HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction. - Wikidata - wikimedia - TriplyDB

HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction.

HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction.

http://www.wikidata.org/entity/Q30159721

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Deciphering the cross talk between hnRNP K and c-Src: the c-Src activation domain in hnRNP K is distinct from a second interaction site Viral infection and human disease--insights from minimotifs HIV Genome-Wide Protein Associations: a Review of 30 Years of Research Impacts of humanized mouse models on the investigation of HIV-1 infection: illuminating the roles of viral accessory proteins in vivo Small molecule inhibitors of the HIV-1 virulence factor, Nef Crystal Structure of the Src Family Kinase Hck SH3-SH2 Linker Regulatory Region Supports an SH3-dominant Activation Mechanism Motif mediated protein-protein interactions as drug targets HIV-1 nef protein structures associated with brain infection and dementia pathogenesis Structural studies and SH3 domain binding properties of a human antiviral salivary proline-rich peptide.Subtle Dynamic Changes Accompany Hck Activation by HIV-1 Nef and are Reversed by an Antiretroviral Kinase Inhibitor.A Discovery Strategy for Selective Inhibitors of c-Src in Complex with the Focal Adhesion Kinase SH3/SH2-binding Region.SH2-catalytic domain linker heterogeneity influences allosteric coupling across the SFK family.Differential sensitivity of Src-family kinases to activation by SH3 domain displacement.Interaction with the Src homology (SH3-SH2) region of the Src-family kinase Hck structures the HIV-1 Nef dimer for kinase activation and effector recruitment The accessory factor Nef links HIV-1 to Tec/Btk kinases in an Src homology 3 domain-dependent manner.In vivo analysis of highly conserved Nef activities in HIV-1 replication and pathogenesis.HIV-1 infection of T cells and macrophages are differentially modulated by virion-associated Hck: a Nef-dependent phenomenon Partial cooperative unfolding in proteins as observed by hydrogen exchange mass spectrometry.Individual Src-family tyrosine kinases direct the degradation or protection of the clock protein Timeless via differential ubiquitylation.HIV-1 Nef interaction influences the ATP-binding site of the Src-family kinase, Hck Interaction between the SH3 domain of Src family kinases and the proline-rich motif of HTLV-1 p13: a novel mechanism underlying delivery of Src family kinases to mitochondria.Structure, dynamics, and Hck interaction of full-length HIV-1 Nef.Molecular priming of Lyn by GPVI enables an immune receptor to adopt a hemostatic role.Competitive displacement of full-length HIV-1 Nef from the Hck SH3 domain by a high-affinity artificial peptide.C-terminal Src kinase-homologous kinase (CHK), a unique inhibitor inactivating multiple active conformations of Src family tyrosine kinases.Effector kinase coupling enables high-throughput screens for direct HIV-1 Nef antagonists with antiretroviral activity.Conformational disturbance in Abl kinase upon mutation and deregulation.Chemical library screens targeting an HIV-1 accessory factor/host cell kinase complex identify novel antiretroviral compounds Opinion: Inhibition of Blood-Brain Barrier Repair as a Mechanism in HIV-1 Disease.Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action Molecular dynamics reveal the essential role of linker motions in the function of cullin-RING E3 ligases Exogenous Nef is an inhibitor of Mycobacterium tuberculosis-induced tumor necrosis factor-alpha production and macrophage apoptosis.Hydrogen exchange mass spectrometry: what is it and what can it tell us?Sequence- and interactome-based prediction of viral protein hotspots targeting host proteins: a case study for HIV Nef.Expression of a Src family kinase in chronic myelogenous leukemia cells induces resistance to imatinib in a kinase-dependent manner.Hematopoietic cell kinase associates with the 40S ribosomal subunit and mediates the ribotoxic stress response to deoxynivalenol in mononuclear phagocytes.Nef alleles from all major HIV-1 clades activate Src-family kinases and enhance HIV-1 replication in an inhibitor-sensitive manner.Short communication: HIV-1 Nef protein carries multiple epitopes suitable for induction of cellular immunity for an HIV vaccine in Africa Identification of Hck inhibitors as hits for the development of antileukemia and anti-HIV agents.Systematic prediction of human membrane receptor interactions.

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P2860

HIV-1 Nef selectively activates Src family kinases Hck, Lyn, and c-Src through direct SH3 domain interaction.

http://www.wikidata.org/entity/Q30159721

description

2006 nî lūn-bûn

@nan

2006 թուականի Յուլիսին հրատարակուած գիտական յօդուած

@hyw

2006 թվականի հուլիսին հրատարակված գիտական հոդված

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2006年の論文

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2006年論文

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2006年論文

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2006年論文

@zh-hk

2006年論文

@zh-mo

2006年論文

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2006年论文

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name

HIV-1 Nef selectively activate ...... direct SH3 domain interaction.

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HIV-1 Nef selectively activate ...... direct SH3 domain interaction.

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HIV-1 Nef selectively activate ...... direct SH3 domain interaction.

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HIV-1 Nef selectively activate ...... direct SH3 domain interaction.

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HIV-1 Nef selectively activate ...... direct SH3 domain interaction.

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Journal of Biological Chemistry

P1476

HIV-1 Nef selectively activate ...... direct SH3 domain interaction.

@en

P2093

Lori Emert-Sedlak

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Ronald P Trible

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Thomas E Smithgall

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P2860

Novel protein-tyrosine kinase gene (hck) preferentially expressed in cells of hematopoietic origin

Identification of a human gene (HCK) that encodes a protein-tyrosine kinase and is expressed in hemopoietic cells

Csk inhibition of c-Src activity requires both the SH2 and SH3 domains of Src

Proline-rich (PxxP) motifs in HIV-1 Nef bind to SH3 domains of a subset of Src kinases and are required for the enhanced growth of Nef+ viruses but not for down-regulation of CD4

Human immunodeficiency virus type 1 Nef binds directly to Lck and mitogen-activated protein kinase, inhibiting kinase activity

The crystal structure of HIV-1 Nef protein bound to the Fyn kinase SH3 domain suggests a role for this complex in altered T cell receptor signaling

Crystal structure of the conserved core of HIV-1 Nef complexed with a Src family SH3 domain

Structure--function relationships in HIV-1 Nef.

Nef stimulates proliferation of glomerular podocytes through activation of Src-dependent Stat3 and MAPK1,2 pathways

A single amino acid in the SH3 domain of Hck determines its high affinity and specificity in binding to HIV-1 Nef protein

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27029-27038

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scholarly article

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10.1074/JBC.M601128200

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P433

37

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281

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16849330

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2892265

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