Flipping the switch: How cysteine oxidation directs tau amyloid conformations |
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Authors: | Danny M Hatters |
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Institution: | Department of Biochemistry and Pharmacology and Bio21 Molecular Science and Biotechnology Institute, The University of Melbourne, Melbourne, Victoria, Australia |
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Abstract: | 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. |
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Keywords: | protein aggregation prion strains tauopathy protein biochemistry tau fibril assembly |
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