Huntingtin fibrils with different toxicity, structure, and seeding potential can be interconverted
J. Mario Isas(Keck Hospital of USC), Ansgar B. Siemer(University of Southern California), Ellisa K. Fultz(University of Southern California), Jeannie Chen(University of Southern California), Hui Xu(University of Southern California), Nitin Pandey(University of Southern California), Anoop Rawat(University of Southern California), Kazuki Teranishi(University of Southern California), Franziska Meier(University of Southern California), Ralf Langen(Keck Hospital of USC), Alan Okada(University of Southern California), Anise Applebaum(University of Southern California)
Cited by 63
Related Papers
Membrane Curvature Induction and Tubulation Are Common Features of Synucleins and Apolipoproteins
|Journal of Biological Chemistry|2010|318
O-GlcNAc modification blocks the aggregation and toxicity of the protein α-synuclein associated with Parkinson's disease
|Nature Chemistry|2015|305
The S100A10 Subunit of the Annexin A2 Heterotetramer Facilitates L2-Mediated Human Papillomavirus Infection
|PLoS ONE|2012|161
Fibrillar Oligomers Nucleate the Oligomerization of Monomeric Amyloid β but Do Not Seed Fibril Formation
|Journal of Biological Chemistry|2009|158
Soluble and Mature Amyloid Fibrils in Drusen Deposits
|Investigative Ophthalmology & Visual Science|2010|153