Get 20M+ Full-Text Papers For Less Than $1.50/day. Start a 7-Day Trial for You or Your Team.

Learn More →

Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease

Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease ABSTRACT Background Alpha‐synuclein plays a central role in the pathophysiology of Parkinson's disease. Three missense mutations in SNCA, the gene encoding alpha‐synuclein, as well as genomic multiplications have been identified as causes for autosomal‐dominantly inherited Parkinsonism. Methods Here, we describe a novel missense mutation in exon 4 of SNCA encoding a H50Q substitution in a patient with dopa‐responsive Parkinson's disease with a family history of parkinsonism and dementia. Results The variant was not observed in public databases or identified in unrelated subjects. Conclusions The substitution's evolutionary conservation and protein modeling provide additional support for pathogenicity as the amino acid perturbs the same amphipathic alpha helical structure as the previously described pathogenic mutations. © 2013 Movement Disorder Society http://www.deepdyve.com/assets/images/DeepDyve-Logo-lg.png Movement Disorders Wiley

Alpha‐synuclein p.H50Q, a novel pathogenic mutation for Parkinson's disease

Download PDF
3 pages

Loading next page...
 
/lp/wiley/alpha-synuclein-p-h50q-a-novel-pathogenic-mutation-for-parkinson-s-JJRcctVedd

References (18)

Publisher
Wiley
Copyright
Copyright © 2013 Movement Disorder Society
ISSN
0885-3185
eISSN
1531-8257
DOI
10.1002/mds.25421
pmid
23457019
Publisher site
See Article on Publisher Site

Abstract

ABSTRACT Background Alpha‐synuclein plays a central role in the pathophysiology of Parkinson's disease. Three missense mutations in SNCA, the gene encoding alpha‐synuclein, as well as genomic multiplications have been identified as causes for autosomal‐dominantly inherited Parkinsonism. Methods Here, we describe a novel missense mutation in exon 4 of SNCA encoding a H50Q substitution in a patient with dopa‐responsive Parkinson's disease with a family history of parkinsonism and dementia. Results The variant was not observed in public databases or identified in unrelated subjects. Conclusions The substitution's evolutionary conservation and protein modeling provide additional support for pathogenicity as the amino acid perturbs the same amphipathic alpha helical structure as the previously described pathogenic mutations. © 2013 Movement Disorder Society

Journal

Movement Disorders – Wiley

Published: Jun 1, 2013

There are no references for this article.