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Dokumenttyp:
journal article 
Autor(en):
Krammer, C; Schätzl, HM; Vorberg, I 
Titel:
Prion-like propagation of cytosolic protein aggregates: insights from cell culture models. 
Abstract:
Amyloid formation is a hallmark of several systemic and neurodegenerative diseases. Extracellular amyloid deposits or intracellular inclusions arise from the conformational transition of normally soluble proteins into highly ordered fibrillar aggregates. Amyloid fibrils are formed by nucleated polymerization, a process also shared by prions, proteinaceous infectious agents identified in mammals and fungi. Unlike so called non-infectious amyloids, the aggregation phenotype of prion proteins can b...    »
 
Zeitschriftentitel:
Prion 
Jahr:
2009 
Band / Volume:
Heft / Issue:
Seitenangaben Beitrag:
206-12 
Sprache:
eng 
Print-ISSN:
1933-6896 
TUM Einrichtung:
r Virologie