Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action - sprookjes - yvandenbroek - TriplyDB

Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action

Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action

http://www.wikidata.org/entity/Q33655043

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Remodeling of the Host Cell Plasma Membrane by HIV-1 Nef and Vpu: A Strategy to Ensure Viral Fitness and Persistence Small molecule inhibitors of the HIV-1 virulence factor, Nef MIiSR: Molecular Interactions in Super-Resolution Imaging Enables the Analysis of Protein Interactions, Dynamics and Formation of Multi-protein Structures The identification of a small molecule compound that reduces HIV-1 Nef-mediated viral infectivity enhancement Molecular design, functional characterization and structural basis of a protein inhibitor against the HIV-1 pathogenicity factor Nef Subtle Dynamic Changes Accompany Hck Activation by HIV-1 Nef and are Reversed by an Antiretroviral Kinase Inhibitor.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.Overlapping effector interfaces define the multiple functions of the HIV-1 Nef polyproline helix.Single-domain antibody-SH3 fusions for efficient neutralization of HIV-1 Nef functions Effector kinase coupling enables high-throughput screens for direct HIV-1 Nef antagonists with antiretroviral activity.Flaviviruses, an expanding threat in public health: focus on dengue, West Nile, and Japanese encephalitis virus.Discovery of a diaminoquinoxaline benzenesulfonamide antagonist of HIV-1 Nef function using a yeast-based phenotypic screen Viral bimolecular fluorescence complementation: a novel tool to study intracellular vesicular trafficking pathways.Antigen processing and remodeling of the endosomal pathway: requirements for antigen cross-presentation.An interdomain binding site on HIV-1 Nef interacts with PACS-1 and PACS-2 on endosomes to down-regulate MHC-I.Association with PAK2 Enables Functional Interactions of Lentiviral Nef Proteins with the Exocyst Complex.Mechanisms of HIV-1 Nef function and intracellular signaling.A Highly Conserved Residue in HIV-1 Nef Alpha Helix 2 Modulates Protein Expression.Identification of a novel binding site between HIV type 1 Nef C-terminal flexible loop and AP2 required for Nef-mediated CD4 downregulation.HIV immune evasion disruption of antigen presentation by the HIV Nef protein.Contributions of HIV-1 Nef to immune dysregulation in HIV-infected patients: a therapeutic target?Viral proteins and Src family kinases: Mechanisms of pathogenicity from a "liaison dangereuse".HIV-1 Nef: Taking Control of Protein Trafficking.Macropinocytosis and TAK1 mediate anti-inflammatory to pro-inflammatory macrophage differentiation by HIV-1 Nef Caught in the act - protein adaptation and the expanding roles of the PACS proteins in tissue homeostasis and disease.HIV-1 Nef and T-cell activation: a history of contradictions.The human immunodeficiency virus type 1 Nef and Vpu proteins downregulate the natural killer cell-activating ligand PVR.Modulation of HIV pathogenesis and T-cell signaling by HIV-1 Nef HIV-I Nef inhibitors: a novel class of HIV-specific immune adjuvants in support of a cure.A Novel Toll-Like Receptor 9 Agonist, MGN1703, Enhances HIV-1 Transcription and NK Cell-Mediated Inhibition of HIV-1-Infected Autologous CD4+ T Cells.HIV-1 Nef sequesters MHC-I intracellularly by targeting early stages of endocytosis and recycling.PACS-2 mediates the ATM and NF-κB-dependent induction of anti-apoptotic Bcl-xL in response to DNA damage Comparative Analysis of Tat-Dependent and Tat-Deficient Natural Lentiviruses.Remodeling of HIV-1 Nef Structure by Src-Family Kinase Binding.A single β-octyl glucoside molecule induces HIV-1 Nef dimer formation in the absence of partner protein binding.

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P2860

Small molecule inhibition of HIV-1-induced MHC-I down-regulation identifies a temporally regulated switch in Nef action

http://www.wikidata.org/entity/Q33655043

description

2010 nî lūn-bûn

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2010 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

@yue

2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

@zh-tw

2010年论文

@wuu

name

Small molecule inhibition of H ...... regulated switch in Nef action

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Small molecule inhibition of H ...... regulated switch in Nef action

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type

label

Small molecule inhibition of H ...... regulated switch in Nef action

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Small molecule inhibition of H ...... regulated switch in Nef action

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prefLabel

Small molecule inhibition of H ...... regulated switch in Nef action

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Small molecule inhibition of H ...... regulated switch in Nef action

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MBC.E10-05-0470

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Molecular Biology of the Cell

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Small molecule inhibition of H ...... regulated switch in Nef action

@en

P2093

Ben Kukull

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

Danielle M Williamson

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

Eric Barklis

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

Gary Thomas

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

Hirokazu Koizumi

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

In-Ja L Byeon

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

Jimmy D Dikeakos

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

Jinwon Jung

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

Jinwoo Ahn

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

Katelyn M Atkins

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

P2860

HIV-1 Nef protein binds to the cellular protein PACS-1 to downregulate class I major histocompatibility complexes

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

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

A tubular EHD1-containing compartment involved in the recycling of major histocompatibility complex class I molecules to the plasma membrane

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

HIV-1 Nef downregulates MHC-I by a PACS-1- and PI3K-regulated ARF6 endocytic pathway

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

The Pro78 residue regulates the capacity of the human immunodeficiency virus type 1 Nef protein to inhibit recycling of major histocompatibility complex class I molecules in an SH3-independent manner.

Conserved residues in the HIV-1 Nef hydrophobic pocket are essential for recruitment and activation of the Hck tyrosine kinase.

Synthetic inhibitors of proline-rich ligand-mediated protein-protein interaction: potent analogs of UCS15A.

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3279-3292

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scholarly article

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10.1091/MBC.E10-05-0470

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19

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21

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Angela M Gronenborn

Matthew Wortman

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2010-08-11T00:00:00Z

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20702582

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2947465

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