Zhuravleva, A and Radford, SE (2014) How tric folds tricky proteins. Cell, 159 (6). 1251 - 1252. ISSN 0092-8674
Abstract
How chaperonins orchestrate the successful folding of even the most elaborate of proteins is a question of central importance. In two recent studies in Cell by Joachimiak et al. and Freund et al.; a new class of TRiC substrate is identified, and how the chaperonin exploits its different subunits to extend its substrate repertoire and direct productive folding is revealed.
Metadata
Item Type: | Article |
---|---|
Authors/Creators: |
|
Dates: |
|
Institution: | The University of Leeds |
Academic Units: | The University of Leeds > Faculty of Biological Sciences (Leeds) > School of Molecular and Cellular Biology (Leeds) |
Depositing User: | Symplectic Publications |
Date Deposited: | 20 Jul 2015 15:51 |
Last Modified: | 03 Nov 2016 10:29 |
Published Version: | http://dx.doi.org/10.1016/j.cell.2014.11.029 |
Status: | Published |
Publisher: | Cell Press |
Identification Number: | 10.1016/j.cell.2014.11.029 |
Related URLs: | |
Open Archives Initiative ID (OAI ID): | oai:eprints.whiterose.ac.uk:85606 |
Download not available
A full text copy of this item is not currently available from White Rose Research Online