The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase (Q34611548)

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English	The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase	scientific article

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scholarly article

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Europe PubMed Central

PubMed publication ID

3 August 2017

The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase (English)

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3 August 2017

allosteric inhibitor

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based on heuristic

inferred from title

Mamuka Kvaratskhelia

15

object named as

Mamuka Kvaratskhelia

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3 August 2017

author name string

Alison Slaughter

1

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3 August 2017

Kellie A Jurado

2

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3 August 2017

Nanjie Deng

3

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3 August 2017

Lei Feng

4

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3 August 2017

Jacques J Kessl

5

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3 August 2017

Nikoloz Shkriabai

6

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3 August 2017

Ross C Larue

7

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3 August 2017

Hind J Fadel

8

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3 August 2017

Pratiq A Patel

9

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3 August 2017

Nivedita Jena

10

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3 August 2017

James R Fuchs

11

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3 August 2017

Eric Poeschla

12

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3 August 2017

Ronald M Levy

13

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3 August 2017

Alan Engelman

14

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3 August 2017

publication date

25 November 2014

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3 August 2017

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3 August 2017

11

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3 August 2017

100

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3 August 2017

copyright license

Creative Commons Attribution 4.0 International

25 November 2014

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April 2022 Public Data File from Crossref

copyright status

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Nucleosomal DNA binding drives the recognition of H3K36-methylated nucleosomes by the PSIP1-PWWP domain

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Allosteric inhibition of HIV-1 integrase activity

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The A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase Inhibitors

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Allosteric integrase inhibitor potency is determined through the inhibition of HIV-1 particle maturation

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Structural basis for high-affinity binding of LEDGF PWWP to mononucleosomes

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HRP2 determines the efficiency and specificity of HIV-1 integration in LEDGF/p75 knockout cells but does not contribute to the antiviral activity of a potent LEDGF/p75-binding site integrase inhibitor

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HIV integrase as a target for antiretroviral therapy

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Small-molecule inhibitors of the LEDGF/p75 binding site of integrase block HIV replication and modulate integrase multimerization

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Psip1/Ledgf p52 binds methylated histone H3K36 and splicing factors and contributes to the regulation of alternative splicing

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New Class of HIV-1 Integrase (IN) Inhibitors with a Dual Mode of Action

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Multimode, Cooperative Mechanism of Action of Allosteric HIV-1 Integrase Inhibitors

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FRET analysis reveals distinct conformations of IN tetramers in the presence of viral DNA or LEDGF/p75.

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Elvitegravir overcomes resistance to raltegravir induced by integrase mutation Y143

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Nucleoprotein intermediates in HIV-1 DNA integration visualized by atomic force microscopy

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A Novel Co-Crystal Structure Affords the Design of Gain-of-Function Lentiviral Integrase Mutants in the Presence of Modified PSIP1/LEDGF/p75

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10.1186/S12977-014-0100-1

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Europe PubMed Central

PubMed publication ID

3 August 2017

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PubMed publication ID

3 August 2017

PubMed publication ID

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3 August 2017

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