It is known that in vivo human Tau protein [17], [20], the human PrP and its pathogenic mutants [16], [21], [22], [36], and human SOD1 pathogenic mutants [18], [23], [24] have the tendency to form fibril deposits in a variety of tissues and thereby cause Alzheimer disease, prion disease, and ALS, respectively, while the rabbit PrP [13], [25], [26] and hen egg white lysozyme [27] do not readily form fibrils and are unlikely to cause neurodegenerative diseases. This evidence concerns the gene SOD1 and early-onset autosomal dominant Alzheimer disease.