| http://purl.uniprot.org/citations/2361961 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2361961 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
| http://purl.uniprot.org/citations/2361961 | http://www.w3.org/2000/01/rdf-schema#comment | "Lotus tetragonolobus agglutinin (LTA) binds preferentially to early embryonic cells in the mouse. The affinity-purified antibody raised against LTA receptors from embryonal carcinoma cells were used to screen a lambda gt11 expression library of F9 embryonal carcinoma cells, resulting in detection of a cDNA clone specifying a new glycoprotein termed "basigin." The glycoprotein has been suggested to be a transmembrane one, and was found to be a new member of the immunoglobulin (Ig) superfamily. The molecular weight of basigin was largely in the range between 43,000 and 66,000, while that of the peptide portion with a putative signal sequence was inferred to be about 30,000. Significant levels of basigin mRNA were detected not only in embryonal carcinoma cells, but also in mouse embryos at 9-15 days of gestation and in various organs of the adult mouse. The Ig-like domain of basigin is unique, since it has strong homology to both the beta-chain of major histocompatibility class II antigen and the Ig V domain. The number of amino acids between the two conserved cysteine residues is intermediate between those of the Ig V and C domains. Therefore, basigin is an interesting protein in connection with the molecular evolution of the superfamily."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.org/dc/terms/identifier | "doi:10.1093/oxfordjournals.jbchem.a123045"xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.org/dc/terms/identifier | "doi:10.1093/oxfordjournals.jbchem.a123045"xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Muramatsu T."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Muramatsu T."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Ozawa M."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Ozawa M."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Kanekura T."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Kanekura T."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Miyazawa S."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Miyazawa S."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Miyauchi T."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Miyauchi T."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Yamaoka A."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/author | "Yamaoka A."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/date | "1990"xsd:gYear |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/name | "J. Biochem."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/pages | "316-323"xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/pages | "316-323"xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/title | "Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen."xsd:string |
| http://purl.uniprot.org/citations/2361961 | http://purl.uniprot.org/core/title | "Basigin, a new, broadly distributed member of the immunoglobulin superfamily, has strong homology with both the immunoglobulin V domain and the beta-chain of major histocompatibility complex class II antigen."xsd:string |