EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
about
Hepatocyte permissiveness to Plasmodium infection is conveyed by a short and structurally conserved region of the CD81 large extracellular domainTspanC8 tetraspanins regulate ADAM10/Kuzbanian trafficking and promote Notch activation in flies and mammalsTetraspanin protein CD9 interacts with metalloprotease CD10 and enhances its release via exosomesDynamic regulation of a GPCR-tetraspanin-G protein complex on intact cells: central role of CD81 in facilitating GPR56-Galpha q/11 associationEWI-2 is a new component of the tetraspanin web in hepatocytes and lymphoid cellsStructural basis of ligand interactions of the large extracellular domain of tetraspanin CD81Specific tetraspanin functionsEWI-2 regulates alpha3beta1 integrin-dependent cell functions on laminin-5EWI-2/CD316 is an inducible receptor of HSPA8 on human dendritic cellsNovel CD9-targeted therapies in gastric cancerThe CD9/CD81 tetraspanin complex and tetraspanin CD151 regulate α3β1 integrin-dependent tumor cell behaviors by overlapping but distinct mechanismsDifferent Domains of CD81 Mediate Distinct Stages of Hepatitis C Virus Pseudoparticle EntryThe CD81 Partner EWI-2wint Inhibits Hepatitis C Virus EntryCD81 and Claudin 1 Coreceptor Association: Role in Hepatitis C Virus EntryThe association of CD81 with tetraspanin-enriched microdomains is not essential for Hepatitis C virus entryTetraspanin functions and associated microdomainsIgSF8: a developmentally and functionally regulated cell adhesion molecule in olfactory sensory neuron axons and synapsesA transgenic insertion on mouse chromosome 17 inactivates a novel immunoglobulin superfamily gene potentially involved in sperm-egg fusionCysteine residues in the large extracellular loop (EC2) are essential for the function of the stress-regulated glycoprotein M6aSingle-molecule analysis of CD9 dynamics and partitioning reveals multiple modes of interaction in the tetraspanin web.Identification and characterization of tumor antigens by using antibody phage display and intrabody strategies.The Ig domain protein CD9P-1 down-regulates CD81 ability to support Plasmodium yoelii infectionThe tetraspanins CD9 and CD81 regulate CD9P1-induced effects on cell migration.Increased density of retinal pigment epithelium in cd81-/- miceProteomics analysis of A33 immunoaffinity-purified exosomes released from the human colon tumor cell line LIM1215 reveals a tissue-specific protein signature.Direct binding of the ligand PSG17 to CD9 requires a CD9 site essential for sperm-egg fusion.The extracellular δ-domain is essential for the formation of CD81 tetraspanin webs.Palmitoylation of tetraspanin proteins: modulation of CD151 lateral interactions, subcellular distribution, and integrin-dependent cell morphology.Differential functions of phospholipid binding and palmitoylation of tumour suppressor EWI2/PGRLMAL/VIP17, a new player in the regulation of NKCC2 in the kidneyCD9 clustering and formation of microvilli zippers between contacting cells regulates virus-induced cell fusion.The absence of Tssc6, a member of the tetraspanin superfamily, does not affect lymphoid development but enhances in vitro T-cell proliferative responses.Contrasting effects of EWI proteins, integrins, and protein palmitoylation on cell surface CD9 organization.EWI-2 and EWI-F link the tetraspanin web to the actin cytoskeleton through their direct association with ezrin-radixin-moesin proteins.Complex N-linked glycans serve as a determinant for exosome/microvesicle cargo recruitment.Interacting regions of CD81 and two of its partners, EWI-2 and EWI-2wint, and their effect on hepatitis C virus infectionLateral organization of membrane proteins: tetraspanins spin their web.Priming of the vascular endothelial growth factor signaling pathway by thrombospondin-1, CD36, and spleen tyrosine kinase.IgLON cell adhesion molecules are shed from the cell surface of cortical neurons to promote neuronal growth.The C-terminal tail of tetraspanin protein CD9 contributes to its function and molecular organization
P2860
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P2860
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
description
2001 nî lūn-bûn
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2001 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի նոյեմբերին հրատարակված գիտական հոդված
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2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@ast
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@en
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@en-gb
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@nl
type
label
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@ast
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@en
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@en-gb
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@nl
prefLabel
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@ast
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@en
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@en-gb
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@nl
P2093
P2860
P921
P356
P1476
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily
@en
P2093
M E Hemler
T V Kolesnikova
P2860
P304
P356
10.1074/JBC.M107338200
P407
P577
2001-11-02T00:00:00Z