EC Number   |
Application |
Reference |
|---|
   3.1.26.13 | analysis |
use of 6-phenylpyrrolocytidine as a sensitive fluorescent reporter group being non-disruptive to structure and the enzymatic activity of RNase H. A RNA/DNA hybrid possessing a single 6-phenylpyrrolocytidine insert is an excellent substrate for HIV-1 RT Ribonuclease H and rapidly reports cleavage of the RNA strand with a 14-fold increase in fluorescence intensity. The 6-phenylpyrrolocytidine-based assay for RNase H is superior to the traditional molecular beacon approach in terms of responsiveness, rapidity and ease. The assay is amenable to high-throughput microplate assay format |
710144 |
| 3.1.26.13 | analysis |
use of a commercially available computed radiography system for dental radiography to produce images from radiolabeled polyacrylamide gel electrophoresis assays and its application for quantitative analyses of the human immunodeficiency virus type 1 reverse transcriptase polymerase-independent ribonuclease H activity monitored by PAGE analysis. The methodology allows quantifying effectively the RNase H catalyses and the obtained data are in good agreement with previous reference works |
710132 |
| 3.1.26.13 | drug development |
RNase H activity is an attractive target for a new class of antiviral drugs |
714475 |
| 3.1.26.13 | drug development |
the enzyme is a drug target |
751686 |
| 3.1.26.13 | drug development |
the enzyme is a target for the development of effective dual HIV-1 IN and RNase H inhibitors |
751811 |
| 3.1.26.13 | drug development |
the HIV RT-associated RNase H is avaluable drug target |
750471 |
| 3.1.26.13 | medicine |
activating the RNase H prematurely inside the virus particles destroys the viral genome and abrogates viral infectivity |
728934 |
| 3.1.26.13 | medicine |
genotypical and statistical analyzes in HIV-1 reverse transcriptase from antiretroviral treatment-naive and antiretroviral treatment-experienced patients. Within the RNase H domain, change K451 is present in 11% of treatment-experienced patients, but not in treatment-naive patients |
695644 |
| 3.1.26.13 | medicine |
the E312Q, G333E, G335D, V365I, A371V and A376S substitutions in RNase H subdomain of HIV-1 reverse transcriptase are present in 26% of subtype B, whereas the G335D and A371V substitutions are commonly observed in 69% and 75% of non-B HIV-1 isolates, respectively. A significant decline is observed in the viral loads of patients that are infected with HIV-1 carrying these substitutions and are subsequently treated with triple drug regimens, even in the case where zidovudine is included in such regimens. Generally, such single substitutions at the connection subdomain or RNase H domain have no influence on drug susceptibility in vitro by themselves. Instead, they generally enhance zidovudine resistance in the presence of excision-enhancing mutations. However, N348I, A376S and Q509L do confer varying amounts of nevirapine resistance by themselves, even in the absence of excision-enhancing mutations |
707178 |
| 3.1.26.13 | medicine |
within the RNase domain, mutation K451R is present in viral isolates of 11% of antiviral treatment-experienced patients but remaining 100% conserved among treatment-naive patients |
695644 |
