Structural variation in amyloid-β fibrils from Alzheimer's disease clinical subtypes

Wei Qiang, Wai-Ming Yau, Jun-Xia Lu, John Collinge () and Robert Tycko ()
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Wei Qiang: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Wai-Ming Yau: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
Jun-Xia Lu: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health
John Collinge: UCL Institute of Neurology
Robert Tycko: Laboratory of Chemical Physics, National Institute of Diabetes and Digestive and Kidney Diseases, National Institutes of Health

Nature, 2017, vol. 541, issue 7636, 217-221

Abstract: Structural differences in 40- and 42-residue-long amyloid-β fibrils seeded in vitro from the cortical tissue of patients with different clinical subtypes of Alzheimer’s disease suggest that different fibril structures form in different disease variants and with different peptide lengths.

Date: 2017
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DOI: 10.1038/nature20814

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