FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
about
Hepatocyte permissiveness to Plasmodium infection is conveyed by a short and structurally conserved region of the CD81 large extracellular domainEWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamilyTspanC8 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 cellsFunction of the tetraspanin CD151-alpha6beta1 integrin complex during cellular morphogenesisTetraspanin12 regulates ADAM10-dependent cleavage of amyloid precursor proteinSpecific tetraspanin functionsEWI-2 regulates alpha3beta1 integrin-dependent cell functions on laminin-5Novel CD9-targeted therapies in gastric cancerThe CD9/CD81 tetraspanin complex and tetraspanin CD151 regulate α3β1 integrin-dependent tumor cell behaviors by overlapping but distinct mechanismsThe CD81 Partner EWI-2wint Inhibits Hepatitis C Virus EntryCD81 and Claudin 1 Coreceptor Association: Role in Hepatitis C Virus EntryTetraspanin CD81 is required for the alpha v beta5-integrin-dependent particle-binding step of RPE phagocytosisCysteine residues in the large extracellular loop (EC2) are essential for the function of the stress-regulated glycoprotein M6aThe tetraspan protein epithelial membrane protein-2 interacts with beta1 integrins and regulates adhesionIdentification 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.Direct binding of the ligand PSG17 to CD9 requires a CD9 site essential for sperm-egg fusion.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/PGRLCD9 clustering and formation of microvilli zippers between contacting cells regulates virus-induced cell fusion.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.CD9P-1 expression correlates with the metastatic status of lung cancer, and a truncated form of CD9P-1, GS-168AT2, inhibits in vivo tumour growthInteracting 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.The C-terminal tail of tetraspanin protein CD9 contributes to its function and molecular organizationEWI-2 negatively regulates TGF-β signaling leading to altered melanoma growth and metastasis.Evolution and Structural Analyses of Glossina morsitans (Diptera; Glossinidae) Tetraspanins.An extracellular site on tetraspanin CD151 determines alpha 3 and alpha 6 integrin-dependent cellular morphology.CD81 and CD9 work independently as extracellular components upon fusion of sperm and oocyte.An optimized isolation of biotinylated cell surface proteins reveals novel players in cancer metastasis.Targeting of tetraspanin proteins--potential benefits and strategiesTspanC8 tetraspanins differentially regulate the cleavage of ADAM10 substrates, Notch activation and ADAM10 membrane compartmentalization.Glioblastoma inhibition by cell surface immunoglobulin protein EWI-2, in vitro and in vivo.Tetraspanins: Small transmembrane proteins with big impact on membrane microdomain structures.
P2860
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P2860
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
description
2001 nî lūn-bûn
@nan
2001 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի փետրվարին հրատարակված գիտական հոդված
@hy
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
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@ast
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@en
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@nl
type
label
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@ast
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@en
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@nl
prefLabel
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@ast
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@en
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@nl
P2093
P356
P1476
FPRP, a major, highly stoichiometric, highly specific CD81- and CD9-associated protein
@en
P2093
P304
P356
10.1074/JBC.M009859200
P407
P577
2001-02-16T00:00:00Z