Internally quenched fluorescent peptide substrates disclose the subsite preferences of human caspases 1, 3, 6, 7 and 8

Biochemical Journal

Volumn 350, Issue 2, 2000, Pages 563-568

  Stennicke, H R ^a   Renatus, M ^a   Meldal, M ^a   Salvesen, G S ^a  

^a BURNHAM INSTITUTE   (United States)

Author keywords

Apoptosis; Protease; Specificity

Indexed keywords

3 NITROTYROSINE; ALANINE; AMINO ACID; ANTHRANILIC ACID; CASPASE; CASPASE 3; CASPASE 6; CASPASE 7; CASPASE 8; FLUORESCENT DYE; GLUTAMIC ACID; GLYCINE; INTERLEUKIN 1BETA CONVERTING ENZYME; SERINE; UNCLASSIFIED DRUG;

ACYLATION; APOPTOSIS; ARTICLE; BINDING AFFINITY; CATALYSIS; ENZYME ACTIVE SITE; ENZYME SPECIFICITY; ENZYME SUBSTRATE; ENZYME SUBSTRATE COMPLEX; HYDROLYSIS; PRIORITY JOURNAL; PROTEIN DEGRADATION;

ALANINE; ANTHRANILIC ACIDS; APOPTOSIS; BINDING SITES; CASPASE 1; CASPASE 3; CASPASE 6; CASPASE 7; CASPASE 8; CASPASE 9; CASPASES; CATALYSIS; ESCHERICHIA COLI; FLUORESCENT DYES; GLYCINE; HUMANS; KINETICS; MODELS, MOLECULAR; PEPTIDES; PROTEIN BINDING; PROTEINS; RECOMBINANT PROTEINS; SERINE; SUBSTRATE SPECIFICITY; TYROSINE;

EID: 0034283578     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/0264-6021:3500563     Document Type: Article

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