Notably, residues forming strong salt bridges (His43, His46, Glu100, Asp101, and Asp109) that contribute to the stabilization of the intramolecular L-shaped interface between the N- and C-terminal parts of SOD1 fibril (Figs. 2a, b, f, g and 3b–e) or hydrogen bonds (Val14 and Asp125) that contribute to the maintenance of the SOD1 fibril structure (Supplementary Fig. 7b–d) are also ALS-associated mutation sites1–5,8,17–22,25,26,29,44–50. This evidence concerns the gene SOD1 and amyotrophic lateral sclerosis.