: insights into requirements for RNase H cleavage
Nucleic Acids Res.
42
8125-8137
2014
Human immunodeficiency virus 1 (P03366)
brenda
Corona, A.; Desantis, J.; Massari, S.; Distinto, S.; Masaoka, T.; Sabatini, S.; Esposito, F.; Manfroni, G.; Maccioni, E.; Cecchetti, V.; Pannecouque, C.; Le Grice, S.; Tramontano, E.; Tabarrini, O.
Studies on cycloheptathiophene-3-carboxamide derivatives as allosteric HIV-1 ribonuclease H inhibitors
ChemMedChem
11
1709-1720
2016
Human immunodeficiency virus type 1 group M subtype B (P03366), Human immunodeficiency virus type 1 group M subtype B BH10 (P03366)
brenda
Kankanala, J.; Kirby, K.A.; Huber, A.D.; Casey, M.C.; Wilson, D.J.; Sarafianos, S.G.; Wang, Z.
Design, synthesis and biological evaluations of N-hydroxy thienopyrimidine-2,4-diones as inhibitors of HIV reverse transcriptase-associated RNase H
Eur. J. Med. Chem.
141
149-161
2017
Human immunodeficiency virus 1
brenda
Wang, L.; Tang, J.; Huber, A.D.; Casey, M.C.; Kirby, K.A.; Wilson, D.J.; Kankanala, J.; Xie, J.; Parniak, M.A.; Sarafianos, S.G.; Wang, Z.
6-Arylthio-3-hydroxypyrimidine-2,4-diones potently inhibited HIV reverse transcriptase-associated RNase H with antiviral activity
Eur. J. Med. Chem.
156
652-665
2018
Human immunodeficiency virus 1
brenda
Wang, L.; Tang, J.; Huber, A.D.; Casey, M.C.; Kirby, K.A.; Wilson, D.J.; Kankanala, J.; Parniak, M.A.; Sarafianos, S.G.; Wang, Z.
6-Biphenylmethyl-3-hydroxypyrimidine-2,4-diones potently and selectively inhibited HIV reverse transcriptase-associated RNase H
Eur. J. Med. Chem.
156
680-691
2018
Human immunodeficiency virus 1
brenda
Tang, J.; Do, H.T.; Huber, A.D.; Casey, M.C.; Kirby, K.A.; Wilson, D.J.; Kankanala, J.; Parniak, M.A.; Sarafianos, S.G.; Wang, Z.
Pharmacophore-based design of novel 3-hydroxypyrimidine-2,4-dione subtypes as inhibitors of HIV reverse transcriptase-associated RNase H tolerance of a nonflexible linker
Eur. J. Med. Chem.
166
390-399
2019
Human immunodeficiency virus 1
brenda
Moelling, K.; Broecker, F.; Russo, G.; Sunagawa, S.
RNase H as gene modifier, driver of evolution and antiviral defense
Front. Microbiol.
8
1745
2017
Human immunodeficiency virus 1
brenda
Li, A.; Li, J.; Johnson, K.A.
HIV-1 reverse transcriptase polymerase and RNase H (ribonuclease H) active sites work simultaneously and independently
J. Biol. Chem.
291
26566-26585
2016
Human immunodeficiency virus 1
brenda
Luczkowiak, J.; Matamoros, T.; Menendez-Arias, L.
Template-primer binding affinity and RNase H cleavage specificity contribute to the strand transfer efficiency of HIV-1 reverse transcriptase
J. Biol. Chem.
293
13351-13363
2018
Human immunodeficiency virus type 1 group O subtype B, Human immunodeficiency virus type 1 group M subtype B (P03366), Human immunodeficiency virus type 1 group O subtype B ESP49, Human immunodeficiency virus type 1 group M subtype B BH10 (P03366)
brenda
Tang, J.; Liu, F.; Nagy, E.; Miller, L.; Kirby, K.A.; Wilson, D.J.; Wu, B.; Sarafianos, S.G.; Parniak, M.A.; Wang, Z.
3-Hydroxypyrimidine-2,4-diones as selective active site inhibitors of HIV reverse transcriptase-associated RNase H design, synthesis, and biochemical evaluations
J. Med. Chem.
59
2648-2659
2016
Human immunodeficiency virus 1
brenda
Oda, M.; Xi, Z.; Inaba, S.; Slack, R.; Ishima, R.
Binding thermodynamics of metal ions to HIV-1 ribonuclease H domain
J. Therm. Anal. Calorim.
135
2647-2653
2019
Human immunodeficiency virus type 1 group M subtype B, Human immunodeficiency virus type 1 group M subtype B BH10
brenda
Boso, G.; Oervell, C.; Somia, N.
The nature of the N-terminal amino acid residue of HIV-1 RNase H is critical for the stability of reverse transcriptase in viral particles
J. Virol.
89
1286-1297
2015
Human immunodeficiency virus 1
-
brenda
Boyer, P.L.; Smith, S.J.; Zhao, X.Z.; Das, K.; Gruber, K.; Arnold, E.; Burke, T.R.; Hughes, S.H.
Developing and evaluating inhibitors against the RNase H active site of HIV-1 reverse transcriptase
J. Virol.
92
e02203-17
2018
Human immunodeficiency virus type 1 group M subtype B (P03366), Human immunodeficiency virus type 1 group M subtype B BH10 (P03366)
brenda
Murelli, R.P.; D'Erasmo, M.P.; Hirsch, D.R.; Meck, C.; Masaoka, T.; Wilson, J.A.; Zhang, B.; Pal, R.K.; Gallicchio, E.; Beutler, J.A.; Le Grice, S.F.
Synthetic alpha-hydroxytropolones as inhibitors of HIV reverse transcriptase ribonuclease H activity
MedChemComm
7
1783-1788
2016
Human immunodeficiency virus 1 (P05959), Human immunodeficiency virus 1, Human immunodeficiency virus 1 RF (P05959)
brenda
Permanasari, E.D.; Yasukawa, K.; Kanaya, S.
Enzymatic activities of RNase H domains of HIV-1 reverse transcriptase with substrate binding domains of bacterial RNases H1 and H2
Mol. Biotechnol.
57
526-538
2015
Human immunodeficiency virus 1
brenda
Ngoutane Mfopa, A.; Corona, A.; Eloh, K.; Tramontano, E.; Frau, A.; Boyom, F.F.; Caboni, P.; Tocco, G.
Uvaria angolensis as a promising source of inhibitors of HIV-1 RT-associated RNA-dependent DNA polymerase and RNase H functions
Nat. Prod. Res.
32
640-647
2018
Human immunodeficiency virus 1
brenda
Zheng, X.; Pedersen, L.C.; Gabel, S.A.; Mueller, G.A.; DeRose, E.F.; London, R.E.
Unfolding the HIV-1 reverse transcriptase RNase H domain - how to lose a molecular tug-of-war
Nucleic Acids Res.
44
1776-1788
2016
Human immunodeficiency virus 1 (P04585), Human immunodeficiency virus 1
brenda
Figiel, M.; Krepl, M.; Poznanski, J.; Golab, A.; Sponer, J.; Nowotny, M.
Coordination between the polymerase and RNase H activity of HIV-1 reverse transcriptase
Nucleic Acids Res.
45
3341-3352
2017
Human immunodeficiency virus 1
brenda
Yang, F.; Zheng, G.; Fu, T.; Li, X.; Tu, G.; Li, Y.H.; Yao, X.; Xue, W.; Zhu, F.
Prediction of the binding mode and resistance profile for a dual-target pyrrolyl diketo acid scaffold against HIV-1 integrase and reverse-transcriptase-associated ribonuclease H
Phys. Chem. Chem. Phys.
20
23873-23884
2018
Human immunodeficiency virus 1
brenda
Slack, R.L.; Spiriti, J.; Ahn, J.; Parniak, M.A.; Zuckerman, D.M.; Ishima, R.
Structural integrity of the ribonuclease H domain in HIV-1 reverse transcriptase
Proteins
83
1526-1538
2015
Human immunodeficiency virus 1 (P03366)
brenda
Herzig, E.; Hizi, A.
The importance of glutamine 294 that affects the ribonuclease H activity of the reverse transcriptase of HIV-2 to viral replication
Virology
483
13-20
2015
Human Immunodeficiency Virus
brenda
Ngcapu, S.; Theys, K.; Libin, P.; Marconi, V.C.; Sunpath, H.; Ndungu, T.; Gordon, M.L.
Characterization of nucleoside reverse transcriptase inhibitor-associated mutations in the RNase H region of HIV-1 subtype C infected individuals
Viruses
9
330-339
2017
Human immunodeficiency virus type 1 subtype C
brenda
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