Nortriptyline inhibits aggregation and neurotoxicity of alpha-synuclein by enhancing reconfiguration of the monomeric form

Nortriptyline inhibits aggregation and neurotoxicity of alpha-synuclein by enhancing reconfiguration of the monomeric form

The pathology of Parkinson's disease and other synucleinopathies is characterized by the formation of intracellular inclusions comprised primarily of misfolded, fibrillar α-synuclein (α-syn). One strategy to slow disease progression is to prevent the misfolding and aggregation of its native mon...

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Bibliographic Details
Main Authors: Timothy J. Collier, Kinshuk R. Srivastava, Craig Justman, Tom Grammatopoulous, Birgit Hutter-Paier, Manuela Prokesch, Daniel Havas, Jean-Christophe Rochet, Fang Liu, Kevin Jock, Patrícia de Oliveira, Georgia L. Stirtz, Ulf Dettmer, Caryl E. Sortwell, Mel B. Feany, Peter Lansbury, Lisa Lapidus, Katrina L. Paumier
Format: Article
Language:English
Published: Elsevier 2017-10-01
Series:Neurobiology of Disease
Subjects:
Alpha-synuclein
Parkinson's disease
Biophysics
Pre-formed fibrils
Transgenic mouse
Transgenic Drosophila
Online Access:http://www.sciencedirect.com/science/article/pii/S0969996117301596

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http://www.sciencedirect.com/science/article/pii/S0969996117301596

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