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Mutation of the two potential glycosylation sites in PGU1 showed that the two residues individually (N318D, N330D) did not affect secreted enzyme activity, but the double mutant caused a 50% reduction in enzyme activity when compared to the wild-type PGU1 transformant.
The abnormal growth and loose structure of starch grain in gif1 mutant caused a significant rise in chalkiness, and the corresponding gene, GIF1 was fine-mapped on chromosome 4, which encode a cell-wall invertase required for carbon partitioning during early grain filling (Wang et al. 2008).
The results showed Kd values of 1.4 × 10−7 mol/L and 5.3 × 10−7 mol/L for YfiBL43P and YfiBL43P/F57A, respectively, revealing that the YfiBL43P/F57A mutant caused a 3.8-fold reduction in the binding affinity compared with the YfiBL43P mutant (Fig. 6F and 6G).
The dsetdb1G19561/Df 2R ED4065 mutant caused a slightly more-severe phenotype than the dsetdb1G19561 mutant (Fig. 1Cb d).
The combination of an activating CM mutant with a deactivating CM mutant caused a hybrid phenotype that neutralized the primary defects caused by these CM mutants in isolation.
It is noted, however, that while over-expression of Cdc42V12 in a fra3/fra4 mutant caused a dramatic loss in commissures, even more severe than over-expression of BcrAbl or Ablwt, no axons were observed leaving the CNS.
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In the case of horse Mb, the His(E7 Val mutant causes a 15-fold decrease in nitrite reduction rate.
The F713A mutant causes a catastrophic mechanical failure due to the loss of the hydrophobic contact between the SH2/SH1 hinge and converter.
This mutant causes a familial ALS, and could not be studied previously due to its high insolubility which is even resistant to solubilization by Triton X-100.
NapF mutant causes a growth defect under anaerobic conditions on glycerol/nitrate medium but is not essential for the activity of periplasmic nitrate reductase [ 59].
Furthermore, overexpression of CMT2B-causing Rab7a mutants caused a strong increase of soluble vimentin (Fig. 4E F).
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