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Title:

Prion protein/protein interactions: fusion with yeast Sup35p-NM modulates cytosolic PrP aggregation in mammalian cells.

Document type:
Journal Article; Research Support, Non-U.S. Gov't
Author(s):
Krammer, C; Suhre, MH; Kremmer, E; Diemer, C; Hess, S; Schätzl, HM; Scheibel, T; Vorberg, I
Abstract:
In mammalian prion diseases, an abnormally folded, aggregated form of the prion protein (PrP(Sc)) appears to catalyze a conformational switch of its cellular isoform (PrP(C)) to an aggregated state. A similar prion-like phenomenon has been reported for the Saccharomyces cerevisiae translation termination factor Sup35p that can adopt a self-propagating conformation. We have compared aggregation propensities of chimeric proteins derived from the Sup35p prion domain NM and PrP in vitro and in the c...     »
Journal title abbreviation:
FASEB J
Year:
2008
Journal volume:
22
Journal issue:
3
Pages contribution:
762-73
Language:
eng
Fulltext / DOI:
doi:10.1096/fj.07-8733com
Pubmed ID:
http://view.ncbi.nlm.nih.gov/pubmed/17928365
Print-ISSN:
0892-6638
TUM Institution:
Institut für Virologie
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