[HTML][HTML] The molecular chaperone TRAP1 in cancer: From the basics of biology to pharmacological targeting
TRAP1, the mitochondrial component of the Hsp90 family of molecular chaperones, displays
important bioenergetic and proteostatic functions. In tumor cells, TRAP1 contributes to shape …
important bioenergetic and proteostatic functions. In tumor cells, TRAP1 contributes to shape …
Structure, function, and inhibitors of the mitochondrial chaperone TRAP1
S Kang, BH Kang - Journal of Medicinal Chemistry, 2022 - ACS Publications
Tumor necrosis factor receptor-associated protein 1 (TRAP1) is a mitochondrial molecular
chaperone modulating cellular metabolism and signaling pathways by altering the …
chaperone modulating cellular metabolism and signaling pathways by altering the …
The mitochondrial chaperone TRAP1 regulates F-ATP synthase channel formation
Binding of the mitochondrial chaperone TRAP1 to client proteins shapes bioenergetic and
proteostatic adaptations of cells, but the panel of TRAP1 clients is only partially defined …
proteostatic adaptations of cells, but the panel of TRAP1 clients is only partially defined …
The mitochondrial HSP90 paralog TRAP1: structural dynamics, interactome, role in metabolic regulation, and inhibitors
The HSP90 paralog TRAP1 was discovered more than 20 years ago; yet, a detailed
understanding of the function of this mitochondrial molecular chaperone remains elusive …
understanding of the function of this mitochondrial molecular chaperone remains elusive …
Structural Communication between the E. coli Chaperones DnaK and Hsp90
MP Grindle, B Carter, JP Alao, K Connors… - International Journal of …, 2021 - mdpi.com
The 70 kDa and 90 kDa heat shock proteins Hsp70 and Hsp90 are two abundant and highly
conserved ATP-dependent molecular chaperones that participate in the maintenance of …
conserved ATP-dependent molecular chaperones that participate in the maintenance of …
Nitric oxide-based regulation of metabolism: Hints from TRAP1 and SIRT3 crosstalk
F Faienza, A Rasola, G Filomeni - Frontiers in Molecular Biosciences, 2022 - frontiersin.org
Nitric oxide (NO) is a gaseous signaling molecule able to modify protein structure and
activity (Rizza and Filomeni, 2017). The addition of the NO moiety to a cysteine thiol is called …
activity (Rizza and Filomeni, 2017). The addition of the NO moiety to a cysteine thiol is called …
New Insights into Hsp90 Structural Plasticity Revealed by cryoEM
K Minari, VH Balasco Serrão, JC Borges - BioChem, 2024 - mdpi.com
Heat Shock Protein 90 (Hsp90) acts as a crucial molecular chaperone, playing an essential
role in activating numerous signaling proteins. The intricate mechanism of Hsp90 involving …
role in activating numerous signaling proteins. The intricate mechanism of Hsp90 involving …
TRAP1 and cyclophilin D compete at OSCP subunit to regulate enzymatic activity and permeability transition pore opening by F-ATP synthase
Binding of the mitochondrial chaperone TRAP1 to client proteins shapes cell bioenergetic
and proteostatic adaptations, but the panel of TRAP1 clients is only partially defined. Here …
and proteostatic adaptations, but the panel of TRAP1 clients is only partially defined. Here …