An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule. - Wikidata - awgldk - TriplyDB

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

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

http://www.wikidata.org/entity/Q33488152

about

Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding site Discovery of an allosteric mechanism for the regulation of HCV NS3 protein function The A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase Inhibitors Multimode, Cooperative Mechanism of Action of Allosteric HIV-1 Integrase Inhibitors New Class of HIV-1 Integrase (IN) Inhibitors with a Dual Mode of Action A new class of multimerization selective inhibitors of HIV-1 integrase A symmetric region of the HIV-1 integrase dimerization interface is essential for viral replication Non-catalytic site HIV-1 integrase inhibitors disrupt core maturation and induce a reverse transcription block in target cells Architecture of a full-length retroviral integrase monomer and dimer, revealed by small angle X-ray scattering and chemical cross-linking Molecular modeling study on the allosteric inhibition mechanism of HIV-1 integrase by LEDGF/p75 binding site inhibitors.A cooperative and specific DNA-binding mode of HIV-1 integrase depends on the nature of the metallic cofactor and involves the zinc-containing N-terminal domain.LEDGF/p75-independent HIV-1 replication demonstrates a role for HRP-2 and remains sensitive to inhibition by LEDGINs The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase.Allosteric inhibitor development targeting HIV-1 integrase.FRET analysis reveals distinct conformations of IN tetramers in the presence of viral DNA or LEDGF/p75.Kuwanon-L as a New Allosteric HIV-1 Integrase Inhibitor: Molecular Modeling and Biological Evaluation.Architecture and assembly of HIV integrase multimers in the absence of DNA substrates Methods for the Analyses of Inhibitor-Induced Aberrant Multimerization of HIV-1 Integrase.Allosteric inhibition of HIV-1 integrase activity.Multimodal mechanism of action of allosteric HIV-1 integrase inhibitors.HIV-1 Integrase-DNA Recognition Mechanisms.Allosteric modulation of protein oligomerization: an emerging approach to drug design."Old Dogs with New Tricks": exploiting alternative mechanisms of action and new drug design strategies for clinically validated HIV targets.HIV-1 integrase multimerization as a therapeutic target.Nuclear landscape of HIV-1 infection and integration.Different Pathways Leading to Integrase Inhibitors Resistance Small-molecule inhibitors of the LEDGF/p75 binding site of integrase block HIV replication and modulate integrase multimerization.Inhibiting the HIV integration process: past, present, and the future.Prospective strategies for targeting HIV-1 integrase function.Development of an AlphaScreen-based HIV-1 integrase dimerization assay for discovery of novel allosteric inhibitors.

P2860

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P2860

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

http://www.wikidata.org/entity/Q33488152

description

2009 nî lūn-bûn

@nan

2009 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի հուլիսին հրատարակված գիտական հոդված

@hy

2009年の論文

@ja

2009年論文

@yue

2009年論文

@zh-hant

2009年論文

@zh-hk

2009年論文

@zh-mo

2009年論文

@zh-tw

2009年论文

@wuu

name

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

@ast

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

@en

type

label

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

@ast

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

@en

prefLabel

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

@ast

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

@en

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P1433

Molecular Pharmacology

P1476

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

@en

P2093

Christopher J McKee

http://www.w3.org/2001/XMLSchema#string

Jacques J Kessl

http://www.w3.org/2001/XMLSchema#string

Jocelyn O Eidahl

http://www.w3.org/2001/XMLSchema#string

Nikolozi Shkriabai

http://www.w3.org/2001/XMLSchema#string

Sonja Hess

http://www.w3.org/2001/XMLSchema#string

Terrence R Burke

http://www.w3.org/2001/XMLSchema#string

Zhuojun Zhao

http://www.w3.org/2001/XMLSchema#string

P2860

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

HIV-1 integrase crosslinked oligomers are active in vitro

LEDGF/p75 functions downstream from preintegration complex formation to effect gene-specific HIV-1 integration

Crystal structure of the HIV-1 integrase catalytic core and C-terminal domains: A model for viral DNA binding

Identification of a small-molecule binding site at the dimer interface of the HIV integrase catalytic domain

Structure of a two-domain fragment of HIV-1 integrase: implications for domain organization in the intact protein.

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

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

HIV-1 integrase forms stable tetramers and associates with LEDGF/p75 protein in human cells

An essential role for LEDGF/p75 in HIV integration

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824-832

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scholarly article

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10.1124/MOL.109.058883

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4

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P478

76

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Mamuka Kvaratskhelia

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2009-07-28T00:00:00Z

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P5875

26701477

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P698

19638533

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P921

allosteric inhibitor

P932

2769043

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