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Volumn 469, Issue 2-3, 2000, Pages 203-207
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The α1/2 helical backbone of the prodomains defines the intrinsic inhibitory specificity in the cathepsin L-like cysteine protease subfamily
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Author keywords
Inhibition kinetics; Papain family; Paramecium; Propeptide; Specificity
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Indexed keywords
CATHEPSIN L;
CATHEPSIN S;
CYSTEINE PROTEINASE;
PAPAIN;
SYNTHETIC PEPTIDE;
CATHEPSIN;
HYBRID PROTEIN;
PROTEINASE;
ANIMAL EXPERIMENT;
ARTICLE;
CHIMERA;
CONFORMATION;
ENZYME INHIBITION;
ENZYME KINETICS;
ENZYME SPECIFICITY;
ENZYME STRUCTURE;
NONHUMAN;
PARAMECIUM;
PRIORITY JOURNAL;
PROTEIN EXPRESSION;
AMINO ACID SEQUENCE;
ANIMAL;
CELL LINE;
CHEMISTRY;
HUMAN;
KINETICS;
MOLECULAR GENETICS;
PROTEIN SECONDARY STRUCTURE;
PROTEIN TERTIARY STRUCTURE;
SEQUENCE ANALYSIS;
STRUCTURE ACTIVITY RELATION;
AMINO ACID SEQUENCE;
ANIMALS;
CATHEPSINS;
CELL LINE;
CYSTEINE ENDOPEPTIDASES;
ENDOPEPTIDASES;
HUMANS;
KINETICS;
MOLECULAR SEQUENCE DATA;
PARAMECIUM;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
RECOMBINANT FUSION PROTEINS;
SEQUENCE ANALYSIS, PROTEIN;
STRUCTURE-ACTIVITY RELATIONSHIP;
SUBSTRATE SPECIFICITY;
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EID: 0034628674
PISSN: 00145793
EISSN: None
Source Type: Journal
DOI: 10.1016/S0014-5793(00)01281-3 Document Type: Article |
Times cited : (31)
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References (25)
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