Showing 141 - 160 results of 145,520 for search '(( a ((((a decrease) OR (linear decrease))) OR (larger decrease)) ) OR ( i largest decrease ))', query time: 0.80s Refine Results
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    Diagnostic plots linear mixed model with MMSE. by Skadi Wilke (2818591)

    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. by Thierry Poynard (38084)

    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. by Aleksandra Lubojemska (10746241)

    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). …”
  14. 154

    In superadditive networks, more enhancers decrease noise and fidelity. by Alvaro Fletcher (15675430)

    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 by Lilia Leisle (11356934)

    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 by Lilia Leisle (11356934)

    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.…”