http://purl.uniprot.org/citations/1709100 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/1709100 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/1709100 | http://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/1709100 | http://purl.org/dc/terms/identifier | "doi:10.1016/0014-4827(91)90351-t"xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.org/dc/terms/identifier | "doi:10.1016/0014-4827(91)90351-t"xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/author | "Hashimoto K."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/author | "Hashimoto K."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/author | "Kato I."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/author | "Kato I."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/author | "Takahara K."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/author | "Takahara K."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/author | "Yaoi Y."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/author | "Yaoi Y."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/date | "1991"xsd:gYear |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/date | "1991"xsd:gYear |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/name | "Exp. Cell Res."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/name | "Exp. Cell Res."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/pages | "180-185"xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/pages | "180-185"xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/title | "Insulin binds to type V collagen with retention of mitogenic activity."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/title | "Insulin binds to type V collagen with retention of mitogenic activity."xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/volume | "194"xsd:string |
http://purl.uniprot.org/citations/1709100 | http://purl.uniprot.org/core/volume | "194"xsd:string |
http://purl.uniprot.org/citations/1709100 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1709100 |
http://purl.uniprot.org/citations/1709100 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/1709100 |