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http://purl.uniprot.org/citations/7531823http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7531823http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/7531823http://www.w3.org/2000/01/rdf-schema#comment"E-SELECTIN is an inducible cell-adhesion molecule on endothelial cells, which mediates the binding of neutrophils and functions as a Ca(2+)-dependent lectin. We have recently identified a 150K glycoprotein as the major ligand for E-selectin on myeloid cells, using a recombinant antibody-like form of mouse E-selectin as an affinity probe. Here we report the isolation of a mouse complementary DNA for this E-selectin ligand (ESL-1). The predicted amino-acid sequence of ESL-1 is 94% identical (over 1,078 amino acids) to the recently identified chicken cysteine-rich fibroblast growth-factor receptor, except for a unique 70-amino-acid aminoterminal domain of mature ESL-1. Fucosylation of ESL-1 is imperative for affinity isolation with E-selectin-IgG. A fucosylated, recombinant antibody-like form of ESL-1, but not of L-selectin, supports adhesion of E-selectin-transfected Chinese hamster ovary cells. Antibodies against ESL-1 block the binding of mouse myeloid cells to E-selectin. ESL-1, with a structure essentially identical to that of a receptor, thus functions as a cell adhesion ligand of E-selectin."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.org/dc/terms/identifier"doi:10.1038/373615a0"xsd:string
http://purl.uniprot.org/citations/7531823http://purl.org/dc/terms/identifier"doi:10.1038/373615a0"xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Kocher H.P."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Kocher H.P."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Vestweber D."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Vestweber D."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Kleuser B."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Kleuser B."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Steegmaier M."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Steegmaier M."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Lenter M."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Lenter M."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Borges E."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Borges E."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Isenmann S."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Isenmann S."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Levinovitz A."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/author"Levinovitz A."xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/date"1995"xsd:gYear
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/name"Nature"xsd:string
http://purl.uniprot.org/citations/7531823http://purl.uniprot.org/core/name"Nature"xsd:string