The normal force between two particles with different equivalent diameters for P3: (a) hertznormal contact force; (b) normal viscous contact force. by Yongfeng Zhu (7361045)

Innovation, nightlights and a continuous measure of city size. by Saul Estrin (8629173)

The tangential force between two particles with different equivalent diameters for P3: (a) elastic tangential contact force; (b) viscous tangential contact force. by Yongfeng Zhu (7361045)

Primers used in q-PCR. by Marwa A. Ali (11973086)

“…Quantitative real-time PCR (qPCR) was performed to detect lncRNA <i>NEAT-1</i> and <i>miRNA374b-5p</i> fold change (FC) in the participants’ sera. Enzyme-Linked Immune Sorbent Assay (ELISA) is used to detect <i>IL6</i>.…”

Statins resulted in smaller neuronal soma size. by Shuk C. Tsoi (21192243)

“…Areas of cell somas in the heterogeneous BrdU-/Hu+ group are significantly smaller in the statin-treated (light blue line) group compared to soma areas in controls (dark blue line, bottom panel). Statin treatment decreased cell sizes in the larger cells more than in the smaller cells as seen in the greater divergence between lines plotted for larger cell somas (bottom panel). …”

The values approximated and calculated for and for the WT and each mutant Abl1 enzyme. by J. Roadnight Sheehan (20141887)

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A visual comparison of the associated resistance data from Table 1 with the values of <i>k</i>_cat, <i>K</i>_M, catalytic efficiency (<i>k</i>_cat/<i>... by J. Roadnight Sheehan (20141887)

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The values for <i>k</i>_cat and <i>K</i>_M are sourced from [19]. by J. Roadnight Sheehan (20141887)

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The values for and with the resultant ΔΔ<i>G</i>_Mut, found through FEP simulations. ΔΔ<i>G</i>_Mut for the wild-type is 0 kcal/mol. by J. Roadnight Sheehan (20141887)

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The table (refined data from [14]) shows the mutants associated with resistance for imatinib, ponatinib, and dasatinib. by J. Roadnight Sheehan (20141887)

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The enzyme states and their relative weights within the system in quasi-equilibrium. by J. Roadnight Sheehan (20141887)

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A heat map to compare the associated resistances outlined in Table 1 and [14] with the IRP values. by J. Roadnight Sheehan (20141887)

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How the variation in inhibitor concentration throughout one day affects the value of IC₅₀/(IC₅₀ + [R]) for different Abl1 inhibitors. by J. Roadnight Sheehan (20141887)

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We define the term “inhibitory reduction prowess” (IRP) as the percentage by which the product formation rate is reduced by from the initial point before inhibitor is introduced to... by J. Roadnight Sheehan (20141887)

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The values calculated for the inhibitor dissociation constant, as detailed in Eqs 10 and 11 and approximated values for the binding rate constants of the inhibitors. by J. Roadnight Sheehan (20141887)

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Values for the calculation of the time-dependent drug concentrations in the system based on observed data found and derived from a variety of sources. by J. Roadnight Sheehan (20141887)

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To bridge two naming conventions (one more suitable to mathematical notation and one more conventional in enzymology), the table matches the rate constants as described in Eq 2 to... by J. Roadnight Sheehan (20141887)

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A cartoon of the simplified model of the Abl1 enzyme system. by J. Roadnight Sheehan (20141887)

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Residence times, <i>t</i>_R, of the inhibitor molecules unbinding from the wild-type from [41] and the rates of calculated from them. by J. Roadnight Sheehan (20141887)

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Various outputs from the model with the drug imatinib. by J. Roadnight Sheehan (20141887)

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