Sentence examples for mutant causes a from inspiring English sources

In the case of horse Mb, the His(E7 Val mutant causes a 15-fold decrease in nitrite reduction rate.

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].

The F713A mutant causes a catastrophic mechanical failure due to the loss of the hydrophobic contact between the SH2/SH1 hinge and converter.

Pre-treatment of cells with 10 μM wortmannin causes an approx. 80% drop in total cellular PtdIns4 P levels, as measured by metabolic labelling with P [ 20, 54, 55], and complete ablation of plasma membrane PtdIns4 P. Conversely, selective depletion of Golgi PtdIns4 P with a Golgi-localized Sac1 mutant causes a reduction in radiolabelled PtdIns4 P levels of approx. 20% [ 56].

The presence of the D12A/D66A mutations in the D12A/D66A/Y254V mutant causes a modest increase in binding affinity (decrease in Kd value) for both dNTP and rNTP, relative to the binding affinities for each of these ligands in complexes formed with the Y254V mutant.

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 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).

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 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.