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 |
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| Authors/Creators: |
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| Dates: |
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| 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 |
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