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Article

ALS mutants of human superoxide dismutase form fibrous aggregates via framework destabilization.

Journal of molecular biology - 19 Sept 2003

DiDonato Michael, Craig Lisa, Huff Mary E, Thayer Maria M, Cardoso Rosa M F, Kassmann Carey J, Lo Terence P, Bruns Cami K, Powers Evan T, Kelly Jeffery W, Getzoff Elizabeth D, Tainer John A

Abstract excerpt

Many point mutations in human Cu,Zn superoxide dismutase (SOD) cause familial amyotrophic lateral sclerosis (FALS), a fatal neurodegenerative disorder in heterozygotes. Here we show that these mutations cluster in protein regions influencing architectural integrity. Furthermore, crystal structures of SOD wild-type and FALS mutant H43R proteins uncover resulting local framework defects. Characterizations of...

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PMID: 12963370
DOI: 10.1016/s0022-2836(03)00889-1

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PubMed metadata and Literature Corpus relationships. Corpus snapshot updated 7 Sept 2026. Manifest publication-graph-cohort-2026-09-08.1.

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