Non-steric-zipper models for pathogenic α-synuclein conformers-Reference-Cited by-同舟云学术

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Non-steric-zipper models for pathogenic α-synuclein conformers

Published:2018-06 Issue:2 Volume:2 Page:026105
ISSN:2473-2877
Container-title:APL Bioengineering
language:en
Short-container-title:APL Bioengineering

Author:

Schuman Brock¹,Won Amy²,Brand-Arzamendi Koroboshka¹,Koprich James B.³,Wen Xiao-Yan¹,Howson Patrick A.³,Brotchie Jonathan M.³,Yip Christopher M.²

Affiliation:

1. St. Michael's Hospital, 30 Bond Street, Toronto, Ontario M5B 1W8, Canada

2. Institute of Biomaterials and Biomedical Engineering, University of Toronto, Toronto, Ontario M5S 3G9, Canada

3. Krembil Institute, Toronto Western Hospital, University Health Network, Toronto, Ontario M5T 2S8, Canada

Funder

Health Canada

Natural Sciences and Engineering Research Council of Canada

Fondation Brain Canada

Publisher

AIP Publishing

Subject

Biomedical Engineering,Biomaterials,Biophysics,Bioengineering

Link

http://aip.scitation.org/doi/pdf/10.1063/1.5023460

Reference55 articles.

1. Quantitative evaluation of congo red binding to amyloid-like proteins with a beta-pleated sheet conformation.

2. Low frequency of ?-synuclein mutations in familial Parkinson's disease

3. α-Synuclein Regulates Neuronal Cholesterol Efflux

4. The role of alpha-synuclein in neurotransmission and synaptic plasticity

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