Mechanism by which a Glutamine to Leucine Substitution at Residue 509 in the Ribonuclease H Domain of HIV-1 Reverse Transcriptase Confers Zidovudine Resistance-Reference-Cited by-同舟云学术

Mechanism by which a Glutamine to Leucine Substitution at Residue 509 in the Ribonuclease H Domain of HIV-1 Reverse Transcriptase Confers Zidovudine Resistance

Published:2008-12-09 Issue:52 Volume:47 Page:14020-14027
ISSN:0006-2960
Container-title:Biochemistry
language:en
Short-container-title:Biochemistry

Author:

Brehm Jessica H.¹,Mellors John W.¹,Sluis-Cremer Nicolas¹

Affiliation:

1. Department of Medicine, Division of Infectious Diseases, University of Pittsburgh, Pittsburgh, Pennsylvania 15261, Graduate School of Public Health, Department of Infectious Diseases and Microbiology, University of Pittsburgh, Pittsburgh, Pennsylvania 15261

Publisher

American Chemical Society (ACS)

Subject

Biochemistry

Link

https://pubs.acs.org/doi/pdf/10.1021/bi8014778

Reference30 articles.

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2. Mechanism for nucleoside analog-mediated abrogation of HIV-1 replication: Balance between RNase H activity and nucleotide excision

3. Relationship between mutations in HIV-1 RNase H domain and nucleoside reverse transcriptase inhibitors resistance mutations in naïve and pre-treated HIV infected patients

4. Selection of Mutations in the Connection and RNase H Domains of Human Immunodeficiency Virus Type 1 Reverse Transcriptase That Increase Resistance to 3′-Azido-3′-Dideoxythymidine

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