Associated Papers
Asparagine endopeptidase cleaves α-synuclein and mediates pathologic activities in Parkinson's disease.
Zhang Z et al.
Nature Structural & Molecular Biology, 2017
Semisynthetic and in Vitro Phosphorylation of Alpha-Synuclein at Y39 Promotes Functional Partly Helical Membrane-Bound States Resembling Those Induced by PD Mutations.
Dikiy I et al.
Acs Chemical Biology, 2016
Activation of tyrosine kinase c-Abl contributes to α-synuclein-induced neurodegeneration.
Brahmachari S et al.
The Journal of Clinical Investigation, 2016
Elucidating the Role of Site-Specific Nitration of α-Synuclein in the Pathogenesis of Parkinson's Disease via Protein Semisynthesis and Mutagenesis.
Burai R et al.
Journal of the American Chemical Society, 2015
Efficient modification of alpha-synuclein serine 129 by protein kinase CK1 requires phosphorylation of tyrosine 125 as a priming event.
Kosten J et al.
Acs Chemical Neuroscience, 2014
Systematic comparison of the effects of alpha-synuclein mutations on its oligomerization and aggregation.
Lázaro DF et al.
Plos Genetics, 2014
c-Abl phosphorylates α-synuclein and regulates its degradation: implication for α-synuclein clearance and contribution to the pathogenesis of Parkinson's disease.
Mahul-Mellier AL et al.
Human Molecular Genetics, 2014
In vitro phosphorylation does not influence the aggregation kinetics of WT α-synuclein in contrast to its phosphorylation mutants.
Schreurs S et al.
International Journal of Molecular Sciences, 2014
Interaction of α-synuclein with vesicles that mimic mitochondrial membranes.
Zigoneanu IG et al.
Biochimica Et Biophysica Acta, 2012
Tyrosine and serine phosphorylation of alpha-synuclein have opposing effects on neurotoxicity and soluble oligomer formation.
Chen L et al.
The Journal of Clinical Investigation, 2009
Alpha-synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers.
Beyer K
Acta Neuropathologica, 2006
Parkinson's disease alpha-synuclein mutations exhibit defective axonal transport in cultured neurons.
Saha AR et al.
Journal of Cell Science, 2004
Identification and characterization of a novel Pyk2/related adhesion focal tyrosine kinase-associated protein that inhibits alpha-synuclein phosphorylation.
Takahashi T et al.
The Journal of Biological Chemistry, 2003
Tyrosine 125 of alpha-synuclein plays a critical role for dimerization following nitrative stress.
Takahashi T et al.
Brain Research, 2002
Multiple phosphorylation of alpha-synuclein by protein tyrosine kinase Syk prevents eosin-induced aggregation.
Negro A et al.
Faseb Journal : Official Publication of the Federation of American Societies for Experimental Biology, 2002
alpha-synuclein is phosphorylated by members of the Src family of protein-tyrosine kinases.
Ellis CE et al.
The Journal of Biological Chemistry, 2001