HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase. - Wikidata - wikimedia - TriplyDB

HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase.

HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase.

http://www.wikidata.org/entity/Q35267783

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HIV-1 integrase crosslinked oligomers are active in vitro HIV-1 integrase inhibitor resistance and its clinical implications Retroviral intasome assembly and inhibition of DNA strand transfer Multifunctional facets of retrovirus integrase Structural and Functional Analyses of the Second-Generation Integrase Strand Transfer Inhibitor Dolutegravir (S/GSK1349572)3′-Processing and strand transfer catalysed by retroviral integrasein crystallo Structural Basis of Mos1 Transposase Inhibition by the Anti-retroviral Drug Raltegravir A historical sketch of the discovery and development of HIV-1 integrase inhibitors Human immunodeficiency virus type 1 integrase: arrangement of protein domains in active cDNA complexes.Specific inhibition of human immunodeficiency virus type 1 (HIV-1) integration in cell culture: putative inhibitors of HIV-1 integrase Unprocessed viral DNA could be the primary target of the HIV-1 integrase inhibitor raltegravir Engineered hyperactive integrase for concerted HIV-1 DNA integration In-Silico docking of HIV-1 integrase inhibitors reveals a novel drug type acting on an enzyme/DNA reaction intermediate.The Role of Caveolin 1 in HIV Infection and Pathogenesis.Identification of an inhibitor-binding site to HIV-1 integrase with affinity acetylation and mass spectrometry.Impact of Y143 HIV-1 integrase mutations on resistance to raltegravir in vitro and in vivo.Subunit-specific protein footprinting reveals significant structural rearrangements and a role for N-terminal Lys-14 of HIV-1 Integrase during viral DNA binding Solution conformations of prototype foamy virus integrase and its stable synaptic complex with U5 viral DNA.Preclinical profile of BI 224436, a novel HIV-1 non-catalytic-site integrase inhibitor HIV-1 IN inhibitors: 2010 update and perspectives Biochemical and pharmacological analyses of HIV-1 integrase flexible loop mutants resistant to raltegravir Use of patient-derived human immunodeficiency virus type 1 integrases to identify a protein residue that affects target site selection Solution conformation and dynamics of the HIV-1 integrase core domain.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.Therapeutic strategies underpinning the development of novel techniques for the treatment of HIV infection.Diketo acid inhibitor mechanism and HIV-1 integrase: implications for metal binding in the active site of phosphotransferase enzymes.Structure-based modeling of the functional HIV-1 intasome and its inhibition Structure-based HIV-1 integrase inhibitor design: a future perspective.Inhibition of human immunodeficiency virus type 1 integration by diketo derivatives S/GSK1349572, a new integrase inhibitor for the treatment of HIV: promises and challenges.New first and second generation inhibitors of human immunodeficiency virus-1 integrase.Large-scale conformational dynamics of the HIV-1 integrase core domain and its catalytic loop mutants Division of labor within human immunodeficiency virus integrase complexes: determinants of catalysis and target DNA capture HIV integrase, a brief overview from chemistry to therapeutics.HIV-1 antiretroviral resistance: scientific principles and clinical applications Retroviral DNA integration: reaction pathway and critical intermediates.Raltegravir is a substrate for SLC22A6: a putative mechanism for the interaction between raltegravir and tenofovir The road to HIV-1 integrase inhibitors: the case for supporting basic research.Retroviral Integrase Structure and DNA Recombination Mechanism In search of authentic inhibitors of HIV-1 integration.

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P2860

HIV-1 integrase inhibitors that compete with the target DNA substrate define a unique strand transfer conformation for integrase.

http://www.wikidata.org/entity/Q35267783

description

2000 nî lūn-bûn

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2000 թուականի Հոկտեմբերին հրատարակուած գիտական յօդուած

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2000 թվականի հոտեմբերին հրատարակված գիտական հոդված

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2000年の論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年論文

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2000年论文

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HIV-1 integrase inhibitors tha ...... er conformation for integrase.

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HIV-1 integrase inhibitors tha ...... er conformation for integrase.

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HIV-1 integrase inhibitors tha ...... er conformation for integrase.

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Proceedings of the National Academy of Sciences of the United States of America

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HIV-1 integrase inhibitors tha ...... er conformation for integrase.

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P2093

Anthony N

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Cole JL

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Egbertson M

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Espeseth AS

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Felock P

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Grobler J

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Hamill T

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Hazuda DJ

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Melamed JY

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Witmer M

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P2860

Atomic resolution structures of the core domain of avian sarcoma virus integrase and its D64N mutant

Structure of the HIV-1 integrase catalytic domain complexed with an inhibitor: a platform for antiviral drug design

X-ray structure of simian immunodeficiency virus integrase containing the core and C-terminal domain (residues 50-293)--an initial glance of the viral DNA binding platform

Inhibitors of strand transfer that prevent integration and inhibit HIV-1 replication in cells

Differential inhibition of HIV-1 preintegration complexes and purified integrase protein by small molecules

Human immunodeficiency virus integration protein expressed in Escherichia coli possesses selective DNA cleaving activity

Crystal structures of catalytic core domains of retroviral integrases and role of divalent cations in enzymatic activity.

Inhibitors of human immunodeficiency virus integrase.

Identification of discrete functional domains of HIV-1 integrase and their organization within an active multimeric complex.

A stable complex between integrase and viral DNA ends mediates human immunodeficiency virus integration in vitro

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11244-11249

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10.1073/PNAS.200139397

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21

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97

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24448504

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11016953

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