Ser129D mutant alpha-synuclein induces earlier motor dysfunction while S129A results in distinctive pathology in a rat model of Parkinson's disease
Alpha-synuclein phosphorylated at serine 129 (S129) is highly elevated in Parkinson's disease patients where it mainly accumulates in the Lewy bodies. Several groups have studied the role of phosphorylation at the S129 in α-synuclein in a rat model for Parkinson's disease using recombinant...
Main Authors: | Fabia Febbraro, Gurdal Sahin, Aina Farran, Sofia Soares, Poul H. Jensen, Deniz Kirik, Marina Romero-Ramos |
---|---|
Format: | Article |
Language: | English |
Published: |
Elsevier
2013-08-01
|
Series: | Neurobiology of Disease |
Subjects: | |
Online Access: | http://www.sciencedirect.com/science/article/pii/S0969996113001022 |
Similar Items
-
Ser129 phosphorylation of endogenous α-synuclein induced by overexpression of polo-like kinases 2 and 3 in nigral dopamine neurons is not detrimental to their survival and function
by: Kerstin Buck, et al.
Published: (2015-06-01) -
Corrigendum to “Ser129D mutant alpha-synuclein induces earlier motor dysfunction while S129A results in distinctive pathology in a rat model of Parkinson's disease” [Neurobiol. Dis. 56 (2013) 48–58]
by: Fabia Febbraro, et al.
Published: (2013-10-01) -
Mechanisms underlying extensive Ser129-phosphorylation in α-synuclein aggregates
by: Shigeki Arawaka, et al.
Published: (2017-06-01) -
α-Synuclein interacts with the switch region of Rab8a in a Ser129 phosphorylation-dependent manner
by: Guowei Yin, et al.
Published: (2014-10-01) -
Organotypic slice culture model demonstrates inter-neuronal spreading of alpha-synuclein aggregates
by: Sara Elfarrash, et al.
Published: (2019-12-01)