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Kit mutants displayed a lower intrinsic kinase activity relative to PDGFRA mutants, while the KIT Exon 11 deletion mutant exhibited the highest intrinsic kinase activity among KIT mutants.
Nearly half (108/233, 46%) of the observed collateral responses were in ciprofloxacin-resistant mutants, while the remaining 125 were distributed between the other three resistance groups (Supplementary Table 2).
The VP19, VP24, VP26 and VP28 constructs were designed to express C- or N-terminal truncated mutants, while the larger VP51A gene was cloned in three separate parts.
The treatment with the UPS inhibitor (2 µΜ MG132, 3hr) induced a formation of small punctated cytoplasmic aggregates of SOD1 mutants, while the distribution of EGFP-LC3 and ALS2 were unchanged (data not shown).
Growth analysis on PC showed only slight decreases in the maximum cell density of the individual single fadD mutants, while the fadD2 mutant exhibited a delayed log phase (Fig. 8A).
The transcriptional fusion level of the pMP2C was almost the same in the two mutants, while the translational fusion level of pMP2L in the gacA inactivated mutant M18ΔG was 2-fold higher than that in the wild type strain M18 (Figure 5B & 5C), indicating that the negative control of GacA activity on phzA2-G2 expressioccurredred at the post-transcriptional level.
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By expression of xylan biosynthetic genes specifically in the xylem vessels of these mutants, it was possible to rescue the strong growth phenotypes of the irx mutants, while all the transformed mutants still showed large decreases in xylose compared to the wild type, to levels resembling that of the respective irx mutant or to an intermediate level between the mutant and the wild type.
The size of one DNA band typically corresponded to the size expected for the replacement mutant while the other matched the wild-type gene.
Quantitative analysis of the ubiquitination profiles clearly revealed an increase in the high molecular weight poly-ubiquitinated UNC-45 for the K704/706/713/717 R (KRcanyon) mutant, while the K637R and K938/943 R mutants were not as strongly poly-ubiquitinated as wild-type UNC-45 (Fig. 4e).
Indeed, this single mutation lowered the methanol concentration for which the initial rates of alcoholysis and hydrolysis are equal from 2 M in CAL-A down to 0.3 M in its mutant, while the exceptional stability of the parental enzyme toward alcohol and temperature was conserved.
At 24 h, no bacteria were recovered from the Δppk2 mutant, while the WT showed 5×107 CFU of bacteria.
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