The yeast Sup35NM domain propagates as a prion in mammalian cells-Reference-Cited by-同舟云学术

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The yeast Sup35NM domain propagates as a prion in mammalian cells

Published:2008-12-29 Issue:2 Volume:106 Page:462-467
ISSN:0027-8424
Container-title:Proceedings of the National Academy of Sciences
language:en
Short-container-title:Proceedings of the National Academy of Sciences

Author:

Krammer C.,Kryndushkin D.,Suhre M. H.,Kremmer E.,Hofmann A.,Pfeifer A.,Scheibel T.,Wickner R. B.,Schatzl H. M.,Vorberg I.

Publisher

Proceedings of the National Academy of Sciences

Subject

Multidisciplinary

Reference42 articles.

1. Nobel Lecture: Prions

2. Evidence for the Conformation of the Pathologic Isoform of the Prion Protein Enciphering and Propagating Prion Diversity

3. Ψ, A cytoplasmic suppressor of super-suppressor in yeast

4. [URE3] as an Altered URE2 Protein: Evidence for a Prion Analog in Saccharomyces cerevisiae

5. Propagation of the yeast prion-like [psi+] determinant is mediated by oligomerization of the SUP35-encoded polypeptide chain release factor.

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