Prion protein interconversions†-Reference-Cited by-同舟云学术

Prion protein interconversions†

Published:2001-02-28 Issue:1406 Volume:356 Page:197-202
ISSN:0962-8436
Container-title:Philosophical Transactions of the Royal Society of London. Series B: Biological Sciences
language:en
Short-container-title:Phil. Trans. R. Soc. Lond. B

Author:

Caughey Byron¹

Affiliation:

1. Laboratory of Persistent Viral Diseases, NIAID/NIH, Rocky Mountain Laboratories, Hamilton, MT 59840, USA ()

Abstract

The transmissible spongiform encephalopathies (TSEs), or prion diseases, remain mysterious neurodegenerative diseases that involve perturbations in prion protein (PrP) structure. This article summarizes our use of in vitro models to describe how PrP is converted to the disease–associated, protease–resistant form. These models reflect many important biological parameters of TSE diseases and have been used to identify inhibitors of the PrP conversion as lead compounds in the development of anti–TSE drugs.

Publisher

The Royal Society

Subject

General Agricultural and Biological Sciences,General Biochemistry, Genetics and Molecular Biology

Link

https://royalsocietypublishing.org/doi/pdf/10.1098/rstb.2000.0765

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