Showing 581 - 600 results of 224,509 for search '(( a ((((teer decrease) OR (a decrease))) OR (linear decrease)) ) OR ( a large decrease ))', query time: 1.12s Refine Results
  1. 581
  2. 582
  3. 583
  4. 584
  5. 585
  6. 586

    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. …”
  7. 587
  8. 588
  9. 589
  10. 590

    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. …”
  11. 591
  12. 592

    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. …”
  13. 593
  14. 594
  15. 595
  16. 596
  17. 597

    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). …”
  18. 598

    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.…”
  19. 599

    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.…”
  20. 600