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largest decrease » largest decreases (Expand Search), marked decrease (Expand Search)
larger decrease » marked decrease (Expand Search)
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a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
largest decrease » largest decreases (Expand Search), marked decrease (Expand Search)
larger decrease » marked decrease (Expand Search)
laser decrease » linear decrease (Expand Search), water decreases (Expand Search), teer decrease (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
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Quantitative decrease of apolipoprotein-A1 by cohort.
Published 2020“…<p>Apolipoprotein-A1 decreased (P<0.001) in the three cohorts, starting early in January 2020 (red line with 95% confidence interval) in the US cohort (lower panel).…”
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Validating the stability of the analysis against nonuniform coverage of a fish’s trajectory.
Published 2023“…The tuning curves either gradually decreased (<b>A</b>), were quasi-uniformly distributed in space (<b>B</b>), or gradually increased (<b>C</b>) with position along the vertical axis of the water tank. …”
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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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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). …”