ArticleJournal of virology2005
High sequence conservation of human immunodeficiency virus type 1 reverse transcriptase under drug pressure despite the continuous appearance of mutations.
Article in Journal of virology, 2005. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
27 citing papers in PubMed, 57 citations in OpenAlex.
- Identifying Conserved Regions in HIV-1 Proteins by Entropy Analysis of Sequence Variability.International journal of molecular sciences · 2026Article
- Spontaneous Mutations in HIV-1 Gag, Protease, RT p66 in the First Replication Cycle and How They Appear: Insights from an In Vitro Assay on Mutation Rates and Types.International journal of molecular sciences · 2020Article
- An Alternative HIV-1 Non-Nucleoside Reverse Transcriptase Inhibition Mechanism: Targeting the p51 Subunit.Molecules (Basel, Switzerland) · 2020Article
- Winning the Tug-of-War Between Effector Gene Design and Pathogen Evolution in Vector Population Replacement Strategies.Frontiers in genetics · 2019Review
- Structural and Preclinical Studies of Computationally Designed Non-Nucleoside Reverse Transcriptase Inhibitors for Treating HIV infection.Molecular pharmacology · 2017Article
- Structural Maturation of HIV-1 Reverse Transcriptase-A Metamorphic Solution to Genomic Instability.Viruses · 2016Review
- Novel Mutations L228I and Y232H Cause Nonnucleoside Reverse Transcriptase Inhibitor Resistance in Combinational Pattern.AIDS research and human retroviruses · 2016Article
- Detection of treatment-resistant infectious HIV after genome-directed antiviral endonuclease therapy.Antiviral research · 2016Article
- Structure-based evaluation of non-nucleoside inhibitors with improved potency and solubility that target HIV reverse transcriptase variants.Journal of medicinal chemistry · 2015Article
- Impact of Y181C and/or H221Y mutation patterns of HIV-1 reverse transcriptase on phenotypic resistance to available non-nucleoside and nucleoside inhibitors in China.BMC infectious diseases · 2014Article
- Structure-based evaluation of C5 derivatives in the catechol diether series targeting HIV-1 reverse transcriptase.Chemical biology & drug design · 2014Article
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- Crystal structures of HIV-1 reverse transcriptase with picomolar inhibitors reveal key interactions for drug design.Journal of the American Chemical Society · 2012Article
- Reverse transcriptase substitution at codons 208 and 228 among treatment-experienced HIV-1 subtype-C-infected Indian patients is strongly associated with thymidine analogue mutations.Journal of acquired immune deficiency syndromes (1999) · 2012Article
- Analysis of selection pressure and mutational pattern of HIV type 1 reverse transcriptase region among treated and nontreated patients.AIDS research and human retroviruses · 2010Article
- Short communication: Nucleotide variation and positively selected sites in HIV type 1 reverse transcriptase among heterosexual transmission pairs.AIDS research and human retroviruses · 2010Article
- Co-lethality studied as an asset against viral drug escape: the HIV protease case.Biology direct · 2010Article
- HIV-1 RT Inhibitors with a Novel Mechanism of Action: NNRTIs that Compete with the Nucleotide Substrate.Viruses · 2010Article
- Nonpolymorphic human immunodeficiency virus type 1 protease and reverse transcriptase treatment-selected mutations.Antimicrobial agents and chemotherapy · 2009Article
Corrections and comments
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Authors and funding
13 authors at 6 institutions in 4 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
To define the extent of sequence conservation in human immunodeficiency virus type 1 (HIV-1) reverse transcriptase (RT) in vivo, the first 320 amino acids of RT obtained from 2,236 plasma-derived samples from a well-defined cohort of 1,704 HIV-1-infected individuals (457 drug naïve and 1,247 drug treated) were analyzed and examined in structural terms. In naïve patients, 233 out of these 320 residues (73%) were conserved (<1% variability). The majority of invariant amino acids clustered into defined regions comprising between 5 and 29 consecutive residues. Of the nine longest invariant regions identified, some contained residues and domains critical for enzyme stability and function. In patients treated with RT inhibitors, despite profound drug pressure and the appearance of mutations primarily associated with resistance, 202 amino acids (63%) remained highly conserved and appeared mostly distributed in regions of variable length. This finding suggests that participation of consecutive residues in structural domains is strictly required for cooperative functions and sustainability of HIV-1 RT activity. Besides confirming the conservation of amino acids that are already known to be important for catalytic activity, stability of the heterodimer interface, and/or primer/template binding, the other 62 new invariable residues are now identified and mapped onto the three-dimensional structure of the enzyme. This new knowledge could be of help in the structure-based design of novel resistance-evading drugs.
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