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Título: | Structural basis of membrane disruption and cellular toxicity by a-synuclein oligomers |
Autor: | Fusco, Giuliana; Chen, Serene W.; Williamson, Philip T. F.; Cascella, Roberta; Perni, Michele; Jarvis, James A.; Cecchi, Cristina; Vendruscolo, Michele; Chiti, Fabrizio; Cremades, Nunilo; Ying, Liming; Dobson, Christopher M.; De Simone, Alfonso | Fecha de publicación: | 15-dic-2017 | Editor: | American Association for the Advancement of Science | Citación: | Science 358 (6369): 1440- (2017) | Resumen: | Oligomeric species populated during the aggregation process of a-synuclein have been linked to neuronal impairment in Parkinson's disease and related neurodegenerative disorders. By using solution and solid-state nuclear magnetic resonance techniques in conjunction with other structural methods, we identified the fundamental characteristics that enable toxic a-synuclein oligomers to perturb biological membranes and disrupt cellular function; these include a highly lipophilic element that promotes strong membrane interactions and a structured region that inserts into lipid bilayers and disrupts their integrity. In support of these conclusions, mutations that target the region that promotes strong membrane interactions by a-synuclein oligomers suppressed their toxicity in neuroblastoma cells and primary cortical neurons. | Descripción: | 5 pags, 3 figs | URI: | http://hdl.handle.net/10261/255964 | DOI: | 10.1126/science.aan6160 | ISSN: | 0036-8075 | E-ISSN: | 1095-9203 |
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