Probing the different chaperone activities of the bacterial HSP70-HSP40 system using a thermolabile luciferase substrate

Proteins: Structure, Function and Bioinformatics

Volumn 79, Issue 6, 2011, Pages 1991-1998

  Sharma, Sandeep K ^a   De Los Rios, Paolo ^b   Goloubinoff, Pierre ^a  

^a UNIVERSITY OF LAUSANNE   (Switzerland)

^b EPFL   (Switzerland)

Author keywords

Chaperone; DnaJ; DnaK; GrpE; Luciferase; Misfolding; Protein aggregation; Thioflavin T; Unfolding

Indexed keywords

ADENOSINE TRIPHOSPHATE; BACTERIAL PROTEIN; BACTERIAL PROTEIN GRPE; CHAPERONE; HEAT SHOCK PROTEIN 40; HEAT SHOCK PROTEIN 70; LUCIFERASE; PROTEIN DNAJ; PROTEIN DNAK; THIOFLAVINE; UNCLASSIFIED DRUG;

ARTICLE; DENATURATION; ENZYME ACTIVITY; ESCHERICHIA COLI; FLUORESCENCE; HEAT STRESS; LIGHT SCATTERING; NONHUMAN; PRIORITY JOURNAL; PROTEIN FOLDING; THERMODYNAMICS;

ADENOSINE TRIPHOSPHATASES; ANIMALS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; FIREFLIES; HEAT-SHOCK PROTEINS; HOT TEMPERATURE; HSP40 HEAT-SHOCK PROTEINS; HSP70 HEAT-SHOCK PROTEINS; LUCIFERASES; MUTATION; PROTEIN FOLDING; PROTEIN STABILITY;

BACTERIA (MICROORGANISMS); ESCHERICHIA COLI; MAMMALIA;

EID: 79955724860     PISSN: 08873585     EISSN: 10970134     Source Type: Journal    
DOI: 10.1002/prot.23024     Document Type: Article

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