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Titel:

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

Dokumenttyp:
Journal Article; Research Support, Non-U.S. Gov't
Autor(en):
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...     »
Zeitschriftentitel:
Proc Natl Acad Sci U S A
Jahr:
2009
Band / Volume:
106
Heft / Issue:
2
Seitenangaben Beitrag:
462-7
Sprache:
eng
Volltext / DOI:
doi:10.1073/pnas.0811571106
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/19114662
Print-ISSN:
0027-8424
TUM Einrichtung:
Institut für Virologie
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