Results 61 to 70 of about 138,190 (352)

Therapeutic Potential of Heat Shock Protein 90 Inhibitors, Geldanamycin, and Analog Compounds in Precision Cancer Therapy

BioMed Target Journal, 2023
Heat shock protein (HSP90) is a molecular chaperone involved in numerous physiological processes. The primary role of this is to assist in the process of protein folding and to restore misfolded proteins to their correct shape.
Atta Mohammed Alzebari, Amjad Mahmood Qadir, Mahmood Sherzad Rafaat, Abbas Salihi   +3 more
doaj   +1 more source

Mutation of the co-chaperone Tsc1 in bladder cancer diminishes Hsp90 acetylation and reduces drug sensitivity and selectivity [PDF]

, 2019
The molecular chaperone Heat shock protein 90 (Hsp90) is essential for the folding, stability, and activity of several drivers of oncogenesis. Hsp90 inhibitors are currently under clinical evaluation for cancer treatment, however their efficacy is ...
Backe, Sarah J, Baker-Williams, Alexander J, Bourboulia, Dimitra, Bratslavsky, Gennady, Bratslavsky, Michael S, Hughes, Michael, Jacob, Joseph M, Mollapour, Mehdi, Sager, Rebecca A, Shapiro, Oleg, Wong, Michael, Woodford, Mark R   +11 more
core   +1 more source

eIF4A inhibitors suppress cell-cycle feedback response and acquired resistance to CDK4/6 inhibition in cancer [PDF]

, 2019
CDK4/6 inhibitors are FDA-approved drugs for estrogen receptor-positive (ER+) breast cancer and are being evaluated to treat other tumor types, including KRAS-mutant non-small cell lung cancer (NSCLC).
Cencic, Regina, Foulkes, William D., Fu, Zheng, Guiot, Marie-Christine, Huang, Sidong, Kong, Tim, Monast, Anie, Park, Morag, Pelletier, Jerry, Pilon, Virginie, Porco, John A., Sangwan, Veena, Xue, Yibo, Zhu, Xianbing   +13 more
core   +1 more source

Peptomer Linkers Enable Kinetic Control over Co‐Delivery of Multiple Chemotherapeutics

Advanced Healthcare Materials, EarlyView.
A key challenge in combinatorial chemotherapeutic drug delivery is independent control over release kinetics, especially with drugs of similar size and structure. Here, peptoid substitutions to proteolytically degradable peptides enabled the design of fast and slow‐releasing drug linkers.
Carolyn M. Watkins, Samuel L. Hallam, Mariah J. Austin, Adrianne M. Rosales   +3 more
wiley   +1 more source

Design of Disruptors of the Hsp90–Cdc37 Interface

Molecules, 2020
The molecular chaperone Hsp90 is a ubiquitous ATPase-directed protein responsible for the activation and structural stabilization of a large clientele of proteins.
Ilda D’Annessa, Naama Hurwitz, Valentina Pirota, Giovanni Luca Beretta, Stella Tinelli, Mark Woodford, Mauro Freccero, Mehdi Mollapour, Nadia Zaffaroni, Haim Wolfson, Giorgio Colombo   +10 more
doaj   +1 more source

A novel N-terminal extension in mitochondrial TRAP1 serves as a thermal regulator of chaperone activity. [PDF]

, 2014
Hsp90 is a conserved chaperone that facilitates protein homeostasis. Our crystal structure of the mitochondrial Hsp90, TRAP1, revealed an extension of the N-terminal β-strand previously shown to cross between protomers in the closed state. In this study,
Agard, David A, Cooke, Roger, Elnatan, Daniel, Lavery, Laura A, Naber, Nariman, Partridge, James R   +5 more
core   +2 more sources

Old and New Approaches to Target the Hsp90 Chaperone.

Current Cancer Drug Targets, 2019
The 90-kDa heat shock protein (Hsp90) is a molecular chaperone which ensures cellular proteostasis by maintaining the folding, stabilization, activation, and degradation of over 400 client proteins.
Jackee N. Sanchez, Trever R. Carter, Mark S. Cohen, B. Blagg   +3 more
semanticscholar   +1 more source

Hsp90: Breaking the Symmetry [PDF]

Molecular Cell, 2015
Hsp90 chaperones receive much attention due to their role in cancer and other pathological conditions, and a tremendous effort of many laboratories has contributed in the past decades to considerable progress in the understanding of their functions. Hsp90 chaperones exist as dimers and, with the help of cochaperones, promote the folding of numerous ...
Mayer, Matthias P., Le Breton, Laura
openaire   +2 more sources

Ferritin‐Doped Nanoparticles Triggered Tumor‐Specific Darkening for Enhanced Photothermal Tumor Ablation and Immune Activation

Advanced Healthcare Materials, EarlyView.
Ferritin‐doped hybrid nanoparticles triggered accurate tumor‐specific hemorrhage for enhanced in situ photothermal therapy and evoked anti‐tumor immunity. Notably, HFn/GA‐Fe specifically induced tumor hemorrhage 12 h after intravenous injection, resulting in visible color darkening. Through photoacoustic imaging, tumor vessels could be clearly observed
Haidong Zha, Xiao Liang, Long Xi, Jiamao Chen, Wenzhao Zhong, Zhen Yuan, Meng Xu, Ying Zheng   +7 more
wiley   +1 more source

Novel starting points for fragment-based drug design against human heat-shock protein 90 identified using crystallographic fragment screening

IUCrJ
Heat-shock protein 90 (HSP90) is a highly active molecular chaperone that plays a crucial role in cellular function. It facilitates the folding, assembly and stability of various oncogenic proteins, particularly kinases and transcription factors involved
Liqing Huang, Weiwei Wang, Zhimin Zhu, Qianhui Li, Minjun Li, Huan Zhou, Qin Xu, Wen Wen, Qisheng Wang, Feng Yu   +9 more
doaj   +1 more source