Review

Nature Reviews Molecular Cell Biology 4, 878-890 (November 2003) | doi:10.1038/nrm1247

Propagation of yeast prions

Mick F. Tuite1 & Brian S. Cox1  About the authors

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Prion proteins have been implicated in various human neurodegenerative disorders and form amyloid deposits in the diseased brain. Uniquely, prion proteins seem to be able to propagate this altered conformational state, generating more of the prion form of the protein and acting as infectious agents. The discovery in yeast of prion proteins that can be inherited stably through generations of cell division provides us with an experimental model that is allowing the mysteries of how prions are propagated to be unravelled.

Author affiliations

  1. Department of Biosciences, University of Kent, Canterbury, Kent CT2 7NJ, UK.

Correspondence to: Mick F. Tuite1 Email: M.F.Tuite@kent.ac.uk

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REFERENCE
Prions
Nature Encyclopaedia of Life Sciences
Nonsense Mutations and Suppression
Nature Encyclopaedia of Life Sciences

NEWS AND VIEWS
Spongiform encephalopathies: Tracking turncoat prion proteins
Nature News and Views (17 Jul 1997)
Prions: The shape of a species barrier
Nature News and Views (08 Mar 2001)
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RESEARCH
The yeast non-Mendelian factor [ETA+] is a variant of [PSI+], a prion-like form of release factor eRF3
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