Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

Parkinson-causing α-synuclein missense mutations shift native tetramers to monomers as a mechanism for disease initiation

β-Sheet-rich α-synuclein (αS) aggregates characterize Parkinson’s disease (PD). αS was long believed to be a natively unfolded monomer, but recent work suggests it also occurs in α-helix-rich tetramers. Crosslinking traps principally tetrameric αS in intact normal neurons, but not after cell lysis,...

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Bibliographic Details
Main Authors: Dettmer, Ulf, Newman, Andrew J., Soldner, Frank, Luth, Eric S., Kim, Nora C., von Saucken, Victoria E., Sanderson, John B., Jaenisch, Rudolf, Bartels, Tim, Selkoe, Dennis
Other Authors: Massachusetts Institute of Technology. Department of Biology
Format: Article
Language:en_US
Published: Nature Publishing Group 2015
Online Access:http://hdl.handle.net/1721.1/98476

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http://hdl.handle.net/1721.1/98476

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