Associated Papers
Exploring the impact of mutation and post-translational modification on α-Synuclein: Insights from molecular dynamics simulations with and without copper.
Savva L et al.
Journal of Inorganic Biochemistry, 2023
Hydration Thermodynamics of Familial Parkinson's Disease-Linked Mutants of α-Synuclein.
Aggarwal L et al.
Journal of Chemical Information and Modeling, 2021
Transient β-hairpin formation in α-synuclein monomer revealed by coarse-grained molecular dynamics simulation.
Yu H et al.
The Journal of Chemical Physics, 2015
Familial Parkinson disease-associated mutations alter the site-specific microenvironment and dynamics of α-synuclein.
Sahay S et al.
The Journal of Biological Chemistry, 2015
Link between the SNCA gene and parkinsonism.
Xu W et al.
Neurobiology of Aging, 2015
Site-specific fluorescence dynamics of α-synuclein fibrils using time-resolved fluorescence studies: effect of familial Parkinson's disease-associated mutations.
Sahay S et al.
Biochemistry, 2014
24450731 (PubMed )
Supplement: bi401543z_si_001.pdf
Structures and free energy landscapes of the A53T mutant-type α-synuclein protein and impact of A53T mutation on the structures of the wild-type α-synuclein protein with dynamics.
Coskuner O et al.
Acs Chemical Neuroscience, 2013
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