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Structural dependence of HET-s amyloid fibril infectivity assessed by cryoelectron microscopy

HET-s is a priori protein of the fungus Podospora anserina which, in the priori state, is active in a self/nonself recognition process called heterokaryon incompatibility. Its prionogenic properties reside in the C-terminal "prion domain." The HET-s prion domain polymerizes in vitro into amyloid... Full description

1st Person: Mizuno, Naoko
Additional Persons: Baxa, Ulrich verfasserin; Steven, Alasdair C. verfasserin; Caspar, Donald verfasserin
Source: in Proceedings of the National Academy of Sciences of the United States of America Vol. 108, No. 8 (2011), p. 3252-3257
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Type of Publication: Article
Language: English
Published: 2011
Keywords: research-article
Online: Volltext
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