The shape of things to come: structural insights into how prion proteins encipher heritable information-Reference-Cited by-同舟云学术

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The shape of things to come: structural insights into how prion proteins encipher heritable information

Published:2022-07-13 Issue:1 Volume:13 Page:
ISSN:2041-1723
Container-title:Nature Communications
language:en
Short-container-title:Nat Commun

Author:

Telling Glenn C.

Funder

U.S. Department of Health & Human Services | NIH | National Institute of Neurological Disorders and Stroke

U.S. Department of Health & Human Services | NIH | National Institute of Allergy and Infectious Diseases

Publisher

Springer Science and Business Media LLC

Subject

General Physics and Astronomy,General Biochemistry, Genetics and Molecular Biology,General Chemistry,Multidisciplinary

Link

https://www.nature.com/articles/s41467-022-31460-8.pdf

Reference13 articles.

1. Prusiner, S. B. In Les Prix Nobel (ed. T. Frängsmyr) 268-323 (Almqvist & Wiksell International, 1998).

2. Telling, G. C. et al. Evidence for the conformation of the pathologic isoform of the prion protein enciphering and propagating prion diversity. Science 274, 2079–2082 (1996).

3. Bessen, R. A. & Marsh, R. F. Distinct PrP properties suggest the molecular basis of strain variation in transmissible mink encephalopathy. J. Virol. 68, 7859–7868 (1994).

4. Riek, R. et al. NMR structure of the mouse prion protein domain PrP(121–231). Nature 382, 180–182 (1996).

5. Prusiner, S. B. et al. Scrapie prions aggregate to form amyloid-like birefringent rods. Cell 35, 349–358 (1983).

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