Showing 601 - 620 results of 224,509 for search '(( a ((((laser decrease) OR (a decrease))) OR (linear decrease)) ) OR ( a large decrease ))', query time: 1.01s Refine Results
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    A large part of T cell signaling associates with the lamellum. by Kole T. Roybal (779123)

    Published 2015
    “…Red indicates an increase and green a decrease in the percentage occurrence of a pattern relative to the previous time point. …”
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    Volitional control frequency and intensity in VH (Kapsner-Smith et al., 2025) by Mara R. Kapsner-Smith (22139315)

    Published 2025
    “…Specifically, unusually large responses to perturbations of vocal auditory feedback cannot be explained by a broader impairment of the ability to make small changes in the vocal parameters <i>F</i>0 or intensity. …”
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    Decreased frequency of sEPSCs in <i>Dyt1</i> heterozygous KO mice. by Fumiaki Yokoi (170876)

    Published 2015
    “…<p>(A) Representative traces for sEPSCs. <i>Dyt1</i> heterozygous KO mice had a significantly decreased frequency of sEPSCs (B), but no change in either the amplitude (C), or rise (D) and decay (E) times of these events. …”
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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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    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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    Optimization of a large-scale signal transduction pathway. by Alexander Mitsos (115316)

    Published 2012
    “…The proposed compartmentalization scheme groups together nodes that share identical in-silico responses under all experimental conditions, thus decreasing the parameters space. (B) Signaling dataset, consisting of 15 cytokines in combinations of two, and 3 inhibitors (including the no-inhibitor treatment), total of 120 experimental treatments (see <a href="http://www.plosone.org/article/info:doi/10.1371/journal.pone.0050085#pone.0050085-Melas2" target="_blank">[48]</a>). …”