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Whilst this instability is negated by metal binding and disulfide formation under normal cellular conditions, the incorporation of additional destabilising factors during aging or disease ( SOD1 mutations, atypical post‐translational modification of residue side chains) can disrupt the incorporation of stabilizing factors and exacerbate instability within the metal‐binding and electrostatic loops of apo‐SOD1, or perturb stabilising factors within the mature holo protein, generating partially or completely misfolded SOD1 protein
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