Disulfide reduction in CD4 domain 1 or 2 is essential for interaction with HIV glycoprotein 120 (gp120), which impairs thioredoxin-driven CD4 dimerization - Wikidata - wikimedia - TriplyDB

Disulfide reduction in CD4 domain 1 or 2 is essential for interaction with HIV glycoprotein 120 (gp120), which impairs thioredoxin-driven CD4 dimerization

Disulfide reduction in CD4 domain 1 or 2 is essential for interaction with HIV glycoprotein 120 (gp120), which impairs thioredoxin-driven CD4 dimerization

http://www.wikidata.org/entity/Q33675700

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Conformational Masking and Receptor-Dependent Unmasking of Highly Conserved Env Epitopes Recognized by Non-Neutralizing Antibodies That Mediate Potent ADCC against HIV-1 Potential role of glutathione in evolution of thiol-based redox signaling sites in proteins From structure to redox: The diverse functional roles of disulfides and implications in disease.Thioredoxin Inhibitors Attenuate Platelet Function and Thrombus Formation.Disulfide Sensitivity in the Env Protein Underlies Lytic Inactivation of HIV-1 by Peptide Triazole Thiols.Thiol-Disulfide Exchange Reactions in the Mammalian Extracellular Environment.High thioredoxin-1 levels in rheumatoid arthritis patients diminish binding and signalling of the monoclonal antibody Tregalizumab Galectin-9 binds to O-glycans on protein disulfide isomerase.

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P2860

Disulfide reduction in CD4 domain 1 or 2 is essential for interaction with HIV glycoprotein 120 (gp120), which impairs thioredoxin-driven CD4 dimerization

http://www.wikidata.org/entity/Q33675700

description

2014 nî lūn-bûn

@nan

2014 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի փետրվարին հրատարակված գիտական հոդված

@hy

2014年の論文

@ja

2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Disulfide reduction in CD4 dom ...... edoxin-driven CD4 dimerization

@ast

Disulfide reduction in CD4 dom ...... edoxin-driven CD4 dimerization

@en

type

label

Disulfide reduction in CD4 dom ...... edoxin-driven CD4 dimerization

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Disulfide reduction in CD4 dom ...... edoxin-driven CD4 dimerization

@en

prefLabel

Disulfide reduction in CD4 dom ...... edoxin-driven CD4 dimerization

@ast

Disulfide reduction in CD4 dom ...... edoxin-driven CD4 dimerization

@en

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P356

JBC.M113.539353

P1433

Journal of Biological Chemistry

P1476

Disulfide reduction in CD4 dom ...... edoxin-driven CD4 dimerization

@en

P2093

Alexio Capovilla

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

Maria Papathanasopoulos

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

Mark Killick

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

Nichole Cerutti

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

Vinesh Jugnarain

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

P2860

CD4 dimers constitute the functional component required for T cell activation

Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody

The CD4 (T4) antigen is an essential component of the receptor for the AIDS retrovirus

Inhibition of CD4+ T cell function by the HIV envelope protein, gp120

Inhibition of human immunodeficiency virus infection by agents that interfere with thiol-disulfide interchange upon virus-receptor interaction

T-lymphocyte T4 molecule behaves as the receptor for human retrovirus LAV

Direct evidence for native CD4 oligomers in lymphoid and monocytoid cells.

The catalytic activity of protein disulfide isomerase is involved in human immunodeficiency virus envelope-mediated membrane fusion after CD4 cell binding.

CD4+ lymphocyte function with early human immunodeficiency virus infection.

Stabilization of HIV-1 gp120-CD4 receptor complex through targeted interchain disulfide exchange

P304

10455-10465

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scholarly article

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10.1074/JBC.M113.539353

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15

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289

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2014-02-18T00:00:00Z

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4036167

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