Title : Altered thiol chemistry in human amyotrophic lateral sclerosis-linked mutants of superoxide dismutase 1.

Pub. Date : 2014 Sep 26

PMID : 25096579






2 Functional Relationships(s)
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Compound Name
Protein Name
Organism
1 In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation. Cysteine superoxide dismutase 1 Homo sapiens
2 In human SOD1 (hSOD1), a conserved disulfide bond and two free cysteine residues can engage in anomalous thiol/disulfide exchange resulting in non-native disulfides, a hallmark of ALS that is related to protein misfolding and aggregation. Cysteine superoxide dismutase 1 Homo sapiens