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
1992
TCP1 complex is a molecular chaperone in tubulin biogenesis
Yaffe M, Farr G, Miklos D, Horwich A, Sternlicht M, Sternlicht H. TCP1 complex is a molecular chaperone in tubulin biogenesis. Nature 1992, 358: 245-248. PMID: 1630491, DOI: 10.1038/358245a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAnimalsCycloheximideDNA-Binding ProteinsIntracellular Signaling Peptides and ProteinsKineticsMacromolecular SubstancesMicrotubule-Associated ProteinsMolecular WeightNuclear ProteinsProtein BiosynthesisProtein ConformationRabbitsReticulocytesRNA, MessengerT-Complex Genome RegionTubulinUbiquitin-Protein LigasesConceptsReticulocyte lysateTubulin subunitsCytosol of eukaryotesComplex polypeptide 1Protease-sensitive conformationRabbit reticulocyte lysateCytosolic chaperonesTubulin biogenesisMajor cytosolic proteinMolecular chaperonesTCP1 complexK proteinCytosolic proteinsΒ heterodimerBiogenesisPolypeptide 1Β-tubulinProteinSubunitsChaperonesMg-ATPK-complexesMolecular targetsNonhydrolysable analogueTubulin