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

Pub. Date : 2014 Sep 26

PMID : 25096579






8 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. Disulfides 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. Disulfides superoxide dismutase 1 Homo sapiens
3 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. Disulfides superoxide dismutase 1 Homo sapiens
4 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. Disulfides superoxide dismutase 1 Homo sapiens
5 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. Disulfides superoxide dismutase 1 Homo sapiens
6 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. Disulfides superoxide dismutase 1 Homo sapiens
7 Here, we adapt recently developed single-bond chemistry techniques to study individual disulfide isomerization reactions in hSOD1. Disulfides superoxide dismutase 1 Homo sapiens
8 Mechanical unfolding of hSOD1 leads to the formation of a polypeptide loop held by the disulfide. Disulfides superoxide dismutase 1 Homo sapiens