Mol Biotechnol. 2006 May;33(1):71-88.

Molecular aspects of disease pathogenesis in the transmissible spongiform encephalopathies.

Source

Laboratory of Persistent Viral Diseases, National Institute of Allergy and Infectious Diseases, Rocky Mountain Laboratories, 903 S. 4th St., Hamilton, MT 59840, USA. spriola@nih.gov

Abstract

The transmissible spongiform encephalopathies (TSE), or prion diseases, are a group of rare, fatal, and transmissible neurodegenerative diseases of mammals for which there are no known viral or bacterial etiological agents. The bovine form of these diseases, bovine spongiform encephalopathy (BSE), has crossed over into humans to cause variant Creutzfeldt-Jakob disease. As a result, BSE and the TSE diseases are now considered a significant threat to human health. Understanding the basic mechanisms of TSE pathogenesis is essential for the development of effective TSE diagnostic tests and anti-TSE therapeutic regimens. This review provides an overview of the molecular mechanisms that underlie this enigmatic group of diseases.

PMID:: 16691009; [PubMed - indexed for MEDLINE]

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Review

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Prions

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Related citations in PubMed

Review Molecular aspects of disease pathogenesis in the transmissible spongiform encephalopathies. [Methods Mol Biol. 2004]
Review Molecular aspects of disease pathogenesis in the transmissible spongiform encephalopathies.
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Cited by 2 PubMed Central articles

Review Prion protein misfolding and disease. [Curr Opin Struct Biol. 2009]
Review Prion protein misfolding and disease.
Moore RA, Taubner LM, Priola SA. Curr Opin Struct Biol. 2009 Feb; 19(1):14-22. Epub 2009 Jan 20.
Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent. [Virology. 2008]
Acute cellular uptake of abnormal prion protein is cell type and scrapie-strain independent.
Greil CS, Vorberg IM, Ward AE, Meade-White KD, Harris DA, Priola SA. Virology. 2008 Sep 30; 379(2):284-93. Epub 2008 Aug 8.

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