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Volumn 19, Issue 7, 2000, Pages 569-574
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GroEL and protein disulfide isomerase each binds with folding intermediates of D-glyceraldehyde-3-phosphate dehydrogenase released from complexes formed with the other
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Author keywords
Assisted folding; Chaperone action; Folding intermediate; GAPDH; GroEL; PDI
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Indexed keywords
CHAPERONE;
CHAPERONIN;
GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE;
PROTEIN DISULFIDE ISOMERASE;
ARTICLE;
COMPLEX FORMATION;
ENZYME DENATURATION;
ENZYME REACTIVATION;
PROTEIN FOLDING;
PROTEIN PROTEIN INTERACTION;
PROTEIN STRUCTURE;
REACTION ANALYSIS;
STRUCTURE ANALYSIS;
ADENOSINE TRIPHOSPHATE;
ANIMALS;
CATTLE;
DRUG SYNERGISM;
GLYCERALDEHYDE 3-PHOSPHATE;
GLYCERALDEHYDE-3-PHOSPHATE DEHYDROGENASES;
GROEL PROTEIN;
MODELS, CHEMICAL;
MOLECULAR CHAPERONES;
PROTEIN BINDING;
PROTEIN DISULFIDE-ISOMERASE;
PROTEIN FOLDING;
PROTEIN RENATURATION;
RABBITS;
TIME FACTORS;
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EID: 0034468723
PISSN: 02778033
EISSN: None
Source Type: Journal
DOI: 10.1023/A:1007146217946 Document Type: Article |
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Times cited : (4)
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References (27)
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