A region within the C-terminal domain of Ure2p is shown to interact with the molecular chaperone Ssa1p by the use of cross-linkers and mass spectrometry-Reference-Cited by-同舟云学术

A region within the C-terminal domain of Ure2p is shown to interact with the molecular chaperone Ssa1p by the use of cross-linkers and mass spectrometry

Published:2010-11-16 Issue:24 Volume:277 Page:5112-5123
ISSN:1742-464X
Container-title:FEBS Journal
language:en
Short-container-title:

Author:

Redeker Virginie,Bonnefoy Jonathan,Le Caer Jean-Pierre,Pemberton Samantha,Laprévote Olivier,Melki Ronald

Publisher

Wiley

Subject

Cell Biology,Molecular Biology,Biochemistry

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2010.07915.x/fullpdf

Reference40 articles.

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3. [URE3] prion propagation in Saccharomyces cerevisiae: requirement for chaperone Hsp104 and curing by overexpressed chaperone Ydj1p;Moriyama;Mol Cell Biol,2000

4. Antagonistic interactions between yeast [PSI(+)] and [URE3] prions and curing of [URE3] by Hsp70 protein chaperone Ssa1p but not by Ssa2p;Schwimmer;Mol Cell Biol,2002

5. [URE3] prion propagation is abolished by a mutation of the primary cytosolic Hsp70 of budding yeast;Roberts;Yeast,2004

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