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Prion-like mechanisms in neurodegenerative diseases

Nature Reviews Neuroscience volume 11, pages 155159 (2010) | Download Citation

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Abstract

Many non-infectious neurodegenerative diseases are associated with the accumulation of fibrillar proteins. These diseases all exhibit features that are reminiscent of those of prionopathies, including phenotypic diversity and the propagation of pathology. Furthermore, emerging studies of amyloid-β, α-synuclein and tau — proteins implicated in common neurodegenerative diseases — suggest that they share key biophysical and biochemical characteristics with prions. Propagation of protein misfolding in these diseases may therefore occur through mechanisms similar to those that underlie prion pathogenesis. If this hypothesis is verified in vivo, it will suggest new therapeutic strategies to block propagation of protein misfolding throughout the brain.

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Acknowledgements

B.F. gratefully acknowledges support from a training grant from the National Institute of Neurological Disorders and Stroke (NINDS). M.I.D. gratefully acknowledges support from the Sandler Family Supporting Foundation, the Muscular Dystrophy Association and NINDS.

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Affiliations

  1. Bess Frost is at the Department of Pathology, Harvard Medical School, Room 630, 77 Avenue Louis Pasteur, Boston, Massachusetts 02115, USA.

    • Bess Frost
  2. Marc I. Diamond is at the Department of Neurology, Washington University School of Medicine, BOX 8111, 660 South Euclid Avenue, St. Louis, Missouri 63110, USA.

    • Marc I. Diamond

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The authors declare no competing financial interests.

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Correspondence to Marc I. Diamond.

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https://doi.org/10.1038/nrn2786

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