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Title:

The yeast Sup35NM domain propagates as a prion in mammalian cells.

Document type:
Journal Article; Research Support, Non-U.S. Gov't
Author(s):
Krammer, C; Kryndushkin, D; Suhre, MH; Kremmer, E; Hofmann, A; Pfeifer, A; Scheibel, T; Wickner, RB; Schätzl, HM; Vorberg, I
Abstract:
Prions are infectious, self-propagating amyloid-like protein aggregates of mammals and fungi. We have studied aggregation propensities of a yeast prion domain in cell culture to gain insights into general mechanisms of prion replication in mammalian cells. Here, we report the artificial transmission of a yeast prion across a phylogenetic kingdom. HA epitope-tagged yeast Sup35p prion domain NM was stably expressed in murine neuroblastoma cells. Although cytosolically expressed NM-HA remained solu...     »
Journal title abbreviation:
Proc Natl Acad Sci U S A
Year:
2009
Journal volume:
106
Journal issue:
2
Pages contribution:
462-7
Language:
eng
Fulltext / DOI:
doi:10.1073/pnas.0811571106
Pubmed ID:
http://view.ncbi.nlm.nih.gov/pubmed/19114662
Print-ISSN:
0027-8424
TUM Institution:
Institut für Virologie
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