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fold decrease » fold increase (Expand Search), fold increased (Expand Search)
ppm decrease » _ decrease (Expand Search), nn decrease (Expand Search), pa decreased (Expand Search)
non decrease » nn decrease (Expand Search), point decrease (Expand Search), note decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
e fold » 5 fold (Expand Search), _ fold (Expand Search), 2 fold (Expand Search)
e non » _ non (Expand Search), a non (Expand Search)
fold decrease » fold increase (Expand Search), fold increased (Expand Search)
ppm decrease » _ decrease (Expand Search), nn decrease (Expand Search), pa decreased (Expand Search)
non decrease » nn decrease (Expand Search), point decrease (Expand Search), note decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
e fold » 5 fold (Expand Search), _ fold (Expand Search), 2 fold (Expand Search)
e non » _ non (Expand Search), a non (Expand Search)
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Cytoskeletal Drugs Modulate Off-Target Protein Folding Landscapes Inside Cells
Published 2020“…The decreased compactness and folding stability of PGK could be explained by the decreased extent of crowding induced by these drugs. …”
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Uncoupling protein-2 is an antioxidant that is up-regulated in the enamel organ of fluoride-treated rats
Published 2020“…Maturation stage incisor enamel organs (EO) were harvested from F<sup>−</sup>-treated rats and mice were assessed to determine if vitamin E ameliorates dental fluorosis. Uncoupling protein-2 (<i>Ucp2</i>) was significantly up-regulated by F<sup>−</sup> (∼1.5 & 2.0 fold for the 50 or 100 ppm F<sup>−</sup> treatment groups, respectively). …”
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Ether induces proteotoxic stress, leading to a decrease in Trx protein and an increase in Hsp90 clients that are joint targets of Trx and Ubx.
Published 2024“…<b>(N)</b> GO enrichment analysis of proteins that increased (red) and decreased by ether, as determined by proteomics profiles of exposed and non-exposed embryos. …”
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