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Amyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis

dc.rights.licenseopenen_US
dc.contributor.authorNGUYEN, Phuong H.
dc.contributor.authorRAMAMOORTHY, Ayyalusamy
dc.contributor.authorSAHOO, Bikash R.
dc.contributor.authorZHENG, Jie
dc.contributor.authorFALLER, Peter
dc.contributor.authorSTRAUB, John E.
dc.contributor.authorDOMINGUEZ, Laura
dc.contributor.authorSHEA, Joan-Emma
dc.contributor.authorDOKHOLYAN, Nikolay V.
dc.contributor.authorDE SIMONE, Alfonso
dc.contributor.authorMA, Buyong
dc.contributor.authorNUSSINOV, Ruth
dc.contributor.authorNAJAFI, Saeed
dc.contributor.authorNGO, Son Tung
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorLOQUET, Antoine
dc.contributor.authorCHIRICOTTO, Mara
dc.contributor.authorGANGULY, Pritam
dc.contributor.authorMCCARTY, James
dc.contributor.authorLI, Mai Suan
dc.contributor.authorHALL, Carol
dc.contributor.authorWANG, Yiming
dc.contributor.authorMILLER, Yifat
dc.contributor.authorMELCHIONNA, Simone
hal.structure.identifierChimie et Biologie des Membranes et des Nanoobjets [CBMN]
dc.contributor.authorHABENSTEIN, Birgit
dc.contributor.authorTIMR, Stepan
dc.contributor.authorCHEN, Jiaxing
dc.contributor.authorHNATH, Brianna
dc.contributor.authorSTRODEL, Birgit
dc.contributor.authorKAYED, Rakez
dc.contributor.authorLESNE, Sylvain
dc.contributor.authorWEI, Guanghong
dc.contributor.authorSTERPONE, Fabio
dc.contributor.authorDOIG, Andrew J.
dc.contributor.authorDERREUMAUX, Philippe
dc.date.accessioned2021-07-01T09:32:23Z
dc.date.available2021-07-01T09:32:23Z
dc.date.issued2021
dc.identifier.issn0009-2665en_US
dc.identifier.urihttps://oskar-bordeaux.fr/handle/20.500.12278/94952
dc.description.abstractEnProtein misfolding and aggregation is observed in many amyloidogenic diseases affecting either the central nervous system or a variety of peripheral tissues. Structural and dynamic characterization of all species along the pathways from monomers to fibrils is challenging by experimental and computational means because they involve intrinsically disordered proteins in most diseases. Yet understanding how amyloid species become toxic is the challenge in developing a treatment for these diseases. Here we review what computer, in vitro, in vivo, and pharmacological experiments tell us about the accumulation and deposition of the oligomers of the (A beta, tau), alpha-synuclein, IAPP, and superoxide dismutase 1 proteins, which have been the mainstream concept underlying Alzheimer's disease (AD), Parkinson's disease (PD), type II diabetes (T2D), and amyotrophic lateral sclerosis (ALS) research, respectively, for many years.
dc.language.isoENen_US
dc.subject.enNanofibers
dc.subject.enPeptides and proteins
dc.subject.enGenetics
dc.subject.enAggregation
dc.subject.enCrystal cleavage
dc.title.enAmyloid Oligomers: A Joint Experimental/Computational Perspective on Alzheimer's Disease, Parkinson's Disease, Type II Diabetes, and Amyotrophic Lateral Sclerosis
dc.typeArticle de revueen_US
dc.identifier.doi10.1021/acs.chemrev.0c01122en_US
dc.subject.halChimie/Matériauxen_US
bordeaux.journalChemical Reviewsen_US
bordeaux.page2545-2647en_US
bordeaux.volume121en_US
bordeaux.hal.laboratoriesInstitut de Chimie & de Biologie des Membranes & des Nano-objets (CBMN) - UMR 5248en_US
bordeaux.issue4en_US
bordeaux.institutionUniversité de Bordeauxen_US
bordeaux.institutionBordeaux INPen_US
bordeaux.institutionCNRSen_US
bordeaux.peerReviewedouien_US
bordeaux.inpressnonen_US
hal.identifierhal-03268585
hal.exportfalse
bordeaux.COinSctx_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.jtitle=Chemical%20Reviews&rft.date=2021&rft.volume=121&rft.issue=4&rft.spage=2545-2647&rft.epage=2545-2647&rft.eissn=0009-2665&rft.issn=0009-2665&rft.au=NGUYEN,%20Phuong%20H.&RAMAMOORTHY,%20Ayyalusamy&SAHOO,%20Bikash%20R.&ZHENG,%20Jie&FALLER,%20Peter&rft.genre=article


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