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A new class of multimerization selective inhibitors of HIV-1 integrase

A new class of multimerization selective inhibitors of HIV-1 integrase

http://www.wikidata.org/entity/Q27683994

about

Distribution and Redistribution of HIV-1 Nucleocapsid Protein in Immature, Mature, and Integrase-Inhibited Virions: a Role for Integrase in Maturation Multiple cellular proteins interact with LEDGF/p75 through a conserved unstructured consensus motif A New Class of Allosteric HIV-1 Integrase Inhibitors Identified by Crystallographic Fragment Screening of the Catalytic Core Domain Retroviral Integrase: Then and Now Structural Basis for Inhibitor-Induced Aggregation of HIV Integrase Retroviral DNA Integration A critical role of the C-terminal segment for allosteric inhibitor-induced aberrant multimerization of HIV-1 integrase.Small-molecule inhibitors of protein-protein interactions: progressing toward the reality.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 Uneven genetic robustness of HIV-1 integrase.Alternative modulation of protein-protein interactions by small molecules 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.LEDGIN-mediated Inhibition of Integrase-LEDGF/p75 Interaction Reduces Reactivation of Residual Latent HIV Computational and synthetic approaches for developing Lavendustin B derivatives as allosteric inhibitors of HIV-1 integrase HIV-1 integrase multimerization as a therapeutic target.Different Pathways Leading to Integrase Inhibitors Resistance 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.Aligning Potency and Pharmacokinetic Properties for Pyridine-Based NCINIs.Indole-based allosteric inhibitors of HIV-1 integrase Rational Design, Synthesis and Evaluation of Coumarin Derivatives as Protein-protein Interaction Inhibitors.Pyrazolo[1,5-a]pyrimidine-based macrocycles as novel HIV-1 inhibitors: a patent evaluation of WO2015123182.Deep analysis of HIV-1 natural variability across HIV-1 variants at residues associated with integrase inhibitor (INI) resistance in INI-naive individuals.Resistance to pyridine-based inhibitor KF116 reveals an unexpected role of integrase in HIV-1 Gag-Pol proteolytic processing.The HIV-1 integrase-LEDGF allosteric inhibitor MUT-A: resistance profile, impairment of virus maturation and infectivity but without influence on RNA packaging or virus immunoreactivity.Cellular and molecular mechanisms of HIV-1 integration targeting.Structure-function analyses unravel distinct effects of allosteric inhibitors of HIV-1 integrase on viral maturation and integration.CLIP-related methodologies and their application to retrovirology.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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P2860

A new class of multimerization selective inhibitors of HIV-1 integrase

http://www.wikidata.org/entity/Q27683994

description

2014 nî lūn-bûn

@nan

2014 թուականի Մայիսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի մայիսին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

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2014年論文

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2014年論文

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2014年論文

@zh-mo

2014年論文

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2014年论文

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name

A new class of multimerization selective inhibitors of HIV-1 integrase

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A new class of multimerization selective inhibitors of HIV-1 integrase

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A new class of multimerization selective inhibitors of HIV-1 integrase

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type

label

A new class of multimerization selective inhibitors of HIV-1 integrase

@ast

A new class of multimerization selective inhibitors of HIV-1 integrase

@en

A new class of multimerization selective inhibitors of HIV-1 integrase

@nl

prefLabel

A new class of multimerization selective inhibitors of HIV-1 integrase

@ast

A new class of multimerization selective inhibitors of HIV-1 integrase

@en

A new class of multimerization selective inhibitors of HIV-1 integrase

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JOURNAL.PPAT.1004171

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A new class of multimerization selective inhibitors of HIV-1 integrase

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Amit Sharma

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Eric Poeschla

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Frances Male

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Frederic D Bushman

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Hind J Fadel

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Jacques J Kessl

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James R Fuchs

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Lei Feng

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Mamuka Kvaratskhelia

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

Nirav Malani

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

P2860

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

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

Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2−ΔΔCT Method

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

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

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

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

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e1004171

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scholarly article

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10.1371/JOURNAL.PPAT.1004171

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5

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10

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Alison Slaughter

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2014-05-29T00:00:00Z

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24874515

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4038613

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