Disulfide dimerization of VILIP-1 involves its unique C-terminal C187 and affects the interaction of the protein with physiological targets, such as guanylate cyclase B. VILIP-1 dimers are accumulated in soluble or aggregated form in the spinal cord of patients with amyotrophic lateral sclerosis (ALS), thereby representing a hallmark of the disease [30,31,32]. Here, NPR2 is linked to amyotrophic lateral sclerosis.