Showing 11,181 - 11,200 results of 122,558 for search '(( 2 e decrease ) OR ( 5 ((nn decrease) OR (((mean decrease) OR (a decrease)))) ))', query time: 1.24s Refine Results
  1. 11181

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  2. 11182

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  3. 11183

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  4. 11184

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  5. 11185

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  6. 11186

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  7. 11187

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  8. 11188

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  9. 11189

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  10. 11190

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  11. 11191

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  12. 11192

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  13. 11193

    Heterogeneous Condensation on Simplified Viral Envelope Protein Structures by Kawkab Ahasan (18784843)

    Published 2025
    “…Complex glycoprotein structures were modeled as cylindrical pillars to analyze condensation rates and active surface areas across a range of <i>p/d</i> ratios (1.0, 1.2, 1.3, 1.7, 2.0, and ∞) and contact angles (θ = 15°, 75°, and 105°, corresponding to <i>f</i> = 3.0, 2.0, and 1.5) to address envelope geometries for a wide variety of viruses. …”
  14. 11194

    Trehalose decreased PAN-induced apoptosis in human podocytes. by Yu-Lin Kang (663806)

    Published 2014
    “…LDH in culture medium of 4 groups was measured, n = 4. (<b>E</b>) Elevated apoptosis in PAN-treated podocytes was decreased by trehalose. …”
  15. 11195
  16. 11196
  17. 11197
  18. 11198
  19. 11199

    Disruption of Spatacsin decreases the regeneration of lysosomes in KO MEFs. by Rita-Eva Varga (784560)

    Published 2015
    “…Student’s t-test: n.s. indicated not significant). <b>(E, E´)</b> Lysosomal processing of the lysosomal protease Cathepsin D (CtsD) is not impaired in KO MEFs (CtsDp: precursor; CtsDm: mature). …”
  20. 11200

    <i>Neisseria meningitidis</i> Type IV Pili Composed of Sequence Invariable Pilins Are Masked by Multisite Glycosylation by Joseph Gault (427444)

    Published 2015
    “…Unlike class I pilins that carry a single glycan, we found that class II pilins display up to 5 glycosylation sites per monomer on the pilus surface. …”