Showing 341 - 360 results of 224,509 for search '(( a ((a decrease) OR (linear decrease)) ) OR ( a ((latent decrease) OR (largest decrease)) ))', query time: 1.54s Refine Results
  1. 341
  2. 342
  3. 343
  4. 344
  5. 345
  6. 346

    Wnt5a expressing tumors demonstrate a decrease in markers of the basal tumor subtype. by Stephanie L. Easter (662168)

    Published 2014
    “…Values are means +/− standard error (n = 6 MMTV-Wnt1, 3 fields per tumor; n = 5 MMTV-Wnt1;MMTV-Wnt5a, 3 fields per tumor). MMTV-Wnt1;MMTV-Wnt5a tumors demonstrated a significant decrease in K6-expressing cells as measured by T-test (* = p<0.05).…”
  7. 347

    Results for four illustrative latent topics specified by a 50-topic CGC LDA model estimated from a corpus with 5,225 documents and a vocabulary of 28,971 words by DM Blei (19075)

    Published 2011
    “…CGC-based topic labels are a subset of the 50 × 500 topic annotation words that are unique to a topic and are words from the CGC vocabulary; these labels are ordered according to decreasing values. …”
  8. 348
  9. 349
  10. 350
  11. 351
  12. 352
  13. 353
  14. 354
  15. 355
  16. 356

    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. …”
  17. 357
  18. 358
  19. 359

    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). …”
  20. 360

    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.…”