Crucial role of protein oligomerization in the pathogenesis of Alzheimer's and Parkinson's diseases

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dc.contributor.authorChoi, Minee L.ko
dc.contributor.authorGandhi, Soniako
dc.date.accessioned2023-02-06T02:00:36Z-
dc.date.available2023-02-06T02:00:36Z-
dc.date.created2023-02-06-
dc.date.created2023-02-06-
dc.date.issued2018-10-
dc.identifier.citationFEBS JOURNAL, v.285, no.19, pp.3631 - 3644-
dc.identifier.issn1742-464X-
dc.identifier.urihttp://hdl.handle.net/10203/305026-
dc.description.abstractMisfolding and aggregation of the proteins amyloid-, tau and alpha-synuclein is the predominant pathology underlying the neurodegenerative disorders, Alzheimer's and Parkinson's disease. While end stage insoluble products of aggregation have been well characterised in human and animal models of disease, accumulating evidence from biophysical, cellular and invivo studies has shown that soluble intermediates of aggregation, or oligomers, may be the key species that mediate toxicity and underlie seeding and spreading in disease. Here, we review the process of protein misfolding, and the intrinsic and extrinsic processes that cause the native states of the key aggregating proteins to undergo conformational change to form oligomers and ultimately fibrils. We discuss the structural features of the key toxic intermediate, and describe the putative mechanisms by which oligomers may cause cell toxicity. Finally, we explore the potential therapeutic approaches raised by the oligomer hypothesis in neurodegenerative disease.-
dc.languageEnglish-
dc.publisherWILEY-
dc.titleCrucial role of protein oligomerization in the pathogenesis of Alzheimer's and Parkinson's diseases-
dc.typeArticle-
dc.identifier.wosid000446566900007-
dc.identifier.scopusid2-s2.0-85051366887-
dc.type.rimsART-
dc.citation.volume285-
dc.citation.issue19-
dc.citation.beginningpage3631-
dc.citation.endingpage3644-
dc.citation.publicationnameFEBS JOURNAL-
dc.identifier.doi10.1111/febs.14587-
dc.contributor.localauthorChoi, Minee L.-
dc.contributor.nonIdAuthorGandhi, Sonia-
dc.description.isOpenAccessN-
dc.type.journalArticleReview-
dc.subject.keywordAuthoralpha-synuclein-
dc.subject.keywordAuthorAlzheimer&apos-
dc.subject.keywordAuthors disease-
dc.subject.keywordAuthoramyloid--
dc.subject.keywordAuthoroligomer-
dc.subject.keywordAuthorParkinson&apos-
dc.subject.keywordAuthors disease-
dc.subject.keywordAuthorprotein misfolding-
dc.subject.keywordAuthortau-
dc.subject.keywordPlusALPHA-SYNUCLEIN OLIGOMERS-
dc.subject.keywordPlusAMYLOID BETA-PEPTIDE-
dc.subject.keywordPlusOXIDATIVE STRESS-
dc.subject.keywordPlusIN-VIVO-
dc.subject.keywordPlusLIPID-PEROXIDATION-
dc.subject.keywordPlusPROMOTES FORMATION-
dc.subject.keywordPlusAPOLIPOPROTEIN-J-
dc.subject.keywordPlusCOMMON FEATURES-
dc.subject.keywordPlusCALCIUM INFLUX-
dc.subject.keywordPlusFIBRIL GROWTH-
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