Open AccessPrion Topology and Toxicity
Author(s) -
Adriano Aguzzi,
Andrew D. Steele
Publication year - 2009
Publication title -
cell
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 26.304
H-Index - 776
eISSN - 1097-4172
pISSN - 0092-8674
DOI - 10.1016/j.cell.2009.05.041
Subject(s) - biology , bovine spongiform encephalopathy , spongiosis , transmissible spongiform encephalopathy , microbiology and biotechnology , scrapie , ubiquitin ligase , ubiquitin , virology , disease , prion protein , genetics , immunology , gene , pathology , medicine
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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