http://purl.uniprot.org/citations/10464288 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10464288 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/10464288 | http://www.w3.org/2000/01/rdf-schema#comment | "We report the primary structure of three novel, putative zinc metalloproteases designated ADAM-TS5, ADAM-TS6, and ADAM-TS7. All have a similar domain organization, comprising a preproregion, a reprolysin-type catalytic domain, a disintegrin-like domain, a thrombospondin type-1 (TS) module, a cysteine-rich domain, a spacer domain without cysteine residues, and a COOH-terminal TS module. These genes are differentially regulated during mouse embryogenesis and in adult tissues, with Adamts5 highly expressed in the peri-implantation period in embryo and trophoblast. These proteins are similar to four other cognate gene products, defining a distinct family of human reprolysin-like metalloproteases, the ADAM-TS family. The other members of the family are ADAM-TS1, an inflammation-induced gene, the procollagen I/II amino-propeptide processing enzyme (PCINP, ADAM-TS2), and proteins predicted by the KIAA0366 and KIAA0688 genes (ADAM-TS3 and ADAM-TS4). Individual ADAM-TS members differ in the number of COOH-terminal TS modules, and some have unique COOH-terminal domains. The ADAM-TS genes are dispersed in human and mouse genomes."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.36.25555"xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.org/dc/terms/identifier | "doi:10.1074/jbc.274.36.25555"xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/author | "Seldin M.F."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/author | "Seldin M.F."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/author | "Apte S.S."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/author | "Apte S.S."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/author | "Hirohata S."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/author | "Hirohata S."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/author | "Hurskainen T.L."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/author | "Hurskainen T.L."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/date | "1999"xsd:gYear |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/name | "J. Biol. Chem."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/pages | "25555-25563"xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/pages | "25555-25563"xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/title | "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/title | "ADAM-TS5, ADAM-TS6, and ADAM-TS7, novel members of a new family of zinc metalloproteases."xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/volume | "274"xsd:string |
http://purl.uniprot.org/citations/10464288 | http://purl.uniprot.org/core/volume | "274"xsd:string |
http://purl.uniprot.org/citations/10464288 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10464288 |
http://purl.uniprot.org/citations/10464288 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/10464288 |