000097182 001__ 97182
000097182 005__ 20210902121905.0
000097182 0247_ $$2doi$$a10.3390/ijms21218043
000097182 0248_ $$2sideral$$a121094
000097182 037__ $$aART-2020-121094
000097182 041__ $$aeng
000097182 100__ $$aGracia, P.$$uUniversidad de Zaragoza
000097182 245__ $$aMultiplicity of a-synuclein aggregated species and their possible roles in disease
000097182 260__ $$c2020
000097182 5060_ $$aAccess copy available to the general public$$fUnrestricted
000097182 5203_ $$aa-Synuclein amyloid aggregation is a defining molecular feature of Parkinson’s disease, Lewy body dementia, and multiple system atrophy, but can also be found in other neurodegenerative disorders such as Alzheimer’s disease. The process of a-synuclein aggregation can be initiated through alternative nucleation mechanisms and dominated by different secondary processes giving rise to multiple amyloid polymorphs and intermediate species. Some aggregated species have more inherent abilities to induce cellular stress and toxicity, while others seem to be more potent in propagating neurodegeneration. The preference for particular types of polymorphs depends on the solution conditions and the cellular microenvironment that the protein encounters, which is likely related to the distinct cellular locations of a-synuclein inclusions in different synucleinopathies, and the existence of disease-specific amyloid polymorphs. In this review, we discuss our current understanding on the nature and structure of the various types of a-synuclein aggregated species and their possible roles in pathology. Precisely defining these distinct a-synuclein species will contribute to understanding the molecular origins of these disorders, developing accurate diagnoses, and designing effective therapeutic interventions for these highly debilitating neurodegenerative diseases.
000097182 536__ $$9info:eu-repo/grantAgreement/ES/MCIU-FEDER/PGC2018-096335-B-100$$9info:eu-repo/grantAgreement/ES/MINECO-FEDER/BFU2015-64119-P
000097182 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000097182 590__ $$a5.923$$b2020
000097182 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b67 / 297 = 0.226$$c2020$$dQ1$$eT1
000097182 591__ $$aCHEMISTRY, MULTIDISCIPLINARY$$b49 / 178 = 0.275$$c2020$$dQ2$$eT1
000097182 592__ $$a1.455$$b2020
000097182 593__ $$aCatalysis$$c2020$$dQ1
000097182 593__ $$aComputer Science Applications$$c2020$$dQ1
000097182 593__ $$aInorganic Chemistry$$c2020$$dQ1
000097182 593__ $$aSpectroscopy$$c2020$$dQ1
000097182 593__ $$aMolecular Biology$$c2020$$dQ1
000097182 593__ $$aOrganic Chemistry$$c2020$$dQ1
000097182 593__ $$aPhysical and Theoretical Chemistry$$c2020$$dQ1
000097182 593__ $$aMedicine (miscellaneous)$$c2020$$dQ1
000097182 655_4 $$ainfo:eu-repo/semantics/review$$vinfo:eu-repo/semantics/publishedVersion
000097182 700__ $$0(orcid)0000-0002-7848-5373$$aCamino, J.D.$$uUniversidad de Zaragoza
000097182 700__ $$aVolpicelli-Daley, L.
000097182 700__ $$0(orcid)0000-0002-9138-6687$$aCremades, N.$$uUniversidad de Zaragoza
000097182 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000097182 773__ $$g21, 21 (2020), 8043 [21 pp]$$pInt. j. mol. sci.$$tInternational Journal of Molecular Sciences$$x1661-6596
000097182 8564_ $$s501262$$uhttps://zaguan.unizar.es/record/97182/files/texto_completo.pdf$$yVersión publicada
000097182 8564_ $$s493485$$uhttps://zaguan.unizar.es/record/97182/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
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000097182 951__ $$a2021-09-02-10:39:01
000097182 980__ $$aARTICLE