[HTML][HTML] The structural basis of eukaryotic chaperonin TRiC/CCT: action and folding

H Kim, J Park, SH Roh - Molecules and Cells, 2024 - Elsevier
Accurate folding of proteins in living cells often requires the cooperative support of molecular
chaperones. Eukaryotic group II chaperonin Tailless complex polypeptide 1-Ring Complex …

Revisiting the chaperonin T‐complex protein‐1 ring complex in human health and disease: A proteostasis modulator and beyond

C Zeng, S Han, Y Pan, Z Huang… - Clinical and …, 2024 - Wiley Online Library
Background Disrupted protein homeostasis (proteostasis) has been demonstrated to
facilitate the progression of various diseases. The cytosolic T‐complex protein‐1 ring …

The conformational landscape of TRiC ring-opening and its underlying stepwise mechanism revealed by cryo-EM

M **, Y Zang, H Wang, Y Cong - QRB Discovery, 2025 - cambridge.org
The TRiC/CCT complex assists in the folding of approximately 10% of cytosolic proteins
through an ATP-driven conformational cycle, playing a crucial role in maintaining protein …

The Hsp60 C-terminus Senses Substrate and Triggers Allosteric ATP Hydrolysis

D Von Salzen, A Rodriguez, A Ullah, RA Bernal - bioRxiv, 2023 - biorxiv.org
The human mitochondrial chaperonin Hsp60/Hsp10 plays an essential role in maintaining
protein homeostasis through an ATP dependent protein refolding mechanism. In the …