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12 bp RNA/DNA hybrid + H2O
?
18mer DNA-RNA hybrid + H2O
?
-
the RNA is labeled with 6-carboxytetramethyl rhodamine at the 3' end and annealed to complementary nonlabeled DNA
-
-
?
3' end-labeled 41-nt RNA annealed to a 77-nt DNA template
DNA + RNA fragments
-
-
the most RNA fragments are cleaved by a combination of primary, secondary primary, and 5-nt cuts
?
5' end-labeled 41-nt RNA annealed to a 77-nt DNA template
DNA + RNA fragments
-
-
The first product observed is the primary cut. The primary cut occurs faster than the secondary cut
?
5' end-labeled 50-nt RNA annealed to a 77-nt DNA template
DNA + RNA fragments
-
-
The first product observed is the primary cut. The primary cut occurs faster than the secondary cut
?
5' end-labeled RNA
RNA fragments
-
cleavage of 267 nt RNA substrate to produce a 47 nt long product, the second cleavage produces RNA fragments that are 38 nt long
-
?
5' RNA-DNA duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
?
5'-end-labeled RNA
RNA fragments
5'-fluorescein-labeled RNA/DNA hybrid + H2O
?
CGK1 + H2O
?
-
RNase H substrate CGK1 is obtained by annealing 5'-cap-labelled R1 5'-m7Gppp*GmAAUACUCAAGCUAUGCAUC-3' with DNA oligonucleotide D1. The RNA oligonucleotide is blocked at the 5' end by adding a guanosyl-5'-5'-guanosine triphosphate cap structure
-
-
?
DNA-15-nucleotide-RNA hybrid + H2O
?
-
-
-
-
?
DNA-16-nucleotide-RNA hybrid + H2O
?
-
-
-
-
?
DNA-17-nucleotide-RNA hybrid + H2O
?
-
-
-
-
?
DNA-18-nucleotide-RNA hybrid + H2O
?
-
-
-
-
?
DNA-DNA hybrid duplex + H2O
?
DNA-RNA hybrid + H2O
DNA + RNA nucleotides
-
-
-
?
DNA-RNA hybrid + H2O
DNA nucleotides + RNA nucleotides
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
double-stranded RNA + H2O
?
poly(rA)n-poly(dT)ne + H2O
?
-
-
-
-
?
RNA-DNA hybrid + H2O
ribonucleotide 5'-phosphomonoester
-
poly(rGdC)
-
-
?
single-stranded RNA + H2O
?
-
-
-
-
?
additional information
?
-
12 bp RNA/DNA hybrid + H2O
?
-
5'-(6-carboxyfluorescein)-labeled 12 base RNA (5'-cggagaugacgg-3') is hybridized with with a 1.5 M equivalent of the complementary DNA
-
-
?
12 bp RNA/DNA hybrid + H2O
?
-
5'-(6-carboxyfluorescein)-labeled 12 base RNA (5'-cggagaugacgg-3') is hybridized with with a 1.5 M equivalent of the complementary DNA
-
-
?
5'-end-labeled RNA
RNA fragments
-
cleavage of 267nt RNA substrate to produce a 47nt long product, the second cleavage produces RNA fragments that are 38nt long.
-
?
5'-end-labeled RNA
RNA fragments
-
cleavage of 267nt RNA substrate to produce a 47nt long product, the second cleavage produces RNA fragments that are 38nt long.
-
?
5'-end-labeled RNA
RNA fragments
-
cleavage of 267nt RNA substrate to produce a 47nt long product, the second cleavage produces RNA fragments that are 38nt long.
-
?
5'-fluorescein-labeled RNA/DNA hybrid + H2O
?
-
-
-
?
5'-fluorescein-labeled RNA/DNA hybrid + H2O
?
-
-
-
?
DNA-DNA hybrid duplex + H2O
?
-
-
-
?
DNA-DNA hybrid duplex + H2O
?
-
-
-
?
DNA-RNA duplex + H2O
?
-
-
-
-
?
DNA-RNA duplex + H2O
?
-
-
-
?
DNA-RNA duplex + H2O
?
-
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
-
?
DNA-RNA hybrid + H2O
?
Avian sarcoma leukosis virus
-
3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
?
DNA-RNA hybrid + H2O
?
Halalkalibacterium halodurans
-
-
-
?
DNA-RNA hybrid + H2O
?
Halalkalibacterium halodurans DSM 18197
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
-
?
DNA-RNA hybrid + H2O
?
-
cleavage site specificity at -17, -12 and -8 from the 5' end positions of the RNA strand in 3' to 5' direction, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
-
?
DNA-RNA hybrid + H2O
?
-
formed by commercial R1 RNA and D1 DNA oligonucleotides, the His-tag affects the cleavage pattern of recombinant RNaseh domain
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
?
DNA-RNA hybrid + H2O
?
-
RNA-DNA hybrid structures: thermodynamics of recognition and impact on reverse viral replication
-
-
?
DNA-RNA hybrid + H2O
?
-
cleavage pattern to 3' end of wild-type and mutant reverse transcriptase/RNase H, HIV-1 reverse transcriptase employs the DNA 3' end-directed primary/secondary RNase H cleavage mechanism during synthesis and strand transfer
-
-
?
DNA-RNA hybrid + H2O
?
-
cleavage site recognition and specificity, mechanism, in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
fluorescent-labeled RNA-DNA duplex of 15, 16, 17, or 18 nucleotide-RNA and in each case 18 nucleotide-DNA, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
RNA-DNA hybrid structures: thermodynamics of recognition and impact on reverse transcriptase-mediated RNase H activity, cleavage sites
-
-
?
DNA-RNA hybrid + H2O
?
-
substrate preparation, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
recessed 5'-end RNA substrates CGK1 annealed from RNA R1, i.e. 5'-GAAUACUCAAGCUAUGCAUC-3', and DNA D1, i.e. 5'-GATGCATAGCTTGAGTATTCTATAGTGAGTCGTATTAA-3', substrate labeling with fluorescein at the 3' end and with dabcyl at the 5' end
-
-
?
DNA-RNA hybrid + H2O
?
-
RNase H specifically hydrolyzes the RNA strand of a RNA/DNA heteroduplex, the ribonuclease H hydrolytic activity is part of the reverse transcriptase
-
-
?
DNA-RNA hybrid + H2O
?
-
the RNaseH activity of HIV-1 reverse transcriptase cleaves the viral genome concomitant with minus strand synthesis during pausing of the reverse transcriptase activity, RNase H cleavage on a hairpin containing RNA template system, overview, pause-related 3' end-directed secondary cuts decreased primer extendibility, relationship between cleavage of the RNA template and extension of a DNA primer, mechanism, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
RNase H cleaves precisely one nucleotide from the tRNA/DNA junction, leaving a ribo-A on the 3' end of the viral minus-strand DNA
-
-
?
DNA-RNA hybrid + H2O
?
-
a Cy3-Tr35/Pd22 RNA-DNA hybrid is cut at approximately 18 base pair upstream from the 3' primer end
-
-
?
DNA-RNA hybrid + H2O
?
-
RNase H specifically hydrolyzes the RNA strand of a RNA/DNA heteroduplex, the ribonuclease H hydrolytic activity is part of the reverse transcriptase
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
?
DNA-RNA hybrid + H2O
?
-
cleavage site recognition and specificity, mechanism, in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
in vitro synthesis of substrates, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
sequence preference for internal cleavage. 3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
DNA-RNA hybrid + H2O
?
-
a Cy3-Tr35/Pd22 RNA-DNA hybrid is cut at approximately 19 base pair upstream from the 3' primer end
-
-
?
DNA-RNA hybrid + H2O
?
-
the RNase H primer grip is important for viral replication and replication fidelity, mutational analysis, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
the RNase H catalytic efficiency and specificity is influences by the RNase H primer grip contacting the DNA primer strand and positioning the template strand near the RNase H active site, overview
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
?
DNA-RNA hybrid + H2O
?
-
-
-
?
DNA-RNA hybrid + H2O
?
a Cy3-Tr35/Pd22 RNA-DNA hybrid is cut at approximately 19 base pair upstream from the 3' primer end
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
limited hydrolysis of ribopolymers when complementary DNA strand is missing or in presence of a complementary RNA strand
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
poor substrate: poly(rG)-poly(dC)
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
poor substrate: poly(rG)-poly(dC)
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
Herpes simplex virus
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
Herpes simplex virus HSV
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
only cleavage of RNA from a RNA-DNA-duplex
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
the RNase H domain of reverse transcriptase catalyses the cleavage of the RNA within DNA-RNA hybrids, both in a polymerase-dependent or independent fashion. Polymerase-dependent: Cleavage occurring at a distance of 18-20 nucleotides behind DNA polymerization. Polymerase-independent: cleavage of the viral RNA for the initiation of second DNA strand synthesis and for removal of the primer tRNA.
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
4-30 nucleotides in length
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
4-30 nucleotides in length
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
Rauscher leukemia virus
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
Rauscher leukemia virus
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
RD-feline leukemia virus
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA-RNA hybrid duplex + H2O
oligonucleotides terminated with 5'-phosphate and 3'-hydroxyl moiety
-
-
-
?
DNA/DNA + H2O
?
RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal, 3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview, cleavage site selection modelling, RNase H activities of human retroviral reverse transcriptases preferentially cleave between two ribonucleotide residues in an RNA chain, and between the penultimate and last ribonucleotide of an extended RNA primer rather than precisely at the RNA-DNA junction, overview
-
-
?
DNA/DNA + H2O
?
RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal, 3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview, RNase H activities of murine retroviral reverse transcriptases preferentially cleave between two ribonucleotide residues in an RNA chain, and between the penultimate and last ribonucleotide of an extended RNA primer rather than precisely at the RNA-DNA junction
-
-
?
double-stranded RNA + H2O
?
substrate of RNase H1
-
-
?
double-stranded RNA + H2O
?
substrate of RNase H1
-
-
?
HTS-1 RNA-DNA + H2O
?
-
-
-
-
?
HTS-1 RNA-DNA + H2O
?
-
-
-
-
?
HTS-1 RNA-DNA + H2O
?
-
-
-
?
HTS-2 RNA-DNA + H2O
?
-
-
-
-
?
HTS-2 RNA-DNA + H2O
?
-
-
-
-
?
HTS-2 RNA-DNA + H2O
?
-
-
-
?
poly(rA)n-poly(dT)n
?
-
-
-
?
poly(rA)n-poly(dT)n
?
-
-
-
?
poly(rA)n-poly(dT)n
?
-
-
-
?
poly(rA)n-poly(dT)n
?
-
-
-
?
poly(rA)n-poly(dT)n
?
-
-
-
?
RNA/DNA hybrid + H2O
?
-
Cy3-labeled 43-nt RNA strand (5'-GGUCUCUCUGGUUAGACCAGAUCUGAGCCUGGGAGCUCUCUGG-3') annealed to a 53-nt DNA strand (5'-CCCTAGTTAGCCAGAGAGCTCCCAGGCTCAGATCTGGTCTAACCAGAGAGACC-3')
-
-
?
RNA/DNA hybrid + H2O
?
i.e. 18 nucleotide 3'-fluorescein-labeled RNA annealed to a complementary 18 nucleotide 5'-dabsyl-modified DNA, RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal, 3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview, substrate binding structure, overview
-
-
?
RNA/DNA hybrid + H2O
?
-
Cy3-labeled 43-nt RNA strand (5'-GGUCUCUCUGGUUAGACCAGAUCUGAGCCUGGGAGCUCUCUGG-3') annealed to a 53-nt DNA strand (5'-CCCTAGTTAGCCAGAGAGCTCCCAGGCTCAGATCTGGTCTAACCAGAGAGACC-3')
-
-
?
RNA/DNA hybrid + H2O
?
-
-
-
-
?
RNA/DNA hybrid + H2O
?
RNase H catalysis by the retroviral enzyme appears to involve a two-metal ion mechanism. Unlike cellular RNases H, the retroviral RNase H displays three different modes of cleavage: internal,3'-end-DNA-directed, and 5'-end-RNA-directed, all three modes of cleavage appear to have essential roles in reverse transcription, overview
-
-
?
RNA/DNA hybrid + H2O
?
-
secondary structure and substrate binding, overview
-
-
?
RNA/DNA hybrid + H2O
?
-
Cy3-labeled 43-nt RNA strand (5'-GGUCUCUCUGGUUAGACCAGAUCUGAGCCUGGGAGCUCUCUGG-3') annealed to a 53-nt DNA strand (5'-CCCTAGTTAGCCAGAGAGCTCCCAGGCTCAGATCTGGTCTAACCAGAGAGACC-3')
-
-
?
additional information
?
-
-
not: ds DNA
-
-
?
additional information
?
-
-
not: poly(rU)-poly(dA), DNA-RNA hybrids without a free RNA-end
-
-
?
additional information
?
-
-
RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
-
-
?
additional information
?
-
Avian sarcoma leukosis virus
-
3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
additional information
?
-
-
heteroduplexes with 5'-O-methylphosphonate units in the antisense strand exhibit a significant increase in RNase H cleavage activity by up to 3fold in comparison with the natural heteroduplex
-
-
?
additional information
?
-
-
cleavage of RNA:DNA hybrid substrate
-
-
?
additional information
?
-
-
the 3'-5' exoribonuclease activity of the HBV RNaseH is determined. The enzyme also shows endolytic activity (EC 3.1.26.4) in DNA oligonucleotide (ODN)-directed RNA cleavage assays are conducted. Substrate specificity of the HBV RNaseH, overview
-
-
?
additional information
?
-
Herpes simplex virus
-
not: ss DNA
-
-
?
additional information
?
-
Herpes simplex virus
-
not: ss RNA
-
-
?
additional information
?
-
Herpes simplex virus
-
not: ds RNA
-
-
?
additional information
?
-
Herpes simplex virus
-
not: ds DNA
-
-
?
additional information
?
-
Herpes simplex virus HSV
-
not: ss DNA
-
-
?
additional information
?
-
Herpes simplex virus HSV
-
not: ss RNA
-
-
?
additional information
?
-
Herpes simplex virus HSV
-
not: ds RNA
-
-
?
additional information
?
-
Herpes simplex virus HSV
-
not: ds DNA
-
-
?
additional information
?
-
-
Herpes simplex virus 1 DNA polymerase shows also RNase H activity and acts in a 3'-to-5' direction, the activity is dependent on the 3'-to-5' exonuclease active site. No RNase H activity of HSV-1 DNA polymerase on RNA-DNA hybrids with 5' RNA termini
-
-
?
additional information
?
-
-
in vitro assays are performed utilizing purified wild-type Pol and the D368A exonuclease-deficient mutant, testing the ability of these enzymes to extend a fluorescently labeled DNA hairpin primer-template and degrade dsDNA and RNA-DNA hybrid hairpin substrates over time, assay of RNase H activity using differentially end-labeled templates with 5' or 3' RNA termini, e.g. 6-FAM-labeled hairpin RNA-DNA substrate with a 3' RNA terminus. Wild-type HSV Pol exhibits readily detectable RNase H activity on this substrate in the 3'-to-5' direction, while the mutant is inactive. Neither wild-type nor D368A Pol exhibits detectable RNase H activity on a substrate with a 5' RNA terminus
-
-
?
additional information
?
-
-
the enzyme is part of the viral reverse transcriptase, RNase H substrate synthesis by the enzyme's RT activity
-
-
?
additional information
?
-
-
the isolated RNase H domain, part of reverse transcriptase, is catalytically active
-
-
?
additional information
?
-
-
in Mg2+, hydrolysis of poly(rAdT) appears to be solely endonucleolytic. In Mn2+, hydrolysis of poly(rAdT) is both endonucleolytic and exonucleolytic. With poly(rGdC) as substrate, hydrolysis is both endonucleolytic and exonucleolytic in either Mg2+ or Mn2+
-
-
?
additional information
?
-
-
the enzyme is essential for retroviral replication
-
-
?
additional information
?
-
-
the enzyme is essential to complete retroviral replication
-
-
?
additional information
?
-
-
the enzyme plays a key role in viral proliferation
-
-
?
additional information
?
-
-
the enzyme is part of the viral reverse transcriptase
-
-
?
additional information
?
-
-
the enzyme is part of the viral reverse transcriptase residing on distinct domains of the enzyme with the DNA polymerase activity
-
-
?
additional information
?
-
-
the enzyme is part of the viral reverse transcriptase, the isolated RNase H domain is inactive at low pH
-
-
?
additional information
?
-
-
the enzyme recognizes 3' ends of DNA and 5' ends of RNA for cleavage, the enzyme cleaves downstream of a nick, recognition of internal cleavage sites, influence of 5' end position of upstream RNA on cleavage of downstream RNA, overview
-
-
?
additional information
?
-
-
the reverse transcriptase possesses different activity domains and shows RNase H, integrase, and DNA polymerase activities
-
-
?
additional information
?
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
-
the RNase H function of HIV RT is required to effectively incorporate viral genetic information into the host cell genome
-
-
?
additional information
?
-
-
HIV reverse transcriptase, HIV-RT, contains two distinct protein domains catalyzing DNA polymerase and RNase H activities
-
-
?
additional information
?
-
the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, the isolated RNase H domain of HIV-1 is inactive, but nuclease activity is reconstituted by introducing the p51 subunit, by adding the thumb and connection subdomains, or by various N-terminal fusions on the RNase H domain, cleavage specificity of RNase H, overview
-
-
?
additional information
?
-
-
the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, the isolated RNase H domain of HIV-1 is inactive, but nuclease activity is reconstituted by introducing the p51 subunit, by adding the thumb and connection subdomains, or by various N-terminal fusions on the RNase H domain, cleavage specificity of RNase H, overview
-
-
?
additional information
?
-
the reverse transcriptase has two enzyme activities, one of which is the RNase H, enzyme-ligand interactions, overview
-
-
?
additional information
?
-
-
the reverse transcriptase has two enzyme activities, one of which is the RNase H, enzyme-ligand interactions, overview
-
-
?
additional information
?
-
3 distinct cleavage modes have been described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
additional information
?
-
-
cleaves RNA only if the RNA is part of an RNA/DNA duplex
-
-
?
additional information
?
-
-
during minus-strand DNA synthesis, RNase H degrades viral RNA sequences, generating potential plus-strand DNA primers
-
-
?
additional information
?
-
-
retroviral RNase H is essential for viral replication
-
-
?
additional information
?
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
-
RNA cleavage in the RNA-DNA hybrids by the various mutant HIV-2 reverse transcriptases, in comparison to the wild-type HIV-1 and HIV-2 reverse transcriptases
-
-
?
additional information
?
-
-
RNAse H is implicated in catalysing the degradation of the RNA strand during conversion of the viral genome into double-stranded DNA
-
-
?
additional information
?
-
the reverse transcriptase-associated RNase H activity introduces nicks into the RNA strand that yield low molecular weight bands in urea-containing denaturing PAGE, which are visualized by fluorescence scanning. The p51 preparation does not yield detectable low-molecular-weight bands, indicating that the reverse transcriptase preparation is not contaminated with RNase activities of bacterial origin
-
-
?
additional information
?
-
-
using specially designed RNA and DNA transfer substrates in vitro to determine how individual invasion sites contribute to the invasion-mediated mechanism of strand transfer, with specific focus on the limits and influences on the apparently crucial intermediate step of hybrid propagation. Investigation of the roles of the RNase H activities of reverse transcriptase and the strand-exchange properties of nucleocapsid protein (NC)
-
-
?
additional information
?
-
-
both of the enzymatic functions of reverse transcriptase, the DNA polymerase and RNase H, are essential for copying the single-stranded RNA genome found in virions into the double-stranded DNA that is inserted into the host genome by IN
-
-
?
additional information
?
-
-
RNaseH assays are performed using an 18-nucleotide 3'-fluorescein-labeled RNA annealed to a complementary 18-nucleotide 5'-dabcyl-conjugated DNA. The increase in fluorescence as a result of RNase H hydrolysis is monitored with a Spectramax Gemini EM fluorescence spectrometer
-
-
?
additional information
?
-
-
the RNase H function of HIV RT is required to effectively incorporate viral genetic information into the host cell genome
-
-
?
additional information
?
-
-
RNA cleavage in the RNA-DNA hybrids by the various mutant HIV-2 reverse transcriptases, in comparison to the wild-type HIV-1 and HIV-2 reverse transcriptases
-
-
?
additional information
?
-
-
not: ss DNA
-
-
?
additional information
?
-
-
not: ss RNA
-
-
?
additional information
?
-
-
not: ds DNA
-
-
?
additional information
?
-
-
the enzyme is essential for retroviral replication
-
-
?
additional information
?
-
-
the enzyme is essential to complete retroviral replication
-
-
?
additional information
?
-
-
the enzyme recognizes 3' ends of DNA and 5' ends of RNA for cleavage, the enzyme cleaves downstream of a nick, recognition of internal cleavage sites, influence of 5' end position of upstream RNA on cleavage of downstream RNA, overview
-
-
?
additional information
?
-
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, i.e. NRTIs
-
-
?
additional information
?
-
-
the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, overview, cleavage site selection modelling, overview, the isolated MoMLV RNase H domain retains enzymatic activity, but is unable to carry out specific cleavages such as removal of the tRNA or PPT primers in vitro, cleavage specificity of RNase H, overview
-
-
?
additional information
?
-
the polymerization-dependent RNase H activity is insufficient to completely degrade the genomic template during minus-strand synthesis, pausing by reverse transcriptase during transcription promotes RNase H cleavages and facilitates strand transfers, overview, cleavage site selection modelling, overview, the isolated MoMLV RNase H domain retains enzymatic activity, but is unable to carry out specific cleavages such as removal of the tRNA or PPT primers in vitro, cleavage specificity of RNase H, overview
-
-
?
additional information
?
-
-
3 distinct cleavage modes are described for retroviral RNases H that are referred to as internal, DNA 3'-end-directed and RNA 5'-end-directed cleavages
-
-
?
additional information
?
-
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
retroviral RNases H display three different modes of cleavage: internal, DNA 3' end-directed, and RNA 5' end-directed
-
-
?
additional information
?
-
RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
-
-
?
additional information
?
-
-
RNase H activity is determined by measuring the [3H]oligo(rA) released from [3H]poly(rA)*p(dT)45
-
-
?
additional information
?
-
-
not: ss DNA
-
-
?
additional information
?
-
-
not: ss RNA
-
-
?
additional information
?
-
-
not: ds DNA
-
-
?
additional information
?
-
LC11-RNase H1 does not exhibit double strand RNase activity
-
-
?
additional information
?
-
-
LC11-RNase H1 does not exhibit double strand RNase activity
-
-
?
additional information
?
-
LC11-RNase H1 does not exhibit double strand RNase activity
-
-
?
additional information
?
-
Tequatrovirus T4
phage T4 RNase H shows 5'-3'exonuclease (EC 3.1.13.2) and flap endonuclease (EC 3.1.99.) activities on dsDNA
-
-
?
additional information
?
-
Tequatrovirus T4
synthetic DNA substrates are used
-
-
?
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(10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-1,9,14-trioxo-6,7,9,14-tetrahydrotetraceno[1,2-g]phthalazin-2(1H)-yl)acetic acid
-
-
(2E)-2-[(4-chlorophenyl)hydrazono]propanoic acid
-
4-chlorophenylhydrazone of pyruvic acid, shows poor inhibitory activity against HIV-1 RNase H because of the storage of one or two carboxylic acid moieties
(2Z)-2-hydroxy-4-oxopent-2-enoic acid
-
-
(E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
i.e. DHBNH, highly specific, noncompetitive, binding site analysis, the inhibitor binds near both the polymerase active site and the non-nucleoside reverse transcriptase inhibitor binding pocket, it specifically interacts with conserved residues Asp186 and Trp229 and has substantial interactions with the backbones of several less well-conserved residues, overview, substituted inhibitor derivatives, that interact with the nucleoside analog RT inhibitor-binding pocket, inhibit both the polymerase and RNH activities of reverse transcriptase, DHBNH interacts with other residues, including Val108, Leu187, Tyr188, Lys223, Phe227, and Leu228
1,3,4,5-tetragalloylapiitol
1,6-dihydroxy-4-methyl-5-(N-phenoxyethanimidoyl)pyridin-2(1H)-one
-
-
1,6-dihydroxy-4-methyl-5-[N-[(4-methylphenyl)methoxy]ethanimidoyl]pyridin-2(1H)-one
-
-
1,6-dihydroxy-5-[N-[(2-methoxyphenyl)methoxy]ethanimidoyl]-4-methylpyridin-2(1H)-one
-
-
1,6-dihydroxy-5-[N-[(4-methoxyphenyl)methoxy]ethanimidoyl]-4-methylpyridin-2(1H)-one
-
-
1,9,11,14-tetrahydroxy-3-[(E)-{[(2-hydroxyphenyl)carbonyl]hydrazono}methyl]-7-methoxy-10-methyl-8,13-dioxo-5,6,8,13-tetrahydrobenzo[a]tetracene-2-carboxylic acid
-
-
1,9,11,14-tetrahydroxy-7-methoxy-10-methyl-3-[(E)-{[(4-methylphenyl)sulfonyl]hydrazono}methyl]-8,13-dioxo-5,6,8,13-tetrahydrobenzo[a]tetracene-2-carboxylic acid
-
-
1,9,11,14-tetrahydroxy-7-methoxy-10-methyl-3-{(E)-[(4-nitrophenyl)hydrazono]methyl}-8,13-dioxo-5,6,8,13-tetrahydrobenzo[a]tetracene-2-carboxylic acid
-
-
1,9,11,14-tetrahydroxy-7-methoxy-10-methyl-8,13-dioxo-3-(1,2,3,4-tetrahydroquinazolin-2-yl)-5,6,8,13-tetrahydrobenzo[a]tetracene-2-carboxylic acid
-
-
1,9,11,14-tetrahydroxy-7-methoxy-10-methyl-8,13-dioxo-3-[(E)-(tetracyclo[5.3.1.03,9.05,9]undec-1-ylimino)methyl]-5,6,8,13-tetrahydrobenzo[a]tetracene-2-carboxylic acid
-
-
1,9,11,14-tetrahydroxy-7-methoxy-10-methyl-8,13-dioxo-3-{(E)-[(phenylcarbonyl)hydrazono]methyl}-5,6,8,13-tetrahydrobenzo[a]tetracene-2-carboxylic acid
-
-
1,9,11,14-tetrahydroxy-7-methoxy-10-methyl-8,13-dioxo-5,6,8,13-tetrahydrobenzo[a]tetracene-2,3-dicarboxylic acid
-
-
1,9,11,14-tetrahydroxy-7-methoxy-3-[(E)-(methoxyimino)methyl]-10-methyl-8,13-dioxo-5,6,8,13-tetrahydrobenzo[a]tetracene-2-carboxylic acid
-
-
1-(4-chlorophenyl)-2-(1-methylethylidene)hydrazine
-
4-chlorophenylhydrazone of acetone, shows poor inhibitory activity against HIV-1 RNase H because of the storage of one or two carboxylic acid moieties
10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-1,9,14-trioxo-6,7,9,14-tetrahydrotetraceno[1,2-g]phthalazine-2(1H)-carboximidamide
-
-
10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-2,3,4,4a,6,7-hexahydropyrimido[2,1-a]tetraceno[1,2-f]isoindole-9,14,17(1H)-trione
-
-
10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-2-phenyl-6,7-dihydrotetraceno[1,2-g]phthalazine-1,9,14(2H)-trione
-
-
10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-2-propyl-6,7-dihydrotetraceno[1,2-g]phthalazine-1,9,14(2H)-trione
-
-
10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-6,7-dihydrotetraceno[1,2-g]phthalazine-1,9,14(2H)-trione
-
-
12,14,17,18-tetrahydroxy-10-methoxy-13-methyl-6,6a,8,9-tetrahydrotetraceno[1',2':5,6]isoindolo[2,1-a]quinazoline-11,16,19(5H)-trione
-
-
15,16-dihydroxy-8-methoxy-12-[(methoxycarbonyl)oxy]-11-methyl-1,9,14-trioxo-2-propyl-1,2,6,7,9,14-hexahydrotetraceno[1,2-g]phthalazin-10-yl acetate
-
-
2'-deoxy-4'-ethyl-3,4-dihydrothymidine
-
-
2'-deoxy-4'-ethynyl-2-fluoroadenosine
-
-
2'-deoxy-4'-methyl-3,4-dihydrothymidine
-
-
2,4,17,18-tetrahydroxy-6-methoxy-3-methyl-7,9b-dihydrotetraceno[1',2':5,6]isoindolo[1,2-b][1,3]benzothiazole-5,16,19(8H)-trione
-
-
2,7-dihydroxy-4-isopropylcyclohepta-2,4,6-trienone
2,7-dihydroxyisoquinoline-1,3(2H,4H)-dione
-
-
2-(10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-1,9,14-trioxo-6,7,9,14-tetrahydrotetraceno[1,2-g]phthalazin-2(1H)-yl)ethyl acetate
-
-
2-(4-fluorophenyl)-N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)acetamide
-
-
2-amino-12-ethyl-7-(1-hydroxypropyl)-8-methylindolizino[1,2-b]quinolin-9(11H)-one
-
mappicine analogue
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
2-aminoisoquinoline-1,3(2H,4H)-dione
-
-
2-chloro-7-(2-cyclohexyl-1-hydroxyethyl)-8-methyl-12-propylindolizino[1,2-b]quinolin-9(11H)-one
-
mappicine analogue
2-hydroxy-4H-isoquinoline-1,3-dione
-
specific inhibition of isolated RNase H domain and of the full length reverse transcriptase, IC50 value for the isolated RNase H domain is 0.00043 mM
2-hydroxy-6-pentadecylbenzoic acid
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
2-hydroxy-6-[(8Z)-pentadec-8-en-1-yl]benzoic acid
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
2-hydroxy-7-(4-hydroxyphenyl)isoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxy-7-iodoisoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxy-7-nitroisoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxy-7-phenylisoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxy-7-[4-(trifluoromethyl)phenyl]isoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxyisoquinoline-1,3(2H,4H)-dione
2-methoxyisoquinoline-1,3(2H,4H)-dione
-
-
2-[(10Z)-heptadec-10-en-1-yl]-6-hydroxybenzoic acid
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
3'-azido-3'-deoxythymidine
3'-azido-3'-deoxythymidine 5'-(dihydrogen phosphate)
-
inhibits RNase H in vitro, but is not selectively active against RNase H. Does not exhibit inhibitory activity against RNase H in the HIV-1 replication process
3'-azido-3'-deoxythymidine 5'-phosphate
-
more sensitive to inhibition with poly(rGdC) than with poly(rAdT) as substrate. Competitive inhibitor with respect to substrate in Mn2+, uncompetitive inhibitor in Mg2+
3,4-dihydroxy-N'-[(E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
-
specific inhibitor of reverse transcriptase RNase H activity (IC50 value is about 0.5 microM) and has relatively limited activity against the DNA polymerase activity of reverse transcriptase. It is non-cytotoxic and inhibits the replication of a variety of drug-resistant HIV-1 reverse transcriptase mutants
3,7-dihydroxytropolones
-
-
3,9,11,14,15-pentahydroxy-7-methoxy-N,N,N,10-tetramethyl-1,8,13-trioxo-1,3,5,6,8,13-hexahydro-2H-tetraceno[1,2-f]isoindol-2-aminium
-
-
3-pentadecylphenol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
3-tridecylphenol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
3-[(10Z)-heptadec-10-en-1-yl]phenol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
3-[(8Z)-pentadec-8-en-1-yl]phenol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
3-[(E)-(carbamimidoylhydrazono)methyl]-1,9,11,14-tetrahydroxy-7-methoxy-10-methyl-8,13-dioxo-5,6,8,13-tetrahydrobenzo[a]tetracene-2-carboxylic acid
-
-
3-[(E)-(tert-butylhydrazono)methyl]-1,9,11,14-tetrahydroxy-7-methoxy-10-methyl-8,13-dioxo-5,6,8,13-tetrahydrobenzo[a]tetracene-2-carboxylic acid
-
-
3-[(E)-[4-[(E)-2-carboxyethenyl]phenyl]diazenyl]-7-[([6-[(E)-[4-[(E)-2-carboxyethenyl]phenyl]diazenyl]-5-hydroxy-7-sulfonatonaphthalen-2-yl]carbamoyl)amino]-4-hydroxynaphthalene-2-sulfonate
-
-
4'-chloro-N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]biphenyl-4-carbohydrazide
-
4-(1-chloro-1,1-difluoromethyl)-4-(2-phenylethynyl)-6-chloro-2H-3,1-benzoxazin-2-one
-
i.e. NNRTI, an efavirenz analogue, IC50 values for wild-type enzyme are 0.000002-0.000005 mM with substrates DNA-17-nucleotide-RNA hybrid or DNA-18-nucleotide-RNA hybrid, and 0.001 mm for substrate DNA-15-nucleotide-RNA hybrid or DNA-16-nucleotide-RNA hybrid, effect on mutant enzymes, overview
4-(10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-1,9,14-trioxo-6,7,9,14-tetrahydrotetraceno[1,2-g]phthalazin-2(1H)-yl)benzoic acid
-
-
4-(5-benzamidothiophen-2-yl)-2,4-dioxobutanoic acid
-
IC50 values determined by two different assay variants
4-(dimethylamino)-N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
-
4-methoxy-N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
-
4-tert-butyl-N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
-
4-[(4'-aminomethyl-1,1'-biphenyl)methyl]-1-hydroxy-1,8-naphthyridin-2-one
4-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxobutanoic acid
-
L-731,988
4-[5-(benzoylamino)thien-2-yl]-2,4-dioxobutanoic acid
-
a diketo acid RNase H inhibitor, IC50 values for wild-type and mutant enzymes are 0.002-0.0035 mM with all substrates, effect on mutant enzymes, overview
4-[5-(benzoylamino)tien-2-yl]-2,4-dioxobutanoic acid
-
diketo acid derivative
4-[5-benzoylamino) thien-2-yl]-2,4-dioxobutanoic acid
-
inhibits RNase H by binding to the active site and chelating the essential Mg2+
5-chloro-2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
-
5-chloro-2-hydroxyisoquinoline-1,3(2H,4H-dione)
-
is not candidate therapeutics because it is cytotoxic
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydro-furan-2-yl-methyl)-carbamoyl] methyl ester
20-25 microM effectively inhibited HIV-1 replication
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl] methyl ester
-
derivative of 5-nitrofuran-2-carboxylic acid carbamoyl methyl ester. 20-25 microM effectively inhibited HIV-1 replication
5-tridecylbenzene-1,3-diol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
5-[(8Z)-pentadec-8-en-1-yl]benzene-1,3-diol
-
isolated from the CH2Cl2 extracts of the sacrotestas of Ginkgo biloba
5-[N-(4-fluorophenoxy)ethanimidoyl]-1,6-dihydroxy-4-methylpyridin-2(1H)-one
-
-
5-[N-(benzyloxy)ethanimidoyl]-1,6-dihydroxy-4-methylpyridin-2(1H)-one
-
-
5-[N-[(2-aminophenyl)methoxy]ethanimidoyl]-1,6-dihydroxy-4-methylpyridin-2(1H)-one
-
-
5-[N-[(2-fluorophenyl)methoxy]ethanimidoyl]-1,6-dihydroxy-4-methylpyridin-2(1H)-one
-
-
5-[N-[(4-fluorophenyl)methoxy]ethanimidoyl]-1,6-dihydroxy-4-methylpyridin-2(1H)-one
-
-
7-(3,4-dihydroxyphenyl)-2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
-
7-(4-fluorophenyl)-2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
-
7-(furan-2-yl)-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
7-benzamido-N,N-diethyl-2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinoline-4-carboxamide
-
-
7-bromo-2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
-
7-chloro-2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
-
8-methoxy-11-methyl-1,9,14-trioxo-2-phenyl-1,2,6,7,9,14-hexahydrotetraceno[1,2-g]phthalazine-10,12,15,16-tetrayl tetraacetate
-
-
8-methoxy-11-methyl-1,9,14-trioxo-2-propyl-1,2,6,7,9,14-hexahydrotetraceno[1,2-g]phthalazine-10,12,15,16-tetrayl tetraacetate
-
-
9,11,14,15-tetrahydroxy-7-methoxy-10-methyl-8,13,16-trioxo-1,2,3a,5,6,8,13,16-octahydrotetraceno[1,2-f][1,3]thiazolo[2,3-a]isoindole-1-carboxylic acid
-
-
acetylshikonin
-
inhibits weakly
BPH218
-
potent inhibitor of ATP-mediated phosphorolytic excision of 3'-terminal zidovudine 5'-monophosphate (in vitro IC50 value is about 2 microM)
capravirine
-
a nonnucleoside reverse transcriptase inhibitor, inhibits the 5' to 3' directed RNase H activity
Cl-
-
the wild-type and mutant enzymes bind the substrate considerably less tightly at higher concentrations
deoxyshikonin
-
inhibits weakly
Dextran sulfate
-
inhibits RNase H in vitro, but is not selectively active against RNase H. Does not exhibit inhibitory activity against RNase H in the HIV-1 replication process
-
dihydroxy benzoyl naphthyl hydrazone
-
also have inhibitory activity against drug-resistant HIV-1 RT variants Y181C RT and Y188l RT. NNRTI Efavirenz shows no inhibitory effect under the same conditions
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
-
RDS 1643, good selectivity and high potency in enzyme and cell culture assay
ethyl 3-(10,12,15,16-tetrahydroxy-8-methoxy-11-methyl-1,9,14-trioxo-6,7,9,14-tetrahydrotetraceno[1,2-g]phthalazin-2(1H)-yl)propanoate
-
-
ethyl 6-hydroxy-2-methoxy-5,7-dioxo-5,6,7,8-tetrahydro-1,6-naphthyridine-8-carboxylate
-
-
GW8248
-
a nonnucleoside reverse transcriptase inhibitor, inhibits the 5' to 3' directed RNase H activity
heparin
-
inhibits RNase H in vitro, but is not selectively active against RNase H. Does not exhibit inhibitory activity against RNase H in the HIV-1 replication process
hyemaloside A
-
isolated from the evergreen tree Eugenia hyemalis
hyemaloside B
-
isolated from the evergreen tree Eugenia hyemalis
hyemaloside C
-
isolated from the evergreen tree Eugenia hyemalis
juglone
-
poor inhibitory activity
madurahydroxylactone
-
a secondary metabolite from the soil bacterium Nonomuraea rubra, belonging to the family of benzo[a]naphthacenequinone antibiotics
methyl 10,15,16-trihydroxy-8-methoxy-11-methyl-1,9,14-trioxo-2-phenyl-1,2,6,7,9,14-hexahydrotetraceno[1,2-g]phthalazin-12-yl carbonate
-
-
methyl 7-benzamido-2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinoline-4-carboxylate
-
-
Mg2+
-
inhibitory at concentrations greater than 10 mM
N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]-4-methylbenzohydrazide
-
N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]-4-phenoxybenzohydrazide
-
N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
-
N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]biphenyl-4-carbohydrazide
-
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)-2-phenylacetamide
-
-
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)-3-nitrobenzamide
-
-
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)-4-fluorobenzamide
-
-
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)acetamide
-
-
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)benzamide
-
-
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)pentanamide
-
-
N-(4-chlorophenyl)-6-hydroxy-2-methoxy-5,7-dioxo-5,6,7,8-tetrahydro-1,6-naphthyridine-8-carboxamide
-
-
N-(4-fluorophenyl)-6-hydroxy-2-methoxy-5,7-dioxo-5,6,7,8-tetrahydro-1,6-naphthyridine-8-carboxamide
-
-
N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone
N-(4-tert-butylbenzoyl)-2-hydroxynaphthaldehyde hydrazone
BBNH, the residue Tyr501 is integral in the binding interaction, mechanism
N-acyl hydrazone analogues
-
-
N-[(4-fluorophenyl)methyl]-2,6-dihydroxy-5,7-dioxo-5,6,7,8-tetrahydro-1,6-naphthyridine-8-carboxamide
-
-
N-[3-(aminocarbonyl)-4,5-dimethyl-2-thienyl]-2-furancarboxamide
naphthazarin
-
inhibits weakly
non-nucleoside reverse transcriptase inhibitors
-
non-nucleotide or non-nucleoside reverse transcriptase inhibitor
-
nonnucleoside reverse transcriptase inhibitor
-
NNRTI
-
nootkatin
-
i.e. 2-hydroxy-5-(3-methyl-2-butenyl)-4-(1-methylethyl)-2,4,6-cycloheptatrien-1-one
nucleoside analog reverse transcriptase inhibitor
-
NRTI
-
nucleoside analog RT inhibitors
-
nucleotide or nucleoside reverse transcriptase inhibitor
-
p-hydroxymercuribenzoate
Herpes simplex virus
-
5 mM lead to 90% inhibition
Phosphonoformate
-
the inhibitor that bind in the reverse transcriptase polymerase domain inhibits also RNase H activity, IC value for the wild-type enzyme is 0.0015 mM versus substrate DNA-18-nucleotide-RNA hybrid, with the other substrates the IC50 value is above 0.025 mM
Phosphonoformic acid
-
inhibits both the polymerase and the RNase H activities
Plumbagin
-
poor inhibitory activity
RNA-DNA duplex with bound drugs
-
two chimeric RNA-DNA duplexes mimicking intermediates of the reverse trancriptase reaction with bound 4,5-disubstituted 2-deoxystreptamine aminoglycosides, i.e. neomycin, paromomycin, and ribostamycin, inhibit specifically and competitively the RNase H cleavage reaction by 60-95% and 15-91%, respectively, overview
-
shikometabolin C
-
inhibits weakly
shikometabolin D
-
inhibits weakly
shikonin
-
inhibits weakly
single-stranded DNA aptamer RT1t49
-
single-stranded RNA aptamer RT1t49
-
tert-butyl [7-(1-hydroxypropyl)-8-methyl-9-oxo-12-(trimethylsilyl)-9,11-dihydroindolizino[1,2-b]quinolin-2-yl]carbamate
-
mappicine analogue
TMC-125
-
a nonnucleoside reverse transcriptase inhibitor, inhibits the 5' to 3' directed RNase H activity
trihydroxybenzoylbiphenyl carboxylate hydrazone
trihydroxybenzoylnaphthyl hydrazone
zidovudine triphosphate
-
i.e. AZTTP
[(4-chlorophenyl) hydrazono] propanedioic acid
-
inhibits the RNase H of HIV-1 reverse transcriptase with potency similar to that of N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone. It is specific for RNase H and does not inhibit the DNA polymerase activity of reverse transcriptase. Inhibits RNase H by binding to the active site and chelating the essential Mg2+
[(4-chlorophenyl)hydrazono]propanedioic acid
-
inhibits by directly chelating Mg2+
[10,12,15,16-tetrakis(cyclohexyloxy)-8-methoxy-11-methyl-1,9,14-trioxo-6,7,9,14-tetrahydrotetraceno[1,2-g]phthalazin-2(1H)-yl]acetic acid
-
-
1,3,4,5-tetragalloylapiitol
-
isolated from the aqueous extract of leaves of the plant Hylodendron gabunensis
1,3,4,5-tetragalloylapiitol
-
extracted from the plant Hylodendron gabunense, also inhibitory effective against HIV-2 RNase H
1,3,4,5-tetragalloylapiitol
-
isolated from the aqueous extract of leaves of the plant Hylodendron gabunensis
2,7-dihydroxy-4-isopropylcyclohepta-2,4,6-trienone
-
2,7-dihydroxy-4-1(methylethyl)-2,4,6-cycloheptatrien-1-one, or beta-thujaplicinol, is not candidate therapeutics because it is cytotoxic
2,7-dihydroxy-4-isopropylcyclohepta-2,4,6-trienone
-
beta-thujaplicinol, tropolone derivative. Inhibitory activity against both HIV-1 RNase H and Escherichia coli RNase H at a concentration of 0.2 microM and 50 microM respectively
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
-
NSC727447
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
-
NSC727447
2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
IC50 values determined by two different assay variants
2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
-
2-hydroxyisoquinoline-1,3(2H,4H)-dione
-
best inhibitor with high selectivity and activity
3'-azido-3'-deoxythymidine
-
-
3'-azido-3'-deoxythymidine
a nucleoside analog RT inhibitor
3'-azido-3'-deoxythymidine
-
-
3'-azido-3'-deoxythymidine
a nucleoside analog RT inhibitor
4-[(4'-aminomethyl-1,1'-biphenyl)methyl]-1-hydroxy-1,8-naphthyridin-2-one
-
potent inhibitor
4-[(4'-aminomethyl-1,1'-biphenyl)methyl]-1-hydroxy-1,8-naphthyridin-2-one
-
potent inhibitor
4-[(4'-aminomethyl-1,1'-biphenyl)methyl]-1-hydroxy-1,8-naphthyridin-2-one
potent inhibitor
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
-
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
-
derivative of 5-nitrofuran-2-carboxylic acid carbamoyl methyl ester
7-(furan-2-yl)-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
-
-
7-(furan-2-yl)-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
-
-
7-(furan-2-yl)-2-hydroxy-isoquinoline-1,3(2H,4H)-dione
-
alpha-thujaplicin
-
i.e. 2-hydroxy-3-(1-methylethyl)-2,4,6-cycloheptatrien-1-one
alpha-thujaplicin
-
tropolone derivative
ardimerin digallate
-
a Ardisia japonica dimeric lactone, structure determination by NMR spectrometry
ardimerin digallate
-
from natural plant of Ardisia japonica
ardimerin digallate
-
a Ardisia japonica dimeric lactone, structure determination by NMR spectrometry
beta-thujaplicin
-
i.e. 2-hydroxy-4-(1-methylethyl)-2,4,6-cycloheptatrien-1-one
beta-thujaplicin
-
tropolone derivative
beta-thujaplicinol
-
i.e. 2,7-dihydroxy-4-(1-methylethyl)-2,4,6-cycloheptatrien-1-one
beta-thujaplicinol
able to inhibit RNase H in the presence of 200 nM HTS-1 RNA-DNA substrate. However, beta-thujaplicinol is not able to inhibit RNase H as the concentration of RNA-DNA substrate is increased
Ca2+
-
competitive inhibitor
Ca2+
competitive inhibitor
efavirenz
-
a nonnucleoside reverse transcriptase inhibitor, inhibits the 5' to 3' directed RNase H activity
efavirenz
-
a non-nucleoside reverse transcriptase inhibitor
gamma-thujaplicin
-
i.e. 2-hydroxy-5-(1-methylethyl)-2,4,6-cycloheptatrien-1-one
gamma-thujaplicin
-
tropolone derivative
illimaquinone
-
inhibits RNase H in vitro, but is not selectively active against RNase H. Does not exhibit inhibitory activity against RNase H in the HIV-1 replication process
KCl
-
at concentrations above 0.05 M
KCl
-
at concentrations greater than 20 mM
KCl
-
at concentrations above 0.05 M
manicol
-
i.e. 1,2,3,4-tetrahydro-2,7-dihydroxy-9-methyl-2-(1-methylethyl)-6H-benzocyclohepten-6-one
manicol
-
tropolone derivative. Inhibitory activity against both HIV-1 RNase H and Escherichia coli RNase H at a concentration of 1.5 microM and 40 microM respectively
N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone
i.e. BBNH, highly specific, a substituted inhibitor derivative, that interacts with the nucleoside analog RT inhibitor-binding pocket, and inhibits both the polymerase and RNH activities of reverse transcriptase
N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone
-
reasonable potency. Bifunctional inhibitor of HIV-1 reverse transcriptase, it inhibits both the reverse transcriptase DNA polymerase and RNase H activities of the enzyme with similar potency (IC50 is about 3 microM)
N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone
-
phenylhydrazone derivative. Inhibits RNase H in vitro, but is not selectively active against RNase H. Exhibits inhibitory activity against RNase H in the HIV-1 replication process
N-[3-(aminocarbonyl)-4,5-dimethyl-2-thienyl]-2-furancarboxamide
-
NSC727448
N-[3-(aminocarbonyl)-4,5-dimethyl-2-thienyl]-2-furancarboxamide
-
NSC727448
nevirapine
-
a nonnucleoside reverse transcriptase inhibitor, inhibits the 5' to 3' directed RNase H activity
non-nucleoside reverse transcriptase inhibitors
i.e. NNRTIs, the association of an NNRTI with reverse transcriptase not only forms the NNRTI pocket, but also alters the relative positions of the RNase H and polymerase domains
-
non-nucleoside reverse transcriptase inhibitors
i.e. NNRTIs
-
non-nucleotide or non-nucleoside reverse transcriptase inhibitor
NNRTI, non-competitive inhibitor that binds a hydrophobic pocket near the polymerase active site of the p66 subunit in HIV-1 reverse transcriptase
-
non-nucleotide or non-nucleoside reverse transcriptase inhibitor
targets the DNA polymerasec activity of reverse transcriptase. Non-competitive inhibitor that binds a hydrophobic pocket near the polymerase active site of the p66 subunit in HIV-1 reverse transcriptase
-
nucleoside analog RT inhibitors
i.e. NRTIs, nucleoside analog RT inhibitors are non-competitive inhibitors that bind a hydrophobic pocket near the polymerase active site of the p66 subunit in HIV-1 reverse transcriptase
-
nucleoside analog RT inhibitors
i.e. NRTIs, nucleoside analog RT inhibitors are non-competitive inhibitors
-
nucleotide or nucleoside reverse transcriptase inhibitor
NRTIs inhibit replication by competing with cellular dNTPs for incorporation into the nascent DNAchain; upon incorporation, the absence of a 3' hydroxyl group on the NRTI prevents additional synthesis and causes premature chain termination
-
nucleotide or nucleoside reverse transcriptase inhibitor
targets the DNA polymerasec activity of reverse transcriptase. NRTIs inhibit replication by competing with cellular dNTPs for incorporation into the nascent DNAchain; upon incorporation, the absence of a 3' hydroxyl group on the NRTI prevents additional synthesis and causes premature chain termination
-
single-stranded DNA aptamer RT1t49
-
inhibits viral RT polymerase and RNase H functions, pre-steady-state and order-of-addition kinetic analyses, ssDNA aptamer competes with primer-template for access to RT, and that addition of a nucleoside analog RT inhibitor to the in vitro reaction enhanced the overall effectiveness of both drugs, while nonnucleoside analog RT inhibitors exhibited simple additivity
-
single-stranded DNA aptamer RT1t49
-
inhibits viral RT polymerase and RNase H functions, pre-steady-state and order-of-addition kinetic analyses, ssDNA aptamer competes with primer-template for access to RT, and that addition of a nucleoside analog RT inhibitor to the in vitro reaction enhanced the overall effectiveness of both drugs, while nonnucleoside analog RT inhibitors exhibited simple additivity
-
single-stranded DNA aptamer RT1t49
-
inhibits viral RT polymerase and RNase H functions, pre-steady-state and order-of-addition kinetic analyses, ssDNA aptamer competes with primer-template for access to RT, and that addition of a nucleoside analog RT inhibitor to the in vitro reaction enhanced the overall effectiveness of both drugs, while nonnucleoside analog RT inhibitors exhibited simple additivity
-
single-stranded RNA aptamer RT1t49
-
inhibits viral RT polymerase and RNase H functions, pre-steady-state and order-of-addition kinetic analyses, ssDNA aptamer competes with primer-template for access to RT, and that addition of a nucleoside analog RT inhibitor to the in vitro reaction enhanced the overall effectiveness of both drugs, while nonnucleoside analog RT inhibitors exhibited simple additivity
-
single-stranded RNA aptamer RT1t49
-
inhibits viral RT polymerase and RNase H functions, pre-steady-state and order-of-addition kinetic analyses, ssDNA aptamer competes with primer-template for access to RT, and that addition of a nucleoside analog RT inhibitor to the in vitro reaction enhanced the overall effectiveness of both drugs, while nonnucleoside analog RT inhibitors exhibited simple additivity
-
single-stranded RNA aptamer RT1t49
-
inhibits viral RT polymerase and RNase H functions, pre-steady-state and order-of-addition kinetic analyses, ssDNA aptamer competes with primer-template for access to RT, and that addition of a nucleoside analog RT inhibitor to the in vitro reaction enhanced the overall effectiveness of both drugs, while nonnucleoside analog RT inhibitors exhibited simple additivity
-
trihydroxybenzoylbiphenyl carboxylate hydrazone
-
-
trihydroxybenzoylbiphenyl carboxylate hydrazone
-
-
trihydroxybenzoylbiphenyl carboxylate hydrazone
-
trihydroxybenzoylnaphthyl hydrazone
-
-
trihydroxybenzoylnaphthyl hydrazone
-
-
trihydroxybenzoylnaphthyl hydrazone
-
tropolone
-
i.e. 2-hydroxy-2,4,6-cycloheptatrien-1-one
additional information
-
not: o-phenanthroline
-
additional information
-
inhibition of hepatitis B virus (HBV) replication by alpha-tropolone, N-hydroxyisoquinolinedione, and N-hydroxypyridinedione ribonuclease H inhibitors. Three compound classes, the alpha-hydroxytropolones, N-hydroxyisoquinolinediones, and N-hydroxypyridinediones are found by inhibitor screening, that suppress viral replication in cells by blocking the HBV RNaseH. These compounds preferentially suppress the plus-polarity DNA strands, induce truncation of the minus-polarity DNA strands, and cause accumulation of extensive RNA:DNA heteroduplexes in capsids as expected from their inhibition of the RNaseH. Seven N-hydroxyisoquinolinediones inhibit HBV replication, but the therapeutic indexes does not improve over what is reported. All nine of the N-hydroxypyridinedioness inhibit HBV replication. The N-hydroxypyridinedione compound class holds potential for antiviral discovery. No inhibition by A10 and A11. Determination of cellular toxicity and EC50 values for HBV replication inhibition in presence of DNA for the inhibitor compounds, overview. Comparison with effects on the human enzyme
-
additional information
-
selectivity of tropolone derivatives for HIV-1 and HIV-2 enzymes, IC50 values, inhibition mechanism, overview
-
additional information
-
development of a fluorescence polarization assay for screening inhibitors against the RNase H activity of HIV-1 reverse transcriptase, two assay variants, overview
-
additional information
-
no inhibition by O-methylated 3,7-dihydroxytropolones and tropolones, IC50 values, overview
-
additional information
-
design of diverse dsDNA thioaptamers with selected thiophosphate backbone substitutions effectively inhibiting the RNase activity of the reverse transcriptase and the viral replication, i.e. thioadaptamer R12-2 or XBY-S2, overview
-
additional information
-
effects of reverse transcriptase polymerase domain inhibitors on RNase H activity dependent on the substrate, overview, no inhibition of RNase H by nucleoside analogue 3'-azido-3'-deoxythymidine triphosphate
-
additional information
-
nonnucleoside reverse transcriptase inhibitors, i.e. NNRTIs, binding to the polymerase domain of HIV-RT interferes with RNase H activity through a long-range effect, which is affected by the structure of the RNA:DNA hybrid substrate, but is independent of NNRTI compound structure and nucleic acid substrate sequence
-
additional information
inhibition mechanism, overview, antiviral activity and cytotoxic effects of inhibitors, overview
-
additional information
-
inhibition mechanism, overview, antiviral activity and cytotoxic effects of inhibitors, overview
-
additional information
-
natural product extracts screening for detection of inhibitors specific for HIV-1 RNase H
-
additional information
one potential class of RNase H inhibitors involves drugs that alter the interactions between the RNase H domain and substrate or that alter the alignment of substrate in the RNase H active site
-
additional information
-
one potential class of RNase H inhibitors involves drugs that alter the interactions between the RNase H domain and substrate or that alter the alignment of substrate in the RNase H active site
-
additional information
screening of 20000 small-molecular-weight compounds for RNase H inhibitors
-
additional information
-
resistance to nucleoside reverse transcriptase inhibitors
-
additional information
-
summary of HIV-1 RNase H inhibitors. Ardimerin has no inhibitory activity against HIV-1 RNase H because of the absence of galloyl unit. Oligonucleotide with 35 base pairs based on the G-quartet inhibits the RNase H and the polymerase. Different oligonucleotides with structural characters of hairpins and dumbbells: 1R4RR4, 2R4RR4, 3R4RR4, 4D4RD4, 5R4D4R, 6R6RR6, 7R6RR6, 8nicked dumbbell, and 9ligared dumbbell. Effective, they do not inhibit the polymerase and RNase H of Mammalia
-
additional information
-
natural product extracts screening for detection of inhibitors specific for HIV-2 RNase H
-
additional information
-
not: o-phenanthroline
-
additional information
-
one potential class of RNase H inhibitors involves drugs that alter the interactions between the RNase H domain and substrate or that alter the alignment of substrate in the RNase H active site
-
additional information
one potential class of RNase H inhibitors involves drugs that alter the interactions between the RNase H domain and substrate or that alter the alignment of substrate in the RNase H active site
-
additional information
-
not: o-phenanthroline
-
additional information
Rauscher leukemia virus
-
not: o-phenanthroline
-
additional information
-
not: o-phenanthroline
-
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0.0005
(E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
Human immunodeficiency virus 1
-
0.00013 - 0.00024
1,3,4,5-tetragalloylapiitol
0.0095
1,4-Naphthoquinone
Human immunodeficiency virus 1
-
-
0.0374
2,7-dihydroxyisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0353
2-(4-fluorophenyl)-N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)acetamide
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.002 - 0.1967
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
0.00043
2-hydroxy-4H-isoquinoline-1,3-dione
Human Immunodeficiency Virus
-
specific inhibition of isolated RNase H domain and of the full length reverse transcriptase, IC50 value for the isolated RNase H domain is 0.00043 mM
0.1703
2-hydroxy-6-pentadecylbenzoic acid
Human immunodeficiency virus 1
-
-
0.0337
2-hydroxy-6-[(8Z)-pentadec-8-en-1-yl]benzoic acid
Human immunodeficiency virus 1
-
-
0.0072
2-hydroxy-7-(4-hydroxyphenyl)isoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.058
2-hydroxy-7-iodoisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.048
2-hydroxy-7-nitroisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0107
2-hydroxy-7-[4-(trifluoromethyl)phenyl]isoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00043 - 0.0059
2-hydroxyisoquinoline-1,3(2H,4H)-dione
0.0585
2-[(10Z)-heptadec-10-en-1-yl]-6-hydroxybenzoic acid
Human immunodeficiency virus 1
-
-
0.0005
3,4-dihydroxy-N'-[(E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
Human immunodeficiency virus 1
-
IC50 value is about 0.5 microM
0.0075
4'-chloro-N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]biphenyl-4-carbohydrazide
Human immunodeficiency virus 1
-
0.00002 - 0.001
4-(1-chloro-1,1-difluoromethyl)-4-(2-phenylethynyl)-6-chloro-2H-3,1-benzoxazin-2-one
0.002
4-(dimethylamino)-N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
Human immunodeficiency virus 1
-
0.012
4-methoxy-N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
Human immunodeficiency virus 1
-
0.003
4-tert-butyl-N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
Human immunodeficiency virus 1
-
0.002 - 0.0035
4-[5-(benzoylamino)thien-2-yl]-2,4-dioxobutanoic acid
Human immunodeficiency virus 1
-
a diketo acid RNase H inhibitor, IC50 values for wild-type and mutant enzymes are 0.002-0.0035 mM with all substrates, effect on mutant enzymes, overview
0.0032 - 0.0047
4-[5-(benzoylamino)tien-2-yl]-2,4-dioxobutanoic acid
0.00038
5-chloro-2-hydroxyisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
inhibits the isolated HIV RNase H domain
0.0038 - 0.0296
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
0.0026 - 0.0322
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydro-furan-2-yl-methyl)-carbamoyl] methyl ester
0.0086
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydrofuran-2-ylmethyl)-carbamoyl] methyl ester
murine leukemia virus
-
for murine leukemia virus reverse transcriptase
0.0066
7-(3,4-dihydroxyphenyl)-2-hydroxyisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0222
7-(4-fluorophenyl)-2-hydroxyisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0289
7-chloro-2-hydroxyisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0011 - 0.0015
ardimerin digallate
0.000308 - 0.00047
beta-thujaplicinol
0.002
BPH218
Human immunodeficiency virus 1
-
in vitro IC50 value is about 2 microM
0.0000084 - 0.000091
capravirine
0.0005 - 0.0012
dihydroxy benzoyl naphthyl hydrazone
0.0000045 - 0.0000637
efavirenz
0.013
ethyl (5E)-6-[1-(4-fluorobenzyl)-1H-pyrrol-2-yl]-2,4-dioxohex-5-enoate
Human immunodeficiency virus 1
-
-
0.0000076 - 0.0000238
GW8248
0.00146
hyemaloside A
Human immunodeficiency virus 1
-
-
0.00119
hyemaloside C
Human immunodeficiency virus 1
-
-
0.05
illimaquinone
Human immunodeficiency virus 1
-
-
0.015
N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]-4-methylbenzohydrazide
Human immunodeficiency virus 1
-
0.007
N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]-4-phenoxybenzohydrazide
Human immunodeficiency virus 1
-
0.015
N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]benzohydrazide
Human immunodeficiency virus 1
-
0.005
N'-[(1E)-(2-methoxynaphthalen-1-yl)methylidene]biphenyl-4-carbohydrazide
Human immunodeficiency virus 1
-
0.0108
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)-3-nitrobenzamide
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0071
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)-4-fluorobenzamide
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0407
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)acetamide
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0057
N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)benzamide
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.003
N-(4-tert-butylbenzoyl)-2-hydroxy-1-naphthaldehyde hydrazone
Human immunodeficiency virus 1
-
IC50 is about 3 microM
0.0032 - 0.005
N-[3-(aminocarbonyl)-4,5-dimethyl-2-thienyl]-2-furancarboxamide
0.000216 - 0.01
nevirapine
0.025
Phosphonoformate
Human immunodeficiency virus 1
-
the inhibitor that bind in the reverse transcriptase polymerase domain inhibits also RNase H activity, IC value for the wild-type enzyme is 0.0015 mM versus substrate DNA-18-nucleotide-RNA hybrid, with the other substrates the IC50 value is above 0.025 mM
0.0000471 - 0.000147
TMC-125
additional information
additional information
-
0.00013
1,3,4,5-tetragalloylapiitol
Human immunodeficiency virus 2
-
25°C
0.00024
1,3,4,5-tetragalloylapiitol
Human immunodeficiency virus 1
-
25°C
0.00024
1,3,4,5-tetragalloylapiitol
Human immunodeficiency virus 1
-
also inhibitory effective against HIV-2 RNase H with an IC50 value of 0.13 microM. Poor selectivity against human RNase H with an IC50 value of 1.5 microM
0.002
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.0025
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus 2
-
pH 8.0, 37°C
0.0066
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus 1
-
wild-type, pH 8.0, 37°C
0.02
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus 1
-
Y501F mutant, pH 8.0, 37°C
0.0706
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus 1
-
Y501W mutant, pH 8.0, 37°C
0.0896
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus 1
-
Y501Az-F mutant, pH 8.0, 37°C
0.1967
2-amino-5,6,7,8-tetrahydro-4H-cyclohepta[b]thiophene-3-carboxamide
Human immunodeficiency virus 1
-
Y501Bp-F mutant, pH 8.0, 37°C
0.00043
2-hydroxyisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
inhibits the isolated HIV RNase H domain in the assay using CGK1 as substrate
0.0006
2-hydroxyisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
using CGK1 as substrate
0.001
2-hydroxyisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
in another assay, using poly(dC:rG) as a template, without inhibitory effect against Escherichia coli RNase H
0.0059
2-hydroxyisoquinoline-1,3(2H,4H)-dione
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.00002 - 0.00005
4-(1-chloro-1,1-difluoromethyl)-4-(2-phenylethynyl)-6-chloro-2H-3,1-benzoxazin-2-one
Human immunodeficiency virus 1
-
i.e. NNRTI, an efavirenz analogue, IC50 values for wild-type enzyme are 0.00002-0.00005 mM with substrates DNA-17-nucleotide-RNA hybrid or DNA-18-nucleotide-RNA hybrid
0.001
4-(1-chloro-1,1-difluoromethyl)-4-(2-phenylethynyl)-6-chloro-2H-3,1-benzoxazin-2-one
Human immunodeficiency virus 1
-
0.001 mM for substrate DNA-15-nucleotide-RNA hybrid or DNA-16-nucleotide-RNA hyb
0.0032
4-[5-(benzoylamino)tien-2-yl]-2,4-dioxobutanoic acid
Human immunodeficiency virus 1
-
HIV-1 RNase H inhibitor, which inhibits the HIV-1 RNase H as part of HIV-reverse transcriptase without influencing the activity of HIV-1-dependent RNA and DNA polymerase
0.0047
4-[5-(benzoylamino)tien-2-yl]-2,4-dioxobutanoic acid
Human immunodeficiency virus 1
-
isolated HIV-RNAse H domain
0.0038
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Human immunodeficiency virus 1
for the CRF01 A_E (93JPNH1) reverse transcriptase. pH 8.0, 37°C
0.0084
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
murine leukemia virus
-
for murine leukemia virus reverse transcriptase, pH 7.8, 37°C
0.0265
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Human immunodeficiency virus 1
for the HIV-1 clade C (93IN101) reverse transcriptase. pH 8.0, 37°C
0.0296
5-nitrofuran-2-carboxylic acid adamantan-1-carbamoyl methyl ester
Human immunodeficiency virus 1
for clade B HIV-1LAI-derived reverse transcriptase-associated RNase H activity. pH 8.0, 37°C
0.0026
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydro-furan-2-yl-methyl)-carbamoyl] methyl ester
Human immunodeficiency virus 1
for the CRF01 A_E (93JPNH1) reverse transcriptase. pH 8.0, 37°C
0.0267
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydro-furan-2-yl-methyl)-carbamoyl] methyl ester
Human immunodeficiency virus 1
for clade B HIV-1LAI-derived reverse transcriptase-associated RNase H activity. pH 8.0, 37°C
0.0322
5-nitrofuran-2-carboxylic acid [[4-(4-bromophenyl)-thiazol-2-yl]-(tetrahydro-furan-2-yl-methyl)-carbamoyl] methyl ester
Human immunodeficiency virus 1
for the HIV-1 clade C (93IN101) reverse transcriptase. pH 8.0, 37°C
0.0011
ardimerin digallate
Human immunodeficiency virus 2
-
pH 8.0, 22°C
0.0015
ardimerin digallate
Human immunodeficiency virus 1
-
pH 8.0, 22°C
0.0015
ardimerin digallate
Human immunodeficiency virus 1
-
without inhibiting both human and Escherichia coli RNase H at a concentration of 200 microM/l
0.000308
beta-thujaplicinol
Human immunodeficiency virus 1
-
wild-type
0.000356
beta-thujaplicinol
Human immunodeficiency virus 1
-
Y501W mutant
0.000386
beta-thujaplicinol
Human immunodeficiency virus 1
-
Y5014-azido-L-Phe mutant
0.00047
beta-thujaplicinol
Human immunodeficiency virus 1
-
Y501F mutant
0.0000084
capravirine
Human immunodeficiency virus 1
-
pH 8.0, 22°C, wild-type enzyme
0.000011
capravirine
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant K103N
0.0000206
capravirine
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant Y181C
0.0000233
capravirine
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant Y188L
0.000091
capravirine
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant K103N/Y181C
0.0005
dihydroxy benzoyl naphthyl hydrazone
Human immunodeficiency virus 1
-
-
0.00065
dihydroxy benzoyl naphthyl hydrazone
Human immunodeficiency virus 1
-
drug-resistant HIV-1 reverse transcriptase variant Y181C reverse transcriptase
0.0012
dihydroxy benzoyl naphthyl hydrazone
Human immunodeficiency virus 1
-
drug-resistant HIV-1 reverse transcriptase variant Y188l reverse transcriptase
0.0000045
efavirenz
Human immunodeficiency virus 1
-
pH 8.0, 22°C, wild-type enzyme
0.0000109
efavirenz
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant Y181C
0.0000281
efavirenz
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant K103N
0.0000493
efavirenz
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant Y188L
0.0000637
efavirenz
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant K103N/Y181C
0.0000076
GW8248
Human immunodeficiency virus 1
-
pH 8.0, 22°C, wild-type enzyme
0.0000106
GW8248
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant K103N
0.0000108
GW8248
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant Y188L
0.0000121
GW8248
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant Y181C
0.0000238
GW8248
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant K103N/Y181C
0.0032
N-[3-(aminocarbonyl)-4,5-dimethyl-2-thienyl]-2-furancarboxamide
Human immunodeficiency virus 1
-
pH 8.0, 37°C
0.005
N-[3-(aminocarbonyl)-4,5-dimethyl-2-thienyl]-2-furancarboxamide
Human immunodeficiency virus 2
-
pH 8.0, 37°C
0.000216
nevirapine
Human immunodeficiency virus 1
-
pH 8.0, 22°C, wild-type enzyme
0.01
nevirapine
Human immunodeficiency virus 1
-
above, pH 8.0, 22°C, mutants K103N, Y181C, Y188L, and K103N/Y181C
0.0000471
TMC-125
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant K103N
0.0000588
TMC-125
Human immunodeficiency virus 1
-
pH 8.0, 22°C, wild-type enzyme
0.000098
TMC-125
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant Y188L
0.0001034
TMC-125
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant Y181C
0.000147
TMC-125
Human immunodeficiency virus 1
-
pH 8.0, 22°C, mutant K103N/Y181C
additional information
additional information
Human immunodeficiency virus 1
-
-
-
additional information
additional information
Simian immunodeficiency virus
-
-
-
additional information
additional information
Human immunodeficiency virus 2
-
-
-
additional information
additional information
Human immunodeficiency virus 1
inhibition of mutant enzymes by DHBNH and antiviral activity, overview
-
additional information
additional information
Human immunodeficiency virus 1
-
inhibition of mutant enzymes by DHBNH and antiviral activity, overview
-
additional information
additional information
Human immunodeficiency virus 1
-
IC50 more than 18 microM for hyemaloside B
-
additional information
additional information
Human immunodeficiency virus 1
-
IC50 value is higher than 96.00 microM for 7-bromo-2-hydroxyisoquinoline-1,3(2H,4H)-dione. IC50 value is higher than 80.0 microM for N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)pentanamide, for 2-hydroxy-7-phenylisoquinoline-1,3(2H,4H)-dione, and for N-(2-hydroxy-1,3-dioxo-1,2,3,4-tetrahydroisoquinolin-7-yl)-2-phenylacetamide. pH 8.0, 37°C
-
additional information
additional information
Human immunodeficiency virus 1
-
IC50 values of different oligonucleotides with structural characters of hairpins and dumbbells: 0.000500 mM for oligonucleotide with 35 base pairs based on the G-quartet motif, 0.0258 mM for 1R4RR4, 0.0262 mM for 2R4RR4, 0.0693 mM for 3R4RR4, 0.0078 mM for 6R6RR6, 0.0297 mM for 7R6RR6, 0.0404 mM for 8nicked dumbbell, and 0.0033 mM for 9ligared dumbbell. IC50 value is much higher than 100 microM for 4D4RD4 and 5R4D4R. [(4-chlorophenyl)hydrazono] propanedioic acid shows an IC50 value of 3 microM against polymerase-independent RNase H activity. Its activity against HIV-1 RNase H in vivo and toxicity in cell culture or in vivo still need to be investigated. IC50 0.0013 mM for 3,7-dihydroxy-tropolone, monosubstituted, and 0.0047 mM for 3,7-dihydroxy-tropolone, unsubstituted
-
additional information
additional information
Human immunodeficiency virus 1
-
the IC50 values for 3-[(8Z)-pentadec-8-en-1-yl]phenol, 3-[(10Z)-heptadec-10-en-1-yl]phenol, 3-tridecylphenol, 3-pentadecylphenol, 5-[(8Z)-pentadec-8-en-1-yl]benzene-1,3-diol, and 5-tridecylbenzene-1,3-diol are above 200 microM
-
additional information
additional information
Human immunodeficiency virus 1
-
Y5014-(phenylcarbonyl)-L-Phe mutant, the IC50 value is above 300 microM
-
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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_VILV
Maedi visna virus (strain 1514)
1506
0
171940
Swiss-Prot
other Location (Reliability: 1)
POL_VILV1
Maedi visna virus (strain 1514 / clone LV1-1KS1)
1506
0
171964
Swiss-Prot
other Location (Reliability: 1)
POL_VILV2
Maedi visna virus (strain 1514 / clone LV1-1KS2)
1506
0
171974
Swiss-Prot
other Location (Reliability: 1)
POL_VILVK
Maedi visna virus (strain KV1772)
1506
0
171957
Swiss-Prot
other Location (Reliability: 1)
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)
A0A2S5B0F5_9BASI
464
0
54092
TrEMBL
other Location (Reliability: 2)
A0A2S5B156_9BASI
648
0
67380
TrEMBL
Mitochondrion (Reliability: 2)
POL_XMRV6
Xenotropic MuLV-related virus (isolate VP62)
1733
0
193862
Swiss-Prot
-
RNH_SULTO
Sulfurisphaera tokodaii (strain DSM 16993 / JCM 10545 / NBRC 100140 / 7)
149
0
16813
Swiss-Prot
-
POL_MLVMS
1738
0
194912
Swiss-Prot
-
RNH_ECOLI
Escherichia coli (strain K12)
155
0
17597
Swiss-Prot
-
RNH_BPT4
305
0
35558
Swiss-Prot
-
POL_FOAMV
1143
0
129742
Swiss-Prot
-
PRP8_YEAST
Saccharomyces cerevisiae (strain ATCC 204508 / S288c)
2413
0
279504
Swiss-Prot
-
RNH_HALSA
Halobacterium salinarum (strain ATCC 700922 / JCM 11081 / NRC-1)
199
0
20981
Swiss-Prot
-
RNH1_ALKHC
Alkalihalobacillus halodurans (strain ATCC BAA-125 / DSM 18197 / FERM 7344 / JCM 9153 / C-125)
196
0
22373
Swiss-Prot
-
GAG_HV1H2
Human immunodeficiency virus type 1 group M subtype B (isolate HXB2)
500
0
55930
Swiss-Prot
-
A0A076Q3N8_9HIV1
1015
0
115049
TrEMBL
-
A7YKL0_9HIV1
1008
0
114184
TrEMBL
-
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D702A/E731A
-
sequences encoding HBV RNaseH residues 809-844 are deleted from pMal-HRHgtC to create pMal-HRHgtCDELTA5. Active site residues D702 and E731 are mutated to alanines to create pMAL-HRHgtC(D702A/E731A) which encodes an inactive RNaseH
D777A
-
the mutant shows loss of catalytic activity
D778A
-
the mutant shows a defect in enzyme activity
K745A
-
the mutant shows a defect in enzyme activity
R703A
-
the mutant shows loss of catalytic activity
R781A
-
the mutant shows a defect in enzyme activity
H264A
-
the mutation causes an about 100fold decrease in kcat under multiple-turnover conditions, but does not alter the Km
D549N
-
unaltered polymerase activity, in the absence and at lower concentrations of Mg2+ the mutant enzyme binds the DNA-DNA substrate more tightly than the wild-type enzyme, at high Mg2+ concentrations the binding is identical for the wild-type and mutant enzymes using DNA-DNA template
A360D
-
mutation decreases the virus titer to about 50% of that of the wild-type virus
C280E
-
mutation does not affect RNase H activity
C280H
-
mutation does not affect RNase H activity
C280L
-
mutation does not affect RNase H activity
C280M
-
mutation does not affect RNase H activity
C280P
-
mutation in either p66 or p51 subunits reduces RNase H activity in comparison to wild-type enzyme, the strand-transfer activity is very low
C280Q
-
mutation does not affect RNase H activity
C280R
-
mutation does not affect RNase H activity
C280W
-
mutation in either p66 or p51 subunits reduces RNase H activity in comparison to wild-type enzyme, the strand-transfer activity is very low
C280Y
-
mutation does not affect RNase H activity
D358N
complete loss of Mg2+ and Mn2+-dependent RNase H activity
D426N
complete loss of Mg2+ and Mn2+-dependent RNase H activity
D469N
enhanced Mn2+ dependent RNase H activity in comparison to Mg2+ dependent RNase H activity
D67N/K70R/T215F/K219Q
the mutant shows reduced sensitivity to inhibitor (E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
E396A
-
mutation decreases the virus titer to about 50% of that of the wild-type virus and has significant effect on the extent of enzyme cleavage
E401Q
complete loss of Mg2+ and Mn2+-dependent RNase H activity
E89K
-
site-directed mutagenesis, foscarnet-resistance mutation, the mutant enzyme shows different sensitivity for inhibitors compared to the wild-type enzyme, overview
G190A
-
site-directed mutagenesis, the mutation confers resistance to non-nucleoside reverse transcriptase inhibitors, and leads to reduced RNase H activity of the reverse transcriptase and to reduced DNA synthesis from tRNALys,3 that correlate with reductions in replication efficiency, the mutant shows reduced fitness compared to the wild-type enzyme
G190S
-
site-directed mutagenesis, the mutation confers resistance to non-nucleoside reverse transcriptase inhibitors, and leads to reduced RNase H activity of the reverse transcriptase and to reduced DNA synthesis from tRNALys,3 that correlate with reductions in replication efficiency, the mutant shows highly reduced fitness compared to the wild-type enzyme
G359S
-
mutation decreases the virus titer to about 50% of that of the wild-type virus
H361A
-
mutation decreases the virus titer to about 25% of that of the wild-type virus and affects the frequency of the generation of linear viral DNAs with aberrant ends
H427A
enhanced Mn2+ dependent RNase H activity in comparison to Mg2+ dependent RNase H activity
H539D
-
site-directed mutagenesis, the mutant enzyme shows an altered cleavage pattern compared to the wild-type enzyme, the mutant is inhibited in performing secondary cleavage directed by the 3' end primer independent of the presence of a hairpin structure or the need to carry out strand displacement
H539F
-
site-directed mutagenesis, the mutant enzyme shows an altered cleavage pattern compared to the wild-type enzyme, the mutant is inhibited in performing secondary cleavage directed by the 3' end primer independent of the presence of a hairpin structure or the need to carry out strand displacement
H539N
-
site-directed mutagenesis, leads to a slowing down in the degradation of the RNA strand, decreases the frequency of reverse transcriptase template-switching by 2fold
H539R
-
site-directed mutagenesis, the mutant enzyme shows an altered cleavage pattern compared to the wild-type enzyme, the mutant is inhibited in performing secondary cleavage directed by the 3' end primer independent of the presence of a hairpin structure or the need to carry out strand displacement
K390A
-
mutation decreases the virus titer less than twofold in comparison of wild-type enzyme
K395A
-
mutation decreases the virus titer less than twofold in comparison of wild-type enzyme
K476A
-
reduces the virus titre
K476C
-
the mutation disrupts the chemical cross-linking while maintaining activity
K65R
-
nucleoside reverse transcriptase inhibitor resistance mutation
L74V
-
nucleoside reverse transcriptase inhibitor resistance mutation
M184I
-
nucleoside reverse transcriptase inhibitor resistance mutation
M41L/D67N/L210W/T215Y/A360V
-
mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP
M41L/D67N/L210W/T215Y/A360V/N348I/E478Q
-
mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP
M41L/D67N/L210W/T215Y/E478Q
-
mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP
M41L/D67N/L210W/T215Y/N348I
-
mutation decreases efficiency of RNase H cleavage and increases excision of AZT in the presence of the pyrophosphate donor ATP
M41L/D67N/L210W/T215Y/N348I/A360V
-
mutant accumulates transiently formed, shorter hybrids that can rebind to reverse transcriptase before the template is irreversibly degraded
N474A
-
reduces the virus titre
P236L
naturally occuring mutations leading to reduced RNase H activity and increased resistance of the reverse trancriptase to NRTIs
Q151N
-
nucleoside reverse transcriptase inhibitor resistance mutation
Q500A
-
reduces the virus titre
T362A
-
mutation decreases the virus titer less than twofold in comparison of wild-type enzyme
T473A
-
abolishes HIV-1 replication
V106A
naturally occuring mutations leading to reduced RNase H activity and increased resistance of the reverse trancriptase to NRTIs
Y459A
enhanced Mn2+ dependent RNase H activity in comparison to Mg2+ dependent RNase H activity
Y5014-(phenylcarbonyl)-L-Phe
-
inserting a benzophenone into the RNase H primer grip (p66501BpF/p51 reverse transcriptase) creates an enzyme that is resistant to beta-thujaplicinol at inhibitor concentrations as high as 300 microM
Y5014-azido-L-Phe
-
nonnatural amino acid substitution introducing an azido function
Y501A
complete loss of activity in comparison to wild-type enzyme
Y501Az-F
-
p-azido-L-phenylalanine (Az-F), site-directed mutagenesis, sensitivity of HIV-1 reverse transcriptase Tyr501 variants to NSC727447 inhibition tested
Y501Bp-F
-
p-benzoyl-L-phenylalanine, site-directed mutagenesis, sensitivity of HIV-1 reverse transcriptase Tyr501 variants to NSC727447 inhibition tested
Y501E
25% activity in comparison to wild-type enzyme
Y501G
complete loss of activity in comparison to wild-type enzyme
Y501H
complete loss of activity in comparison to wild-type enzyme
Y501L
complete loss of activity in comparison to wild-type enzyme
Y501Q
complete loss of activity in comparison to wild-type enzyme
Y501R
90% activity in comparison to wild-type enzyme, the mutant is completely resistant to N-(4-tert-butylbenzoyl)-2-hydroxynaphthaldehyde hydrazone inhibition
Y501S
complete loss of activity in comparison to wild-type enzyme
Q294A
-
6.6fold RNase H activity compared to wild-type
Q294C
-
9.2fold RNase H activity compared to wild-type
Q294E
-
4.0fold RNase H activity compared to wild-type
Q294H
-
4.2fold RNase H activity compared to wild-type
Q294M
-
4.3fold RNase H activity compared to wild-type
Q294N
-
4.9fold RNase H activity compared to wild-type
Q294P
-
5.1fold RNase H activity compared to wild-type
Q294Q/Q294R
-
4.2fold RNase H activity compared to wild-type, Gln294 is modified in p54subunit, Q in p68, R in p54
Q294R
-
4.8fold RNase H activity compared to wild-type
Q294S
-
6.9fold RNase H activity compared to wild-type
Q294W
-
5.1fold RNase H activity compared to wild-type
Q294Y
-
4.8fold RNase H activity compared to wild-type
D549N
-
unaltered polymerase activity, in the absence and at lower concentrations of Mg2+ the mutant enzyme binds the DNA-DNA substrate more tightly than the wild-type enzyme, at high Mg2+ concentrations the binding is identical for the wild-type and mutant enzymes using DNA-DNA template
-
E478Q
-
unaltered polymerase activity, in the absence and at lower concentrations of Mg2+ the mutant enzyme binds the DNA-DNA substrate more tightly than the wild-type enzyme, at high Mg2+ concentrations the binding is identical for the wild-type and mutant enzymes using DNA-DNA template
-
C654S
the mutant shows wild type activity
D599N/H742N
the RNase H activity of the mutant is seriously impaired
D224A
two Moloney murine leukemia virus reverse transcriptase variants (named MRT-D224A and MRT-D524A) as a negative control, in which the catalytically important residue for the reverse transcription activity, Asp224 and that for the RNase H activity, Asp524, are substituted with Ala, respectively
D524A
two Moloney murine leukemia virus reverse transcriptase variants (named MRT-D224A and MRT-D524A) as a negative control, in which the catalytically important residue for the reverse transcription activity, Asp224 and that for the RNase H activity, Asp524, are substituted with Ala, respectively
A558V
-
site-directed mutagenesis, the mutation in the enzyme primer grip results in about 3fold increased viral mutation rates compared to the wild-type enzyme/virus, reduced titer
Q559L
-
site-directed mutagenesis, the mutation in the enzyme primer grip results in about 3fold increased viral mutation rates compared to the wild-type enzyme/virus
S557A
-
site-directed mutagenesis, the mutation in the enzyme primer grip results in about 3fold increased viral mutation rates compared to the wild-type enzyme/virus, reduced titer
T590A
-
site-directed mutagenesis, the mutation in the enzyme primer grip results in similar viral mutation rates compared to the wild-type enzyme/virus
Y586A
-
site-directed mutagenesis, the mutant virus is not stable and cannot be expressed, no colonies
Y586F
-
site-directed mutagenesis, the mutation in the enzyme primer grip results in 17fold increased viral mutation rates compared to the wild-type enzyme/virus
D1853A
failure of D1853A and R1937A mutants of scPrp8 to grow on 5-fluoroorotic acid plates, lethal mutation
D1853N
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
D1854A
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
D1854N
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
E1960K
mutant of prp8-101
K1864E
prp8-D143, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
N1869D
prp8-151, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
N1869D/S1970R
prp8-152, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
R1937A
failure of D1853A and R1937A mutants of scPrp8 to grow on 5-fluoroorotic acid plates, lethal mutation
R1937K
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
T1855A
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
T1936A
cell viability assay monitoring the effects of exchanging invariant Prp8 residues D1853, D1854, T1855, T1936 and R1937 as indicated. After selection of clones, the culture and serial dilutions are spotted and grown at the temperatures 16, 25, 30, and 37°C for 2 days
T1982A
prp8-153, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
T1982A, SA1966/7AG
prp8-154, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
T1982A,V1987A
prp8-155, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
V1870N
prp8-162, that suppress second-step defects in the 5'splice site, 3'splice site or branch point sequence map to the present Prp8 region
C724A
Tequatrovirus T4
site-directed mutagenesis
L242I
Tequatrovirus T4
naturally occuring mutation, the substitution does not affect the structure of RNase H and its role in providing the das-effect remains unclear
V43I
Tequatrovirus T4
naturally occuring mutation, the V43I substitution may lead to disposition of H4 helix, responsible for the interaction with the first base pairs of 5' end of branched DNA. These structural changes may affect unwinding of the first base pairs of gapped or nicked DNA generating a short flap and therefore may stabilize the DNA-enzyme complex
E478Q
-
unaltered polymerase activity, in the absence and at lower concentrations of Mg2+ the mutant enzyme binds the DNA-DNA substrate more tightly than the wild-type enzyme, at high Mg2+ concentrations the binding is identical for the wild-type and mutant enzymes using DNA-DNA template
E478Q
-
site-directed mutagenesis, RNase H domain active site mutation, inactive mutant
D549N
-
have remarkable effects on viral replication by reducing the level of RNAse H activity
D549N
-
site-directed mutagenesis, leads to a slowing down in the degradation of the RNA strand, decreases the frequency of reverse transcriptase template-switching by 2fold
E478Q
-
have remarkable effects on viral replication by reducing the level of RNAse H activity
E478Q
-
mutant lacks RNase H function
E478Q
-
RNase H-minus reverse transcriptase mutant. Comparison of the time course of 591R priming activity with wild type reverse transcriptase or an RNase H-minus reverse transcriptase mutant (E478Q) in the presence and absence of HIV-1 nucleocapsid protein (NC) to probe RNase H function
K103N
-
site-directed mutagenesis, NNRTI-resistance mutation, the mutant enzyme shows different sensitivity for inhibitors compared to the wild-type enzyme, overview
K103N
naturally occuring mutations leading to reduced RNase H activity and increased resistance of the reverse trancriptase to NRTIs
K103N
-
site-directed mutagenesis, mutation of the nonnucleoside reverse transcriptase inhibitor binding site residue reduces the inhibitory effects of nonnucleoside reverse transcriptase inhibitors
K103N
-
site-directed mutagenesis, the mutation confers resistance to non-nucleoside reverse transcriptase inhibitors, and leads to reduced RNase H activity of the reverse transcriptase and to reduced DNA synthesis from tRNALys,3 that correlate with reductions in replication efficiency, the mutant shows a fitness similar to the wild-type enzyme
K103N/Y181C
-
site-directed mutagenesis, mutation of the nonnucleoside reverse transcriptase inhibitor binding site residue reduces the inhibitory effects of nonnucleoside reverse transcriptase inhibitors
K103N/Y181C
-
non-nucleoside reverse transcriptase inhibitor (NNRTI) resistant mutant
V106A/Y181C
the mutant shows reduced sensitivity to inhibitor (E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
V106A/Y181C
-
non-nucleoside reverse transcriptase inhibitor (NNRTI) resistant mutant
Y181C
naturally occuring mutations leading to reduced RNase H activity and increased resistance of the reverse trancriptase to NRTIs
Y181C
-
site-directed mutagenesis, mutation of the nonnucleoside reverse transcriptase inhibitor binding site residue reduces the inhibitory effects of nonnucleoside reverse transcriptase inhibitors
Y181C
the mutant shows reduced sensitivity to inhibitor (E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
Y188L
-
site-directed mutagenesis, mutation of the nonnucleoside reverse transcriptase inhibitor binding site residue reduces the inhibitory effects of nonnucleoside reverse transcriptase inhibitors
Y188L
the mutant shows reduced sensitivity to inhibitor (E)-3,4-dihydroxy-N'-((2-methoxynaphthalen-1-yl)methylene)benzohydrazide
Y501F
85% activity in comparison to wild-type enzyme, the mutant remains sensitive to N-(4-tert-butylbenzoyl)-2-hydroxynaphthaldehyde hydrazone inhibition
Y501F
-
site-directed mutagenesis, sensitivity of HIV-1 reverse transcriptase Tyr501 variants to NSC727447 inhibition tested
Y501F
-
site-directed mutagenesis. IC50 for beta-thujaplicinol is comparable to wild-type value
Y501W
100% activity in comparison to wild-type enzyme, 6fold decreased sensitivity to inhibition N-(4-tert-butylbenzoyl)-2-hydroxynaphthaldehyde hydrazone
Y501W
-
site-directed mutagenesis, sensitivity of HIV-1 reverse transcriptase Tyr501 variants to NSC727447 inhibition tested
Y501W
-
site-directed mutagenesis. IC50 for beta-thujaplicinol is comparable to wild-type value
additional information
-
design of four Moloney murine leukaemia virus/Avian myeloblastosis virus chimeric reverse transcriptases (named MRT-AF, MRT-AP, MRT-AT and MRT-AR)
additional information
-
generation of a 3'-to-5' exonuclease-deficient mutant, D368A Pol. Wild-type and D368A mutant DNA polymerase exhibit similar polymerase activities, but the mutant enzyme is drastically impaired for 3'-to-5' exonuclease activity, with no activity detected even at high enzyme-to-DNA substrate ratios. The mutant shows no detectable ability to excise RNA with either a 3' or 5' terminus in contrast to the wild-type enzyme. Wild-type HSV Pol exhibits readily detectable RNase H activity on 6-FAM-labeled hairpin RNA-DNA substrate with a 3' RNA terminus in the 3'-to-5' direction, while the mutant is inactive. Neither wild-type nor D368A Pol exhibits detectable RNase H activity on a substrate with a 5' RNA terminus
additional information
-
deletion of the 3 C-terminal residues of RNase H domain leads to strong inhibition of RNA cleavage activity
additional information
-
mutations of the RNase H domain of reverse transcriptase result in noninfectious virus particles
additional information
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
-
identification of mutations in nucleoside reverse transcriptase inhibitor-treated patients. 3 mutations are found exclusively in nucleoside reverse transcriptase inhibitor-treated isolates. 9 mutations in the connection and 6 mutations in the RNase H are associated with nucleoside reverse transcriptase inhibitor treatment in subtype B. Some of them lay in or close to amino acid residues which contact nucleic acid or near the RNase H active site. Several of the residues have been recently associated to nucleoside reverse transcriptase inhibitor exposure or increase drug resistance to nucleoside reverse transcriptase inhibitor
additional information
-
mutations in the C-terminus of HIV-1 reverse transcriptase, C-terminal reverse transcriptase mutations are resistant to both nucleoside analog reverse transcriptase inhibitor and nonnucleoside reverse transcriptase inhibitor. Other mutations are reviewed
additional information
mutations in the polymerase domain can affect RNase H activity by affecting the position of the template-primer or the structure of the RNase H domain itself. Aptamer inhibition of RNase H activity. Aptamer 12.01 and Aptamer M302 at varying concentrations (0, 50, 200, 1000 nM) are incubated with radiolabeled primer and an RNA template. Aptamers do not inhibit the RNase H activity of wild-type HIV-1 reverse transcriptase
additional information
-
mutations in the polymerase domain can affect RNase H activity by affecting the position of the template-primer or the structure of the RNase H domain itself. Aptamer inhibition of RNase H activity. Aptamer 12.01 and Aptamer M302 at varying concentrations (0, 50, 200, 1000 nM) are incubated with radiolabeled primer and an RNA template. Aptamers do not inhibit the RNase H activity of wild-type HIV-1 reverse transcriptase
additional information
-
single methylphosphonate substitutions of the RNase H primer grip
additional information
-
site-directed mutagenesis can affect the binding enzyme/substrate, resulting in a decrease in the RNAse H activity. Mutations in positions 448 and 505 have no effect on virus titre
additional information
-
TAMs refers to mutants that contain the following amino acid substitutions M41L/D67N/L210W/T215Y. Thymidine analogue-associated mutations (TAMs) in reverse transcriptase cause resistance to 3'-azido-3'-deoxythymidine (AZT) through excision of the incorporated monophosphate
additional information
the isolated HIV-1 RNase H domain is inactive, but the addition of various N-terminal extensions restores some RNase H activity. Changes at Trp266 and Phe61 in HIV-1 reverse transcriptase, both of which render the RNase H incapable of generating the polypurine tract (PPT) primer or removing the PPT primer once it has been extended primer grip residue Tyr501 in HIV-1 reverse transcriptase appears to be a particularly important substrate contact residue because changes at this site profoundly affect both the RNase H activity and proper substrate recognition
additional information
-
mutagenesis of Gln294 of the reverse transcriptase to find out how various amino acids, other that Gln and Pro at position 294 of HIV-2 reverse transcriptase affect the enzyme's RNase H activity. All modifications of HIV-2 reverse transcriptase Gln294 lead to an increase of the RNase H activity of the enzyme relative to the wild-type and also support the observations that residue 294 in the p54 subunit is the major contributor to the level of this activity in HIV-2 reverse transcriptase
additional information
-
construction of a mutant Mo-MLV RNase H lacking the putative helix C, surface mapping and substrate binding determinants, overview
additional information
-
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
mutations in reverse transcriptase outside of the polymerase domain may have clinical significance in resistance to nucleoside analog RT inhibitors, NRTIs, e.g. 3'-azido-3'-deoxythymidine, mutations in the RNase H domain that decrease RNase H activity can increase the resistance of reverse transcriptase to NRTIs, overview
additional information
design of four Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases (named MRT-AF, MRT-AP, MRT-AT and MRT-AR)
additional information
-
design of four Moloney murine leukemia virus/avian myeloblastosis virus chimeric reverse transcriptases (named MRT-AF, MRT-AP, MRT-AT and MRT-AR)
additional information
-
isolated RNase H domain of Moloney murine leukemia virus reverse transcriptase is enzymatically active, but the activity is low and exhibits a greatly relaxed substrate specificity. Primer grip residue Tyr586 in Moloney murine leukemia virus reverse transcriptase appears to be a particularly important substrate contact residue because changes at this site profoundly affect both the RNase H activity and proper substrate recognition
additional information
all mutants are associated with dramatic growth defects and produced both cold- and temperature-sensitive phenotypes on mutation to asparagine
additional information
-
all mutants are associated with dramatic growth defects and produced both cold- and temperature-sensitive phenotypes on mutation to asparagine
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Catalytically distinct conformations of the ribonuclease H of HIV-1 reverse transcriptase by substrate cleavage patterns and inhibition by azidothymidylate and N-ethylmaleimide
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equine infectious anemia virus, Human immunodeficiency virus 1, equine infectious anemia virus EIAV
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Human immunodeficiency virus 1, Human immunodeficiency virus 2
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Human immunodeficiency virus 1
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Human immunodeficiency virus 1
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Proc. Natl. Acad. Sci. USA
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Human immunodeficiency virus 1
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human foamy virus
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Human immunodeficiency virus 1
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Inhibition of human immunodeficiency virus type 1 reverse transcriptase, RNase H, and integrase activities by hydroxytropolones
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Human immunodeficiency virus 1
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Human Immunodeficiency Virus
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Mueller, G.A.; Pari, K.; DeRose, E.F.; Kirby, T.W.; London, R.E.
Backbone dynamics of the RNase H domain of HIV-1 reverse transcriptase
Biochemistry
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Human immunodeficiency virus 1
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Li, T.K.; Barbieri, C.M.; Lin, H.C.; Rabson, A.B.; Yang, G.; Fan, Y.; Gaffney, B.L.; Jones, R.A.; Pilch, D.S.
Drug targeting of HIV-1 RNA.DNA hybrid structures: thermodynamics of recognition and impact on reverse transcriptase-mediated ribonuclease H activity and viral replication
Biochemistry
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Human immunodeficiency virus 1
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Somasunderam, A.; Ferguson, M.R.; Rojo, D.R.; Thiviyanathan, V.; Li, X.; O'Brien, W.A.; Gorenstein, D.G.
Combinatorial selection, inhibition, and antiviral activity of DNA thioaptamers targeting the RNase H domain of HIV-1 reverse transcriptase
Biochemistry
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Human immunodeficiency virus 1
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Shaw-Reid, C.A.; Feuston, B.; Munshi, V.; Getty, K.; Krueger, J.; Hazuda, D.J.; Parniak, M.A.; Miller, M.D.; Lewis, D.
Dissecting the effects of DNA polymerase and ribonuclease H inhibitor combinations on HIV-1 reverse-transcriptase activities
Biochemistry
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2005
Human immunodeficiency virus 1
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Purohit, V.; Balakrishnan, M.; Kim, B.; Bambara, R.A.
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Human immunodeficiency virus 1
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Schultz, S.J.; Zhang, M.; Champoux, J.J.
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Human immunodeficiency virus 1, Moloney murine leukemia virus
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Human immunodeficiency virus 1, Moloney murine leukemia virus
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Mbisa, J.L.; Nikolenko, G.N.; Pathak, V.K.
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murine leukemia virus
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Budihas, S.R.; Gorshkova, I.; Gaidamakov, S.; Wamiru, A.; Bona, M.K.; Parniak, M.A.; Crouch, R.J.; McMahon, J.B.; Beutler, J.A.; Le Grice, S.F.J.
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Nucleic Acids Res.
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Human Immunodeficiency Virus
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Hang, J.Q.; Li, Y.; Yang, Y.; Cammack, N.; Mirzadegan, T.; Klumpp, K.
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Biochem. Biophys. Res. Commun.
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Human immunodeficiency virus 1
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Himmel, D.M.; Sarafianos, S.G.; Dharmasena, S.; Hossain, M.M.; McCoy-Simandle, K.; Ilina, T.; Clark, A.D.; Knight, J.L.; Julias, J.G.; Clark, P.K.; Krogh-Jespersen, K.; Levy, R.M.; Hughes, S.H.; Parniak, M.A.; Arnold, E.
HIV-1 reverse transcriptase structure with RNase H inhibitor dihydroxy benzoyl naphthyl hydrazone bound at a novel site
ACS Chem. Biol.
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Human immunodeficiency virus 1 (P03366), Human immunodeficiency virus 1
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Kissel, J.D.; Held, D.M.; Hardy, R.W.; Burke, D.H.
Single-stranded DNA aptamer RT1t49 inhibits RT polymerase and RNase H functions of HIV type 1, HIV type 2, and SIVCPZ RTs
AIDS Res. Hum. Retroviruses
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2007
Human immunodeficiency virus 1, Human immunodeficiency virus 2, Simian immunodeficiency virus
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Marchand, C.; Beutler, J.A.; Wamiru, A.; Budihas, S.; Moellmann, U.; Heinisch, L.; Mellors, J.W.; Le Grice, S.F.; Pommier, Y.
Madurahydroxylactone derivatives as dual inhibitors of human immunodeficiency virus type 1 integrase and RNase H
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Human immunodeficiency virus 1
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Purohit, V.; Roques, B.P.; Kim, B.; Bambara, R.A.
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Human immunodeficiency virus 1
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Takada, K.; Bermingham, A.; OKeefe, B.R.; Wamiru, A.; Beutler, J.A.; Le Grice, S.F.; Lloyd, J.; Gustafson, K.R.; McMahon, J.B.
An HIV RNase H inhibitory 1,3,4,5-tetragalloylapiitol from the African plant Hylodendron gabunensis
J. Nat. Prod.
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Human immunodeficiency virus 1, Human immunodeficiency virus 2
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Dat, N.T.; Bae, K.; Wamiru, A.; McMahon, J.B.; Le Grice, S.F.; Bona, M.; Beutler, J.A.; Kim, Y.H.
A dimeric lactone from Ardisia japonica with inhibitory activity for HIV-1 and HIV-2 ribonuclease H
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Human immunodeficiency virus 1, Human immunodeficiency virus 2
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Lim, D.; Gregorio, G.G.; Bingman, C.; Martinez-Hackert, E.; Hendrickson, W.A.; Goff, S.P.
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Moloney murine leukemia virus
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The HIV-1 reverse transcriptase mutants G190S and G190A, which confer resistance to non-nucleoside reverse transcriptase inhibitors, demonstrate reductions in RNase H activity and DNA synthesis from tRNALys,3 that correlate with reductions in replication effciciency
Virology
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Virus Res.
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Moloney murine leukemia virus, Moloney murine leukemia virus (P03355), Human immunodeficiency virus 1 (P03366), Human immunodeficiency virus 1
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Wendeler, M.; Lee, H.F.; Bermingham, A.; Miller, J.T.; Chertov, O.; Bona, M.K.; Baichoo, N.S.; Ehteshami, M.; Beutler, J.; OKeefe, B.R.; Goette, M.; Kvaratskhelia, M.; Le Grice, S.
Vinylogous ureas as a novel class of inhibitors of reverse transcriptase-associated ribonuclease H activity
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Human immunodeficiency virus 1, Human immunodeficiency virus 2
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Heinrich, J.; Mathur, S.; Matskevich, A.A.; Moelling, K.
Oligonucleotide-mediated retroviral RNase H activation leads to reduced HIV-1 titer in patient-derived plasma
AIDS
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Ehteshami, M.; Goette, M.
Effects of mutations in the connection and RNase H domains of HIV-1 reverse transcriptase on drug susceptibility
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Human immunodeficiency virus 1
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Updegrove, T.; Wilf, N.; Sun, X.; Wartell, R.M.
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Biochemistry
47
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2008
Escherichia coli
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Pena, V.; Rozov, A.; Fabrizio, P.; Luehrmann, R.; Wahl, M.C.
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Moloney murine leukemia virus, Avian sarcoma leukosis virus, Human immunodeficiency virus 1 (P03366)
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Human immunodeficiency virus 1, Human immunodeficiency virus 2
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Roquebert, B.; Marcelin, A.G.
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Human immunodeficiency virus 1
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Characterization of Moloney murine leukaemia virus/avian myeloblastosis virus chimeric reverse transcriptases
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Avian myeloblastosis virus, Moloney murine leukemia virus (P03355), Moloney murine leukemia virus
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Ehteshami, M.; Beilhartz, G.L.; Scarth, B.J.; Tchesnokov, E.P.; McCormick, S.; Wynhoven, B.; Harrigan, P.R.; Goette, M.
Connection domain mutations N348I and A360V in HIV-1 reverse transcriptase enhance resistance to 3-azido-3-deoxythymidine through both RNase H-dependent and -independent mechanisms
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Human immunodeficiency virus 1
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Billamboz, M.; Bailly, F.; Barreca, M.L.; De Luca, L.; Mouscadet, J.F.; Calmels, C.; Andreola, M.L.; Witvrouw, M.; Christ, F.; Debyser, Z.; Cotelle, P.
Design, synthesis, and biological evaluation of a series of 2-hydroxyisoquinoline-1,3(2H,4H)-diones as dual inhibitors of human immunodeficiency virus type 1 integrase and the reverse transcriptase RNase H domain
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Human immunodeficiency virus 1
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Fuji, H.; Urano, E.; Futahashi, Y.; Hamatake, M.; Tatsumi, J.; Hoshino, T.; Morikawa, Y.; Yamamoto, N.; Komano, J.
Derivatives of 5-nitrofuran-2-carboxylic acid carbamoyl methyl ester inhibit RNase H activity associated with HIV-1 reverse transcriptase
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murine leukemia virus
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Sarafianos, S.G.; Marchand, B.; Das, K.; Himmel, D.M.; Parniak, M.A.; Hughes, S.H.; Arnold, E.
Structure and function of HIV-1 reverse transcriptase: molecular mechanisms of polymerization and inhibition
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Human immunodeficiency virus 1
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Rigby, S.T.; Rose, A.E.; Hanson, M.N.; Bambara, R.A.
Mechanism analysis indicates that recombination events in HIV-1 initiate and complete over short distances, explaining why recombination frequencies are similar in different sections of the genome
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Human immunodeficiency virus 1
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Beilhartz, G.L.; Wendeler, M.; Baichoo, N.; Rausch, J.; Le Grice, S.; Goette, M.
HIV-1 Reverse Transcriptase Can Simultaneously Engage Its DNA/RNA Substrate at Both DNA Polymerase and RNase H Active Sites: Implications for RNase H Inhibition
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Human immunodeficiency virus 1
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Bokesch, H.R.; Wamiru, A.; Le Grice, S.F.; Beutler, J.A.; McKee, T.C.; McMahon, J.B.
HIV-1 ribonuclease H inhibitory phenolic glycosides from Eugenia hyemalis
J. Nat. Prod.
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Human immunodeficiency virus 1
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Yu, F.; Liu, X.; Zhan, P.; De Clercq, E.
Recent advances in the research of HIV-1 RNase H inhibitors
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Human immunodeficiency virus 1
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Dash, C.; Scarth, B.J.; Badorrek, C.; Goette, M.; Le Grice, S.F.
Examining the ribonuclease H primer grip of HIV-1 reverse transcriptase by charge neutralization of RNA/DNA hybrids
Nucleic Acids Res.
36
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Human immunodeficiency virus 1
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Li, N.; Wang, Y.; Pothukuchy, A.; Syrett, A.; Husain, N.; Gopalakrisha, S.; Kosaraju, P.; Ellington, A.D.
Aptamers that recognize drug-resistant HIV-1 reverse transcriptase
Nucleic Acids Res.
36
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Human immunodeficiency virus 1 (P03366), Human immunodeficiency virus 1
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Post, K.; Kankia, B.; Gopalakrishnan, S.; Yang, V.; Cramer, E.; Saladores, P.; Gorelick, R.J.; Guo, J.; Musier-Forsyth, K.; Levin, J.G.
Fidelity of plus-strand priming requires the nucleic acid chaperone activity of HIV-1 nucleocapsid protein
Nucleic Acids Res.
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Human immunodeficiency virus 1
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Lee, J.S.; Hattori, M.; Kim, J.
Inhibition of HIV-1 protease and RNase H of HIV-1 reverse transcriptase activities by long chain phenols from the sarcotestas of Ginkgo biloba
Planta Med.
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Human immunodeficiency virus 1
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Santos, A.F.; Lengruber, R.B.; Soares, E.A.; Jere, A.; Sprinz, E.; Martinez, A.M.; Silveira, J.; Sion, F.S.; Pathak, V.K.; Soares, M.A.
Conservation patterns of HIV-1 RT connection and RNase H domains: identification of new mutations in NRTI-treated patients
PLoS ONE
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Human immunodeficiency virus 1
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Abdur, R.; Gerlits, O.O.; Gan, J.; Jiang, J.; Salon, J.; Kovalevsky, A.Y.; Chumanevich, A.A.; Weber, I.T.; Huang, Z.
Novel complex MAD phasing and RNase H structural insights using selenium oligonucleotides
Acta Crystallogr. Sect. D
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2014
Halalkalibacterium halodurans (Q9KEI9), Halalkalibacterium halodurans DSM 18197 (Q9KEI9)
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Kirby, K.A.; Marchand, B.; Ong, Y.T.; Ndongwe, T.P.; Hachiya, A.; Michailidis, E.; Leslie, M.D.; Sietsema, D.V.; Fetterly, T.L.; Dorst, C.A.; Singh, K.; Wang, Z.; Parniak, M.A.; Sarafianos, S.G.
Structural and inhibition studies of the RNase H function of xenotropic murine leukemia virus-related virus reverse transcriptase
Antimicrob. Agents Chemother.
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Human immunodeficiency virus 1, Moloney murine leukemia virus, Xenotropic MuLV-related virus (A1Z651), Xenotropic MuLV-related virus
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Alla, N.R.; Nicholson, A.W.
Evidence for a dual functional role of a conserved histidine in RNA-DNA heteroduplex cleavage by human RNase H1
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Homo sapiens
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Tannous, E.; Yokoyama, K.; You, D.J.; Koga, Y.; Kanaya, S.
A dual role of divalent metal ions in catalysis and folding of RNase H1 from extreme halophilic archaeon Halobacterium sp. NRC-1
FEBS Open Bio
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Halobacterium sp., Halobacterium sp. NRC-1
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Stafford, K.A.; Ferrage, F.; Cho, J.H.; Palmer, A.G.
Side chain dynamics of carboxyl and carbonyl groups in the catalytic function of Escherichia coli ribonuclease H
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Escherichia coli
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Babu, C.S.; Dudev, T.; Lim, C.
Differential role of the protein matrix on the binding of a catalytic aspartate to Mg2+ vs Ca2+: application to ribonuclease H
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Escherichia coli, Moloney murine leukemia virus (P03355)
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Rosen, L.E.; Kathuria, S.V.; Matthews, C.R.; Bilsel, O.; Marqusee, S.
Non-native structure appears in microseconds during the folding of E. coli RNase H
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Escherichia coli (P0A7Y4), Escherichia coli
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Zhou, D.; Chung, S.; Miller, M.; Grice, S.F.; Wlodawer, A.
Crystal structures of the reverse transcriptase-associated ribonuclease H domain of xenotropic murine leukemia-virus related virus
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Xenotropic MuLV-related virus (A1Z651), Xenotropic MuLV-related virus
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Ko, C.; Shin, Y.C.; Park, W.J.; Kim, S.; Kim, J.; Ryu, W.S.
Residues Arg703, Asp777, and Arg781 of the RNase H domain of hepatitis B virus polymerase are critical for viral DNA synthesis
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Hepatitis B virus
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Hayer, J.; Rodriguez, C.; Germanidis, G.; Deleage, G.; Zoulim, F.; Pawlotsky, J.M.; Combet, C.
Ultradeep pyrosequencing and molecular modeling identify key structural features of hepatitis B virus RNase H, a putative target for antiviral intervention
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Hepatitis B virus
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Sipova, H.; Springer, T.; Rejman, D.; Simak, O.; Petrova, M.; Novak, P.; Rosenbergova, S.; Pav, O.; Liboska, R.; Barvik, I.; Stepanek, J.; Rosenberg, I.; Homola, J.
5'-O-Methylphosphonate nucleic acids--new modified DNAs that increase the Escherichia coli RNase H cleavage rate of hybrid duplexes
Nucleic Acids Res.
42
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2014
Escherichia coli
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Tannous, E.; Kanaya, S.
Divalent metal ion-induced folding mechanism of RNase H1 from extreme halophilic archaeon Halobacterium sp. NRC-1
PLoS ONE
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Halobacterium sp. (Q9HSF6), Halobacterium sp., Halobacterium sp. NRC-1 (Q9HSF6)
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Smyshlyaev, G.; Voigt, F.; Blinov, A.; Barabas, O.; Novikova, O.
Acquisition of an Archaea-like ribonuclease H domain by plant L1 retrotransposons supports modular evolution
Proc. Natl. Acad. Sci. USA
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2013
Arabidopsis thaliana
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Nguyen, T.N.; Angkawidjaja, C.; Kanaya, E.; Koga, Y.; Takano, K.; Kanaya, S.
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Sulfurisphaera tokodaii (F9VN79), Sulfurisphaera tokodaii, Sulfurisphaera tokodaii DSM 16993 (F9VN79)
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Leo, B.; Hartl, M.J.; Schweimer, K.; Mayr, F.; Woehrl, B.M.
Insights into the structure and activity of prototype foamy virus RNase H
Retrovirology
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14
2012
Human spumaretrovirus
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Leo, B.; Schweimer, K.; Roesch, P.; Hartl, M.J.; Woehrl, B.M.
The solution structure of the prototype foamy virus RNase H domain indicates an important role of the basic loop in substrate binding
Retrovirology
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73
2012
Human spumaretrovirus (P14350)
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Villa, J.A.; Pike, D.P.; Patel, K.B.; Lomonosova, E.; Lu, G.; Abdulqader, R.; Tavis, J.E.
Purification and enzymatic characterization of the hepatitis B virus ribonuclease H, a new target for antiviral inhibitors
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Hepatitis B virus
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Edwards, T.C.; Mani, N.; Dorsey, B.; Kakarla, R.; Rijnbrand, R.; Sofia, M.J.; Tavis, J.E.
Inhibition of HBV replication by N-hydroxyisoquinolinedione and N-hydroxypyridinedione ribonuclease H inhibitors
Antiviral Res.
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Hepatitis B virus
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Lawler, J.L.; Mukherjee, P.; Coen, D.M.
Herpes simplex virus 1 DNA polymerase RNase H activity acts in a 3'-to-5' direction and is dependent on the 3'-to-5' exonuclease active site
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Human alphaherpesvirus 1
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Kholod, N.; Sivogrivov, D.; Latypov, O.; Mayorov, S.; Kuznitsyn, R.; Kajava, A.V.; Shlyapnikov, M.; Granovsky, I.
Single substitution in bacteriophage T4 RNase H alters the ratio between its exo- and endonuclease activities
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Tequatrovirus T4 (P13319)
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