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The measured A620nm was related to the one measured from control containing 0 ng/ml human IL-1β.
For clarity, median FRET efficiencies measured in the presence of TEVp constructs were normalized to median FRET efficiencies measured from control cells transfected with the reporter construct alone.
In the absence of rapamycin, in cells transfected with 125 ng sTEVp, there was a small decrease in median FRET efficiency (to 96% of the FRET efficiency measured from control cells transfected with C34V alone; n = 77, ncontrol = 74).
In these cells, there was little background protease activity: the median FRET efficiency in the absence of rapamycin was 84% of the median FRET efficiency measured from control cells transfected with C34V-FKBP12-TEVct C34V-FKBP12-TEVct C34V-FKBP12-TEVct
In cells transfected with 300 ng pBud-sol-sTEVp and 100 ng of mem-C34V, the median FRET efficiency in the absence of rapamycin was 98% of the FRET efficiency measured from control cells transfected with mem-C34V alone (n = 21, ncontrol = 45).
As shown in Fig. 5Bi, the median FRET efficiency of cells transfected with 300 ng of pBud-sol-sTEVp and 100 ng of C34V was 97% of the FRET efficiency measured from control cells expressing C34V alone (P>0.05, n = 30, ncontrol = 36).
Similar(47)
Randomly selected junctions between outer pillar cells and Deiters' cells of the 1st row, and between Deiters' cells of the 2nd and 3rd row were measured from three control and mutant cochleas each.
Contents in the seedlings treated with S1 and S3 fungi were 1.42- and 1.46- fold, respectively, of those measured from the control.
Strontium sorption uncertainty is calculated from the analytical uncertainty of the initial and final solution concentrations and the uncertainty associated with a small amount of strontium inherent in the substrate measured from substrate control experiments.
The fluorescence recovery measured from the control cells, could now be reproduced by a simulation, in which 96% of EYFP had a diffusion coefficient of D = 50±5 µm2/s, and 4% of D = 1±0.1 µm2/s (Figure 5H).
In all cases, the decrease of the initial peak resulted in the appearance of a new single product peak that had a surface area equal to the surface area decrease of the substrate peak (measured from a control experiment in the absence of enzyme).
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