1999
Global unfolding of a substrate protein by the Hsp100 chaperone ClpA
Weber-Ban E, Reid B, Miranker A, Horwich A. Global unfolding of a substrate protein by the Hsp100 chaperone ClpA. Nature 1999, 401: 90-93. PMID: 10485712, DOI: 10.1038/43481.Peer-Reviewed Original ResearchConceptsSubstrate proteinsATP-dependent degradationGreen fluorescent protein GFPHydrogen exchange experimentsStable monomeric proteinFluorescent protein GFPNon-native formsChaperone ClpAChaperone familyEukaryotic proteinsProtease ClpPPresence of ATPChaperonin GroELHexameric ringClpAProteasome functionProtein GFPProtein structureMonomeric proteinNative proteinGlobal unfoldingProteinCentral channelRecognition peptideClpAP
1998
Maturation of Human Cyclin E Requires the Function of Eukaryotic Chaperonin CCT
Won K, Schumacher R, Farr G, Horwich A, Reed S. Maturation of Human Cyclin E Requires the Function of Eukaryotic Chaperonin CCT. Molecular And Cellular Biology 1998, 18: 7584-7589. PMID: 9819444, PMCID: PMC109339, DOI: 10.1128/mcb.18.12.7584.Peer-Reviewed Original ResearchConceptsHuman cyclin EChaperonin CCTCyclin EEukaryotic cytosolic chaperonin CCTCytosolic chaperonin CCTEukaryotic chaperonin CCTLarge oligomeric assembliesYeast-based screenG1/S phase transitionCyclin-dependent kinase CDK2ATP-dependent processS phase transitionCCT complexPresence of ATPProteasomal actionCCT functionHuman proteinsKinase CDK2Oligomeric assembliesHuman cellsNative stateCDK2ProteinMaturationBiogenesis
1997
Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL
Goldberg M, Zhang J, Sondek S, Matthews C, Fox R, Horwich A. Native-like structure of a protein-folding intermediate bound to the chaperonin GroEL. Proceedings Of The National Academy Of Sciences Of The United States Of America 1997, 94: 1080-1085. PMID: 9037009, PMCID: PMC19747, DOI: 10.1073/pnas.94.4.1080.Peer-Reviewed Original ResearchConceptsNative-like structureChaperonin GroELDihydrofolate reductaseProtein-folding intermediatesNative dihydrofolate reductaseStopped-flow fluorescence experimentsNonnative proteinsSubstrate proteinsProductive foldingPresence of ATPHuman dihydrofolate reductaseHydrogen-deuterium exchangeGroELPrimary structureProteinCentral channelHydrophobic interactionsFluorescence experimentsGroESFoldingSpeciesReductaseNMR spectroscopyDistant partsATP
1996
Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction
Weissman J, Rye H, Fenton W, Beechem J, Horwich A. Characterization of the Active Intermediate of a GroEL–GroES-Mediated Protein Folding Reaction. Cell 1996, 84: 481-490. PMID: 8608602, DOI: 10.1016/s0092-8674(00)81293-3.Peer-Reviewed Original ResearchConceptsCis ternary complexProtein foldingRelease of GroESAddition of GroESFolding reactionTernary complexNonhydrolyzable ATP analogGroES releaseProtein folding reactionSubstrate proteinsPresence of ATPGroEL mutantGroEL-GroESGroEL complexNonnative substratesATP hydrolysisGroESComplete foldingSubstrate flexibilityATP analogFoldingFluorescence anisotropyActive stateATPRecent studies