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Volumn 277, Issue 30, 2002, Pages 27378-27384
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Unexpected crucial role of residue 272 in substrate specificity of fibroblast collagenase
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Author keywords
[No Author keywords available]
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Indexed keywords
AMINO ACIDS;
COLLAGEN;
DEGRADATION;
DISSOCIATION;
ENZYMES;
SUBSTRATES;
PROTEOLYTIC ACTIVITIES;
BIOCHEMISTRY;
AMINO ACID;
ASPARTIC ACID;
COLLAGEN TYPE 1;
COLLAGENASE;
GLYCINE;
HELICASE;
MATRIX METALLOPROTEINASE;
PEPTIDE;
STROMELYSIN;
AMINO ACID SEQUENCE;
AMINO ACID SUBSTITUTION;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
COLLAGEN DEGRADATION;
CONTROLLED STUDY;
DISSOCIATION CONSTANT;
ENZYME ACTIVE SITE;
ENZYME ACTIVITY;
ENZYME SPECIFICITY;
ENZYME SUBSTRATE COMPLEX;
EXTRACELLULAR MATRIX;
FIBROBLAST;
MOLECULAR DYNAMICS;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DEGRADATION;
AMINO ACID SEQUENCE;
ANIMALS;
ASPARTIC ACID;
BINDING SITES;
CATTLE;
COLLAGEN;
DOSE-RESPONSE RELATIONSHIP, DRUG;
ELECTROPHORESIS, POLYACRYLAMIDE GEL;
GELATIN;
GLYCINE;
KINETICS;
MATRIX METALLOPROTEINASE 8;
MODELS, MOLECULAR;
MOLECULAR SEQUENCE DATA;
MUTATION;
PLASMIDS;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT PROTEINS;
SEQUENCE HOMOLOGY, AMINO ACID;
STAPHYLOCOCCUS PHAGE 3A;
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EID: 0037178891
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M201367200 Document Type: Article |
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Times cited : (34)
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References (53)
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