Structural basis for drug resistance mechanisms for non-nucleoside inhibitors of HIV reverse transcriptase (Q37099790)

18 August 2017

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title

Structural basis for drug resistance mechanisms for non-nucleoside inhibitors of HIV reverse transcriptase (English)

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18 August 2017

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Jingshan Ren

1

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author name string

David K Stammers

series ordinal

2

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18 August 2017

3 March 2008

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18 August 2017

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18 August 2017

134

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18 August 2017

1-2

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18 August 2017

157-170

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The phenylmethylthiazolylthiourea nonnucleoside reverse transcriptase (RT) inhibitor MSK-076 selects for a resistance mutation in the active site of human immunodeficiency virus type 2 RT.

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Crystal structures of clinically relevant Lys103Asn/Tyr181Cys double mutant HIV-1 reverse transcriptase in complexes with ATP and non-nucleoside inhibitor HBY 097.

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Complexes of HIV-1 reverse transcriptase with inhibitors of the HEPT series reveal conformational changes relevant to the design of potent non-nucleoside inhibitors

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Structures of Tyr188Leu mutant and wild-type HIV-1 reverse transcriptase complexed with the non-nucleoside inhibitor HBY 097: inhibitor flexibility is a useful design feature for reducing drug resistance

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The Lys103Asn mutation of HIV-1 RT: a novel mechanism of drug resistance

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Structure of a covalently trapped catalytic complex of HIV-1 reverse transcriptase: implications for drug resistance

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Structure of HIV-1 reverse transcriptase bound to an inhibitor active against mutant reverse transcriptases resistant to other nonnucleoside inhibitors.

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Identification of a putative binding site for [2',5'-bis-O-(tert-butyldimethylsilyl)-beta-D-ribofuranosyl]-3'-spiro-5''-(4''-amino-1'',2''-oxathiole-2'',2''-dioxide)thymine (TSAO) derivatives at the p51-p66 interface of HIV-1 reverse transcriptase.

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Human immunodeficiency virus type 1 reverse transcriptase dimer destabilization by 1-[Spiro[4"-amino-2",2" -dioxo-1",2" -oxathiole-5",3'-[2', 5'-bis-O-(tert-butyldimethylsilyl)-beta-D-ribofuranosyl]]]-3-ethylthy mine

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Structure of the binding site for nonnucleoside inhibitors of the reverse transcriptase of human immunodeficiency virus type 1

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Mechanism of inhibition of HIV-1 reverse transcriptase by nonnucleoside inhibitors.

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Probing nonnucleoside inhibitor-induced active-site distortion in HIV-1 reverse transcriptase by transient kinetic analyses

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L-743, 726 (DMP-266): a novel, highly potent nonnucleoside inhibitor of the human immunodeficiency virus type 1 reverse transcriptase

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10.1016/J.VIRUSRES.2007.12.018

7 January 2021

Identifiers

DOI

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18 August 2017

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PubMed ID

18313784