Two families of chaperonin: physiology and mechanism
AL Horwich, WA Fenton, E Chapman… - Annu. Rev. Cell Dev …, 2007 - annualreviews.org
Chaperonins are large ring assemblies that assist protein folding to the native state by
binding nonnative proteins in their central cavities and then, upon binding ATP, release the …
binding nonnative proteins in their central cavities and then, upon binding ATP, release the …
Mechanism of the eukaryotic chaperonin: protein folding in the chamber of secrets
Chaperonins are key components of the cellular chaperone machinery. These large,
cylindrical complexes contain a central cavity that binds to unfolded polypeptides and …
cylindrical complexes contain a central cavity that binds to unfolded polypeptides and …
Chaperonins: two rings for folding
H Yébenes, P Mesa, IG Muñoz, G Montoya… - Trends in biochemical …, 2011 - cell.com
Chaperonins are ubiquitous chaperones found in Eubacteria, eukaryotic organelles (group
I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a …
I), Archaea and the eukaryotic cytosol (group II). They all share a common structure and a …
4.0-Å resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement
Y Cong, ML Baker, J Jakana… - Proceedings of the …, 2010 - National Acad Sciences
The essential double-ring eukaryotic chaperonin TRiC/CCT (TCP1-ring complex or
chaperonin containing TCP1) assists the folding of∼ 5–10% of the cellular proteome. Many …
chaperonin containing TCP1) assists the folding of∼ 5–10% of the cellular proteome. Many …
Crystal structure of the open conformation of the mammalian chaperonin CCT in complex with tubulin
IG Muñoz, H Yébenes, M Zhou, P Mesa… - Nature structural & …, 2011 - nature.com
Protein folding is assisted by molecular chaperones. CCT (chaperonin containing TCP-1, or
TRiC) is a 1-MDa oligomer that is built by two rings comprising eight different 60-kDa …
TRiC) is a 1-MDa oligomer that is built by two rings comprising eight different 60-kDa …
Allosteric regulation of chaperonins
A Horovitz, KR Willison - Current opinion in structural biology, 2005 - Elsevier
Chaperonins are molecular machines that facilitate protein folding by undergoing energy
(ATP)-dependent movements that are coordinated in time and space by complex allosteric …
(ATP)-dependent movements that are coordinated in time and space by complex allosteric …
Allosteric mechanisms in chaperonin machines
R Gruber, A Horovitz - Chemical Reviews, 2016 - ACS Publications
Chaperonins are nanomachines that facilitate protein folding by undergoing energy (ATP)-
dependent movements that are coordinated in time and space owing to complex allosteric …
dependent movements that are coordinated in time and space owing to complex allosteric …
The TRiC/CCT chaperonin and its role in uncontrolled proliferation
DY Wang, K Kamuda, G Montoya, P Mesa - HSF1 and Molecular …, 2020 - Springer
The cell cycle is a sophisticated space-time regulated mechanism where a wide variety of
protein modules and complexes associate functioning in a concerted manner to regulate …
protein modules and complexes associate functioning in a concerted manner to regulate …
Mechanism of lid closure in the eukaryotic chaperonin TRiC/CCT
All chaperonins mediate ATP-dependent polypeptide folding by confining substrates within
a central chamber. Intriguingly, the eukaryotic chaperonin TRiC (also called CCT) uses a …
a central chamber. Intriguingly, the eukaryotic chaperonin TRiC (also called CCT) uses a …
[HTML][HTML] Friends in need: How chaperonins recognize and remodel proteins that require folding assistance
G Stan, GH Lorimer, D Thirumalai - Frontiers in Molecular …, 2022 - frontiersin.org
Chaperonins are biological nanomachines that help newly translated proteins to fold by
rescuing them from kinetically trapped misfolded states. Protein folding assistance by the …
rescuing them from kinetically trapped misfolded states. Protein folding assistance by the …