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

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

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

http://www.wikidata.org/entity/Q27677549

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Multifunctional facets of retrovirus integrase Distribution and Redistribution of HIV-1 Nucleocapsid Protein in Immature, Mature, and Integrase-Inhibited Virions: a Role for Integrase in Maturation Allosteric Inhibition of Human Immunodeficiency Virus Integrase Dual inhibition of HIV-1 replication by integrase-LEDGF allosteric inhibitors is predominant at the post-integration stage.A new class of multimerization selective inhibitors of HIV-1 integrase Discovery of BI 224436, a Noncatalytic Site Integrase Inhibitor (NCINI) of HIV-1 A New Class of Allosteric HIV-1 Integrase Inhibitors Identified by Crystallographic Fragment Screening of the Catalytic Core Domain Non-catalytic site HIV-1 integrase inhibitors disrupt core maturation and induce a reverse transcription block in target cells Structural Basis for Inhibitor-Induced Aggregation of HIV Integrase A critical role of the C-terminal segment for allosteric inhibitor-induced aberrant multimerization of HIV-1 integrase.The mechanism of H171T resistance reveals the importance of Nδ-protonated His171 for the binding of allosteric inhibitor BI-D to HIV-1 integrase.HIV-1 IN/Pol recruits LEDGF/p75 into viral particles HIV-1 Gag as an Antiviral Target: Development of Assembly and Maturation Inhibitors.Host Factors in Retroviral Integration and the Selection of Integration Target Sites.Methods for the Analyses of Inhibitor-Induced Aberrant Multimerization of HIV-1 Integrase.The Competitive Interplay between Allosteric HIV-1 Integrase Inhibitor BI/D and LEDGF/p75 during the Early Stage of HIV-1 Replication Adversely Affects Inhibitor Potency.Multimodal mechanism of action of allosteric HIV-1 integrase inhibitors.Computational and synthetic approaches for developing Lavendustin B derivatives as allosteric inhibitors of HIV-1 integrase LEDGINs, non-catalytic site inhibitors of HIV-1 integrase: a patent review (2006 - 2014).Allosteric modulation of protein oligomerization: an emerging approach to drug design.HIV-1 integrase multimerization as a therapeutic target.TALEN knockout of the PSIP1 gene in human cells: analyses of HIV-1 replication and allosteric integrase inhibitor mechanism.Allosteric HIV-1 Integrase Inhibitors Lead to Premature Degradation of the Viral RNA Genome and Integrase in Target Cells.Allosteric HIV-1 integrase inhibitors promote aberrant protein multimerization by directly mediating inter-subunit interactions: Structural and thermodynamic modeling studies.HIV-1 Integrase Binds the Viral RNA Genome and Is Essential during Virion Morphogenesis.Indole-based allosteric inhibitors of HIV-1 integrase Pyrazolo[1,5-a]pyrimidine-based macrocycles as novel HIV-1 inhibitors: a patent evaluation of WO2015123182.Minimizing the Contribution of Enterohepatic Recirculation to Clearance in Rat for the NCINI Class of Inhibitors of HIV.Resistance to pyridine-based inhibitor KF116 reveals an unexpected role of integrase in HIV-1 Gag-Pol proteolytic processing.Structure-function analyses unravel distinct effects of allosteric inhibitors of HIV-1 integrase on viral maturation and integration.Quinolines from the cyclocondensation of isatoic anhydride with ethyl acetoacetate: preparation of ethyl 4-hydroxy-2-methylquinoline-3-carboxylate and derivatives Synthesis and Evaluation of Aryl Quinolines as HIV-1 Integrase Multimerization Inhibitors Recent advances in the discovery of small-molecule inhibitors of HIV-1 integrase

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

http://www.wikidata.org/entity/Q27677549

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2013 nî lūn-bûn

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2013 թուականի Մայիսին հրատարակուած գիտական յօդուած

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2013 թվականի մայիսին հրատարակված գիտական հոդված

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2013年の論文

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2013年論文

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2013年論文

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The A128T Resistance Mutation ...... ric HIV-1 Integrase Inhibitors

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The A128T Resistance Mutation ...... ric HIV-1 Integrase Inhibitors

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The A128T Resistance Mutation ...... ric HIV-1 Integrase Inhibitors

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JBC.M112.443390

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Journal of Biological Chemistry

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The A128T Resistance Mutation ...... ric HIV-1 Integrase Inhibitors

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Alan Engelman

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Alison Slaughter

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Amit Sharma

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Hiroaki Mitsuya

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Jacques J Kessl

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James R Fuchs

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Lei Feng

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Nikolozi Shkriabai

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Nivedita Jena

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Pratiq A Patel

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P2860

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

Retroviral intasome assembly and inhibition of DNA strand transfer

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

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

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

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

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

NMRPipe: a multidimensional spectral processing system based on UNIX pipes

Phasercrystallographic software

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15813-20

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10.1074/JBC.M112.443390

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22

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288

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Mamuka Kvaratskhelia

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2013-05-31T00:00:00Z

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23615903

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allosteric inhibitor

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3668738

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