Title : Deamidation of asparagine to aspartate destabilizes Cu, Zn superoxide dismutase, accelerates fibrillization, and mirrors ALS-linked mutations.

Pub. Date : 2013 Oct 23

PMID : 24066782






3 Functional Relationships(s)
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Compound Name
Protein Name
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1 The reactivity of asparagine residues in Cu, Zn superoxide dismutase (SOD1) to deamidate to aspartate remains uncharacterized; its occurrence in SOD1 has not been investigated, and the biophysical effects of deamidation on SOD1 are unknown. Aspartic Acid superoxide dismutase 1 Homo sapiens
2 Deamidation is, nonetheless, chemically equivalent to Asn-to-Asp missense mutations in SOD1 that cause amyotrophic lateral sclerosis (ALS). Aspartic Acid superoxide dismutase 1 Homo sapiens
3 Site-directed mutagenesis was used to successively substitute these asparagines with aspartate (to mimic deamidation) according to their predicted deamidation rate, yielding: N26D, N26D/N131D, and N26D/N131D/N139D SOD1. Aspartic Acid superoxide dismutase 1 Homo sapiens