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. …”

Surface-Enhanced Raman Scattering Imaging of Dynamic pH Changes in Lysosomes during Cancer Cell Invasion on a Microfluidic Chip by Sijia Liu (1751842)

(TiO₂)_1–<i>x</i>(TaON)_<i>x</i> Solid Solution for Band Engineering of Anatase TiO₂ by Atsushi Suzuki (176891)

“…Band engineering of anatase TiO₂ was achieved by means of an anatase (TiO₂)_1–<i>x</i>(TaON)_<i>x</i> (TTON) solid solution. …”

(TiO₂)_1–<i>x</i>(TaON)_<i>x</i> Solid Solution for Band Engineering of Anatase TiO₂ by Atsushi Suzuki (176891)

“…Band engineering of anatase TiO₂ was achieved by means of an anatase (TiO₂)_1–<i>x</i>(TaON)_<i>x</i> (TTON) solid solution. …”

A novel cytostatic form of autophagy in sensitization of non-small cell lung cancer cells to radiation by vitamin D and the vitamin D analog, EB 1089 by Khushboo Sharma (686941)

Video_2_NudC L279P Mutation Destabilizes Filamin A by Inhibiting the Hsp90 Chaperoning Pathway and Suppresses Cell Migration.MP4 by Min Liu (45756)

Video_3_NudC L279P Mutation Destabilizes Filamin A by Inhibiting the Hsp90 Chaperoning Pathway and Suppresses Cell Migration.MP4 by Min Liu (45756)

Video_1_NudC L279P Mutation Destabilizes Filamin A by Inhibiting the Hsp90 Chaperoning Pathway and Suppresses Cell Migration.MP4 by Min Liu (45756)

pRPS6 and proliferation rates of starved Vasa2+/Piwi1+ cells were independent on the daytime of refeeding, and phospho-RPS6 was found in S- and M-phase Vasa2+/Piwi1+ cells. by Eudald Pascual-Carreras (12115380)

The effect of feeding and starvation on the proliferative competence and onset of cell cycle re-entry in all cell cycle-gated cells. by Eudald Pascual-Carreras (12115380)

Identification of lysine (K) residues that mediate M1 stability. by Chenxi Wang (284364)