1998
Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins
Kim S, Schilke B, Craig E, Horwich A. Folding in vivo of a newly translated yeast cytosolic enzyme is mediated by the SSA class of cytosolic yeast Hsp70 proteins. Proceedings Of The National Academy Of Sciences Of The United States Of America 1998, 95: 12860-12865. PMID: 9789005, PMCID: PMC23633, DOI: 10.1073/pnas.95.22.12860.Peer-Reviewed Original ResearchConceptsOrnithine transcarbamoylaseYeast cytosolic enzymesCytosolic enzymeNative stateCytosolic Hsp70 proteinsGalpha transducinCytosolic chaperoninEukaryotic cytosolYeast Hsp70Chaperone actionPosttranslational mannerYeast cytosolCytosolic proteinsHSP70 proteinHomotrimeric enzymeProteinSpecific activity
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
1996
5 Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol
Willison K, Horwich A. 5 Structure and Function of Chaperonins in Archaebacteria and Eukaryotic Cytosol. 1996, 107-136. DOI: 10.1016/b978-012237455-5/50006-3.Peer-Reviewed Original ResearchChaperonin-containing TCP-1Eukaryotic cytosolEukaryotic cellsTCP-1Protein foldingUnfolded proteinsChaperoninCytoskeletal proteinsSubunit speciesFunctional analysisGeneral functionProteinArchaebacteriaGeneral affinityCytosolFoldingSpecific affinityGenesSpeciesAffinityActinTubulinFunctionCellsUnusual type
1991
A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1
Trent J, Nimmesgern E, Wall J, Hartl F, Horwich A. A molecular chaperone from a thermophilic archaebacterium is related to the eukaryotic protein t-complex polypeptide-1. Nature 1991, 354: 490-493. PMID: 1836250, DOI: 10.1038/354490a0.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphatasesAmino Acid SequenceAnimalsArchaeal ProteinsBacterial ProteinsBase SequenceDNA-Binding ProteinsHeat-Shock ProteinsIntracellular Signaling Peptides and ProteinsMiceMicrotubule-Associated ProteinsMolecular ChaperonesMolecular Sequence DataNuclear ProteinsSaccharomyces cerevisiaeSequence Homology, Nucleic AcidSulfolobusT-Complex Genome RegionTemperatureUbiquitin-Protein LigasesConceptsComplex polypeptide 1Molecular chaperonesEukaryotic cytosolThermophilic archaebacteriumPolypeptide 1Ubiquitous eukaryotic proteinThermophilic factor 55Homo-oligomeric complexesMajor heat shock proteinsHeat shock proteinsChaperone componentsEukaryotic proteinsEssential proteinsProtein TAbundant proteinsSulfolobus shibataeComplex bindsS. shibataeChaperonesPrimary structureTF55ChaperoninProteinArchaebacteriaTCP1