Showing 241 - 260 results of 226,904 for search '(( a ((peer decrease) OR (a decrease)) ) OR ( i ((largest decrease) OR (larger decrease)) ))', query time: 1.48s Refine Results
  1. 241
  2. 242
  3. 243
  4. 244
  5. 245
  6. 246
  7. 247
  8. 248
  9. 249

    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. …”
  10. 250
  11. 251
  12. 252
  13. 253
  14. 254
  15. 255
  16. 256

    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). …”
  17. 257

    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.…”
  18. 258

    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. 259
  20. 260

    Spatial information is significantly decreased in dCA1 and vCA1 in APP/PS1 mice. by Udaysankar Chockanathan (18510288)

    Published 2024
    “…Histograms show the mean firing rate for the corresponding neuron along each segment of the virtual track. (B) In dCA1, spatial information was decreased in APP/PS1 mice relative to C57BL/6 controls (mean ± std: C57BL/6 = 0.132 ± 0.048, APP/PS1 = 0.128 ± 0.051, p < 0.005, two-sided Wilcoxon rank-sum test, n<sub>C57BL/6</sub> = 305 units from 5 recording sessions, n<sub>APP/PS1</sub> = 180 units from 4 recording sessions). …”