Recent advances in therapeutic strategies for triple-negative breast cancer

Y Li, H Zhang, Y Merkher, L Chen, N Liu… - Journal of hematology & …, 2022 - Springer
Triple-negative breast cancer (TNBC) is the most malignant subtype of breast cancer (BC)
with a poor prognosis. Current treatment options are limited to surgery, adjuvant …

Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities

C Hu, J Yang, Z Qi, H Wu, B Wang, F Zou, H Mei… - MedComm, 2022 - Wiley Online Library
The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …

Induced protein degradation: an emerging drug discovery paradigm

AC Lai, CM Crews - Nature reviews Drug discovery, 2017 - nature.com
Small-molecule drug discovery has traditionally focused on occupancy of a binding site that
directly affects protein function, and this approach typically precludes targeting proteins that …

Structural modification aimed for improving solubility of lead compounds in early phase drug discovery

B Das, ATK Baidya, AT Mathew, AK Yadav… - Bioorganic & Medicinal …, 2022 - Elsevier
Many lead compounds fail to reach clinical trials despite being potent because of low
bioavailability attributed to their insufficient solubility making solubility a primary and crucial …

The role of ligand efficiency metrics in drug discovery

AL Hopkins, GM Keserü, PD Leeson… - Nature reviews Drug …, 2014 - nature.com
The judicious application of ligand or binding efficiency metrics, which quantify the
molecular properties required to obtain binding affinity for a drug target, is gaining traction in …

Heat-shock proteins: chaperoning DNA repair

L Dubrez, S Causse, N Borges Bonan, B Dumétier… - Oncogene, 2020 - nature.com
Cells are repeatedly exposed to environmental or endogenous stresses that can alter
normal cell behavior and increase cell vulnerability. In order to ensure tissue integrity and …

Hsp90 molecular chaperone inhibitors: are we there yet?

L Neckers, P Workman - Clinical cancer research, 2012 - aacrjournals.org
Heat shock protein (Hsp) 90 is an ATP-dependent molecular chaperone that is exploited by
malignant cells to support activated oncoproteins, including many cancer-associated …

Old and new approaches to target the Hsp90 chaperone

J Sanchez, TR Carter, MS Cohen… - Current cancer drug …, 2020 - ingentaconnect.com
The 90-kDa heat shock protein (Hsp90) is a molecular chaperone that ensures cellular
proteostasis by maintaining the folding, stabilization, activation, and degradation of over 400 …

Heat shock protein 90 inhibitors: an update on achievements, challenges, and future directions

L Li, L Wang, QD You, XL Xu - Journal of medicinal chemistry, 2019 - ACS Publications
Hsp90 is one of the most important chaperones involved in regulating the maturation of
more than 300 client proteins, many of which are closely associated with refractory diseases …

Targeting protein–protein interactions as an anticancer strategy

AA Ivanov, FR Khuri, H Fu - Trends in pharmacological sciences, 2013 - cell.com
The emergence and convergence of cancer genomics, targeted therapies, and network
oncology have significantly expanded the landscape of protein–protein interaction (PPI) …