Therefore, pathogenesis of neurodegenerative diseases is commonly driven by the dysfunction of corresponding IDPs, and the normal and pathogenic behavior of such disease-related IDPs are controlled by other IDPs.
The author declares that the research was conducted in the absence of any commercial or financial relationships that could be construed as a potential conflict of interest. I am thankful to Alexey Uversky for careful reading and editing this manuscript. Ajroud-Driss, S. Sporadic and hereditary amyotrophic lateral sclerosis ALS. Acta , — Barmada, S. Bellotti, V. Biological activity and pathological implications of misfolded proteins. Life Sci. Bentmann, E. FEBS J. Bonda, D. The sirtuin pathway in ageing and Alzheimer disease: mechanistic and therapeutic considerations.
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This provides a safe, isolated place for the protein to refold before being ejected. Instead, Hartl says, chaperones that sequester unfolded proteins from the distracting, packed environment inside the cell act more like a catalyst. He suspects that the structural intermediates adopted by proteins on the way to their final 3-D conformation that scientists have observed in test tubes are likely also present during the folding process inside GroEL.