Pan-and isoform-specific inhibition of Hsp90: Design strategy and recent advances

J Yu, C Zhang, C Song - European Journal of Medicinal Chemistry, 2022 - Elsevier
In the past few decades, the development of heat shock protein 90 (Hsp90) inhibitors for
cancer treatment has not stopped. About twenty compounds have been evaluated in the …

Recent advances toward the development of Hsp90 C-terminal inhibitors

E Amatya, BSJ Blagg - Bioorganic & Medicinal Chemistry Letters, 2023 - Elsevier
Abstract Heat shock protein 90 (Hsp90) is a dynamic protein which serves to ensure proper
folding of nascent client proteins, regulate transcriptional responses to environmental stress …

Magnoflorine attenuates inflammatory responses in RA by regulating the PI3K/Akt/NF-κB and Keap1-Nrf2/HO-1 signalling pathways in vivo and in vitro

Y Shen, X Fan, Y Qu, M Tang, Y Huang, Y Peng, Q Fu - Phytomedicine, 2022 - Elsevier
Background As a prolonged autoimmune disorder, rheumatoid arthritis (RA) is characterised
by synovial hyperplasia and the erosion of bone and cartilage. Magnoflorine (MAG) is the …

Development of a first-in-class small-molecule inhibitor of the C-terminal Hsp90 dimerization

S Bhatia, L Spanier, D Bickel, N Dienstbier… - ACS central …, 2022 - ACS Publications
Heat shock proteins 90 (Hsp90) are promising therapeutic targets due to their involvement in
stabilizing several aberrantly expressed oncoproteins. In cancerous cells, Hsp90 expression …

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 …

Identification of Hsp90 inhibitors with anti-Plasmodium activity

D Posfai, AL Eubanks, AI Keim, KY Lu… - Antimicrobial agents …, 2018 - Am Soc Microbiol
Malaria remains a global health burden partly due to Plasmodium parasite resistance to first-
line therapeutics. The molecular chaperone heat shock protein 90 (Hsp90) has emerged as …

Structure-activity relationships of Benzothiazole-based Hsp90 C-Terminal-domain inhibitors

J Dernovšek, Ž Zajec, M Durcik, LP Mašič, M Gobec… - Pharmaceutics, 2021 - mdpi.com
Heat shock protein 90 (Hsp90) is a chaperone responsible for the maturation of many
cancer-related proteins, and is therefore an important target for the design of new anticancer …

Modulation of human Hsp90α conformational dynamics by allosteric ligand interaction at the C-terminal domain

DL Penkler, Ö Tastan Bishop - Scientific Reports, 2019 - nature.com
Recent years have seen heat shock protein 90 kDa (Hsp90) attract significant interest as a
viable drug target, particularly for cancer. To date, designed inhibitors that target the ATPase …

[HTML][HTML] Crystal structure of the middle and C-terminal domains of Hsp90α labeled with a coumarin derivative reveals a potential allosteric binding site as a drug target

S Peng, J Woodruff, PK Pathak, RL Matts… - … Section D: Structural …, 2022 - scripts.iucr.org
The 90 kDa heat-shock protein (Hsp90) is an abundant molecular chaperone that is
essential to activate, stabilize and regulate the function of a plethora of client proteins. As …

[HTML][HTML] Dihydropyridines allosterically modulate Hsp90 providing a novel mechanism for heat shock protein co-induction and neuroprotection

MS Roe, B Wahab, Z Török, I Horváth, L Vigh… - Frontiers in Molecular …, 2018 - frontiersin.org
Chaperones play a pivotal role in protein homeostasis, but with age their ability to clear
aggregated and damaged protein from cells declines. Tau pathology is a driver of a variety …