Dnajc7 binds natively folded structural elements in tau to inhibit amyloid formation

HIGHLIGHTS

  • who: Zhiqiang Hou from the Center forUniversity of Texas Southwestern Medical Center, Dallas, TX, United States have published the paper: DnaJC7 binds natively folded structural elements in tau to inhibit amyloid formation, in the Journal: NATURE COMMUNICATIONS NATURE COMMUNICATIONS
  • what: The authors report that DnaJC7 directly influences the aggregation properties of the microtubule-associated protein tau. The authors show differences in affinity between WT tau and an aggregation-prone disease-associated P301L tau mutant that can be explained by changes in the tau conformation, suggesting that DnaJC7 preferentially binds to the natively folded conformations of . . .

     

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