(PDF) Mutations in the Connection Domain of HIV-1 Reverse

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 - United States

doi 10.1073/pnas.0609642104

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Date

December 19, 2006

Authors

G. N. Nikolenko

K. A. Delviks-Frankenberry

Publisher

Proceedings of the National Academy of Sciences

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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 - United States

doi 10.1073/pnas.0609642104

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Connection Domain Mutations N348I and A360V in HIV-1 Reverse Transcriptase Enhance Resistance to 3′-Azido-3′-Deoxythymidine Through Both RNase H-Dependent and -Independent Mechanisms

Connection Domain Mutations in HIV-1 Reverse Transcriptase Do Not Impact Etravirine Susceptibility and Virologic Responses to Etravirine-Containing Regimens

The Antiretrovirus Drug 3'-Azido-3'-Deoxythymidine Increases the Retrovirus Mutation Rate.

Sanctuary Growth of Human Immunodeficiency Virus in the Presence of 3'-Azido-3'-Deoxythymidine.

Comparison of the Intracellular Metabolism of 3′-Azido-3′-Deoxythymidine and 3′-Fluoro-3′-Deoxythymidine in Lymphocytes in the Presence of 5-Fluoro-2′-Deoxyuridine

Primer ID Informs Next-Generation Sequencing Platforms and Reveals Preexisting Drug Resistance Mutations in the HIV-1 Reverse Transcriptase Coding Domain

Mutations at Codon 184 in Simian Immunodeficiency Virus Reverse Transcriptase Confer Resistance to the (-) Enantiomer of 2',3'-Dideoxy-3'-Thiacytidine.

In Vivo Efficacy of Zidovudine (3'-Azido-3'-Deoxythymidine) in Experimental Gram-Negative-Bacterial Infections.

Identification of a 3-Aminoimidazo[1,2-A]pyridine Inhibitor of HIV-1 Reverse Transcriptase