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Incubation with increasing concentrations of ZnSO4 further demonstrated the inability of the Y372F mutant to support zinc accumulation into vesicular compartments (Fig. 5D).
Considering the importance of purine and pyrimidine in lipopolysaccharide (LPS) properties, disability of purL mutant to support infective juvenile formation may be due to the LPS modification.
We hypothesized that the inability of the Y372F mutant to support zinc storage in vesicular compartments would affect cell viability when cells are challenged with toxic extracellular zinc concentrations.
To better define the biochemistry of PARP-dependent mADPR formation, we reconstituted PARP-1 deficient DT40 cells with either WT or various mutant forms of PARP-1 (Figure 2), and determined the capacity of each mutant to support two correlates of O/N stress-induced mADPR formation: NAD degradation and TRPM2 activation.
To evaluate the functional consequences of IST1 phosphorylation by ULK3, we tested the ability of the IST1R 4SA mutant to support the abscission checkpoint.
However, the inability of the PKD1SSAA/SSAA mutant to support embryo development now shows that phosphoryation of Ser/Ser is essential for PKD1 function in vivo.
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The ability of core protein mutants to support the synthesis of DNA was analyzed by transfecting HepG2 cells with two plasmids.
We note with interest, however, that Sin3a association with the HCF-1 Basic region mutants in HeLa cells correlates with the ability of these mutants to support G1-to-S phase progression in these same cells.
The resulting cultures were spotted on tryptophan-deficient or tryptophan-deficient media containing 5-FOA and grown at 23°C to determine the ability of the dna2 mutants to support growth.
Figure 6F requires genetic evidence, such as analysis of della mutants, to support the model.
This previous paper used cells transfected with various siRNAs and/or LXR mutants to support their conclusions.
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