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Interestingly, SD treatments did not promote heading in the mutant; however, the LD treatment promoted heading in the mutant at low temperatures.
A little unexpectedly, we found that both the trimeric and dimeric enzymes of E. coli, RecBCDEc and RecBCEc (lacking RecD), were competent not only to protect the ΔrecCBD strain of P. syringae from UV and MMC treatment, but also in supporting the growth of the mutant at low temperature, suggesting that both RecBCDEc and RecBCEc complexes retain functional activity at 4°C.
Furthermore, the double mutant resembled the tph-1 mutant at low bacterial levels and the daf-7 mutant at high bacterial levels, suggesting that these genes act in parallel rather than in a linear pathway.
Stabilization of substrate binding by the additional phenylalanine residue near the heme moiety in the I369F mutant via stacking interactions of the aromatic rings may contribute to the high rate of CBZ turnover observed with this mutant at low CBZ concentrations.
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In addition, we found a floral organ number increase in dp1 mutants at low penetration.
In several mutants at low substrate concentrations, the maximum level of ampicillin production was increased up to 1.5-fold, and the ratio of the synthetic rate over the hydrolytic rate was increased 5 15-fold.
The abdominal wall defect is seen in both Vangl2 Lp/Lp and Celsr1 Crsh/Crsh mutants, at low incidence (<5% and ~10%, respectively).
It should be noted that the essential character of the early proton release has not been proven, as BR retains its proton-pumping activity even when proton release occurs after uptake, as happens in a number of BR mutants, at low pH and in some close homologues of BR.
Quantitative pyrosequencing showed that the m.4175G>A mutation was present at high levels of heteroplasmy in skeletal muscle (90% mutant load); at low levels (5% mutant load) in a urinary sediment-derived DNA sample, but undetectable in all other DNA samples.
Some of these processes were also statistically enriched in genes identified comparing the mutant and the parental strains and particularly in genes more expressed in the mutant strain at low pressure and in the parental at high pressure (Additional file 19: Table S12).
For instance, the dnaE2.2 mutant shifted at low PykA concentration and growth rate while dnaE2.6 and dnaC30 shifted at high PykA concentrations and growth rates (Fig. 4).
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