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Volumn 148, Issue 6, 2002, Pages 1757-1765
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The Escherichia coli small heat-shock proteins IbpA and IbpB prevent the aggregation of endogenous proteins denatured in vivo during extreme heat shock
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Author keywords
DnaK; Protein aggregation; lactamase precursor
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Indexed keywords
BETA LACTAMASE;
CHAPERONE;
ENZYME PRECURSOR;
FRUCTOSE BISPHOSPHATE ALDOLASE;
GLUCOSE;
HEAT SHOCK PROTEIN;
PROTEIN LBPA;
PROTEIN LBPB;
UNCLASSIFIED DRUG;
DNAK PROTEIN, E COLI;
ESCHERICHIA COLI PROTEIN;
HEAT SHOCK PROTEIN 70;
IBPA PROTEIN, E COLI;
IBPB PROTEIN, E COLI;
ARTICLE;
CELL VIABILITY;
CENTRIFUGATION;
CONTROLLED STUDY;
ENZYME INACTIVATION;
ENZYME RENATURATION;
ESCHERICHIA COLI;
GENE DELETION;
HEAT SHOCK;
IN VITRO STUDY;
IN VIVO STUDY;
INCUBATION TIME;
NONHUMAN;
OPERON;
PRIORITY JOURNAL;
PROTEIN AGGREGATION;
PROTEIN BINDING;
PROTEIN DENATURATION;
PROTEIN FOLDING;
PROTEIN ISOLATION;
PROTEIN LOCALIZATION;
PROTEIN STABILITY;
TEMPERATURE;
WILD TYPE;
BIOLOGICAL MODEL;
CHEMISTRY;
GENE EXPRESSION;
GENETICS;
HEAT SHOCK RESPONSE;
METABOLISM;
PHYSIOLOGY;
BACTERIA (MICROORGANISMS);
ESCHERICHIA COLI;
NEGIBACTERIA;
BETA-LACTAMASES;
ESCHERICHIA COLI;
ESCHERICHIA COLI PROTEINS;
GENE DELETION;
GENE EXPRESSION;
HEAT-SHOCK PROTEINS;
HEAT-SHOCK RESPONSE;
HSP70 HEAT-SHOCK PROTEINS;
MODELS, GENETIC;
MOLECULAR CHAPERONES;
OPERON;
PROTEIN DENATURATION;
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EID: 0035987265
PISSN: 13500872
EISSN: None
Source Type: Journal
DOI: 10.1099/00221287-148-6-1757 Document Type: Article |
Times cited : (91)
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References (27)
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