The chaperonin cycle cannot substitute for prolyl isomerase activity, but GroEL alone promotes productive folding of a cyclophilin-sensitive substrate to a cyclophilin-resistant form

EMBO Journal

Volumn 16, Issue 15, 1997, Pages 4568-4578

  Von Ahsen, Oliver ^a   Tropschug, Maximilian ^a   Pfanner, Nikolaus ^a   Rassow, Joachim ^a  

^a UNIVERSITY OF FREIBURG   (Germany)

Author keywords

Cyclophilin; GroEL; Peptidyl prolyl cis trans isomerase; Protein folding

Indexed keywords

CHAPERONIN; CYCLOPHILIN; ISOMERASE;

ARTICLE; CONTROLLED STUDY; ENZYME ACTIVITY; ENZYME SUBSTRATE; ISOMERISM; NONHUMAN; PRIORITY JOURNAL; PROTEIN DENATURATION; PROTEIN FOLDING; PROTEIN PROTEIN INTERACTION; PROTEIN TERTIARY STRUCTURE;

AMINO ACID ISOMERASES; ANIMALS; CARRIER PROTEINS; CHAPERONINS; FUNGAL PROTEINS; GROEL PROTEIN; GROES PROTEIN; NEUROSPORA CRASSA; PEPTIDYLPROLYL ISOMERASE; PROTEIN CONFORMATION; PROTEIN FOLDING; RECOMBINANT FUSION PROTEINS; SUBSTRATE SPECIFICITY; TETRAHYDROFOLATE DEHYDROGENASE;

EID: 0030837026     PISSN: 02614189     EISSN: None     Source Type: Journal    
DOI: 10.1093/emboj/16.15.4568     Document Type: Article

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