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http://purl.uniprot.org/citations/10356396http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10356396http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/10356396http://www.w3.org/2000/01/rdf-schema#comment"Matrix metalloproteinases (MMPs) catalyze extracellular matrix degradation. Control of their activity is a promising target for therapy of diseases characterized by abnormal connective tissue turnover. MMPs are expressed as latent proenzymes that are activated by proteolytic cleavage that triggers a conformational change in the propeptide (cysteine switch). The structure of proMMP-2 reveals how the propeptide shields the catalytic cleft and that the cysteine switch may operate through cleavage of loops essential for propeptide stability."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.org/dc/terms/identifier"doi:10.1126/science.284.5420.1667"xsd:string
http://purl.uniprot.org/citations/10356396http://purl.org/dc/terms/identifier"doi:10.1126/science.284.5420.1667"xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Schneider G."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Schneider G."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Morgunova E."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Morgunova E."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Lindqvist Y."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Lindqvist Y."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Bergmann U."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Bergmann U."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Isupov M."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Isupov M."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Tryggvason K."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Tryggvason K."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Tuuttila A."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/author"Tuuttila A."xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/date"1999"xsd:gYear
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/name"Science"xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/pages"1667-1670"xsd:string
http://purl.uniprot.org/citations/10356396http://purl.uniprot.org/core/pages"1667-1670"xsd:string