Heterogeneous responses and isoform compensation dim the therapeutic window of Hsp90 ATP-binding inhibitors in cancer

X Tang, C Chang, D Mosallaei… - … and Cellular Biology, 2022 - Am Soc Microbiol
The rare capacity for heat shock protein 90 (Hsp90) chaperones to support almost the entire
cellular signaling network was viewed as a potential breakthrough to combat tumor …

Anticancer inhibitors of Hsp90 function: beyond the usual suspects

G Garg, A Khandelwal, BSJ Blagg - Advances in cancer research, 2016 - Elsevier
The 90-kDa heat-shock protein (Hsp90) is a molecular chaperone responsible for the
stability and function of a wide variety of client proteins that are critical for cell growth and …

Targeting the C-terminus of Hsp90 as a cancer therapy

J McConnell, Y Wang, S McAlpine - Heat Shock Protein Inhibitors: Success …, 2016 - Springer
Classical Hsp90 inhibitors target the N-terminal ATP binding site. While these inhibitors
have had some clinical success, treatment with these molecules leads to a dramatic …

The sensitivity to Hsp90 inhibitors of both normal and oncogenically transformed cells is determined by the equilibrium between cellular quiescence and activity

PC Echeverria, K Bhattacharya, A Joshi, T Wang… - PLoS …, 2019 - journals.plos.org
The molecular chaperone Hsp90 is an essential and highly abundant central node in the
interactome of eukaryotic cells. Many of its large number of client proteins are relevant to …

[HTML][HTML] Post-translational modification and conformational state of Heat Shock Protein 90 differentially affect binding of chemically diverse small molecule inhibitors

K Beebe, M Mollapour, B Scroggins, C Prodromou… - Oncotarget, 2013 - ncbi.nlm.nih.gov
Abstract Heat shock protein 90 (Hsp90) is an essential molecular chaperone in eukaryotes
that facilitates the conformational maturation and function of a diverse protein clientele …

Hsp90 inhibition: Elimination of shock and stress

AS Duerfeldt, BSJ Blagg - Bioorganic & medicinal chemistry letters, 2010 - Elsevier
The 90kDa heat shock proteins (Hsp90) represent a class of molecular chaperones
responsible for the maturation and stabilization of many oncogenic proteins. Disrupting the …

Post-translational modification of heat-shock protein 90: impact on chaperone function

BT Scroggins, L Neckers - Expert opinion on drug discovery, 2007 - Taylor & Francis
Heat-shock protein 90 (Hsp90) is a molecular chaperone required for the stability and
function of many signaling proteins that are often activated, mutated or overexpressed in …

[HTML][HTML] Heat shock protein 90 targeting therapy: state of the art and future perspective

M Tatokoro, F Koga, S Yoshida, K Kihara - EXCLI journal, 2015 - ncbi.nlm.nih.gov
Abstract Heat shock protein 90 (Hsp90) is an ATP-dependent molecular chaperone that
plays a role in stabilizing and activating more than 200 client proteins. It is required for the …

Impact of posttranslational modifications on the anticancer activity of Hsp90 inhibitors

MR Woodford, D Dunn, JB Miller, S Jamal… - Advances in cancer …, 2016 - Elsevier
Molecular chaperones are essential for guarding proteins that are indispensable for normal
cellular functions. Heat shock protein 90 (Hsp90) is a vital molecular chaperone in …

Investigation of the Hsp90 C-terminal binding site, novel inhibitors and isoform-dependent client proteins

LB Peterson - 2012 - kuscholarworks.ku.edu
The heat shock proteins represent an important class of pro-survival proteins that are
intimately involved in cell survival, adaptation to cellular stress, and protein management …