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
2019
Hsp110 mitigates α-synuclein pathology in vivo
Taguchi YV, Gorenberg EL, Nagy M, Thrasher D, Fenton WA, Volpicelli-Daley L, Horwich AL, Chandra SS. Hsp110 mitigates α-synuclein pathology in vivo. Proceedings Of The National Academy Of Sciences Of The United States Of America 2019, 116: 24310-24316. PMID: 31685606, PMCID: PMC6883785, DOI: 10.1073/pnas.1903268116.Peer-Reviewed Original ResearchConceptsΑ-synuclein pathologyOverexpression of Hsp110Α-synuclein aggregationPresynaptic protein α-synucleinΑ-synuclein seedsΑ-synuclein oligomersLewy bodiesMouse modelParkinson's diseaseCell culture modelSynaptic proteomeΑ-synucleinProtein α-synucleinPathologyCulture modelDiseaseMammalian cell culture modelsProtein changesOverexpressionVivoHsp110Molecular facilitatorsMiceUnbiased analysisBrain
2001
GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated
Chaudhuri T, Farr G, Fenton W, Rospert S, Horwich A. GroEL/GroES-Mediated Folding of a Protein Too Large to Be Encapsulated. Cell 2001, 107: 235-246. PMID: 11672530, DOI: 10.1016/s0092-8674(01)00523-2.Peer-Reviewed Original Research
1991
Protein folding causes an arrest of preprotein translocation into mitochondria in vivo.
Wienhues U, Becker K, Schleyer M, Guiard B, Tropschug M, Horwich A, Pfanner N, Neupert W. Protein folding causes an arrest of preprotein translocation into mitochondria in vivo. Journal Of Cell Biology 1991, 115: 1601-1609. PMID: 1757464, PMCID: PMC2289212, DOI: 10.1083/jcb.115.6.1601.Peer-Reviewed Original ResearchMeSH KeywordsAminopterinBiological TransportIntracellular MembranesKineticsL-Lactate DehydrogenaseL-Lactate Dehydrogenase (Cytochrome)Membrane PotentialsMitochondriaProtein ConformationProtein PrecursorsProtein Processing, Post-TranslationalRecombinant Fusion ProteinsSaccharomyces cerevisiaeTetrahydrofolate DehydrogenaseConceptsMitochondrial protein uptakeTranslocation contact sitesAmino-terminal thirdStable tertiary structureDihydrofolate reductase domainImport pathwayPreprotein translocationHybrid proteinProtein foldingMitochondrial membraneTranslocation sitesContact sitesCytochrome b2Fusion proteinPolypeptide segmentsYeast cellsReductase domainTertiary structureProtein uptakeDihydrofolate reductaseProteinMitochondriaMembraneVivoFoldingChaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate
Martin J, Langer T, Boteva R, Schramel A, Horwich A, Hartl F. Chaperonin-mediated protein folding at the surface of groEL through a 'molten globule'-like intermediate. Nature 1991, 352: 36-42. PMID: 1676490, DOI: 10.1038/352036a0.Peer-Reviewed Original ResearchConceptsChaperonin-mediated proteinMolten globule-like intermediateMolten globule stateGroEL proteinProtein monomersMonomeric enzymeProtein structureTertiary structureATP moleculesGlobule stateGeneral mechanismMg-ATPGroESGroELFoldingProteinActive processPolypeptideEnzymeChain foldingConformationVivo