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largest decrease » largest decreases (Expand Search), marked decrease (Expand Search)
linear decrease » linear increase (Expand Search)
larger decrease » marked decrease (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
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Diagnostic plots linear mixed model with MMSE.
Published 2023“…</p><p>Conclusion</p><p>Treatment of the acute medical condition is associated with a fast decrease in delirium severity. Given the high incidence and prevalence of delirium in hospitalized older patients and its detrimental impact on cognition, abilities and personal independence further research needs to be done.…”
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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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HFD induces LDs and decreases ER and mitochondria in nephrocytes.
Published 2021“…(<b>E</b>) Low and high magnification views of pericardial nephrocytes (dotted outlines) from STD and HFD larvae, showing that HFD decreases mitochondria (marked with anti-ATP5A) and ER (marked with anti-KDEL) but increases LDs (marked with LipidTOX). …”
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In superadditive networks, more enhancers decrease noise and fidelity.
Published 2023“…<p>(A) Superadditivity is implemented in our model by linearly increasing <i>k</i><sub>on</sub> rates and linearly decreasing <i>k</i><sub>off</sub> rates. …”
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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.…”