Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan. - Wikidata - wikimedia - TriplyDB

Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

http://www.wikidata.org/entity/Q37247060

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Decoding protein networks during virus entry by quantitative proteomics Principles of Virus Uncoating: Cues and the Snooker Ball Comparative analysis of disease pathogenesis and molecular mechanisms of New World and Old World arenavirus infections.Lassa Virus Cell Entry via Dystroglycan Involves an Unusual Pathway of Macropinocytosis.IFITMs restrict the replication of multiple pathogenic viruses Lassa Virus Cell Entry Reveals New Aspects of Virus-Host Cell Interaction Studies of Lassa Virus Cell Entry.Axl can serve as entry factor for Lassa virus depending on the functional glycosylation of dystroglycan.Screening and Identification of Lassa Virus Entry Inhibitors from an FDA-Approved Drug Library

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P2860

Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

http://www.wikidata.org/entity/Q37247060

description

article científic

@ca

article scientifique

@fr

articolo scientifico

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artigo científico

@pt

bilimsel makale

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scientific article published on 20 December 2012

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

@en

Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

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type

label

Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

@en

Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

@nl

prefLabel

Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

@en

Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

@nl

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Cellular Microbiology

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Cell entry of Lassa virus induces tyrosine phosphorylation of dystroglycan.

@en

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Christelle Pythoud

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

Marie-Laurence Moraz

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

Sylvia Rothenberger

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

P2860

Tyrosine phosphorylation of beta-dystroglycan at its WW domain binding motif, PPxY, recruits SH2 domain containing proteins

Dystroglycan, a scaffold for the ERK-MAP kinase cascade.

X-ray structure of the arenavirus glycoprotein GP2 in its postfusion hairpin conformation

Adhesion-dependent tyrosine phosphorylation of (beta)-dystroglycan regulates its interaction with utrophin

Molecular recognition by LARGE is essential for expression of functional dystroglycan

Identification of alpha-dystroglycan as a receptor for lymphocytic choriomeningitis virus and Lassa fever virus

SH3 domain-mediated interaction of dystroglycan and Grb2

Localization of cranin (dystroglycan) at sites of cell-matrix and cell-cell contact: recruitment to focal adhesions is dependent upon extracellular ligands

Distribution of dystroglycan in normal adult mouse tissues

Membrane organization of the dystrophin-glycoprotein complex

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689-700

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scholarly article

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10.1111/CMI.12078

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5

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15

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Antonella Pasquato

Kevin P Campbell

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2012-12-20T00:00:00Z

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234030960

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23279385

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phosphorylation

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3805106

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