Search alternatives:
ng decrease » nn decrease (Expand Search), _ decrease (Expand Search), gy decreased (Expand Search)
we decrease » _ decrease (Expand Search), nn decrease (Expand Search), mean decrease (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
10 ng » 100 ng (Expand Search), 10 mg (Expand Search), 10 nm (Expand Search)
ng decrease » nn decrease (Expand Search), _ decrease (Expand Search), gy decreased (Expand Search)
we decrease » _ decrease (Expand Search), nn decrease (Expand Search), mean decrease (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
10 ng » 100 ng (Expand Search), 10 mg (Expand Search), 10 nm (Expand Search)
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Changes of miR-132-3p in peritoneal dialysis patients with different duration.
Published 2024Subjects: -
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Regulation of TGF-<i>β</i>1 protein expression by MiR-132-3p was verified using WB.
Published 2024Subjects: -
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Effect of 10 ng of IL-1β and IL-1Ra in a preliminary recording of the LFPs in the OB.
Published 2025“…<p>A) A single dose of 10 ng of IL-1β decreased the amplitude of LFPs in the OB immediately after its microinjection, reaching a maximum effect at approximately 10 min and remaining constant for at least 45 min. …”
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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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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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