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Parkinson Disease: HELP
Articles by James A. Jarvis
Based on 1 article published since 2010
(Why 1 article?)

Between 2010 and 2020, James A. Jarvis wrote the following article about Parkinson Disease.
+ Citations + Abstracts
1 Article Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers. 2017

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. ·Department of Chemistry, University of Cambridge, Cambridge CB2 1EW, UK. · Department of Life Sciences, Imperial College London, London SW7 2AZ, UK. · Centre for Biological Sciences and Institute for Life Sciences, University of Southampton, Southampton SO17 1BJ, UK. · Department of Experimental and Clinical Biomedical Sciences, Section of Biochemistry, University of Florence, 50134 Florence, Italy. · Biocomputation and Complex Systems Physics Institute (BIFI), Joint Unit BIFI-Instituto de Química Física "Rocasolano" (Consejo Superior de Investigaciones Científicas), University of Zaragoza, 50018 Zaragoza, Spain. · Molecular Medicine, National Heart and Lung Institute, Imperial College London, London SW7 2AZ, UK. ·Science · Pubmed #29242346.

ABSTRACT: Oligomeric species populated during the aggregation process of α-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 α-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 α-synuclein oligomers suppressed their toxicity in neuroblastoma cells and primary cortical neurons.