Determination of protease cleavage site motifs using mixture-based oriented peptide libraries

Nature Biotechnology

Volumn 19, Issue 7, 2001, Pages 661-667

  Turk, B E ^a   Huang, L L ^a   Piro, E T ^a   Cantley, L C ^a  

^a HARVARD MEDICAL SCHOOL   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

BIOSYNTHESIS; ENZYME INHIBITION; ENZYMES; GENES;

CLEAVAGE SITE MOTIFS;

BIOTECHNOLOGY;

MATRIX METALLOPROTEINASE; NEUROCAN; PEPTIDE LIBRARY; PROTEINASE; PROTEOGLYCAN; UNCLASSIFIED DRUG;

AMINO TERMINAL SEQUENCE; ANIMAL TISSUE; ARTICLE; CARBOXY TERMINAL SEQUENCE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME STRUCTURE; ENZYME SUBSTRATE; MOLECULAR RECOGNITION; NONHUMAN; PRIORITY JOURNAL; PROTEIN TARGETING; RAT; SEQUENCE HOMOLOGY; STRUCTURE ACTIVITY RELATION; STRUCTURE ANALYSIS; VALIDATION PROCESS;

AMINO ACID MOTIFS; AMINO ACID SEQUENCE; ANIMALS; BINDING SITES; DOSE-RESPONSE RELATIONSHIP, DRUG; HUMANS; KINETICS; LECTINS, C-TYPE; MATRIX METALLOPROTEINASE 2; MATRIX METALLOPROTEINASES; MOLECULAR SEQUENCE DATA; NERVE TISSUE PROTEINS; PEPTIDE LIBRARY; PEPTIDES; PROTEIN BINDING; PROTEOCHONDROITIN SULFATES; RATS; RECOMBINANT PROTEINS; SEQUENCE HOMOLOGY, AMINO ACID; SUBSTRATE SPECIFICITY;

ANIMALIA;

EID: 0034946412     PISSN: 10870156     EISSN: None     Source Type: Journal    
DOI: 10.1038/90273     Document Type: Article

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