RRM1 and amyotrophic lateral sclerosis: Of importance to ALS and mutations found in TDP‐43 connected to ALS, one of the most significantly shifted residues is D169, which is a mutated to a glycine residue in ALS patients (Figure 1b,d), previously reported to (i) disrupt the ATP‐binding capacity of the RRM1 domain (Dang & Song, 2020), (ii) disrupt phase separation‐induced by NEAT1 RNA binding to TDP‐43 (Wang et al., 2020), and (iii) was shown to increase thermal stability of a TDP‐43(1–265) construct (Chiang et al., 2016).