SFP1-mediated prion-dependent lethality is caused by increased Sup35 aggregation and alleviated by Sis1-Reference-Cited by-同舟云学术

SFP1-mediated prion-dependent lethality is caused by increased Sup35 aggregation and alleviated by Sis1

Published:2016-10-12 Issue:12 Volume:21 Page:1290-1308
ISSN:1356-9597
Container-title:Genes to Cells
language:en
Short-container-title:Genes Cells

Author:

Matveenko Andrew G.¹²³,Drozdova Polina B.²³,Belousov Mikhail V.²,Moskalenko Svetlana E.¹²,Bondarev Stanislav A.²³,Barbitoff Yury A.²,Nizhnikov Anton A.¹²⁴,Zhouravleva Galina A.²³

Affiliation:

1. St Petersburg Branch; Vavilov Institute of General Genetics of the Russian Academy of Sciences; St Petersburg Russia

2. Department of Genetics and Biotechnology; Saint Petersburg State University; St Petersburg Russia

3. Laboratory of Amyloid Biology; Saint Petersburg State University; St Petersburg Russia

4. All-Russia Research Institute for Agricultural Microbiology; Pushkin St Petersburg Russia

Funder

Saint Petersburg State University

President of the Russian Federation

Russian Foundation for Basic Research

Publisher

Wiley

Subject

Cell Biology,Genetics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/gtc.12444/fullpdf

Reference68 articles.

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3. The majority of yeast UPF1 co-localizes with polyribosomes in the cytoplasm;Atkin;Mol. Biol. Cell,1995

4. In Sup35p filaments (the [PSI+] prion), the globular C-terminal domains are widely offset from the amyloid fibril backbone;Baxa;Mol. Microbiol.,2011

5. A split zinc-finger protein is required for normal yeast growth;Blumberg;Gene,1991

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