000117233 001__ 117233
000117233 005__ 20240319080954.0
000117233 0247_ $$2doi$$a10.1007/s00018-022-04166-9
000117233 0248_ $$2sideral$$a128638
000117233 037__ $$aART-2022-128638
000117233 041__ $$aeng
000117233 100__ $$aCascella, R.
000117233 245__ $$aEffects of oligomer toxicity, fibril toxicity and fibril spreading in synucleinopathies; 35244787
000117233 260__ $$c2022
000117233 5060_ $$aAccess copy available to the general public$$fUnrestricted
000117233 5203_ $$aProtein misfolding is a general hallmark of protein deposition diseases, such as Alzheimer’s disease or Parkinson’s disease, in which different types of aggregated species (oligomers, protofibrils and fibrils) are generated by the cells. Despite widespread interest, the relationship between oligomers and fibrils in the aggregation process and spreading remains elusive. A large variety of experimental evidences supported the idea that soluble oligomeric species of different proteins might be more toxic than the larger fibrillar forms. Furthermore, the lack of correlation between the presence of the typical pathological inclusions and disease sustained this debate. However, recent data show that the ß-sheet core of the a-Synuclein (aSyn) fibrils is unable to establish persistent interactions with the lipid bilayers, but they can release oligomeric species responsible for an immediate dysfunction of the recipient neurons. Reversibly, such oligomeric species could also contribute to pathogenesis via neuron-to-neuron spreading by their direct cell-to-cell transfer or by generating new fibrils, following their neuronal uptake. In this Review, we discuss the various mechanisms of cellular dysfunction caused by aSyn, including oligomer toxicity, fibril toxicity and fibril spreading. © 2022, The Author(s).
000117233 536__ $$9info:eu-repo/grantAgreement/ES/MCIU-MINECO-FEDER/PGC2018-096335-B-100
000117233 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000117233 590__ $$a8.0$$b2022
000117233 592__ $$a2.371$$b2022
000117233 591__ $$aCELL BIOLOGY$$b36 / 191 = 0.188$$c2022$$dQ1$$eT1
000117233 593__ $$aCell Biology$$c2022$$dQ1
000117233 591__ $$aBIOCHEMISTRY & MOLECULAR BIOLOGY$$b36 / 285 = 0.126$$c2022$$dQ1$$eT1
000117233 593__ $$aCellular and Molecular Neuroscience$$c2022$$dQ1
000117233 593__ $$aPharmacology$$c2022$$dQ1
000117233 593__ $$aMolecular Medicine$$c2022$$dQ1
000117233 593__ $$aMolecular Biology$$c2022$$dQ1
000117233 594__ $$a12.8$$b2022
000117233 655_4 $$ainfo:eu-repo/semantics/article$$vinfo:eu-repo/semantics/publishedVersion
000117233 700__ $$aBigi, A.
000117233 700__ $$0(orcid)0000-0002-9138-6687$$aCremades, N.$$uUniversidad de Zaragoza
000117233 700__ $$aCecchi, C.
000117233 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000117233 773__ $$g79, 3 (2022), 174 [20 pp]$$pCell. mol. life sci.$$tCellular and Molecular Life Sciences$$x1420-682X
000117233 8564_ $$s1757105$$uhttps://zaguan.unizar.es/record/117233/files/texto_completo.pdf$$yVersión publicada
000117233 8564_ $$s2455570$$uhttps://zaguan.unizar.es/record/117233/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000117233 909CO $$ooai:zaguan.unizar.es:117233$$particulos$$pdriver
000117233 951__ $$a2024-03-18-13:28:27
000117233 980__ $$aARTICLE