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Article

Mutations in the connection domain of HIV-1 reverse transcriptase increase 3'-azido-3'-deoxythymidine resistance.

Proceedings of the National Academy of Sciences of the United States of America - 2 Jan 2007

Nikolenko Galina N, Delviks-Frankenberry Krista A, Palmer Sarah, Maldarelli Frank, Fivash Matthew J, Coffin John M, Pathak Vinay K

Abstract excerpt

We previously proposed that a balance between nucleotide excision and template RNA degradation plays an important role in nucleoside reverse transcriptase inhibitor (NRTI) resistance. To explore the predictions of this concept, we analyzed the role of patient-derived C-terminal domains of HIV-1 reverse transcriptase (RT) in NRTI resistance. We found that when the polymerase domain contained previously described...

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Share to Acquired Immunodeficiency Syndrome
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Methodology Data sources Editorial policy Privacy About Contact Helena Bioinformatics

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Share to Protein Structure, Tertiary

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Source

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Identifiers

PMID: 17179211
DOI: 10.1073/pnas.0609642104
PMCID: PMC1765458

Provenance

PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-07.1.

Source receipt: pubmed, retrieved 7 Sept 2026.

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Mutations in the connection domain of HIV-1 reverse transcriptase increase 3'-azido-3'-deoxythymidine resistance.PMID 17179211Read ↗

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