RDF/XMLNTriplesTurtleShow queryShare
SubjectPredicateObject
http://purl.uniprot.org/citations/1709100http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1709100http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/1709100http://www.w3.org/2000/01/rdf-schema#comment"The abilities of eight extracellular matrix proteins, fibronectin, vitronectin, laminin, and collagen types I, II, III, IV, and V to bind insulin were examined by binding studies with insulin conjugated with peroxidase. At a physiological pH and ionic strength, type V collagen bound to insulin most strongly. The other types of collagen, laminin, and vitronectin also bound insulin with affinity lower than that of type V collagen. The insulin-binding site of type V collagen was in a 30-kDa CNBr fragment of the alpha 1 (V) chain. Analysis of the amino acid sequence showed that this 30-kDa fragment was identical to the heparin-binding fragment of type V collagen. The insulin-binding sites of laminin and vitronectin were located in the A chain and in the heparin-binding domain, respectively. Insulin bound to type V collagen stimulated the synthesis of DNA by mouse mammary tumor MTD cells, indicating that bound insulin retained mitogenic activity."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.org/dc/terms/identifier"doi:10.1016/0014-4827(91)90351-t"xsd:string
http://purl.uniprot.org/citations/1709100http://purl.org/dc/terms/identifier"doi:10.1016/0014-4827(91)90351-t"xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/author"Hashimoto K."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/author"Hashimoto K."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/author"Kato I."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/author"Kato I."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/author"Takahara K."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/author"Takahara K."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/author"Yaoi Y."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/author"Yaoi Y."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/date"1991"xsd:gYear
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/name"Exp. Cell Res."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/name"Exp. Cell Res."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/pages"180-185"xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/pages"180-185"xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/title"Insulin binds to type V collagen with retention of mitogenic activity."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/title"Insulin binds to type V collagen with retention of mitogenic activity."xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/volume"194"xsd:string
http://purl.uniprot.org/citations/1709100http://purl.uniprot.org/core/volume"194"xsd:string
http://purl.uniprot.org/citations/1709100http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1709100
http://purl.uniprot.org/citations/1709100http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/1709100