Ontology highlight
ABSTRACT:
SUBMITTER: Vilar M
PROVIDER: S-EPMC2438424 | biostudies-literature | 2008 Jun
REPOSITORIES: biostudies-literature
Vilar Marçal M Chou Hui-Ting HT Lührs Thorsten T Maji Samir K SK Riek-Loher Dominique D Verel Rene R Manning Gerard G Stahlberg Henning H Riek Roland R
Proceedings of the National Academy of Sciences of the United States of America 20080612 25
The aggregation of proteins into amyloid fibrils is associated with several neurodegenerative diseases. In Parkinson's disease it is believed that the aggregation of alpha-synuclein (alpha-syn) from monomers by intermediates into amyloid fibrils is the toxic disease-causative mechanism. Here, we studied the structure of alpha-syn in its amyloid state by using various biophysical approaches. Quenched hydrogen/deuterium exchange NMR spectroscopy identified five beta-strands within the fibril core ...[more]