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http://purl.uniprot.org/citations/27176742http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27176742http://www.w3.org/1999/02/22-rdf-syntax-ns#typehttp://purl.uniprot.org/core/Journal_Citation
http://purl.uniprot.org/citations/27176742http://www.w3.org/2000/01/rdf-schema#comment"The proteasome is a multicatalytic protease responsible for the degradation of misfolded proteins. We have synthesized fluorogenic substrates in which the peptide chain was systematically elongated from two to six amino acids and evaluated the effect of peptide length on all three catalytic activities of human 20S proteasome. In the cases of five- and six-membered peptides, we have also synthesized libraries of fluorogenic substrates. Kinetic analysis revealed that six-amino-acid substrates are significantly better for chymotrypsin-like and caspase-like activity than shorter peptidic substrates. In the case of trypsin-like activity, a five-amino-acid substrate was optimal."xsd:string
http://purl.uniprot.org/citations/27176742http://purl.org/dc/terms/identifier"doi:10.1515/hsz-2016-0176"xsd:string
http://purl.uniprot.org/citations/27176742http://purl.org/dc/terms/identifier"doi:10.1515/hsz-2016-0176"xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/author"Drag M."xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/author"Drag M."xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/author"Rut W."xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/author"Rut W."xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/date"2016"xsd:gYear
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/name"Biol. Chem."xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/name"Biol. Chem."xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/pages"921-926"xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/pages"921-926"xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/title"Human 20S proteasome activity towards fluorogenic peptides of various chain lengths."xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/title"Human 20S proteasome activity towards fluorogenic peptides of various chain lengths."xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/volume"397"xsd:string
http://purl.uniprot.org/citations/27176742http://purl.uniprot.org/core/volume"397"xsd:string
http://purl.uniprot.org/citations/27176742http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27176742
http://purl.uniprot.org/citations/27176742http://www.w3.org/2004/02/skos/core#exactMatchhttp://purl.uniprot.org/pubmed/27176742
http://purl.uniprot.org/citations/27176742http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27176742
http://purl.uniprot.org/citations/27176742http://xmlns.com/foaf/0.1/primaryTopicOfhttps://pubmed.ncbi.nlm.nih.gov/27176742
http://purl.uniprot.org/uniprot/P28066http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/27176742
http://purl.uniprot.org/uniprot/P28074http://purl.uniprot.org/core/citationhttp://purl.uniprot.org/citations/27176742