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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 …
with a poor prognosis. Current treatment options are limited to surgery, adjuvant …
Heat shock proteins: Biological functions, pathological roles, and therapeutic opportunities
The heat shock proteins (HSPs) are ubiquitous and conserved protein families in both
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …
prokaryotic and eukaryotic organisms, and they maintain cellular proteostasis and protect …
Induced protein degradation: an emerging drug discovery paradigm
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 …
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
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 …
bioavailability attributed to their insufficient solubility making solubility a primary and crucial …
The role of ligand efficiency metrics in drug discovery
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 …
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 …
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 …
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 …
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 …
more than 300 client proteins, many of which are closely associated with refractory diseases …
Targeting protein–protein interactions as an anticancer strategy
The emergence and convergence of cancer genomics, targeted therapies, and network
oncology have significantly expanded the landscape of protein–protein interaction (PPI) …
oncology have significantly expanded the landscape of protein–protein interaction (PPI) …