Associated Papers
Alpha-synuclein fibril structures cluster into distinct classes.
Milchberg MH et al.
Biophysical Journal, 2025
Mouse α-synuclein fibrils are structurally and functionally distinct from human fibrils associated with Lewy body diseases.
Sokratian A et al.
Science Advances, 2024
Intramolecular interaction kinetically regulates fibril formation by human and mouse α-synuclein.
Ohgita T et al.
Scientific Reports, 2023
TRIM11 Prevents and Reverses Protein Aggregation and Rescues a Mouse Model of Parkinson's Disease.
Zhu G et al.
Cell Reports, 2020
Two C-terminal sequence variations determine differential neurotoxicity between human and mouse α-synuclein.
Landeck N et al.
Molecular Neurodegeneration, 2020
Alpha-synuclein is a DNA binding protein that modulates DNA repair with implications for Lewy body disorders.
Schaser AJ et al.
Scientific Reports, 2019
Sequence- and seed-structure-dependent polymorphic fibrils of alpha-synuclein.
Tanaka G et al.
Biochimica Et Biophysica Acta. Molecular Basis of Disease, 2019
Molecular determinants of α-synuclein mutants' oligomerization and membrane interactions.
Tsigelny IF et al.
Acs Chemical Neuroscience, 2015
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
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
alpha-Synuclein A53T substitution associated with Parkinson disease also marks the divergence of Old World and New World primates.
Hamilton BA
Genomics, 2004
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