Results 21 to 30 of about 58,138 (243)
Hsp90: Breaking the Symmetry [PDF]
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
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Thermotolerance is a remarkable virulence attribute of Aspergillus fumigatus, but the consequences of heat shock (HS) to the cell membrane of this fungus are unknown, although this structure is one of the first to detect changes in ambient temperature ...
João Henrique Tadini Marilhano Fabri +6 more
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Aim: Present study was done to understand the dimerization of HER2/ERBB2 in normal and cancer cells using in-silico study. Methods: Pathway analysis was done using Reactome.
Jayasree Santhanakrishnan +2 more
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The present study aimed to explore the pathway through which Heat Shock Protein 70 (HSP70) is involved in inflammation and sepsis and the possible interaction with glutamine, an essential nutrient during sepsis. We also evaluated the possible interaction
Ioanna Plati +5 more
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Activation of the complement component 5a (C5a) and nuclear factor κB (NF-κB) signaling is an important feature of myocardial ischemia/reperfusion (I/R) injury and recent studies show that morphine postconditioning (MP) attenuates the myocardial injury ...
Tu Rong-Hui +7 more
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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 +3 more
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Silence of STAT3 Enhances SNX-2112-induced Apoptosis of Esophageal Cancer Stem Cells
Objective To investigate the effect of STAT3 silence on SNX-2112-induced apoptosis of esophageal cancer stem cells. Methods shSTAT3 lentiviral vector was designed and constructed. Esophageal cancer stem cells were transfected with shSTAT3 vector and then
XU Dandan, CHEN Suhong, WANG Ying
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Design of Disruptors of the Hsp90–Cdc37 Interface
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 +10 more
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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
Heat shock protein 90 (HSP90) is a highly conserved and essential molecular chaperone involved in maturation and activation of signaling proteins in eukaryotes. HSP90 operates as a dimer in a conformational cycle driven by ATP binding and hydrolysis. HSP90 often functions together with co-chaperones that regulate the conformational cycle and/or load a ...
Kadota, Yasuhiro, Shirasu, Ken
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