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Volumn 277, Issue 25, 2002, Pages 22260-22270
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Binding of hydrophobic peptides to several non-catalytic sites promotes peptide hydrolysis by all active sites of 20 S proteasomes. Evidence for peptide-induced channel opening in the α-rings
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Author keywords
[No Author keywords available]
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Indexed keywords
CATALYSIS;
CHEMICAL ACTIVATION;
HYDROLYSIS;
HYDROPHOBICITY;
YEAST;
PEPTIDES;
BIOCHEMISTRY;
CASPASE;
CHYMOTRYPSIN;
MUTANT PROTEIN;
PEPTIDE DERIVATIVE;
POTASSIUM ION;
PROTEASOME;
TRYPSIN;
ALLOSTERISM;
ARTICLE;
BINDING SITE;
CHANNEL GATING;
ENZYME ACTIVATION;
ENZYME ACTIVE SITE;
ENZYME CONFORMATION;
HYDROLYSIS;
HYDROPHOBICITY;
MUTATION;
PRIORITY JOURNAL;
PROTEIN BINDING;
PROTEIN DEGRADATION;
NON-PROGRAMMATIC;
ALLOSTERIC SITE;
ANIMALS;
BINDING SITES;
CASPASES;
CATALYTIC DOMAIN;
CHYMOTRYPSIN;
CYSTEINE ENDOPEPTIDASES;
DOSE-RESPONSE RELATIONSHIP, DRUG;
HYDROLYSIS;
KINETICS;
MULTIENZYME COMPLEXES;
MUSCLES;
MUTATION;
PEPTIDE HYDROLASES;
PEPTIDES;
POTASSIUM CHLORIDE;
PROTEASOME ENDOPEPTIDASE COMPLEX;
PROTEIN BINDING;
PROTEIN CONFORMATION;
RABBITS;
RECOMBINANT PROTEINS;
SACCHAROMYCES CEREVISIAE;
TIME FACTORS;
TRYPSIN;
EUKARYOTA;
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EID: 0037151122
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M112360200 Document Type: Article |
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Times cited : (166)
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References (37)
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