| http://purl.uniprot.org/citations/2954816 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2954816 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2954816 | http://www.w3.org/2000/01/rdf-schema#comment | "The lymphocyte-function-associated antigen-1 (LFA-1), the complement receptor type 3 (CR3) and the antigen p150,95 are cell-surface glycoproteins. They are heterodimeric complexes, each containing a unique alpha-subunit noncovalently associated with a common beta-subunit. We have purified the beta-subunit from human spleen and obtained limited peptide sequences. What appears to be the complete primary structure for the fully processed beta-subunit was obtained by cDNA sequencing of clones from a phorbol ester (PMA) stimulated U937 cDNA library. There are five possible glycosylation sites and a transmembrane segment. The sequence contains a high level of cysteine (7.6%), with 24 of the 57 cysteine residues being found in three repeating units each with eight residues. The entire primary structure has 47% identity to a subunit of a fibronectin binding protein from chicken fibroblasts. It seems that LFA-1, CR3 and p150,95 antigens may belong to an extended family of cell surface molecules including the fibronectin binding protein."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.org/dc/terms/identifier | "doi:10.1002/j.1460-2075.1987.tb04838.x"xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.org/dc/terms/identifier | "doi:10.1002/j.1460-2075.1987.tb04838.x"xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Gagnon J."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Gagnon J."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Willis A.C."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Willis A.C."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Hildreth J.E."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Hildreth J.E."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Law S.K.A."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Law S.K.A."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Wong A.J."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Wong A.J."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Wells C.E."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/author | "Wells C.E."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/date | "1987"xsd:gYear |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/name | "EMBO J."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/pages | "915-919"xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/pages | "915-919"xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/title | "The primary structure of the beta-subunit of the cell surface adhesion glycoproteins LFA-1, CR3 and p150,95 and its relationship to the fibronectin receptor."xsd:string |
| http://purl.uniprot.org/citations/2954816 | http://purl.uniprot.org/core/title | "The primary structure of the beta-subunit of the cell surface adhesion glycoproteins LFA-1, CR3 and p150,95 and its relationship to the fibronectin receptor."xsd:string |