Platelet moesin interacts with PECAM-1 (CD31).

Item

http://www.wikidata.org/entity/Q47773051

description

2003 nî lūn-bûn

@nan

2003年の論文

@ja

2003年学术文章

@wuu

2003年学术文章

@zh-cn

2003年学术文章

@zh-hans

2003年学术文章

@zh-my

2003年学术文章

@zh-sg

2003年學術文章

@yue

2003年學術文章

@zh

2003年學術文章

@zh-hant

name

Platelet moesin interacts with PECAM-1 (CD31).

@en

Platelet moesin interacts with PECAM-1

@nl

type

Item

label

Platelet moesin interacts with PECAM-1 (CD31).

@en

Platelet moesin interacts with PECAM-1

@nl

prefLabel

Platelet moesin interacts with PECAM-1 (CD31).

@en

Platelet moesin interacts with PECAM-1

@nl

P1476

Platelet moesin interacts with PECAM-1 (CD31).

@en

P2093

Karin M Hoffmeister

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

Kerstin Seifert

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

Maria-Andreea Gamulescu

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

Markus Tingart

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

P2860

Recruitment and activation of SHP-1 protein-tyrosine phosphatase by human platelet endothelial cell adhesion molecule-1 (PECAM-1). Identification of immunoreceptor tyrosine-based inhibitory motif-like binding motifs and substrates

PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily

Moesin: a member of the protein 4.1-talin-ezrin family of proteins

Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of platelet/endothelial cell adhesion molecule-1 (PECAM-1) that are required for the cellular association and activation of the protein-tyrosine phosphatase, SHP-2

Molecular and cellular properties of PECAM-1 (endoCAM/CD31): a novel vascular cell-cell adhesion molecule

Regulation of F-actin binding to platelet moesin in vitro by both phosphorylation of threonine 558 and polyphosphatidylinositides

Regulation mechanism of ERM (ezrin/radixin/moesin) protein/plasma membrane association: possible involvement of phosphatidylinositol turnover and Rho-dependent signaling pathway

Rho-kinase phosphorylates COOH-terminal threonines of ezrin/radixin/moesin (ERM) proteins and regulates their head-to-tail association

Purification of an 80,000-dalton protein that is a component of the isolated microvillus cytoskeleton, and its localization in nonmuscle cells

Moesin interacts with the cytoplasmic region of intercellular adhesion molecule-3 and is redistributed to the uropod of T lymphocytes during cell polarization

P304

211-217

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

P31

scholarly article

P356

10.1080/0953710031000118830

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

P433

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

P478

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

P50

Hervé Falet

P577

2003-06-01T00:00:00Z

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

P698

12850829

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