Showing 6,881 - 6,900 results of 24,758 for search '(( e point decrease ) OR ( 100 ((mean decrease) OR (((nn decrease) OR (a decrease)))) ))', query time: 0.98s Refine Results
  1. 6881
  2. 6882
  3. 6883
  4. 6884
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  14. 6894

    Charge Density Analysis of Heterohalogen (Cl···F) and Homohalogen (F···F) Intermolecular Interactions in Molecular Crystals: Importance of the Extent of Polarizability by Venkatesha R. Hathwar (1727917)

    Published 2011
    “…Intermolecular Cl···F interaction in 2-chloro-4-fluorobenzoic acid is attractive in nature (type II interaction) while the nature of F···F interactions in 4-fluorobenzamide shows indication of a minor decrease in repulsion (type I interaction), though the extent of polarization on the fluorine atom is arguably small.…”
  15. 6895

    Charge Density Analysis of Heterohalogen (Cl···F) and Homohalogen (F···F) Intermolecular Interactions in Molecular Crystals: Importance of the Extent of Polarizability by Venkatesha R. Hathwar (1727917)

    Published 2011
    “…Intermolecular Cl···F interaction in 2-chloro-4-fluorobenzoic acid is attractive in nature (type II interaction) while the nature of F···F interactions in 4-fluorobenzamide shows indication of a minor decrease in repulsion (type I interaction), though the extent of polarization on the fluorine atom is arguably small.…”
  16. 6896
  17. 6897
  18. 6898

    Percentage of <i>C</i>. <i>albicans</i> NCPF 3153 and <i>C</i>. <i>parapsilosis</i> ATCC 22019 growth, measured as the OD<sub>600</sub>, induced by the C1 compound in relation to t... by Barbara Chudzik (2985669)

    Published 2019
    “…*—the lowest concentration at which a statistically significant decrease in OD in comparison with the control was noted, as determined by one-way ANOVA and a post-hoc Tukey test. …”
  19. 6899
  20. 6900

    Proteomic Analysis Reveals Novel Molecules Involved in Insulin Signaling Pathway by Yiguo Wang (2644723)

    Published 2006
    “…In addition, we also found that calcium/calmodulin-dependent protein serine kinase (CASK), a key protein in protein-targeting and vesicle transport in neurons, forms a complex with two unidentified phosphotyrosine proteins pp100 and pp95 in response to insulin-stimulation, though CASK is not itself tyrosine phosphorylated. …”