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About 10,000 papers for “Reverse transcriptase”

reverse transcriptase

2024

Citation: 'reverse transcriptase' in the IUPAC Compendium of Chemical Terminology, 5th ed.; International Union of Pure and Applied Chemistry; 2025. Online version 5.0.0, 2025. 10.1351/goldbook.09724 • License: The IUPAC Gold Book is licensed under Creative Commons Attribution-ShareAlike CC BY-SA 4.0 International for individual terms. Requests for commercial usage of the compendium should be directed to IUPAC.

Cited by 0Open access

Reverse Transcriptase

Gary F. Gerard, Donna K. Fox, Margret Nathan et al. · Molecular Biotechnology · 1997

Cited by 116

Reverse Transcriptase

National Cancer Institute · Definitions · 2020

Ope n Pe e r Re v ie w on Qe ios Ope

Cited by 26Open access

Reverse Transcriptase

R T D'aquila, D Zhang, A M Caliendo et al. · 1993

transcriptase. immunodeficiency virus type 1 reverse by a mutation in codon 65 of the human Resistance to 2',3'-dideoxycytidine conferred

Cited by 0

Reverse Transcriptase

Mark A. Wainberga B C · 2016

The emergence of HIV-1 drug resistance remains a major obstacle in antiviral therapy. M184I/V and E138K are signature muta-tions of clinical relevance in HIV-1 reverse transcriptase (RT) for the nucleoside reverse transcriptase inhibitors (NRTIs) lami-vudine (3TC) and emtricitabine (FTC) and the second-generation (new) nonnucleoside reverse transcriptase inhibitor (NNRTI) rilpivirine (RPV), respectively, and the E138Kmutation has also been shown to be selected by etravirine in cell culture. The E138Kmutation was recently shown to compensate for the low enzyme processivity and viral fitness associated with the M184I/Vmutations through enhanced deoxynucleoside triphosphate (dNTP) usage, while the M184I/Vmutations compensated for defects in polymerization rates associated with the E138Kmutations under conditions of high dNTP concentrations. The M184I mutation was also shown to enhance resistance to RPV and ETR when present together with the E138Kmutation. These mutual compensatory effects might also enhance transmission rates of viruses containing these twomutations. Therefore, we performed tissue culture studies to investigate the evolutionary dynamics of these viruses. Through experiments in which E138K-containing viruses were selected with 3TC-FTC and in whichM184I/V viruses were selected with ETR, we demonstrated that ETR was able to select for the E138Kmutation in viruses containing theM184I/Vmutations and that the M184I/Vmuta-tions consistently emerged when E138K viruses were selected with 3TC-FTC.We also performed biochemical subunit-selective mutational analyses to investigate the impact of the E138Kmutation on RT function and interactions with theM184I mutation. We now show that the E138Kmutation decreased rates of polymerization, impaired RNase H activity, and conferred ETR resis-

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