Search alternatives:
ppm decrease » _ decrease (Expand Search), pa decreased (Expand Search), 026 decrease (Expand Search)
nn decrease » _ decrease (Expand Search), mean decrease (Expand Search), gy decreased (Expand Search)
c decrease » c decreased (Expand Search), _ decrease (Expand Search), rc decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
50 c » 5 c (Expand Search), 50 μ (Expand Search), 50 _ (Expand Search)
ppm decrease » _ decrease (Expand Search), pa decreased (Expand Search), 026 decrease (Expand Search)
nn decrease » _ decrease (Expand Search), mean decrease (Expand Search), gy decreased (Expand Search)
c decrease » c decreased (Expand Search), _ decrease (Expand Search), rc decreased (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
50 c » 5 c (Expand Search), 50 μ (Expand Search), 50 _ (Expand Search)
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Decreased phosphorylation of EIF2α underlies the impairment of arsenite-induced SG formation in LSM12-depleted cells.
Published 2020“…Control<sup>shRNA</sup> and <i>LSM12</i><sup>shRNA</sup> cells were incubated with 0.4-M sorbitol for the indicated time before co-staining with anti-ATXN2 antibody (red), anti-G3BP1 antibody (green), and Hoechst 33258 (blue). (B, C) LSM12 depletion decreases the arsenite-induced phosphorylation of EIF2α. …”
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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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The GluN2B-C456Y mutation decreases recombinant NMDAR currents and alters receptor properties.
Published 2020“…<p>(A) The GluN2B-C456Y mutation strongly decreases diheteromeric GluN1/GluN2B NMDAR currents in <i>Xenopus</i> oocytes. …”
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Decreased activity of FASII favors the cold growth of the <i>ΔcshA</i> strain.
Published 2020“…<p><b>(A)</b><i>fapR</i> mRNA levels decrease in ACC and biotin related suppressor strains. …”
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Expression of IR21a, IR93a, and IR25a proteins decreases in DOCCs at the late third instar.
Published 2021“…Right: <i>Ir21a>GFP-</i>labeled DOCCs express IR21a (Fig 4A), IR93a (Fig 4C) and IR25a (Fig 4E) proteins at 72 hr AEL (top), which are significantly decreased at 120 hr AEL (bottom). …”
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