1997
Chaperonin-Mediated Folding in the Eukaryotic Cytosol Proceeds through Rounds of Release of Native and Nonnative Forms
Farr G, Scharl E, Schumacher R, Sondek S, Horwich A. Chaperonin-Mediated Folding in the Eukaryotic Cytosol Proceeds through Rounds of Release of Native and Nonnative Forms. Cell 1997, 89: 927-937. PMID: 9200611, DOI: 10.1016/s0092-8674(00)80278-0.Peer-Reviewed Original ResearchConceptsRounds of releaseSubstrate proteinsNonnative formsNative formChaperonin-mediated foldingEukaryotic cytosolic chaperoninATP-dependent foldingIntact Xenopus oocytesCytosolic chaperoninBacterial chaperoninsEukaryotic cytosolChaperoninNative stateXenopus oocytesEssential roleSingle roundFoldingProteinActinTubulinOverall mechanismGroELTransducinCytosolSmall fraction
1993
A polypeptide bound by the chaperonin groEL is localized within a central cavity.
Braig K, Simon M, Furuya F, Hainfeld J, Horwich A. A polypeptide bound by the chaperonin groEL is localized within a central cavity. Proceedings Of The National Academy Of Sciences Of The United States Of America 1993, 90: 3978-3982. PMID: 8097882, PMCID: PMC46429, DOI: 10.1073/pnas.90.9.3978.Peer-Reviewed Original ResearchConceptsChaperonin GroELGroEL complexEscherichia coli chaperonin GroELOligomeric protein complexesDihydrofolate reductaseMolten globule-like intermediateCentral cavityPolypeptide chain foldingChaperonin ringsChaperonin complexProtein complexesCellular compartmentsDHFR moleculeMonomeric membersPresence of MgATPGroELNative stateEssential roleCompact conformationPolypeptideComplexesCochaperoninChaperoninMultiple sitesIntermediates