S1 Data - by Miki Doi (15347878)

“…<div><p>In this study, we examined the effect of a bundled approach to blood collection for blood culture on decreasing contamination. …”

A Novel Type of PSMA-Targeting Ligands via β‑Branched Aromatic α‑Amino Acid Modification, Bearing Enhanced Tumor Targeting and Reduced Renal Toxicity by Zong-Xiao Liu (22177765)

“…With average renal uptake of less than 10%ID/g, as opposed to 25%ID/g for [⁶⁸Ga]Ga-<b>PSMA-617</b>, this substantial decrease in renal accumulation translates to a significantly improved safety profile by minimizing nephrotoxic risks. …”

A Novel Type of PSMA-Targeting Ligands via β‑Branched Aromatic α‑Amino Acid Modification, Bearing Enhanced Tumor Targeting and Reduced Renal Toxicity by Zong-Xiao Liu (22177765)

“…With average renal uptake of less than 10%ID/g, as opposed to 25%ID/g for [⁶⁸Ga]Ga-<b>PSMA-617</b>, this substantial decrease in renal accumulation translates to a significantly improved safety profile by minimizing nephrotoxic risks. …”

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. …”

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. …”

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. …”