An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule.
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Crystal structure of the HIV-1 integrase core domain in complex with sucrose reveals details of an allosteric inhibitory binding siteDiscovery of an allosteric mechanism for the regulation of HCV NS3 protein functionThe A128T Resistance Mutation Reveals Aberrant Protein Multimerization as the Primary Mechanism of Action of Allosteric HIV-1 Integrase InhibitorsMultimode, Cooperative Mechanism of Action of Allosteric HIV-1 Integrase InhibitorsNew Class of HIV-1 Integrase (IN) Inhibitors with a Dual Mode of ActionA new class of multimerization selective inhibitors of HIV-1 integraseA symmetric region of the HIV-1 integrase dimerization interface is essential for viral replicationNon-catalytic site HIV-1 integrase inhibitors disrupt core maturation and induce a reverse transcription block in target cellsArchitecture of a full-length retroviral integrase monomer and dimer, revealed by small angle X-ray scattering and chemical cross-linkingMolecular 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 LEDGINsThe 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 substratesMethods 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 ResistanceSmall-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.
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
P2093
P2860
P356
P1476
An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule.
@en
P2093
Christopher J McKee
Jacques J Kessl
Jocelyn O Eidahl
Nikolozi Shkriabai
Sonja Hess
Terrence R Burke
Zhuojun Zhao
P2860
P304
P356
10.1124/MOL.109.058883
P577
2009-07-28T00:00:00Z