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Trends Neurosci. 2010 Jul;33(7):317-25. doi: 10.1016/j.tins.2010.04.003. Epub 2010 May 20.

The propagation of prion-like protein inclusions in neurodegenerative diseases.

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MRC Laboratory of Molecular Biology, Hills Road, Cambridge, CB2 0QH, UK.


The most common neurodegenerative diseases, including Alzheimer's disease and Parkinson's disease, are characterized by the misfolding of a small number of proteins that assemble into ordered aggregates in affected brain cells. For many years, the events leading to aggregate formation were believed to be entirely cell-autonomous, with protein misfolding occurring independently in many cells. Recent research has now shown that cell non-autonomous mechanisms are also important for the pathogenesis of neurodegenerative diseases with intracellular filamentous inclusions. The intercellular transfer of inclusions made of tau, alpha-synuclein, huntingtin and superoxide dismutase 1 has been demonstrated, revealing the existence of mechanisms reminiscent of those by which prions spread through the nervous system.

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