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Flipping the switch: How cysteine oxidation directs tau amyloid conformations.
Journal of Biological Chemistry  (IF5.157),  Pub Date : 2021-10-15, DOI: 10.1016/j.jbc.2021.101309
Danny M Hatters

Tau can adopt distinct fibril conformations in different human neurodegenerative diseases, which may invoke distinct pathological mechanisms. In a recent issue, Weismiller et al. showed that intramolecular disulfide links between cys291 and cys322 for a specific tau isoform containing four microtubule-binding repeats direct the formation of a structurally distinct amyloid polymorph. These findings have implications in how oxidative stress can flip switches of tau polymorphism in these diseases.