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[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 …
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 …
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
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 …
through an ATP-driven conformational cycle, playing a crucial role in maintaining protein …
The Hsp60 C-terminus Senses Substrate and Triggers Allosteric ATP Hydrolysis
The human mitochondrial chaperonin Hsp60/Hsp10 plays an essential role in maintaining
protein homeostasis through an ATP dependent protein refolding mechanism. In the …
protein homeostasis through an ATP dependent protein refolding mechanism. In the …