Amyotrophic lateral sclerosis disease-related mutations disrupt the dimerization of superoxide dismutase 1 - A comparative molecular dynamics simulation study - ScienceDirect
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Genetics of amyotrophic lateral sclerosis: seeking therapeutic targets in the era of gene therapy
Cu/Zn Superoxide Dismutase Forms Amyloid Fibrils under Near-Physiological Quiescent Conditions: The Roles of Disulfide Bonds and Effects of Denaturant
Amyotrophic lateral sclerosis disease-related mutations disrupt the dimerization of superoxide dismutase 1 - A comparative molecular dynamics simulation study - ScienceDirect
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Misfolding-Associated Exposure of Natively Buried Residues in Mutant SOD1 Facilitates Binding to TRAF6 - ScienceDirect
Molecular dynamics of far positioned surface mutations of Cu/Zn SOD1 promotes altered structural stability and metal-binding site: Structural clues to the pathogenesis of amyotrophic lateral sclerosis - ScienceDirect
Amyotrophic lateral sclerosis disease-related mutations disrupt the dimerization of superoxide dismutase 1 - A comparative molecular dynamics simulation study - ScienceDirect
Frontiers Bridging the Bridging Imidazolate in the Bimetallic Center of the Cu/Zn SOD1 and ALS
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Comprehensive in silico analysis and molecular dynamics of the superoxide dismutase 1 (SOD1) variants related to amyotrophic lateral sclerosis
T54R mutation destabilizes the dimer of superoxide dismutase 1 T54R by inducing steric clashes at the dimer interface - RSC Advances (RSC Publishing) DOI:10.1039/C9RA09870D
The biophysics of superoxide dismutase-1 and amyotrophic lateral sclerosis, Quarterly Reviews of Biophysics
Amyotrophic lateral sclerosis disease-related mutations disrupt the dimerization of superoxide dismutase 1 - A comparative molecular dynamics simulation study - ScienceDirect
Effects of Protein Crowders and Charge on the Folding of Superoxide Dismutase 1 Variants: A Computational Study
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