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Volumn 275, Issue 38, 2000, Pages 29648-29653
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The propeptide domain of membrane type 1-matrix metalloproteinase acts as an intramolecular chaperone when expressed in trans with the mature sequence in COS-1 cells
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Author keywords
[No Author keywords available]
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Indexed keywords
CHAPERONE;
COMPLEMENTARY DNA;
GELATINASE;
MATRIX METALLOPROTEINASE;
PEPTIDE;
AMINO ACID SEQUENCE;
ANIMAL CELL;
ARTICLE;
ENZYME ACTIVITY;
GENE SEQUENCE;
GENETIC TRANSFECTION;
MEMBRANE BINDING;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN EXPRESSION;
PROTEIN FOLDING;
STRUCTURE ACTIVITY RELATION;
AMINO ACID SEQUENCE;
ANIMALS;
COS CELLS;
DNA, COMPLEMENTARY;
GENE EXPRESSION REGULATION, ENZYMOLOGIC;
MATRIX METALLOPROTEINASE 1;
MOLECULAR CHAPERONES;
MOLECULAR SEQUENCE DATA;
PROTEIN PRECURSORS;
SEQUENCE ALIGNMENT;
ANIMALIA;
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EID: 0034703025
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M001920200 Document Type: Article |
Times cited : (39)
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References (30)
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