In vivo aggregation of presynaptic alpha-synuclein is not influenced by its phosphorylation at serine-129

In vivo aggregation of presynaptic alpha-synuclein is not influenced by its phosphorylation at serine-129

Abnormal aggregation of the α-synuclein protein is a key molecular feature of Parkinson's disease and other neurodegenerative diseases. The precise mechanisms that trigger α-synuclein aggregation are unclear, and it is not known what role aggregation plays in disease pathogenesis. Here we use a...

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Bibliographic Details
Main Authors: Leah J. Weston, Zoe T. Cook, Teresa L. Stackhouse, Mehtab K. Sal, Baergen I. Schultz, Zachary J.C. Tobias, Valerie R. Osterberg, Nicole L. Brockway, Saheli Pizano, Greta Glover, Tamily A. Weissman, Vivek K. Unni
Format: Article
Language:English
Published: Elsevier 2021-05-01
Series:Neurobiology of Disease
Subjects:
Alpha-synuclein
Parkinson's disease
Protein aggregation
Zebrafish
FRAP
in vivo imaging
Online Access:http://www.sciencedirect.com/science/article/pii/S0969996121000401

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http://www.sciencedirect.com/science/article/pii/S0969996121000401

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