Unleashing the full potential of Hsp90 inhibitors as cancer therapeutics through simultaneous inactivation of Hsp90, Grp94, and TRAP1 [PDF]
, 2020 Cancer therapeutics: Extending a drug's reach A new drug that blocks heat shock proteins (HSPs), helper proteins that are co-opted by cancer cells to promote tumor growth, shows promise for cancer treatment.
Chae, Young Chan +10 more
core +1 more source
Co-crystalization and in vitro biological characterization of 5-Aryl-4-(5-substituted-2-4-dihydroxyphenyl)-1,2,3-thiadiazole Hsp90 inhibitors [PDF]
, 2012 A potential therapeutic strategy for targeting cancer that has gained much interest is the inhibition of the ATP binding and ATPase activity of the molecular chaperone Hsp90.
Chrisostomos Prodromou +7 more
core +10 more sources
mSystems, 2018 The 90-kDa heat shock protein (HSP90) of eukaryotes is a highly abundant and essential chaperone required for the maturation of regulatory and signal proteins.
Eugenia Bifeld +5 more
doaj +3 more sources
The Major Heat Shock Proteins, Hsp70 and Hsp90, in 2-Methoxyestradiol-Mediated Osteosarcoma Cell Death Model [PDF]
, 2020 2-Methoxyestradiol is one of the natural 17β-estradiol derivatives and a potential novel anticancer agent currently being under evaluation in advanced phases of clinical trials.
Cappello F. +8 more
core +1 more source
Could Upregulated Hsp70 Protein Compensate for the Hsp90-Silence-Induced Cell Death in Glioma Cells? [PDF]
, 2014 The molecular chaperone heat shock protein 90 alpha (Hsp90α) has been recognized in various tumours including glioma. This pilot study using a proteomic approach analyses the downstream effects of Hsp90 inhibition using 17-allylamino-17 ...
Khan, Zarine Jamsher +3 more
core +4 more sources
Heat Shock Protein 90 (Hsp90) Expression and Breast Cancer [PDF]
Pharmaceuticals, 2012 Hsp90 is an abundant protein in mammalian cells. It forms several discrete complexes, each containing distinct groups of co-chaperones that assist protein folding and refolding during stress, protein transport and degradation. It interacts with a variety of proteins that play key roles in breast neoplasia including estrogen receptors, tumor suppressor ...
Zagouri, F. +3 more
openaire +4 more sources
Cytosolic chaperones influence the fate of a toxin dislocated from the endoplasmic reticulum [PDF]
, 2008 The plant cytotoxin ricin enters target mammalian cells by receptor-mediated endocytosis and undergoes retrograde transport to the endoplasmic reticulum (ER).
Argent +32 more
core +4 more sources
The small-molecule kinase inhibitor D11 counteracts 17-AAG-mediated up-regulation of HSP70 in brain cancer cells. [PDF]
PLoS ONE, 2017 Many types of cancer express high levels of heat shock proteins (HSPs) that are molecular chaperones regulating protein folding and stability ensuring protection of cells from potentially lethal stress.
Susanne Schaefer +2 more
doaj +1 more source
Bacterial Hsp90 Facilitates the Degradation of Aggregation-Prone Hsp70–Hsp40 Substrates
Frontiers in Molecular Biosciences, 2021 In eukaryotes, the 90-kDa heat shock proteins (Hsp90s) are profusely studied chaperones that, together with 70-kDa heat shock proteins (Hsp70s), control protein homeostasis.
Bruno Fauvet +6 more
doaj +1 more source
New Insights on Heat Shock Proteins as Regulators of Reactive Oxygen Species Across Various Stressors in Diseases. [PDF]
Cell Biochem FunctABSTRACT Living beings are persistently challenged by stress. Stress can be induced by internal stressors and external stressors. External stressors, including radiation, heat, heavy metals, nutritional imbalances, infections, and psychological stress, can induce protein denaturation, leading to misfolded or aggregated proteins.
Kumar PS +5 more
europepmc +2 more sources