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Amyotrophic lateral sclerosis disease-related mutations disrupt the dimerization of superoxide dismutase 1 - A comparative molecular dynamics simulation study - ScienceDirect

Amyotrophic lateral sclerosis disease-related mutations disrupt the dimerization of superoxide dismutase 1 - A comparative molecular dynamics simulation study - ScienceDirect

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Molecular dynamics analysis of superoxide dismutase 1 mutations suggests decoupling between mechanisms underlying ALS onset and progression - Computational and Structural Biotechnology Journal

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

Comprehensive in silico analysis and molecular dynamics of the superoxide dismutase 1 (SOD1) variants related to amyotrophic lateral sclerosis

Amyotrophic lateral sclerosis - ScienceDirect

Antioxidants, Free Full-Text

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

Comprehensive in silico analysis and molecular dynamics of the superoxide dismutase 1 (SOD1) variants related to amyotrophic lateral sclerosis

Brain Sciences, Free Full-Text

Amyotrophic lateral sclerosis: a neurodegenerative disorder poised for successful therapeutic translation

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

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