http://purl.uniprot.org/citations/19643669 | http://www.w3.org/1999/02/22-rdf-syntax-ns#type | http://purl.uniprot.org/core/Journal_Citation |
http://purl.uniprot.org/citations/19643669 | http://www.w3.org/2000/01/rdf-schema#comment | "When mast cells are activated they can respond by releasing their secretory granule compounds, including mast cell-specific proteases of chymase, tryptase and carboxypeptidase A (MC-CPA) type. MC-CPA is a dominant protein component of the mast cell granule and the MC-CPA gene is extremely highly expressed. Despite this, relatively little has been known of its biological function. However, the recent generation of mouse strains lacking MC-CPA has opened up new possibilities for investigations related to this protease. This recent development has revealed a role for MC-CPA in regulating innate immunity responses, including the degradation of harmful substances such as the vasoconstrictive factor endothelin 1 and snake venom toxins. Here, we summarize the current knowledge of MC-CPA."xsd:string |
http://purl.uniprot.org/citations/19643669 | http://purl.org/dc/terms/identifier | "doi:10.1016/j.it.2009.04.008"xsd:string |
http://purl.uniprot.org/citations/19643669 | http://purl.uniprot.org/core/author | "Knight S.D."xsd:string |
http://purl.uniprot.org/citations/19643669 | http://purl.uniprot.org/core/author | "Wernersson S."xsd:string |
http://purl.uniprot.org/citations/19643669 | http://purl.uniprot.org/core/author | "Pejler G."xsd:string |
http://purl.uniprot.org/citations/19643669 | http://purl.uniprot.org/core/author | "Henningsson F."xsd:string |
http://purl.uniprot.org/citations/19643669 | http://purl.uniprot.org/core/date | "2009"xsd:gYear |
http://purl.uniprot.org/citations/19643669 | http://purl.uniprot.org/core/name | "Trends Immunol"xsd:string |
http://purl.uniprot.org/citations/19643669 | http://purl.uniprot.org/core/pages | "401-408"xsd:string |
http://purl.uniprot.org/citations/19643669 | http://purl.uniprot.org/core/title | "Novel insights into the biological function of mast cell carboxypeptidase A."xsd:string |
http://purl.uniprot.org/citations/19643669 | http://purl.uniprot.org/core/volume | "30"xsd:string |
http://purl.uniprot.org/citations/19643669 | http://www.w3.org/2004/02/skos/core#exactMatch | http://purl.uniprot.org/pubmed/19643669 |
http://purl.uniprot.org/citations/19643669 | http://xmlns.com/foaf/0.1/primaryTopicOf | https://pubmed.ncbi.nlm.nih.gov/19643669 |
http://purl.uniprot.org/uniprot/#_B2R941-mappedCitation-19643669 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19643669 |
http://purl.uniprot.org/uniprot/#_P15088-mappedCitation-19643669 | http://www.w3.org/1999/02/22-rdf-syntax-ns#object | http://purl.uniprot.org/citations/19643669 |
http://purl.uniprot.org/uniprot/P15088 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19643669 |
http://purl.uniprot.org/uniprot/B2R941 | http://purl.uniprot.org/core/mappedCitation | http://purl.uniprot.org/citations/19643669 |