Results 31 to 40 of about 137,496 (252)
BIIB021: A novel inhibitor to heat shock protein 90–addicted oncology
Tumor Biology, 2017 Heat shock protein 90 is induced in response to the cell stress. Its overexpression has been reported in many cancers with poor prognosis. It acts as a chaperone to the client proteins, especially the activated oncoproteins in malignancies to protect ...
Liang Yan +4 more
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Heat shock protein 90 inhibition: rationale and clinical potential
Therapeutic Advances in Medical Oncology, 2012 Heat shock protein 90 (HSP90) is a molecular chaperone protein essential for cellular survival. Functionally, HSPs promote proper protein folding, prevent misfolding, and restore three-dimensional protein structure which is critical following toxic ...
Robert B. Den, Bo Lu
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Heat Shock Protein 90: The Cancer Chaperone
Journal of Biosciences, 2007 Heat shock protein 90 (Hsp90) is a molecular chaperone required for the stability and function of a number of conditionally activated and/or expressed signalling proteins, as well as multiple mutated, chimeric, and/or over-expressed signalling proteins, that promote cancer cell growth and/or survival.
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Impact of Heat-Shock Protein 90 on Cancer Metastasis [PDF]
Future Oncology, 2009 Cancer metastasis is the result of complex processes, including alteration of cell adhesion/motility in the microenvironment and neoangiogenesis, that are necessary to support cancer growth in tissues distant from the primary tumor. The molecular chaperone heat-shock protein 90 (Hsp90), also termed the 'cancer chaperone', plays a crucial role in ...
Shinji, Tsutsumi +2 more
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Effect of EPA on Hsp90 and GRα protein expression in multiple myeloma drug-resistant cells
BMC Cancer, 2021 Background Approximately 20% of MM patients harbor glucocorticoid (GC) resistance and are not responsive to therapeutic effect. Chaperoneheat-shock proteins Hsp90 is needed for ligand docking, The imbalance of Hsp90/GRα (glucocorticoid receptor α) may be
Shenghao Wu +5 more
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Conserved binding mode but diverse interfaces of MreC‐PBP2 interactions
FEBS Letters, EarlyView.The crystal structure of abMreC reveals a conserved two β‐barrel architecture and provides structural insights into its role within the bacterial elongasome. The abMreC–abPBP2 complex model identifies the molecular basis of MreC‐mediated PBP2 recognition, contributing to the regulation of peptidoglycan synthesis.
Hyunseok Jang +4 more
wiley +1 more source
Cell ReportsSummary: Heat shock can be a lethal stressor. Previously, we described a CUL-6/cullin-ring ubiquitin ligase complex in the nematode Caenorhabditis elegans that is induced by intracellular intestinal infection and proteotoxic stress and that promotes ...
Mario Bardan Sarmiento +3 more
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Trans-spliced heat shock protein 90 modulates encystation in Giardia lamblia.
PLoS Neglected Tropical Diseases, 2014 BackgroundHsp90 from Giardia lamblia is expressed by splicing of two independently transcribed RNA molecules, coded by genes named HspN and HspC located 777 kb apart.
Rishi Kumar Nageshan +3 more
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Molecular Oncology, EarlyView.BCL9 and BCL9L drive bladder cancer progression by enhancing β‐catenin signaling, promoting proliferation, migration, invasion, and organoid growth. Genetic depletion of BCL9(L) suppresses malignant phenotypes, while pharmacological disruption of the β‐catenin/BCL9(L) complex with ZW4864 inhibits canonical Wnt signaling and tumor‐associated cellular ...
Roland Kotolloshi +11 more
wiley +1 more source
Temperature stress response of heat shock protein 90 (Hsp90) in the clam Paphia undulata
Aquaculture and Fisheries, 2018 The Heat shock proteins (HSPs) are a group of molecular chaperones that play a crucial role in cell response to various stresses. A full-length cDNA of the heat shock protein 90 (PuHsp90) was cloned and sequenced from the clam Paphia undulata ...
Xiangyang Lin, Xiangwei Wu, Xiande Liu
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