Hepatocyte permissiveness to Plasmodium infection is conveyed by a short and structurally conserved region of the CD81 large extracellular domain - Wikidata - awgldk - TriplyDB

Hepatocyte permissiveness to Plasmodium infection is conveyed by a short and structurally conserved region of the CD81 large extracellular domain

Hepatocyte permissiveness to Plasmodium infection is conveyed by a short and structurally conserved region of the CD81 large extracellular domain

http://www.wikidata.org/entity/Q21090524

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Malaria parasite pre-erythrocytic stage infection: gliding and hiding Structural basis of ligand interactions of the large extracellular domain of tetraspanin CD81 Selection and refinement: the malaria parasite's infection and exploitation of host hepatocytes The association of CD81 with tetraspanin-enriched microdomains is not essential for Hepatitis C virus entry Imaging of Plasmodium Liver Stages to Drive Next-Generation Antimalarial Drug Discovery The Ig domain protein CD9P-1 down-regulates CD81 ability to support Plasmodium yoelii infection Suppression of mRNAs encoding tegument tetraspanins from Schistosoma mansoni results in impaired tegument turnover Malaria parasite development in the mosquito and infection of the mammalian host.Plasmodium P36 determines host cell receptor usage during sporozoite invasion Liver immunology.Distinct regions of the large extracellular domain of tetraspanin CD9 are involved in the control of human multinucleated giant cell formation Interacting regions of CD81 and two of its partners, EWI-2 and EWI-2wint, and their effect on hepatitis C virus infection Lateral organization of membrane proteins: tetraspanins spin their web.Discovery of HDAC inhibitors with potent activity against multiple malaria parasite life cycle stages A chemical genomic analysis of decoquinate, a Plasmodium falciparum cytochrome b inhibitor Molecular insights into a tetraspanin in the hydatid tapeworm Echinococcus granulosus In silico directed mutagenesis identifies the CD81/claudin-1 hepatitis C virus receptor interface.Skin-draining lymph node priming is sufficient to induce sterile immunity against pre-erythrocytic malaria.In Vitro Analysis of the Interaction between Atovaquone and Proguanil against Liver Stage Malaria Parasites.CD81 and hepatitis C virus (HCV) infection.CD81-receptor associations--impact for hepatitis C virus entry and antiviral therapies.Scavenger receptor class B, type I: a promising immunotherapy target.New insights into the tetraspanin Tspan5 using novel monoclonal antibodies.CD81 is required for rhoptry discharge during host cell invasion by Plasmodium yoelii sporozoites.[Plasmodium sporozoite entry pathways during malaria liver infection].Design and Synthesis of Terephthalic Acid-Based Histone Deacetylase Inhibitors with Dual-Stage Anti-Plasmodium Activity.The Promise of Systems Biology Approaches for Revealing Host Pathogen Interactions in Malaria.Two inhibitors of yeast plasma membrane ATPase 1 (ScPma1p): toward the development of novel antifungal therapies.Evolutionary Analysis Provides Insight Into the Origin and Adaptation of HCV.UCT943, a Next-Generation Plasmodium falciparum PI4K Inhibitor Preclinical Candidate for the Treatment of Malaria Hepatitis C virus enters liver cells using the CD81 receptor complex proteins calpain-5 and CBLB Plasmodium sporozoites can invade hepatocytic cells independently of the Ephrin receptor A2

P2860

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P2860

Hepatocyte permissiveness to Plasmodium infection is conveyed by a short and structurally conserved region of the CD81 large extracellular domain

http://www.wikidata.org/entity/Q21090524

description

2008 nî lūn-bûn

@nan

2008 թուականի Փետրուարին հրատարակուած գիտական յօդուած

@hyw

2008 թվականի փետրվարին հրատարակված գիտական հոդված

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2008年の論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年論文

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2008年论文

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name

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Hepatocyte permissiveness to P ...... D81 large extracellular domain

@en

P2093

Cécile Arduise

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Dominique Mazier

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Khemais Farhati

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Patrick Froissard

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Samir Yalaoui

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Sergine Zougbédé

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Stéphanie Charrin

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P2860

Characterization of hepatitis C virus E2 glycoprotein interaction with a putative cellular receptor, CD81.

The major CD9 and CD81 molecular partner. Identification and characterization of the complexes

EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily

Identification of amino acid residues in CD81 critical for interaction with hepatitis C virus envelope glycoprotein E2.

EWI-2 is a new component of the tetraspanin web in hepatocytes and lymphoid cells

Selective tetraspan-integrin complexes (CD81/alpha4beta1, CD151/alpha3beta1, CD151/alpha6beta1) under conditions disrupting tetraspan interactions

Infectious hepatitis C virus pseudo-particles containing functional E1-E2 envelope protein complexes

Initiation of hepatitis C virus infection is dependent on cholesterol and cooperativity between CD81 and scavenger receptor B type I

Robust hepatitis C virus infection in vitro.

Tetraspanins in viral infections: a fundamental role in viral biology?

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e1000010

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scholarly article

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10.1371/JOURNAL.PPAT.1000010

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2

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Eric Rubinstein

Claude Boucheix

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2008-02-01T00:00:00Z

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