Proliferation of amyloid-β42 aggregates occurs through a secondary nucleation mechanism

By Samuel I. A. Cohen, S. Linse, L. Luheshi, Erik Hellstrand, Duncan A. White, L. Rajah, Daniel E. Otzen, Michele Vendruscolo, Christopher M. Dobson, Tuomas P. J. Knowles. Proceedings of the National Academy of Sciences of the United States of America, 2013

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Solution conditions determine the relative importance of nucleation and growth processes in α-synuclein aggregation (2014, methodology): “, through an enhanced rate of fragmentation (4)].”
Molecular mechanisms of protein aggregation from global fitting of kinetic models (2016, methodology): “…(primary nucleation, elongation and fragmentation on the one hand and primary nucleation, elongation and surface-catalyzed nucleation on the other hand) are fitted to the same data set (A β 42, used in Cohen et al. 28 ), first fitting each concentration individually, and then using global fitting.”
Protein Misfolding, Amyloid Formation, and Human Disease: A Summary of Progress Over the Last Decade. (2017, background): “The 40- and 42-residue fragments of the β amyloid precursor protein (βAPP), denoted Aβ40 and Aβ42, that are associated with hereditary Alzheimer disease and with hereditary cerebral hemorrhage with amyloidosis have been studied intensively and represent a particularly important source of information”
The Role of Amyloid-β Oligomers in Toxicity, Propagation, and Immunotherapy (2016, background): “It was also noticed that oligomers can form from secondary nucleation (Cohen et al., 2013).”