Literature DB >> 25480290

How TriC folds tricky proteins.

Anastasia Zhuravleva1, Sheena E Radford2.   

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.
Copyright © 2014 Elsevier Inc. All rights reserved.

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Year:  2014        PMID: 25480290     DOI: 10.1016/j.cell.2014.11.029

Source DB:  PubMed          Journal:  Cell        ISSN: 0092-8674            Impact factor:   41.582


  3 in total

1.  Identification of chaperones in a MPP+-induced and ATRA/TPA-differentiated SH-SY5Y cell PD model.

Authors:  Hongrong Xie; Hui Hu; Ming Chang; Dongya Huang; Xiaobo Gu; Xinli Xiong; Ran Xiong; Linsen Hu; Gang Li
Journal:  Am J Transl Res       Date:  2016-12-15       Impact factor: 4.060

2.  Structural and functional insights into TRiC chaperonin from a psychrophilic yeast, Glaciozyma antarctica.

Authors:  Nur Athirah Yusof; Shazilah Kamaruddin; Farah Diba Abu Bakar; Nor Muhammad Mahadi; Abdul Munir Abdul Murad
Journal:  Cell Stress Chaperones       Date:  2019-01-16       Impact factor: 3.667

3.  Regulation of GPCR expression through an interaction with CCT7, a subunit of the CCT/TRiC complex.

Authors:  Samuel Génier; Jade Degrandmaison; Pierrick Moreau; Pascale Labrecque; Terence E Hébert; Jean-Luc Parent
Journal:  Mol Biol Cell       Date:  2016-10-05       Impact factor: 4.138

  3 in total

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