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 ResearchMeSH KeywordsAlpha-SynucleinAnimalsBrainDisease Models, AnimalGreen Fluorescent ProteinsHEK293 CellsHSP110 Heat-Shock ProteinsHumansMice, TransgenicParkinson DiseaseSpinal CordSynucleinopathiesConceptsΑ-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
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