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http://purl.uniprot.org/citations/15060079http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15060079http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/15060079http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Citation
http://purl.uniprot.org/citations/15060079http://www.w3.org/2000/01/rdf-schema#comment"Serum mannose-binding protein (MBP) neutralizes invading microorganisms by binding to cell surface carbohydrates and activating MBP-associated serine proteases-1, -2, and -3 (MASPs). MASP-2 subsequently cleaves complement components C2 and C4 to activate the complement cascade. To analyze the mechanisms of activation and substrate recognition by MASP-2, zymogen and activated forms have been produced, and MBP.MASP-2 complexes have been created. These preparations have been used to show that MBP modulates MASP-2 activity in two ways. First, MBP stimulates MASP-2 autoactivation by increasing the rate of autocatalysis when MBP.MASP-2 complexes bind to a glycan-coated surface. Second, MBP occludes accessory C4-binding sites on MASP-2 until activation occurs. Once these sites become exposed, MASP-2 binds to C4 while separate structural changes create a functional catalytic site able to cleave C4. Only activated MASP-2 binds to C2, suggesting that this substrate interacts only near the catalytic site and not at accessory sites. MASP-1 cleaves C2 almost as efficiently as MASP-2 does, but it does not cleave C4. Thus MASP-1 probably enhances complement activation triggered by MBP.MASP-2 complexes, but it cannot initiate activation itself."xsd:string
http://purl.uniprot.org/citations/15060079http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m401318200"xsd:string
http://purl.uniprot.org/citations/15060079http://purl.org/dc/terms/identifier"doi:10.1074/jbc.m401318200"xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/author"Wallis R."xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/author"Wallis R."xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/author"Chen C.-B."xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/author"Chen C.-B."xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/date"2004"xsd:gYear
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/name"J. Biol. Chem."xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/pages"26058-26065"xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/pages"26058-26065"xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/title"Two mechanisms for mannose-binding protein modulation of the activity of its associated serine proteases."xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/title"Two mechanisms for mannose-binding protein modulation of the activity of its associated serine proteases."xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15060079http://purl.uniprot.org/core/volume"279"xsd:string
http://purl.uniprot.org/citations/15060079http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15060079
http://purl.uniprot.org/citations/15060079http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15060079
http://purl.uniprot.org/citations/15060079http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/15060079
http://purl.uniprot.org/citations/15060079http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15060079
http://purl.uniprot.org/citations/15060079http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/15060079