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http://purl.uniprot.org/citations/3004934http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3004934http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/3004934http://www.w3.org/2000/01/rdf-schema#comment"cDNA clones coding for human S-protein have been isolated using monoclonal antibodies to screen a cDNA library in pEX. These clones are shown to be authentic S-protein clones on the basis of sequence, composition and immunological criteria. The complete open reading frame sequence for S-protein has been determined and shows it to be a single polypeptide chain of 459 amino acids preceded by a cleaved leader peptide of 19 residues. No evidence was found for polymorphism of S-protein suggesting that different molecular weight forms arise by proteolytic degradation. Of the first 44 amino-terminal residues 42 are identical with the so-called somatomedin B peptide suggesting that S-protein is the somatomedin B precursor. Striking homology is found in the rest of the sequence with the serum spreading factor, vitronectin, which has also been shown to contain somatomedin B sequences at its amino terminus. We conclude that S-protein and vitronectin are identical and discuss the relevance of this finding to the coagulation and complement pathways."xsd:string
http://purl.uniprot.org/citations/3004934http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1985.tb04058.x"xsd:string
http://purl.uniprot.org/citations/3004934http://purl.org/dc/terms/identifier"doi:10.1002/j.1460-2075.1985.tb04058.x"xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/author"Jenne D.E."xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/author"Jenne D.E."xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/author"Stanley K.K."xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/author"Stanley K.K."xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/date"1985"xsd:gYear
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/date"1985"xsd:gYear
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/name"EMBO J."xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/pages"3153-3157"xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/pages"3153-3157"xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/title"Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion."xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/title"Molecular cloning of S-protein, a link between complement, coagulation and cell-substrate adhesion."xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/3004934http://purl.uniprot.org/core/volume"4"xsd:string
http://purl.uniprot.org/citations/3004934http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3004934
http://purl.uniprot.org/citations/3004934http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/3004934
http://purl.uniprot.org/citations/3004934http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3004934
http://purl.uniprot.org/citations/3004934http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/3004934
http://purl.uniprot.org/embl-cds/CAA26933.1http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3004934
http://purl.uniprot.org/uniprot/P04004http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/3004934