13C and 15N resonance assignments of alpha synuclein fibrils amplified from Lewy Body Dementia tissue
(2023) Biomolecular NMR Assignments, 17 (2), pp. 281-286.
Barclay, A.M.a , Dhavale, D.D.b , Borcik, C.G.c d , Milchberg, M.H.c e , Kotzbauer, P.T.b , Rienstra, C.M.c d e f
a Center for Biophysics and Quantitative Biology, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States
b Department of Neurology, Washington University School of Medicine, St. Louis, MO 63110, United States
c Department of Biochemistry, University of Wisconsin-Madison, Madison, WI 53706, United States
d National Magnetic Resonance Facility at Madison, University of Wisconsin-Madison, Madison, WI 53706, United States
e Graduate Program in Biophysics, University of Wisconsin-Madison, Madison, WI 53706, United States
f Department of Chemistry, University of Illinois at Urbana-Champaign, Urbana, IL 61801, United States
Abstract
Fibrils of the protein α-synuclein (Asyn) are implicated in the pathogenesis of Parkinson Disease, Lewy Body Dementia, and Multiple System Atrophy. Numerous forms of Asyn fibrils have been studied by solid-state NMR and resonance assignments have been reported. Here, we report a new set of 13C, 15N assignments that are unique to fibrils obtained by amplification from postmortem brain tissue of a patient diagnosed with Lewy Body Dementia. © 2023, The Author(s), under exclusive licence to Springer Nature B.V.
Author Keywords
Fibrils; Lewy Body Dementia; Parkinson Disease; Polymorphism; αSynuclein
Funding details
National Institutes of HealthNIHNS075321, NS097799, NS110436
National Institute on AgingNIAF32GM149118, P41GM136463, R01GM123455
National Institute of General Medical SciencesNIGMS
National Institute of Neurological Disorders and StrokeNINDS
Michael J. Fox Foundation for Parkinson’s ResearchMJFF
Document Type: Article
Publication Stage: Final
Source: Scopus