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The expression level of E2F (related to cell division) in rad mutant was clearly lower than WT at one and three days, and that of Zinc fingers (related to protein binding) was much lower at 1 day (Fig. 1).
The hrk1Δ mutant was clearly distinct from the hog1Δ mutant in oxidative stress response (Fig. 5).
However, the XCC3358 insertion mutant was clearly and reproducibly altered in pathogenicity, showing a clear delay in symptom development in comparison to the wild-type strain (Figure 5A).
As shown in Figure 4D, Pc2 and the SIM1 deletion mutant bound to GST-SUMO1, whereas binding of the SIM2 or double SIM mutant was clearly reduced.
This explanation was ruled out, as the level of GFP expression in the m8 toxic mutant was clearly lower than the GFP level in wt yeast cells.
The internalization of A546-TF and TRITC-De into cells transfected with the CA mutant was clearly inhibited (50.4%±12.6% SD and 79.8% ±8.00 SD, respectively) in contrast to wt transfected cells, in which A546-TF and TRITC-De were efficiently internalized (91.8%±6.3% SD and 93.7%±2.8% SD, respectively).
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Comparisons in the cellulase activity between the wild type as the control and the mutant under various buffer pH values and temperatures showed that the cellulase activities of the mutant were clearly higher than that of the control, particularly for neutral pH and lower and higher temperatures.
Thus, AChE586-599 and the F3/A mutant were clearly able to interact with one another.
Although there is evidence that Trask can also be cleaved at sites other than R368 [12], this does not impact the interpretation of our experiment, since the M10 (R368D) mutant is clearly fully resistant to cleavage in our experiments.
Leaf discs from the pdx1 mutant were clearly more sensitive to the high light treatment than WT discs: both signals were enhanced in the mutant compared to WT.
The DIF-less phenotypes of the dimB null mutant were clearly recovered by constitutive expression of As-dimB, indicating that the function of As-DimB is equivalent to that of Dd-DimB (Fig. 6C).
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