1997
Platelet Endothelial Cell Adhesion Molecule-1 Is Phosphorylatable by c-Src, Binds Src-Src homology 2 Domain, and Exhibits Immunoreceptor Tyrosine-based Activation Motif-like Properties*
Lu T, Barreuther M, Davis S, Madri J. Platelet Endothelial Cell Adhesion Molecule-1 Is Phosphorylatable by c-Src, Binds Src-Src homology 2 Domain, and Exhibits Immunoreceptor Tyrosine-based Activation Motif-like Properties*. Journal Of Biological Chemistry 1997, 272: 14442-14446. PMID: 9162084, DOI: 10.1074/jbc.272.22.14442.Peer-Reviewed Original ResearchMeSH KeywordsGenes, srcHumansPhosphorylationPlatelet Endothelial Cell Adhesion Molecule-1Point MutationReceptors, ImmunologicSrc Homology DomainsTyrosineConceptsSrc homology 2C-SrcGST-SrcCytoplasmic tailImmunoreceptor tyrosineCytoplasmic domain sequencesEndothelial cell adhesion molecule-1Src SH2 domainCell-cell bordersPECAM-1 functionsPECAM-1PECAM-1 phosphorylationUnidentified phosphoproteinsProtein associatesHomology 2Kinase assaysSignal transductionGlutathione S-transferaseSheet migrationConfluent endothelial cellsActivation motifConsensus sequenceDomain sequencesDomain interactionsEndothelial cells
1988
Distribution of a 69-kD laminin-binding protein in aortic and microvascular endothelial cells: modulation during cell attachment, spreading, and migration.
Yannariello-Brown J, Wewer U, Liotta L, Madri J. Distribution of a 69-kD laminin-binding protein in aortic and microvascular endothelial cells: modulation during cell attachment, spreading, and migration. Journal Of Cell Biology 1988, 106: 1773-1786. PMID: 2967300, PMCID: PMC2115051, DOI: 10.1083/jcb.106.5.1773.Peer-Reviewed Original Research