for an amyloid‐disease mutant of FUS protein.[58] FUS protein is a widely studied system for the relationships between amyloid formation and phase separation,[59, 60] which shares with galectin‐3′s NTD a scarcity of negative charges and multiple aromatic residues that promote phase separation via π‐π or cation‐π interactions with its arginine‐glycine‐rich domain (Figure S8A, Supporting Information).[22, 61] Therefore, NTD's two charged residues likely regulate its assembly tendency and prevent rapid fiber formation driven by the prion‐like nature of this region (Figure 2B). Here, FUS is linked to amyloidosis.