Associated Papers
In silico analysis of alpha-synuclein protein variants and posttranslational modifications related to Parkinson's disease.
da Silva ANR et al.
Journal of Cellular Biochemistry, 2024
Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein.
Ohgita T et al.
Scientific Reports, 2023
Two C-terminal sequence variations determine differential neurotoxicity between human and mouse α-synuclein.
Landeck N et al.
Molecular Neurodegeneration, 2020
Sequence- and seed-structure-dependent polymorphic fibrils of alpha-synuclein.
Tanaka G et al.
Biochimica Et Biophysica Acta. Molecular Basis of Disease, 2019
The A53T mutation is key in defining the differences in the aggregation kinetics of human and mouse α-synuclein.
Kang L et al.
Journal of the American Chemical Society, 2011
Structural role of compensatory amino acid replacements in the α-synuclein protein.
Losasso V et al.
Biochemistry, 2011
The effect of amino acid substitution in the imperfect repeat sequences of alpha-synuclein on fibrillation.
Harada R et al.
Biochimica Et Biophysica Acta, 2009
E46K Parkinson's-linked mutation enhances C-terminal-to-N-terminal contacts in alpha-synuclein.
Rospigliosi CC et al.
Journal of Molecular Biology, 2009
Characterization of conformational and dynamic properties of natively unfolded human and mouse alpha-synuclein ensembles by NMR: implication for aggregation.
Wu KP et al.
Journal of Molecular Biology, 2008
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