Molecular cloning of the CD9 antigen. A new family of cell surface proteins.Boucheix C., Benoit P., Frachet P., Billard M., Worthington R.E., Gagnon J., Uzan G.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA], PROTEIN SEQUENCE OF 2-5CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 266:117-122 (1991)Cited in1
cDNA cloning and expression of platelet p24/CD9. Evidence for a new family of multiple membrane-spanning proteins.Lanza F., Wolf D., Fox C.F., Kieffer N., Seyer J.M., Fried V.A., Coughlin S.R., Phillips D.R., Jennings L.K.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA], PARTIAL PROTEIN SEQUENCECategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 266:10638-10645 (1991)Cited in1
Identification of the motility-related protein (MRP-1), recognized by monoclonal antibody M31-15, which inhibits cell motility.Miyake M., Koyama M., Seno M., Ikeyama S.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Exp. Med. 174:1347-1354 (1991)Cited in1
Organization of the human CD9 gene.Rubinstein E., Benoit P., Billard M., Plaisance S., Prenant M., Uzan G., Boucheix C.View abstractCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]TissueLeukocyteCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenomics 16:132-138 (1993)Cited in1
The tetraspanin CD9 is preferentially expressed on the human CD4(+)CD45RA+ naive T cell population and is involved in T cell activation.Kobayashi H., Hosono O., Iwata S., Kawasaki H., Kuwana M., Tanaka H., Dang N.H., Morimoto C.View abstractCited forNUCLEOTIDE SEQUENCE [MRNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCClin. Exp. Immunol. 137:101-108 (2004)Cited in1
Identification of a human growth inhibition gene 2 (GIG2).Kim J.W.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (SEP-2003)Cited in1
No title available.SeattleSNPs variation discovery resourceCited forNUCLEOTIDE SEQUENCE [GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (SEP-2003)Cited in2
No title available.Mural R.J., Istrail S., Sutton G.G., Florea L., Halpern A.L., Mobarry C.M., Lippert R., Walenz B., Shatkay H.[...], Venter J.C.Cited forNUCLEOTIDE SEQUENCE [LARGE SCALE GENOMIC DNA]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)Submission Submitted to EMBL/GenBank/DDBJ databases (SEP-2005)Cited in99+
The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC).The MGC Project TeamView abstractCited forNUCLEOTIDE SEQUENCE [LARGE SCALE MRNA]TissueOvaryCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCGenome Res. 14:2121-2127 (2004)Cited in99+99+
Purification and partial characterization of CD9 antigen of human platelets.Higashihara M., Takahata K., Yatomi Y., Nakahara K., Kurokawa K.View abstractCited forPROTEIN SEQUENCE OF 2-21TissuePlateletCategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCFEBS Lett. 264:270-274 (1990)Cited in1
Suppression of cell motility and metastasis by transfection with human motility-related protein (MRP-1/CD9) DNA.Ikeyama S., Koyama M., Yamaoko M., Sasada R., Miyake M.View abstractCited forFUNCTION IN CELL MOTILITY AND METASTASISCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Exp. Med. 177:1231-1237 (1993)Cited in1
CD9-regulated adhesion. Anti-CD9 monoclonal antibody induce pre-B cell adhesion to bone marrow fibroblasts through de novo recognition of fibronectin.Masellis-Smith A., Shaw A.R.View abstractCited forFUNCTION IN CELL ADHESIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Immunol. 152:2768-2777 (1994)Cited in1
Structural requirements for the inhibitory action of the CD9 large extracellular domain in sperm/oocyte binding and fusion.Higginbottom A., Takahashi Y., Bolling L., Coonrod S.A., White J.M., Partridge L.J., Monk P.N.View abstractCited forFUNCTION IN SPERM-EGG FUSIONCategoriesFunctionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochem. Biophys. Res. Commun. 311:208-214 (2003)Cited in1
Tetraspanins CD9 and CD81 function to prevent the fusion of mononuclear phagocytes.Takeda Y., Tachibana I., Miyado K., Kobayashi M., Miyazaki T., Funakoshi T., Kimura H., Yamane H., Saito Y.[...], Mekada E.View abstractCited forFUNCTION, INTERACTION WITH CD81CategoriesFunction, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Cell Biol. 161:945-956 (2003)Cited in4Mapped to3
Evidence for specific tetraspanin homodimers: inhibition of palmitoylation makes cysteine residues available for cross-linking.Kovalenko O.V., Yang X., Kolesnikova T.V., Hemler M.E.View abstractCited forSUBUNITCategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochem. J. 377:407-417 (2004)Cited in1
Differential stability of tetraspanin/tetraspanin interactions: role of palmitoylation.Charrin S., Manie S., Oualid M., Billard M., Boucheix C., Rubinstein E.View abstractCited forPALMITOYLATION AT CYS-9; CYS-78; CYS-79; CYS-87; CYS-218 AND CYS-219, MUTAGENESIS OF CYS-9; CYS-78; CYS-79; CYS-87; CYS-218 AND CYS-219CategoriesPTM / Processing, Disease & VariantsSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCFEBS Lett. 516:139-144 (2002)Cited in1Mapped to5
The major CD9 and CD81 molecular partner. Identification and characterization of the complexes.Charrin S., Le Naour F., Oualid M., Billard M., Faure G., Hanash S.M., Boucheix C., Rubinstein E.View abstractCited forINTERACTION WITH PTGFRNCategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 276:14329-14337 (2001)Cited in2Mapped to10
EWI-2 is a major CD9 and CD81 partner and member of a novel Ig protein subfamily.Stipp C.S., Kolesnikova T.V., Hemler M.E.View abstractCited forINTERACTION WITH IGSF8CategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCJ. Biol. Chem. 276:40545-40554 (2001)Cited in5Mapped to15
Tetraspanin family member CD9 inhibits Aggrus/podoplanin-induced platelet aggregation and suppresses pulmonary metastasis.Nakazawa Y., Sato S., Naito M., Kato Y., Mishima K., Arai H., Tsuruo T., Fujita N.View abstractCited forFUNCTION, INTERACTION WITH PDPNCategoriesFunction, InteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBlood 112:1730-1739 (2008)Cited in2Mapped to5
DHHC2 affects palmitoylation, stability, and functions of tetraspanins CD9 and CD151.Sharma C., Yang X.H., Hemler M.E.View abstractCited forPALMITOYLATIONCategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Biol. Cell 19:3415-3425 (2008)Cited in3Mapped to7
Palmitoylation supports the association of tetraspanin CD63 with CD9 and integrin alphaIIbbeta3 in activated platelets.Israels S.J., McMillan-Ward E.M.View abstractCited forPALMITOYLATION, SUBCELLULAR LOCATION, TISSUE SPECIFICITY, INTERACTION WITH CD63, IDENTIFICATION IN A COMPLEX WITH ITGB3 AND CD63CategoriesPTM / Processing, Expression, Interaction, Subcellular LocationSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCThromb. Res. 125:152-158 (2010)Cited in2
Initial characterization of the human central proteome.Burkard T.R., Planyavsky M., Kaupe I., Breitwieser F.P., Buerckstuemmer T., Bennett K.L., Superti-Furga G., Colinge J.View abstractCited forIDENTIFICATION BY MASS SPECTROMETRY [LARGE SCALE ANALYSIS]CategoriesSequencesSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBMC Syst. Biol. 5:17-17 (2011)Cited in99+99+
CD81 controls sustained T cell activation signaling and defines the maturation stages of cognate immunological synapses.Rocha-Perugini V., Zamai M., Gonzalez-Granado J.M., Barreiro O., Tejera E., Yanez-Mo M., Caiolfa V.R., Sanchez-Madrid F.View abstractCited forINTERACTION WITH CD81CategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCMol. Cell. Biol. 33:3644-3658 (2013)Cited in4Mapped to2
Distinct regions of the large extracellular domain of tetraspanin CD9 are involved in the control of human multinucleated giant cell formation.Hulme R.S., Higginbottom A., Palmer J., Partridge L.J., Monk P.N.View abstractCited forDISULFIDE BONDSCategoriesPTM / ProcessingSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCPLoS ONE 9:E116289-E116289 (2014)Cited in1Mapped to5
The CD9, CD81, and CD151 EC2 domains bind to the classical RGD-binding site of integrin alphavbeta3.Yu J., Lee C.Y., Changou C.A., Cedano-Prieto D.M., Takada Y.K., Takada Y.View abstractCited forINTERACTION WITH INTEGRIN ITGAV:ITGB3CategoriesInteractionSourceUniProtKB reviewed (Swiss-Prot)PubMedEurope PMCBiochem. J. 474:589-596 (2017)Cited in5Mapped to10