000065317 001__ 65317
000065317 005__ 20200117221626.0
000065317 0247_ $$2doi$$a10.1016/j.nbd.2017.07.009
000065317 0248_ $$2sideral$$a104239
000065317 037__ $$aART-2018-104239
000065317 041__ $$aeng
000065317 100__ $$0(orcid)0000-0002-9138-6687$$aCremades, N.$$uUniversidad de Zaragoza
000065317 245__ $$aThe contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases
000065317 260__ $$c2018
000065317 5060_ $$aAccess copy available to the general public$$fUnrestricted
000065317 5203_ $$aMany neurodegenerative disorders, including Alzheimer''s, Parkinson''s and the prion diseases, are characterized by a conformational conversion of normally soluble proteins or peptides into pathological species, by a process of misfolding and self-assembly that leads ultimately to the formation of amyloid fibrils. Recent studies support the idea that multiple intermediate species with a wide variety of degrees of neuronal toxicity are generated during such processes. The development of a high level of knowledge of the nature and structure of the pathogenic amyloid species would significantly enhance efforts to underline the molecular origins of these disorders and also to develop both accurate diagnoses and effective therapeutic interventions for these types of conditions. In this review, we discuss recent biophysical and structural information concerning different types of amyloid aggregates and the way in which such information can guide rational therapeutic approaches designed to target specific pathogenic events that occur during the development of these highly debilitating and increasingly common diseases.
000065317 540__ $$9info:eu-repo/semantics/openAccess$$aby$$uhttp://creativecommons.org/licenses/by/3.0/es/
000065317 590__ $$a5.16$$b2018
000065317 591__ $$aNEUROSCIENCES$$b47 / 266 = 0.177$$c2018$$dQ1$$eT1
000065317 592__ $$a2.665$$b2018
000065317 593__ $$aNeurology$$c2018$$dQ1
000065317 655_4 $$ainfo:eu-repo/semantics/review$$vinfo:eu-repo/semantics/publishedVersion
000065317 700__ $$aDobson, C.M.
000065317 7102_ $$11002$$2060$$aUniversidad de Zaragoza$$bDpto. Bioq.Biolog.Mol. Celular$$cÁrea Bioquímica y Biolog.Mole.
000065317 773__ $$g109 (2018), 178-190$$pNeurobiol. dis.$$tNEUROBIOLOGY OF DISEASE$$x0969-9961
000065317 8564_ $$s527078$$uhttps://zaguan.unizar.es/record/65317/files/texto_completo.pdf$$yVersión publicada
000065317 8564_ $$s92482$$uhttps://zaguan.unizar.es/record/65317/files/texto_completo.jpg?subformat=icon$$xicon$$yVersión publicada
000065317 909CO $$ooai:zaguan.unizar.es:65317$$particulos$$pdriver
000065317 951__ $$a2020-01-17-21:57:29
000065317 980__ $$aARTICLE