Search alternatives:
ng decrease » nn decrease (Expand Search), _ decrease (Expand Search), we decrease (Expand Search)
d decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
ng decrease » nn decrease (Expand Search), _ decrease (Expand Search), we decrease (Expand Search)
d decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
a decrease » _ decrease (Expand Search), _ decreased (Expand Search), _ decreases (Expand Search)
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12341
Inflammation and hyperoxia decreases fractional anisotropy in corpus callosum.
Published 2012“…(B) Significant decrease of FA was observed in the corpus callosum of the injured groups (LN, VH, LH) compared with control group (VN) due to a significant increase of D⊥ (i.e. myelination defect). …”
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12342
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12343
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12344
Intraperitoneal injection protocol for inhibitors (A), inhibitors DAS and Y27632 reduced intestinal permeability (B) and intestinal adult worm burden (C) of infected mice.
Published 2025“…Each group had five replicates. <b>C:</b> DAS and Y27632 reduced intestinal adult worm burden at 5 dpi. …”
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12346
Intramolecularly Coordinated (6-(Diphenylphosphino)acenaphth-5-yl)stannanes. Repulsion vs Attraction of P- and Sn-Containing Substituents in the <i>peri</i> Positions
Published 2014“…The gas-phase structures of <b>2</b>–<b>5</b>, <b>8</b>, and the triarylstannyl cations ArPh<sub>2</sub>Sn<sup>+</sup> (<b>7a</b>) and [ArPh<sub>2</sub>Sn·NCMe]<sup>+</sup> (<b>7b</b>) were obtained by geometry optimization at the B3PW91/TZ level of theory. …”
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12347
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12348
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12349
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12350
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12351
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12352
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12353
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12354
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12355
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12356
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12357
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12358
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12359
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”
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12360
Heterogeneous Condensation on Simplified Viral Envelope Protein Structures
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. …”