Prion Topology and Toxicity

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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Published in:Cell 2009-06, Vol.137 (6), p.994-996
Main Authors: Aguzzi, Adriano, Steele, Andrew D.
Format: Article
Language:English
Subjects:
Animals
Humans
Mice
Prion Diseases - metabolism
PrPC Proteins - chemistry
PrPC Proteins - metabolism
Ubiquitin-Protein Ligases - chemistry
Ubiquitin-Protein Ligases - metabolism
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description 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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source ScienceDirect Journals
subjects Animals
Humans
Mice
Prion Diseases - metabolism
PrPC Proteins - chemistry
PrPC Proteins - metabolism
Ubiquitin-Protein Ligases - chemistry
Ubiquitin-Protein Ligases - metabolism
title Prion Topology and Toxicity
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