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Prion topology and toxicity


Aguzzi, A; Steele, A D (2009). Prion topology and toxicity. Cell, 137(6):994-996.

Abstract

Inactivation of mahogunin, an E3 ubiquitin ligase, causes a spongiform encephalopathy resembling prion disease. Chakrabarti and Hegde (2009) now report that prion proteins with aberrant topologies inactivate mahogunin, providing a plausible explanation for certain aspects of prion pathology.

Inactivation of mahogunin, an E3 ubiquitin ligase, causes a spongiform encephalopathy resembling prion disease. Chakrabarti and Hegde (2009) now report that prion proteins with aberrant topologies inactivate mahogunin, providing a plausible explanation for certain aspects of prion pathology.

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8 citations in Web of Science®
8 citations in Scopus®
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Additional indexing

Item Type:Journal Article, refereed, further contribution
Communities & Collections:04 Faculty of Medicine > University Hospital Zurich > Institute of Neuropathology
Dewey Decimal Classification:570 Life sciences; biology
610 Medicine & health
Language:English
Date:2009
Deposited On:23 Jun 2009 09:31
Last Modified:05 Apr 2016 13:16
Publisher:Elsevier
ISSN:0092-8674
Publisher DOI:https://doi.org/10.1016/j.cell.2009.05.041
PubMed ID:19524502
Permanent URL: https://doi.org/10.5167/uzh-19402

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