Prions articles within Nature Chemistry

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• Article | 20 November 2017

  Structure-based inhibitors of tau aggregation

  Tau aggregation is associated with Alzheimer's disease and dozens of related dementias. Now atomic structures of the aggregation-prone segment VQIINK in repeat 2 of tau have been reported. Inhibitors designed using these structures block seeding by full-length tau better than inhibitors that target the VQIVYK aggregation segment in repeat 3.

  • P. M. Seidler
  • , D. R. Boyer
  •  & D. S. Eisenberg

• Article | 03 April 2017

  A 31-residue peptide induces aggregation of tau's microtubule-binding region in cells

  The self-propagation of misfolded conformations of tau occurs in neurodegenerative diseases, including Alzheimer's disease. The microtubule-binding region, tau_244-372, reproduces much of the aggregation behaviour of tau in cells and animal models. Now, it has been shown that a 31-residue peptide from tau's R3 domain forms a cross-β conformation that efficiently seeds aggregation of tau_244-372 in cells.

  • Jan Stöhr
  • , Haifan Wu
  •  & William F. DeGrado