Abstract: The pharmacokinetics and key technologies of the present invention are summarized in FIG. 1. Particularly, malignant misfolded proteins such as mutant huntingtin and alpha-synuclein are coagulated and grow into oligomeric coagulum ({circle around (1)}, {circle around (2)}, fibrillar coagulum ({circle around (3)}) and eventually inclusion body ({circle around (4)}). Young neurons produce a large amount of Nt-Arg through N-terminal arginylation ({circle around (5)}) of vesicle chaperones such as BiP secreted into the cytoplasm, and then arginylated BiP (R-BiP) is secreted binds to the misfolded proteins ({circle around (6)}). As a ligand, the Nt-Arg of R-BiP binds to the p62 ZZ domain ({circle around (7)}), and the normally inactivated closed form of p62 is changed to an open form, leading to structural activation ({circle around (8)}). As a result, PB1 and LC3-binding domains are exposed.