(PDF) Connection Domain Mutations N348I and A360V in HIV-1

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

Journal of Biological Chemistry - United States

doi 10.1074/jbc.m803521200

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Date

June 10, 2008

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American Society for Biochemistry & Molecular Biology (ASBMB)

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Amanote Research

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

Journal of Biological Chemistry - United States

doi 10.1074/jbc.m803521200

Full Text

Abstract

Categories

Date

Authors

Publisher

Related search

Mutations in the Connection Domain of HIV-1 Reverse Transcriptase Increase 3'-Azido-3'-Deoxythymidine Resistance

N348I in HIV-1 Reverse Transcriptase Decreases Susceptibility to Tenofovir and Etravirine in Combination With Other Resistance Mutations

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

Combinatorial Selection, Inhibition, and Antiviral Activity of DNA Thioaptamers Targeting the RNase H Domain of HIV-1 Reverse Transcriptase†

RNase H Domain Mutations Affect the Interaction Between Moloney Murine Leukemia Virus Reverse Transcriptase and Its Primer-Template.

Mn2+ Suppressor Mutations and Biochemical Communication Between Ty1 Reverse Transcriptase and RNase H Domains

3-Hydroxypyrimidine-2,4-Diones as Selective Active Site Inhibitors of HIV Reverse Transcriptase-Associated RNase H: Design Synthesis, and Biochemical Evaluations

3-Hydroxypyrimidine-2,4-Diones as Selective Active Site Inhibitors of HIV Reverse Transcriptase-Associated RNase H: Design Synthesis, and Biochemical Evaluations

Template-Primer Binding Affinity and RNase H Cleavage Specificity Contribute to the Strand Transfer Efficiency of HIV-1 Reverse Transcriptase