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

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

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

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

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

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

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

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

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

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

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

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

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

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

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

“…The rapid initial condensation fills up the gap between the pillars, reducing the active surface area and leading to a gradual decrease and a plateau in the condensation rate. …”

Primer sequences for qPCR. by Tucker Hopkins (20790529)

“…Furthermore, when S2R + <i>Drosophila</i> cells are incubated at high temperatures, there is a marked decrease in Akt phosphorylation, directly supporting the notion that elevated temperatures can inhibit insulin signaling in a cell-autonomous manner, independent of Ilp levels. …”

Source data for graphs. by Tucker Hopkins (20790529)

“…Furthermore, when S2R + <i>Drosophila</i> cells are incubated at high temperatures, there is a marked decrease in Akt phosphorylation, directly supporting the notion that elevated temperatures can inhibit insulin signaling in a cell-autonomous manner, independent of Ilp levels. …”

The reagents used in this study. by Tucker Hopkins (20790529)

“…Furthermore, when S2R + <i>Drosophila</i> cells are incubated at high temperatures, there is a marked decrease in Akt phosphorylation, directly supporting the notion that elevated temperatures can inhibit insulin signaling in a cell-autonomous manner, independent of Ilp levels. …”

Study timeline and methodological overview. by Robert Botelho (20308297)

Longitudinal assessment of animal weights and tumor metrics. by Robert Botelho (20308297)

Fig 7 - by Keith Fraser (1868587)

Modelled seroprevalence estimates (coloured regions) compared with real data (black). by Keith Fraser (1868587)

Densities of pAkt/tAkt bands from Western blots were quantified. by Tucker Hopkins (20790529)

High temperatures regulate the insulin signaling pathway. by Tucker Hopkins (20790529)

The constitutively active form of insulin receptor and knockdown of FoxO block high temperature-mediated body fat loss. by Tucker Hopkins (20790529)

Table of parameters. by Keith Fraser (1868587)

High-affinity choline Uptake (HACU) in the Cortex, Striatum, and Hippocampus of non-tumor and tumor-bearing mice. by Robert Botelho (20308297)