HIV-1 integrase crosslinked oligomers are active in vitro - Wikidata - awgldk - TriplyDB

HIV-1 integrase crosslinked oligomers are active in vitro

HIV-1 integrase crosslinked oligomers are active in vitro

http://www.wikidata.org/entity/Q24556625

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Dynamic dissociating homo-oligomers and the control of protein function Virological and cellular roles of the transcriptional coactivator LEDGF/p75 Structural basis for functional tetramerization of lentiviral integrase DNA minicircles clarify the specific role of DNA structure on retroviral integration Functional and structural characterization of the integrase from the prototype foamy virus A Novel Co-Crystal Structure Affords the Design of Gain-of-Function Lentiviral Integrase Mutants in the Presence of Modified PSIP1/LEDGF/p75 A possible role for the asymmetric C-terminal domain dimer of Rous sarcoma virus integrase in viral DNA binding Retroviral Integrase: Then and Now Functional coupling between HIV-1 integrase and the SWI/SNF chromatin remodeling complex for efficient in vitro integration into stable nucleosomes Retroviral DNA Integration Biochemical Characterization of Kat1: a Domesticated hAT-Transposase that Induces DNA Hairpin Formation and MAT-Switching LEDGF dominant interference proteins demonstrate prenuclear exposure of HIV-1 integrase and synergize with LEDGF depletion to destroy viral infectivity HIV virions as nanoscopic test tubes for probing oligomerization of the integrase enzyme.Structural basis for HIV-1 DNA integration in the human genome, role of the LEDGF/P75 cofactor Architecture of a full-length retroviral integrase monomer and dimer, revealed by small angle X-ray scattering and chemical cross-linking In vitro recombination catalyzed by bacterial class 1 integron integrase IntI1 involves cooperative binding and specific oligomeric intermediates Efficient and specific internal cleavage of a retroviral palindromic DNA sequence by tetrameric HIV-1 integrase.The lentiviral integrase binding protein LEDGF/p75 and HIV-1 replication.Mass spectrometry-based footprinting of protein-protein interactions An unusual helix turn helix motif in the catalytic core of HIV-1 integrase binds viral DNA and LEDGF.An allosteric mechanism for inhibiting HIV-1 integrase with a small molecule.The HIV-1 integrase mutations Y143C/R are an alternative pathway for resistance to Raltegravir and impact the enzyme functions.Novel approaches to inhibiting HIV-1 replication.Solution conformations of prototype foamy virus integrase and its stable synaptic complex with U5 viral DNA.GCN2 phosphorylates HIV-1 integrase and decreases HIV-1 replication by limiting viral integration.The HIV-1 integrase α4-helix involved in LTR-DNA recognition is also a highly antigenic peptide element Changes in the accessibility of the HIV-1 Integrase C-terminus in the presence of cellular proteins.Biochemical and pharmacological analyses of HIV-1 integrase flexible loop mutants resistant to raltegravir 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.Structural properties of HIV integrase. Lens epithelium-derived growth factor oligomers.Resistance to integrase inhibitors.Structure-based modeling of the functional HIV-1 intasome and its inhibition Retrovirus Integrase-DNA Structure Elucidates Concerted Integration Mechanisms.Physical trapping of HIV-1 synaptic complex by different structural classes of integrase strand transfer inhibitors.Peptides that inhibit HIV-1 integrase by blocking its protein-protein interactions.Retroviral DNA integration: reaction pathway and critical intermediates.Relationship between the oligomeric status of HIV-1 integrase on DNA and enzymatic activity.Retroviral integrase proteins and HIV-1 DNA integration Retroviral Integrase Structure and DNA Recombination Mechanism Allosteric inhibitor development targeting HIV-1 integrase.

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P2860

HIV-1 integrase crosslinked oligomers are active in vitro

http://www.wikidata.org/entity/Q24556625

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2005 nî lūn-bûn

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2005 թուականին հրատարակուած գիտական յօդուած

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2005 թվականին հրատարակված գիտական հոդված

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2005年の論文

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年学术文章

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2005年學術文章

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name

HIV-1 integrase crosslinked oligomers are active in vitro

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HIV-1 integrase crosslinked oligomers are active in vitro

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HIV-1 integrase crosslinked oligomers are active in vitro

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type

label

HIV-1 integrase crosslinked oligomers are active in vitro

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HIV-1 integrase crosslinked oligomers are active in vitro

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HIV-1 integrase crosslinked oligomers are active in vitro

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HIV-1 integrase crosslinked oligomers are active in vitro

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HIV-1 integrase crosslinked oligomers are active in vitro

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HIV-1 integrase crosslinked oligomers are active in vitro

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Nucleic Acids Research

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HIV-1 integrase crosslinked oligomers are active in vitro

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Anne Caumont-Sarcos

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

Aurélie Faure

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

Christina Calmels

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Cécile Desjobert

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Laura Tarrago-Litvak

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Michel Castroviejo

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Simon Litvak

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Vincent Parissi

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P2860

Functional interactions of human immunodeficiency virus type 1 integrase with human and yeast HSP60

DNA binding induces dissociation of the multimeric form of HIV-1 integrase: a time-resolved fluorescence anisotropy study

Three-dimensional structure of the Tn5 synaptic complex transposition intermediate

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

Studies on transformation of Escherichia coli with plasmids

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

Human immunodeficiency virus type 1 integrase: arrangement of protein domains in active cDNA complexes.

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

Dissecting the role of the N-terminal domain of human immunodeficiency virus integrase by trans-complementation analysis

Structural determinants of metal-induced conformational changes in HIV-1 integrase.

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977-86

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scholarly article

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2600258

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10.1093/NAR/GKI241

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3

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33

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8015640

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15718297

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549407

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