SOD1 oligomers in amyotrophic lateral sclerosis

Curr Opin Struct Biol. 2021 Feb:66:225-230. doi: 10.1016/j.sbi.2020.12.002. Epub 2021 Jan 16.

Abstract

Identifying nonnative, trimeric forms of SOD1 trimers as the toxic species, rather than large aggregates revolutionizes our understanding of ALS pathophysiology. Large protein aggregates, what was previously thought as the central cause of neurodegeneration, play protective role and are not responsible for neuronal death. SOD1 trimers are implicated at the molecular, cellular, and organismal level. Understanding the formation of the nonnative trimer and its role in the cell, leading to cell death, holds the key to developing a new standard of therapeutics for ALS and for other neurodegenerative diseases. This review highlights recent advances of knowledge for the role of SOD1 oligomers in ALS.

Publication types

  • Research Support, N.I.H., Extramural
  • Research Support, Non-U.S. Gov't
  • Review

MeSH terms

  • Amyotrophic Lateral Sclerosis* / genetics
  • Humans
  • Mutation
  • Superoxide Dismutase-1 / genetics

Substances

  • SOD1 protein, human
  • Superoxide Dismutase-1