Molecular structure of β-amyloid fibrils in Alzheimer's disease brain tissue.

By Jun-xia Lu, W. Qiang, Wai-Ming Yau, C. Schwieters, S. Meredith, R. Tycko. Cell, 2013

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Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, methodology): “Recently, however, fibrils amenable to TEM and ssNMR investigation have been generated in vitro from synthetic Aβ40 following seeding with material extracted post mortem from the brains of Alzheimer disease patients (84).”
Distinct tau prion strains propagate in cells and mice and define different tauopathies (2014, background): “For example, amyloid b protein forms at least two distinct, self-propagating fibrillar conformations in vitro (Petkova et al., 2005) and in vivo (Lu et al., 2013).”