α-Synuclein aggregation alters tyrosine hydroxylase phosphorylation and immunoreactivity: Lessons from viral transduction of knockout mice
- 12 February 2008
- journal article
- research article
- Published by Elsevier in Neuroscience Letters
- Vol. 435 (1) , 24-29
- https://doi.org/10.1016/j.neulet.2008.02.014
Abstract
No abstract availableKeywords
This publication has 42 references indexed in Scilit:
- Dopamine promotes α‐synuclein aggregation into SDS‐resistant soluble oligomers via a distinct folding pathwayThe FASEB Journal, 2005
- α-Synuclein Is Required for the Fibrillar Nature of Ubiquitinated Inclusions Induced by Proteasomal Inhibition in Primary NeuronsJournal of Biological Chemistry, 2004
- α-synuclein locus duplication as a cause of familial Parkinson's diseasePublished by Elsevier ,2004
- α-Synuclein Lowers p53-dependent Apoptotic Response of Neuronal CellsPublished by Elsevier ,2002
- Accelerated Oligomerization by Parkinson's Disease Linked α‐Synuclein MutantsAnnals of the New York Academy of Sciences, 2000
- Stoichiometry of Tyrosine Hydroxylase Phosphorylation in the Nigrostriatal and Mesolimbic Systems In VivoJournal of Neurochemistry, 2000
- Mice Lacking α-Synuclein Display Functional Deficits in the Nigrostriatal Dopamine SystemNeuron, 2000
- Effects of Phosphorylation of Serine 40 of Tyrosine Hydroxylase on Binding of Catecholamines: Evidence for a Novel Regulatory MechanismBiochemistry, 1998
- α-Synuclein in filamentous inclusions of Lewy bodies from Parkinson’s disease and dementia with Lewy bodiesProceedings of the National Academy of Sciences, 1998
- In Vitro Phosphorylation of Bovine Adrenal Chromaffin Cell Tyrosine Hydroxylase by Endogenous Protein KinasesJournal of Neurochemistry, 1989