HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis - Wikidata - thesis-toulmin - TriplyDB

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

http://www.wikidata.org/entity/Q21146434

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The histone chaperone protein Nucleosome Assembly Protein-1 (hNAP-1) binds HIV-1 Tat and promotes viral transcription ELMO1 and Dock180, a bipartite Rac1 guanine nucleotide exchange factor, promote human glioma cell invasion.Tetramerization of SAMHD1 is required for biological activity and inhibition of HIV infection Structural Basis of Membrane Targeting by the Dock180 Family of Rho Family Guanine Exchange Factors (Rho-GEFs)Lentiviral Vpx accessory factor targets VprBP/DCAF1 substrate adaptor for cullin 4 E3 ubiquitin ligase to enable macrophage infection A hydrophobic binding surface on the human immunodeficiency virus type 1 Nef core is critical for association with p21-activated kinase 2.Dedicator of Cytokinesis 2 in Cell Signaling Regulation and Disease Development.HIV-1 Nef-mediated T-cell activation and chemotaxis are decoupled using a HIV-1/SIVpbj1.9. chimeric nef variant.Clearance of apoptotic cells: implications in health and disease HIV-1 Nef interferes with T-lymphocyte circulation through confined environments in vivo.Tyr724 phosphorylation of ELMO1 by Src is involved in cell spreading and migration via Rac1 activation.Modifications in host cell cytoskeleton structure and function mediated by intracellular HIV-1 Tat protein are greatly dependent on the second coding exon Reconstitution and molecular analysis of an active human immunodeficiency virus type 1 Nef/p21-activated kinase 2 complex.Self-association of the Lentivirus protein, Nef HIV/simian immunodeficiency virus (SIV) accessory virulence factor Vpx loads the host cell restriction factor SAMHD1 onto the E3 ubiquitin ligase complex CRL4DCAF1.Dynamic evolution of the human immunodeficiency virus type 1 pathogenic factor, Nef.Structural constraints on human immunodeficiency virus type 1 Nef function.Specific recognition of Rac2 and Cdc42 by DOCK2 and DOCK9 guanine nucleotide exchange factors.Proteomic profiling of SupT1 cells reveal modulation of host proteins by HIV-1 Nef variants Recent progress in the genetics of diabetic microvascular complications.Dynamin 2 is required for the enhancement of HIV-1 infectivity by Nef.ELMO3 is a novel biomarker for diagnosis and prognosis of non-small cell lung cancer CyclinA2-Cyclin-dependent Kinase Regulates SAMHD1 Protein Phosphohydrolase Domain.Association with PAK2 Enables Functional Interactions of Lentiviral Nef Proteins with the Exocyst Complex.Antiviral activity of a Rac GEF inhibitor characterized with a sensitive HIV/SIV fusion assay HIV-1 Nef impairs heterotrimeric G-protein signaling by targeting Gα(i2) for degradation through ubiquitination.Human immunodeficiency virus type 1 Nef: adapting to intracellular trafficking pathways.HIV-1 Nef: at the crossroads DOCK2 confers immunity and intestinal colonization resistance to Citrobacter rodentium infection.DOCK2 is a microglial specific regulator of central nervous system innate immunity found in normal and Alzheimer's disease brain.The Antagonism of HIV-1 Nef to SERINC5 Particle Infectivity Restriction Involves the Counteraction of Virion-Associated Pools of the Restriction Factor.Human N-myristoyltransferases form stable complexes with lentiviral nef and other viral and cellular substrate proteins.Adding new dimensions: towards an integrative understanding of HIV-1 spread.Proteomics in the investigation of HIV-1 interactions with host proteins.Primate Lentiviruses Modulate NF-κB Activity by Multiple Mechanisms to Fine-Tune Viral and Cellular Gene Expression.HIV-1 Nef and Vpu are functionally redundant broad-spectrum modulators of cell surface receptors, including tetraspanins.Expression of Nef downregulates CXCR4, the major coreceptor of human immunodeficiency virus, from the surfaces of target cells and thereby enhances resistance to superinfection.Proteomic analysis of HIV-1 Nef cellular binding partners reveals a role for exocyst complex proteins in mediating enhancement of intercellular nanotube formation.Modulation of HIV pathogenesis and T-cell signaling by HIV-1 Nef The host-cell restriction factor SERINC5 restricts HIV-1 infectivity without altering the lipid composition and organization of viral particles.

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P2860

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

http://www.wikidata.org/entity/Q21146434

description

2004 nî lūn-bûn

@nan

2004 թուականի Յունուարին հրատարակուած գիտական յօդուած

@hyw

2004 թվականի հունվարին հրատարակված գիտական հոդված

@hy

2004年の論文

@ja

2004年論文

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2004年論文

@zh-hant

2004年論文

@zh-hk

2004年論文

@zh-mo

2004年論文

@zh-tw

2004年论文

@wuu

name

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@ast

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@en

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@en-gb

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@nl

type

label

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@ast

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@en

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@en-gb

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@nl

altLabel

HIV-1 Nef Binds the DOCK2–ELMO1 Complex to Activate Rac and Inhibit Lymphocyte Chemotaxis

@en

prefLabel

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@ast

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@en

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@en-gb

HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@nl

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JOURNAL.PBIO.0020006

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HIV-1 Nef binds the DOCK2-ELMO1 complex to activate rac and inhibit lymphocyte chemotaxis

@en

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Ajit Janardhan

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

Brian Hill

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

Jacek Skowronski

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

Michael P Myers

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

P2860

Activation of Vav by Nef induces cytoskeletal rearrangements and downstream effector functions

HIV-1 Entry Cofactor: Functional cDNA Cloning of a Seven-Transmembrane, G Protein-Coupled Receptor

Endocytosis of major histocompatibility complex class I molecules is induced by the HIV–1 Nef protein

Identification of a major co-receptor for primary isolates of HIV-1

CED-12/ELMO, a novel member of the CrkII/Dock180/Rac pathway, is required for phagocytosis and cell migration

Unconventional Rac-GEF activity is mediated through the Dock180-ELMO complex

A conserved binding motif defines numerous candidate target proteins for both Cdc42 and Rac GTPases

Characterization of human RNA polymerase III identifies orthologues for Saccharomyces cerevisiae RNA polymerase III subunits.

Co-localization of HIV-1 Nef with the AP-2 adaptor protein complex correlates with Nef-induced CD4 down-regulation

Mechanism of Nef-induced CD4 endocytosis: Nef connects CD4 with the mu chain of adaptor complexes.

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10.1371/JOURNAL.PBIO.0020006

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14737186

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314466

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