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Volumn 278, Issue 40, 2003, Pages 38247-38253
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Antifolding activity of the SecB chaperone is essential for secretion of HasA, a quickly folding ABC pathway substrate
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Author keywords
[No Author keywords available]
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Indexed keywords
ADENOSINETRIPHOSPHATE;
ESCHERICHIA COLI;
FLUORESCENCE;
HYDROGEN BONDS;
SECRETION PATHWAY;
BIOCHEMISTRY;
ABC TRANSPORTER;
ADENOSINE TRIPHOSPHATE;
CHAPERONE;
GUANIDINE;
MUTANT PROTEIN;
PROTEIN HASA;
PROTEIN SECB;
TRYPTOPHAN;
UNCLASSIFIED DRUG;
AMINO TERMINAL SEQUENCE;
ARTICLE;
CARBOXY TERMINAL SEQUENCE;
ESCHERICHIA COLI;
FLUORESCENCE;
HYDROGEN BOND;
NONHUMAN;
PRIORITY JOURNAL;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN SECONDARY STRUCTURE;
PROTEIN SECRETION;
PROTEIN TERTIARY STRUCTURE;
SERRATIA MARCESCENS;
SIGNAL TRANSDUCTION;
WILD TYPE;
ADENOSINE TRIPHOSPHATE;
BACTERIAL PROTEINS;
CARRIER PROTEINS;
CIRCULAR DICHROISM;
DOSE-RESPONSE RELATIONSHIP, DRUG;
ESCHERICHIA COLI;
GUANIDINE;
HYDROGEN BONDING;
KINETICS;
MEMBRANE PROTEINS;
MODELS, STATISTICAL;
MUTATION;
PLASMIDS;
PROTEIN BINDING;
PROTEIN FOLDING;
PROTEIN STRUCTURE, SECONDARY;
PROTEIN STRUCTURE, TERTIARY;
SERRATIA MARCESCENS;
TEMPERATURE;
TIME FACTORS;
ULTRAVIOLET RAYS;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
NEGIBACTERIA;
SERRATIA MARCESCENS;
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EID: 0141532228
PISSN: 00219258
EISSN: None
Source Type: Journal
DOI: 10.1074/jbc.M302322200 Document Type: Article |
Times cited : (26)
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References (35)
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