Tyrosine 136 phosphorylation of α-synuclein aggregates in the Lewy body dementia brain: involvement of serine 129 phosphorylation by casein kinase 2
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Title
Tyrosine 136 phosphorylation of α-synuclein aggregates in the Lewy body dementia brain: involvement of serine 129 phosphorylation by casein kinase 2
Authors
Keywords
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Journal
Acta Neuropathologica Communications
Volume 9, Issue 1, Pages -
Publisher
Springer Science and Business Media LLC
Online
2021-11-12
DOI
10.1186/s40478-021-01281-9
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Note: Only part of the references are listed.- Genetic deletion of Polo-like kinase 2 reduces alpha-synuclein serine-129 phosphorylation in presynaptic terminals but not Lewy bodies
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- Phosphorylation regulates the binding of intrinsically disordered proteins via a flexible conformation selection mechanism
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- Prion-Like Seeding of Misfolded α-Synuclein in the Brains of Dementia with Lewy Body Patients in RT-QUIC
- (2017) Kazunori Sano et al. MOLECULAR NEUROBIOLOGY
- Phosphorylated exogenous alpha-synuclein fibrils exacerbate pathology and induce neuronal dysfunction in mice
- (2017) Mantia Karampetsou et al. Scientific Reports
- Efficient Modification of Alpha-Synuclein Serine 129 by Protein Kinase CK1 Requires Phosphorylation of Tyrosine 125 as a Priming Event
- (2014) Jonas Kosten et al. ACS Chemical Neuroscience
- c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease
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- In Vitro Phosphorylation Does not Influence the Aggregation Kinetics of WT α-Synuclein in Contrast to Its Phosphorylation Mutants
- (2014) Sarah Schreurs et al. INTERNATIONAL JOURNAL OF MOLECULAR SCIENCES
- Tyrosine phosphorylation of histone H2A by CK2 regulates transcriptional elongation
- (2014) Harihar Basnet et al. NATURE
- Folding of an intrinsically disordered protein by phosphorylation as a regulatory switch
- (2014) Alaji Bah et al. NATURE
- α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson’s disease and multiple system atrophy?
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- In vivo modulation of polo-like kinases supports a key role for PLK2 in Ser129 α-synuclein phosphorylation in mouse brain
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- Superiority of PLK-2 as α-synuclein phosphorylating agent relies on unique specificity determinants
- (2012) Mauro Salvi et al. BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS
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- (2012) M. Salvi et al. BIOCHIMICA ET BIOPHYSICA ACTA-PROTEINS AND PROTEOMICS
- Elucidating the Role of C-Terminal Post-Translational Modifications Using Protein Semisynthesis Strategies: α-Synuclein Phosphorylation at Tyrosine 125
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- Tyrosine and serine phosphorylation of α-synuclein have opposing effects on neurotoxicity and soluble oligomer formation
- (2009) Li Chen et al. JOURNAL OF CLINICAL INVESTIGATION
- Protein kinase CK2 catalyzes tyrosine phosphorylation in mammalian cells
- (2008) Greg Vilk et al. CELLULAR SIGNALLING
- Phosphorylation at Ser-129 but Not the Phosphomimics S129E/D Inhibits the Fibrillation of α-Synuclein
- (2008) Katerina E. Paleologou et al. JOURNAL OF BIOLOGICAL CHEMISTRY
- Specificity and Regulation of Casein Kinase-Mediated Phosphorylation of ??-Synuclein
- (2008) Elisa A. Waxman et al. JOURNAL OF NEUROPATHOLOGY AND EXPERIMENTAL NEUROLOGY
- Localization of CKII β subunits in Lewy bodies of Parkinson's disease
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