2020
Chaperonin-assisted protein folding: a chronologue
Horwich AL, Fenton WA. Chaperonin-assisted protein folding: a chronologue. Quarterly Reviews Of Biophysics 2020, 53: e4. PMID: 32070442, DOI: 10.1017/s0033583519000143.Peer-Reviewed Original ResearchMeSH KeywordsAdenosine TriphosphateAmino AcidsAnimalsCarbon DioxideChaperoninsCytosolDimerizationHeat-Shock ProteinsHumansHydrophobic and Hydrophilic InteractionsKineticsMiceMitochondriaMutationNeurosporaProtein ConformationProtein DenaturationProtein FoldingRibonuclease, PancreaticRibulose-Bisphosphate CarboxylaseSurface PropertiesTemperature
2001
Mechanisms of protein folding
Grantcharova V, Alm E, Baker D, Horwich A. Mechanisms of protein folding. Current Opinion In Structural Biology 2001, 11: 70-82. PMID: 11179895, DOI: 10.1016/s0959-440x(00)00176-7.Peer-Reviewed Original ResearchConceptsEscherichia coli chaperonin GroELNon-native proteinsATP-dependent formationCo-chaperonin GroESLowest free energy pathChaperonin GroELProtein foldingUnfolded proteinsLarge proteinsGroELNative stateNative structureContact orderProteinChaperoninKinetic trapsFoldingChaperonesGroESFree energy pathPolypeptideComplexes
1999
Chaperone rings in protein folding and degradation
Horwich A, Weber-Ban E, Finley D. Chaperone rings in protein folding and degradation. Proceedings Of The National Academy Of Sciences Of The United States Of America 1999, 96: 11033-11040. PMID: 10500119, PMCID: PMC34237, DOI: 10.1073/pnas.96.20.11033.Peer-Reviewed Original ResearchConceptsSubstrate proteinsNon-native formsProcess of foldingCellular proteinsDegradation chamberProtein foldingStep of recognitionProteolytic complexRing assemblyDivergent fatesConformational changesNative stateProteinChaperoninFoldingCentral cavityCooperative interactionsATPPolypeptideFateChaperonesCompartmentalizationVital roleMotifProtease
1998
STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING
Sigler P, Xu Z, Rye H, Burston S, Fenton W, Horwich A. STRUCTURE AND FUNCTION IN GroEL-MEDIATED PROTEIN FOLDING. Annual Review Of Biochemistry 1998, 67: 581-608. PMID: 9759498, DOI: 10.1146/annurev.biochem.67.1.581.Peer-Reviewed Original ResearchConceptsProtein foldingNative stateMechanism of chaperoninsCis ternary complexAsymmetric conformational changesFinal native stateNonnative polypeptidesCochaperonin GroESGroEL ringTrans ringATP hydrolysisGenetic informationChaperonin moleculesConformational changesFolding processFoldingTernary complexPolypeptideGroESATPBiochemical investigationsFinal stepChaperoninGroELComplexes
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
Putting a lid on protein folding: structure and function of the co-chaperonin, GroES
Fenton W, Weissman J, Horwich A. Putting a lid on protein folding: structure and function of the co-chaperonin, GroES. Cell Chemical Biology 1996, 3: 157-161. PMID: 8807841, DOI: 10.1016/s1074-5521(96)90257-4.Peer-Reviewed Original Research5 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
1995
Unliganded GroEL at 2.8 Å: structure and functional implications
Sigler P, Horwich A. Unliganded GroEL at 2.8 Å: structure and functional implications. Philosophical Transactions Of The Royal Society B Biological Sciences 1995, 348: 113-119. PMID: 7770481, DOI: 10.1098/rstb.1995.0052.Peer-Reviewed Original ResearchConceptsATP-binding pocketCentral channelUnfolded polypeptidesApical domainThree-dimensional structureExtensive mutagenesisMutational studiesDyad symmetryC-terminusDistinct domainsGroELATP analogBiochemical studiesStructural scaffoldFunctional implicationsHigh saltSubunitsDomainChaperoninGroESMutagenesisEntire lengthCrystal formsPolypeptideSymmetric ring
1993
High-resolution gold labeling
Hainfeld J, Furuya F, Carbone K, Simon M, Lin B, Braig K, Horwich A, Safer D, Blechschmidt B, Sprinzl M, Ofengand J, Boublik M. High-resolution gold labeling. Microscopy And Microanalysis 1993, 51: 330-331. DOI: 10.1017/s0424820100147491.Peer-Reviewed Original ResearchGroEL complexDihydrofolate reductaseNascent polypeptide chainsChaperonin GroELMacromolecular complexesOligomeric complexesSmall proteinsActive proteinPolypeptide chainGroELChaperoninGold clustersCentral cavityGold labelingSpecific sitesGold compoundsModel substrateProteinMacromolecular sitesComplexesExternal surfaceRibosomesReductaseSitesChainA 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
1992
Chapter 26 Chaperonin-mediated protein folding
Horwich A, Caplan S, Wall J, Hartl F. Chapter 26 Chaperonin-mediated protein folding. New Comprehensive Biochemistry 1992, 22: 329-337. DOI: 10.1016/s0167-7306(08)60103-9.Peer-Reviewed Original ResearchFunction of GroELPrimary amino acid sequenceAmino acid sequenceLinear genomic DNAActive tertiary structureRelated organellesProtein foldingCentral dogmaAcid sequenceGenetic informationGenomic DNAQuaternary structureRNA messageSpontaneous foldingPrimary structureActive conformationDNA templateIntact cellsTertiary structureMolecular biologyPolypeptide chainAmino acidsBiological membranesProteinChaperonin
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
1989
Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria
Cheng M, Hartl F, Martin J, Pollock R, Kalousek F, Neuper W, Hallberg E, Hallberg R, Horwich A. Mitochondrial heat-shock protein hsp60 is essential for assembly of proteins imported into yeast mitochondria. Nature 1989, 337: 620-625. PMID: 2645524, DOI: 10.1038/337620a0.Peer-Reviewed Original Research