Prions as adaptive conduits of memory and inheritance
Author:
Publisher
Springer Science and Business Media LLC
Subject
Genetics (clinical),Genetics,Molecular Biology
Link
http://www.nature.com/articles/nrg1616.pdf
Reference162 articles.
1. James, L. C. & Tawfik, D. S. Conformational diversity and protein evolution — a 60-year-old hypothesis revisited. Trends Biochem. Sci. 28, 361–368 (2003).
2. Prusiner, S. B. Novel proteinaceous infectious particles cause scrapie. Science 216, 136–144 (1982).
3. Wickner, R. B. [URE3] as an altered URE2 protein: evidence for a prion analog in Saccharomyces cerevisiae. Science 264, 566–569 (1994).
4. Si, K., Lindquist, S. & Kandel, E. R. A neuronal isoform of the Aplysia CPEB has prion-like properties. Cell 115, 879–891 (2003). This paper shows that ApCPEB can function as a prion in yeast, and that the prion conformation is the most active in stimulating translation of CPEB-regulated mRNA. Together with data from reference 99, the authors propose that the formation of ApCPEB prions in specifically stimulated synapses helps to maintain long-term synaptic changes that are associated with memory storage.
5. Prusiner, S. B. Prion Biology and Diseases (Cold Spring Harbor Laboratory Press, New York, 2004).
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