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@article{Fusco:2017:10.1126/science.aan6160,
author = {Fusco, G and Chen, SW and Williamson, PTF and Cascella, R and Perni, M and Jarvis, JA and Cecchi, C and Vendruscolo, M and Chiti, F and Cremades, N and Ying, L and Dobson, CM and De, Simone A},
doi = {10.1126/science.aan6160},
journal = {Science},
pages = {1440--1443},
title = {Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers},
url = {http://dx.doi.org/10.1126/science.aan6160},
volume = {358},
year = {2017}
}

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TY  - JOUR
AB  - 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.
AU  - Fusco,G
AU  - Chen,SW
AU  - Williamson,PTF
AU  - Cascella,R
AU  - Perni,M
AU  - Jarvis,JA
AU  - Cecchi,C
AU  - Vendruscolo,M
AU  - Chiti,F
AU  - Cremades,N
AU  - Ying,L
AU  - Dobson,CM
AU  - De,Simone A
DO  - 10.1126/science.aan6160
EP  - 1443
PY  - 2017///
SN  - 0036-8075
SP  - 1440
TI  - Structural basis of membrane disruption and cellular toxicity by α-synuclein oligomers
T2  - Science
UR  - http://dx.doi.org/10.1126/science.aan6160
UR  - https://www.ncbi.nlm.nih.gov/pubmed/29242346
UR  - https://science.sciencemag.org/content/358/6369/1440/
UR  - http://hdl.handle.net/10044/1/55490
VL  - 358
ER  -

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