Showing 61 - 80 results of 145,675 for search '(( a a decrease ) OR ((( 50 nn decrease ) OR ( 50 ((mg decrease) OR (we decrease)) ))))', query time: 0.72s Refine Results
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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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    Global Land Use Change Impacts on Soil Nitrogen Availability and Environmental Losses by Jing Wang (6206297)

    Published 2025
    “…However, how global land use changes impact soil N supply and potential N loss remains elusive. By compiling a global data set of 1,782 paired observations from 185 publications, we show that land use conversion from natural to managed ecosystems significantly reduced NNM by 7.5% (−11.5, −2.8%) and increased NN by 150% (86, 194%), indicating decreasing N availability while increasing potential N loss through denitrification and nitrate leaching. …”
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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.…”
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    Decreased activity of FASII favors the cold growth of the <i>ΔcshA</i> strain. by Vanessa Khemici (814639)

    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. by Jordan J. Tyrrell (10535989)

    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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