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Titel:

Prion-like propagation of cytosolic protein aggregates: insights from cell culture models.

Dokumenttyp:
Journal Article
Autor(en):
Krammer, C; Schätzl, HM; Vorberg, I
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:
3
Heft / Issue:
4
Seitenangaben Beitrag:
206-12
Sprache:
eng
PubMed:
http://view.ncbi.nlm.nih.gov/pubmed/19901539
Print-ISSN:
1933-6896
TUM Einrichtung:
Institut für Virologie
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