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Dokumenttyp:
journal article 
Autor(en):
Krammer, C; Kremmer, E; Schätzl, HM; Vorberg, I 
Titel:
Dynamic interactions of Sup35p and PrP prion protein domains modulate aggregate nucleation and seeding. 
Abstract:
Prions are self-propagating infectious protein aggregates of mammals and fungi. The exact mechanism of prion formation is poorly understood. In a recent study, a comparative analysis of the aggregation propensities of chimeric proteins derived from the yeast Sup35p and mouse PrP prion proteins was performed in neuroblastoma cells. The cytosolic expression of the Sup35p domains NM, PrP and fusion proteins thereof revealed that the carboxyterminal domain of PrP (PrP90-230) mediated aggregate forma...    »
 
Zeitschriftentitel:
Prion 
Jahr:
2008 
Band / Volume:
Heft / Issue:
Seitenangaben Beitrag:
99-106 
Sprache:
eng 
Print-ISSN:
1933-6896 
TUM Einrichtung:
r Virologie