Investigating the presence of doubly phosphorylated α‐synuclein at tyrosine 125 and serine 129 in idiopathic Lewy body diseases
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Title
Investigating the presence of doubly phosphorylated α‐synuclein at tyrosine 125 and serine 129 in idiopathic Lewy body diseases
Authors
Keywords
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Journal
BRAIN PATHOLOGY
Volume -, Issue -, Pages -
Publisher
Wiley
Online
2020-04-24
DOI
10.1111/bpa.12845
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Note: Only part of the references are listed.- Generation of Monoclonal Antibodies against Phosphorylated α-Synuclein at Serine 129: Research Tools for Synucleinopathies
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- (2014) Jonas Kosten et al. ACS Chemical Neuroscience
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- Divergent effects of the H50Q and G51DSNCAmutations on the aggregation of α-synuclein
- (2014) Nicola J. Rutherford et al. JOURNAL OF NEUROCHEMISTRY
- α-Synucleinopathy associated with G51D SNCA mutation: a link between Parkinson’s disease and multiple system atrophy?
- (2013) Aoife P. Kiely et al. ACTA NEUROPATHOLOGICA
- Elucidating the Role of C-Terminal Post-Translational Modifications Using Protein Semisynthesis Strategies: α-Synuclein Phosphorylation at Tyrosine 125
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- (2008) Elisa A. Waxman et al. ACTA NEUROPATHOLOGICA
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