The A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase Inhibitors (Q27677549)

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

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instance of

scholarly article

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title

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

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main subject

cell biology

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allosteric inhibitor

1 reference

based on heuristic

inferred from title

author

Mamuka Kvaratskhelia

series ordinal

13

object named as

Mamuka Kvaratskhelia

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Alan N Engelman

series ordinal

11

object named as

Alan Engelman

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author name string

Lei Feng

series ordinal

1

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Amit Sharma

series ordinal

2

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Alison Slaughter

series ordinal

3

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Nivedita Jena

series ordinal

4

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Yasuhiro Koh

series ordinal

5

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Nikolozi Shkriabai

series ordinal

6

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Ross C Larue

series ordinal

7

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Pratiq A Patel

series ordinal

8

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Hiroaki Mitsuya

series ordinal

9

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Jacques J Kessl

series ordinal

10

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James R Fuchs

series ordinal

12

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language of work or name

English

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publication date

31 May 2013

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published in

Journal of Biological Chemistry

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volume

288

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issue

22

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page(s)

15813-20

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cites work

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20 March 2017

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

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20 March 2017

Rational design of small-molecule inhibitors of the LEDGF/p75-integrase interaction and HIV replication

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20 March 2017

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20 March 2017

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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20 March 2017

LEDGF/p75 is essential for nuclear and chromosomal targeting of HIV-1 integrase in human cells

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PubMed Central

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Crystal structure of the catalytic domain of HIV-1 integrase: similarity to other polynucleotidyl transferases

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Features and development of Coot

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20 March 2017

Phasercrystallographic software

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PubMed Central

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20 March 2017

Optimal description of a protein structure in terms of multiple groups undergoing TLS motion

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20 March 2017

Refinement of macromolecular structures by the maximum-likelihood method

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20 March 2017

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20 March 2017

Identification of an evolutionarily conserved domain in human lens epithelium-derived growth factor/transcriptional co-activator p75 (LEDGF/p75) that binds HIV-1 integrase

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20 March 2017

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

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29 September 2017

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

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29 September 2017

A novel method for determining the inhibitory potential of anti-HIV drugs

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29 September 2017

An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule

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29 September 2017

Dynamic modulation of HIV-1 integrase structure and function by cellular lens epithelium-derived growth factor (LEDGF) protein

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29 September 2017

Dose-response curve slope sets class-specific limits on inhibitory potential of anti-HIV drugs

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29 September 2017

Retroviral DNA integration: reaction pathway and critical intermediates

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29 September 2017

Structural basis for the recognition between HIV-1 integrase and transcriptional coactivator p75.

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PubMed Central

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29 September 2017

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29 September 2017

LEDGF/p75 interferes with the formation of synaptic nucleoprotein complexes that catalyze full-site HIV-1 DNA integration in vitro: implications for the mechanism of viral cDNA integration

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PubMed Central

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2 June 2018

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21 January 2018

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retrieved

12 December 2020

based on heuristic

inferred from PubMed ID database lookup

Identifiers

DOI

10.1074/JBC.M112.443390

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PMC publication ID

3668738

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PubMed publication ID

23615903

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