PNAS

Structure of the complex between the cytosolic chaperonin CCT and phosducin-like protein

The three-dimensional structure of the complex formed between the cytosolic chaperonin CCT (chaperonin containing TCP-1) and phosducin (Pdc)-like protein (PhLP), a regulator of CCT activity, has been ...
Europe PMC

Effects of Austenitization Temperature and Pre-Deformation on CCT Diagrams of 23MnNiCrMo5-3 Steel.

The combined effect of deformation temperature and strain value on the continuous cooling transformation (CCT) diagram of low-alloy steel with 0.23% C, 1.17% Mn, 0.79% Ni, 0.44% Cr, and 0.22% Mo was ...
The EMBO Journal

Structure of eukaryotic prefoldin and of its complexes with unfolded actin and the cytosolic chaperonin CCT

The biogenesis of the cytoskeletal proteins actin and tubulin involves interaction of nascent chains of each of the two proteins with the oligomeric protein prefoldin (PFD) and their subsequent ...
The EMBO Journal

Eukaryotic chaperonin CCT stabilizes actin and tubulin folding intermediates in open quasi‐native conformations

Three‐dimensional reconstruction from cryoelectron micrographs of the eukaryotic cytosolic chaperonin CCT complexed to tubulin shows that CCT interacts with tubulin (both the α and β isoforms) using ...
PNAS

4.0-Å resolution cryo-EM structure of the mammalian chaperonin TRiC/CCT reveals its unique subunit arrangement

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 TRiC substrates cannot be folded ...
Nature

CCT complex restricts neuropathogenic protein aggregation via autophagy

Aberrant protein aggregation is controlled by various chaperones, including CCT (chaperonin containing TCP-1)/TCP-1/TRiC. Mutated CCT4/5 subunits cause sensory neuropathy and CCT5 expression is ...