PCAIs disrupt actin filaments in NCI-H23 cells. by Matthew D. Gregory (19929096)

Measurement of micturition behavior in the rats. by Takafumi Kabuto (14797727)

Metabolome data of the discovery cohort. by Feng Gao (3548)

“…The results showed that compared with HC, five metabolites, including DL-stachydrine, D-(+)-pipecolinic acid, furazolidone, L-arginine and 5α-dihydrotestosterone glucuronide were significantly elevated and one metabolite, prenylcysteine, was significantly decreased in the serum of OC, and that the increase in L-arginine and the decrease in prenylcysteine led to impaired urea cycling and a high risk of developing atherosclerosis, respectively. …”

Primers used for RT-PCR. by Quankuan Gu (20539301)

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”

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

“…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. …”