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Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis
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Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis
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Journal Article
Glutathionylation potentiates benign superoxide dismutase 1 variants to the toxic forms associated with amyotrophic lateral sclerosis
2013
Overview
Dissociation of superoxide dismutase 1 dimers is enhanced by glutathionylation, although the dissociation constants reported to date are imprecise. We have quantified the discreet dissociation constants for wild-type superoxide dismutase 1 and six naturally occurring sequence variants, in their unmodified and glutathionylated forms, at the ratios expressed. Unmodified superoxide dismutase 1 variants that shared similar dissociation constants with SOD1
WT
had disproportionately increased dissociation constants when glutathionylated. This defines a key role for glutathionylation in superoxide dismutase 1 associated familial amyotrophic lateral sclerosis.
Publisher
Nature Publishing Group UK,Nature Publishing Group
Subject
/ 82
/ 82/58
/ Amyotrophic lateral sclerosis
/ Amyotrophic Lateral Sclerosis - genetics
/ Amyotrophic Lateral Sclerosis - metabolism
/ Benign
/ Humanities and Social Sciences
/ Humans
/ Kinetics
/ Recombinant Proteins - chemistry
/ Recombinant Proteins - genetics
/ Recombinant Proteins - metabolism
/ Science
/ Superoxide Dismutase - chemistry
/ Superoxide Dismutase - genetics
