65317 20200117221626.0 doi 10.1016/j.nbd.2017.07.009 sideral 104239 ART-2018-104239 eng (orcid)0000-0002-9138-6687 Cremades, N. Universidad de Zaragoza The contribution of biophysical and structural studies of protein self-assembly to the design of therapeutic strategies for amyloid diseases 2018 Access copy available to the general public Unrestricted Many 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. info:eu-repo/semantics/openAccess by http://creativecommons.org/licenses/by/3.0/es/ 5.16 2018 NEUROSCIENCES 47 / 266 = 0.177 2018 Q1 T1 2.665 2018 Neurology 2018 Q1 info:eu-repo/semantics/review info:eu-repo/semantics/publishedVersion Dobson, C.M. 1002 060 Universidad de Zaragoza Dpto. Bioq.Biolog.Mol. Celular Área Bioquímica y Biolog.Mole. 109 (2018), 178-190 Neurobiol. dis. NEUROBIOLOGY OF DISEASE 0969-9961 527078 http://zaguan.unizar.es/record/65317/files/texto_completo.pdf Versión publicada 92482 http://zaguan.unizar.es/record/65317/files/texto_completo.jpg?subformat=icon icon Versión publicada oai:zaguan.unizar.es:65317 articulos driver 2020-01-17-21:57:29 ARTICLE