Search alternatives:
fold decrease » fold increase (Expand Search), fold increased (Expand Search)
ppm decrease » _ decrease (Expand Search), nn decrease (Expand Search), pa decreased (Expand Search)
nm decrease » nn decrease (Expand Search), _ decrease (Expand Search), we decrease (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
5 nm » 5 mm (Expand Search), 5 cm (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)
nm decrease » nn decrease (Expand Search), _ decrease (Expand Search), we decrease (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
5 nm » 5 mm (Expand Search), 5 cm (Expand Search)
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GSK343 decreased neuroblastoma viability, proliferation, and motility.
Published 2021“…By 24 hours, there was a significant decrease in the area of the scratch healed (indicating decreased motility) in cells treated with GSK343 compared to untreated cells. …”
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SETD2 mediates the binding of MALAT1 and pSmads.
Published 2020“…<b>D,</b> Smad2 linker region mutations decrease its capability to form protein complex with PPM1A and SETD2 proteins. …”
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Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket
Published 2021“…We confirmed experimentally that the interaction is predominantly driven by electrostatic forces, and using noncanonical amino acids as photo-cross-linkers, we identified 16 residues in ASIC1a contributing to Big Dyn binding. Covalently tethering Big Dyn to its ASIC1a binding site dramatically decreased the proton sensitivity of channel activation, suggesting that Big Dyn stabilizes a resting conformation of ASIC1a and dissociates from its binding site during channel opening.…”
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Dynorphin Neuropeptides Decrease Apparent Proton Affinity of ASIC1a by Occluding the Acidic Pocket
Published 2021“…We confirmed experimentally that the interaction is predominantly driven by electrostatic forces, and using noncanonical amino acids as photo-cross-linkers, we identified 16 residues in ASIC1a contributing to Big Dyn binding. Covalently tethering Big Dyn to its ASIC1a binding site dramatically decreased the proton sensitivity of channel activation, suggesting that Big Dyn stabilizes a resting conformation of ASIC1a and dissociates from its binding site during channel opening.…”
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S5 Data -
Published 2023“…On the other hand, the IC analysis showed a gradual decrease in chlorite ions in the acidic sodium chlorite solution. …”
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Number of significant genes and fold change.
Published 2023“…Adult fear responses to a predator odor were decreased only by PN10-14 treatment and the infant Shock alone and Shock+mother did not differ.…”