Solid-state NMR structure of a pathogenic fibril of full-length human [alpha]-synuclein

• Published in: Nature structural & molecular biology Vol. 23; no. 5; p. 409
• Main Authors: Tuttle, Marcus D, Comellas, Gemma, Nieuwkoop, Andrew J, Covell, Dustin J, Berthold, Deborah A, Kloepper, Kathryn D, Courtney, Joseph M, Kim, Jae K, Barclay, Alexander M, Kendall, Amy, Wan, William, Stubbs, Gerald, Schwieters, Charles D, Lee, Virginia M Y, George, Julia M, Rienstra, Chad M
• Format: Journal Article
• Language: English
• Published: New York Nature Publishing Group 01.05.2016
• Subjects: Data collection; Molecular biology; Neurons; NMR; Nuclear magnetic resonance; Parkinson's disease; Pathogens; Peptides; Residues; Sample preparation; Topology

PD is pathologically characterized by Lewy bodies and Lewy neurites1, intracytoplasmic aggregates containing -synuclein (-syn) fibrils1. Exogenous -syn fibrils seed Lewy body and Lewy neuritelike inclusions in cell culture models2,3, and neuron-to-neuron -syn transmission propagates PD-like patholog...