Molecular mechanisms underlying the impact of mutations in SOD1 on its conformational properties associated with amyotrophic lateral sclerosis as revealed with molecular modelling

Research output: Contribution to journal › Article › peer-review

Aggregates, ALS, Copper, Elastic networks, Hydrogen bonds, Misfolding, SOD1, Protein Structure, Secondary, Mutation/genetics, Humans, Models, Molecular, Amyotrophic Lateral Sclerosis/enzymology, Hydrogen Bonding, Superoxide Dismutase-1/chemistry, Survival Analysis, Conserved Sequence, Protein Conformation, Amino Acids/genetics, Evolution, Molecular, PROTEIN, COPPER, ELASTIC NETWORK MODELS, MUTANTS, THERMAL-STABILITY, FLEXIBILITY, HYDROGEN-BONDS, ANISOTROPIC RESPONSE, ZN SUPEROXIDE-DISMUTASE

ID: 9539704