Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates.

@article{Liu2012OutofregisterS,
  title={Out-of-register β-sheets suggest a pathway to toxic amyloid aggregates.},
  author={Cong Liu and Minglei Zhao and Lin Jiang and Pin-Nan Cheng and Jiyong Park and Michael R. Sawaya and Anna Pensalfini and Dawei Gou and Arnold J. Berk and Charles G. Glabe and James S Nowick and David S. Eisenberg},
  journal={Proceedings of the National Academy of Sciences of the United States of America},
  year={2012},
  volume={109 51},
  pages={
          20913-8
        }
}
Although aberrant protein aggregation has been conclusively linked to dozens of devastating amyloid diseases, scientists remain puzzled about the molecular features that render amyloid fibrils or small oligomers toxic. Here, we report a previously unobserved type of amyloid fibril that tests as cytotoxic: one in which the strands of the contributing β-sheets are out of register. In all amyloid fibrils previously characterized at the molecular level, only in-register β-sheets have been observed… CONTINUE READING

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