The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.
High-level resistance to (-) enantiomeric 2'-deoxy-3'-thiacytidine in vitro is due to one amino acid substitution in the catalytic site of human immunodeficiency virus type 1 reverse transcriptase
Open accessAbstract
Passage of human immunodeficiency virus type 1 in the presence of increasing 2'-deoxy-3'-thiacytidine (3TC) concentrations results in high-level (> 100-fold) 3TC-resistant viruses. All 3TC-resistant viruses possess a substitution at the second codon (from a methionine into an isoleucine) at position 184 within the highly conserved motif (YMDD) of human immunodeficiency virus type 1 reverse transcriptase. 3TC-resistant viruses were cross-resistant to the (-) enantiomer of the fluorinated derivative of BCH-189 but remained susceptible to 2',3'-dideoxyinosine and 2',3'-dideoxycytidine. The susceptibilities of the 3TC-resistant viruses to the (+) enantiomers of BCH-189 and the fluorinated derivative of BCH-189 demonstrate an enantiomeric specificity for viruses selected under these conditions. Introduction of an isoleucine substitution at codon 184 into a background of two known 3'-azido-3'-deoxythymidine resistance mutations (amino acids 41 and 215) restored the susceptibility of this virus to 3'-azido-3'-deoxythymidine.
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Sodroski, J. G., Rosen, C. A., & Haseltine, W. A. (1984) · Science · doi:10.1126/science.6330891 · Cited by 770
Coates, J. A., Cammack, N., Jenkinson, H. J., Jowett, A. J., Jowett, M. I., Pearson, B. A., Penn, C. R., Rouse, P. L., Viner, K. C., & Cameron, J. M. (1992) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.36.4.733 · Cited by 240
Self-citation
Cited by
In Vitro Antiretroviral Properties of S/GSK1349572, a Next-Generation HIV Integrase Inhibitor
Kobayashi, M., Yoshinaga, T., Seki, T., Wakasa-Morimoto, C., Brown, K. W., Ferris, R., Foster, S. A., Hazen, R. J., Miki, S., Suyama-Kagitani, A., et al. (2011) · Antimicrobial Agents and Chemotherapy · doi:10.1128/aac.01209-10 · Cited by 382
Comparison of Sequential Three-Drug Regimens as Initial Therapy for HIV-1 Infection
Robbins, G. K., De Gruttola, V., Shafer, R. W., Smeaton, L. M., Snyder, S. W., Pettinelli, C., Dubé, M. P., Fischl, M. A., Pollard, R. B., Delapenha, R., et al. (2003) · New England Journal of Medicine · doi:10.1056/nejmoa030264 · Cited by 351
Molecular mechanisms of HIV-1 resistance to nucleoside reverse transcriptase inhibitors (NRTIs)
Sluis-Cremer, N., Arion, D., & Parniak*, M. A. (2000) · Cellular and Molecular Life Sciences · doi:10.1007/pl00000626 · Cited by 117
Mimtsoudis, I., Tsachouridou, O., Akinosoglou, K., & Metallidis, S. (2024) · Viruses · doi:10.3390/v16091392 · Cited by 13
Byun, H., Papathanasopoulos, M. A., Steegen, K., & Basson, A. E. (2024) · Viruses · doi:10.3390/v16121888 · Cited by 5
Metadata
- Authors
- Boucher, C. A., Cammack, N., Schipper, P., Schuurman, R., Rouse, P., Wainberg, M. A., & Cameron, J. M.
- Venue
- Antimicrobial Agents and Chemotherapy
- Publisher
- American Society for Microbiology
- Published
- 1993-10
- Volume
- 37
- Issue
- 10
- Pages
- 2231-2234
- ISSN
- 0066-4804 (ISSN-L)
- 1098-6596
- OpenAlex
- W2045953763
- Cited by
- 313
- References
- 2
- FWCI
- 12.60
- Type
- journal article
- Language
- en
- Open access
- green
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- CoChat. (2026). Citation check: High-level resistance to (-) enantiomeric 2'-deoxy-3'-thiacytidine in vitro is due to one amino acid substitution in the catalytic site of human immunodeficiency virus type 1 reverse transcriptase. https://app.cochat.ai/papers/10.1128/aac.37.10.2231
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- Boucher, C. A., Cammack, N., Schipper, P., Schuurman, R., Rouse, P., Wainberg, M. A., & Cameron, J. M. (1993). High-level resistance to (-) enantiomeric 2'-deoxy-3'-thiacytidine in vitro is due to one amino acid substitution in the catalytic site of human immunodeficiency virus type 1 reverse transcriptase. Antimicrobial Agents and Chemotherapy. https://doi.org/10.1128/aac.37.10.2231
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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