Associated Papers
Aromaticity at position 39 in α-synuclein: A modulator of amyloid fibril assembly and membrane-bound conformations.
Buratti FA et al.
Protein Science : a Publication of the Protein Society, 2022
The Pathological G51D Mutation in Alpha-Synuclein Oligomers Confers Distinct Structural Attributes and Cellular Toxicity.
Xu CK et al.
Molecules (basel, Switzerland), 2022
Role of Tyr-39 for the Structural Features of α-Synuclein and for the Interaction with a Strong Modulator of Its Amyloid Assembly.
Palomino-Hernandez O et al.
International Journal of Molecular Sciences, 2020
Activation of tyrosine kinase c-Abl contributes to α-synuclein-induced neurodegeneration.
Brahmachari S et al.
The Journal of Clinical Investigation, 2016
C-Terminal Tyrosine Residue Modifications Modulate the Protective Phosphorylation of Serine 129 of α-Synuclein in a Yeast Model of Parkinson's Disease.
Kleinknecht A et al.
Plos Genetics, 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
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
Alpha-Synuclein conformation affects its tyrosine-dependent oxidative aggregation.
Ruf RA et al.
Biochemistry, 2008
Alpha-synuclein structure, posttranslational modification and alternative splicing as aggregation enhancers.
Beyer K
Acta Neuropathologica, 2006
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
alpha-synuclein is phosphorylated by members of the Src family of protein-tyrosine kinases.
Ellis CE et al.
The Journal of Biological Chemistry, 2001
Select a paper to view details