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Exact(6)

This mutant is responsible for familial amyotrophic lateral sclerosis, a chronic, progressive neuromuscular disorder [ 72].

Similarly, the enhanced phosphatase activity of the AHK4 receiver domain in the wol mutant is responsible for the wol phenotype [ 47] (Fig. 10).

Considering the known role of VIP1 as an enhancer of Agrobacterium infectivity, it is likely that higher VIP1 expression in roots of the wrky17 mutant is responsible for the increased susceptibility to Agrobacterium.

Both the complementation experiment and the targeted deletion of laeA show that the mutation in laeA in the D15 mutant is responsible for the acidification defect in the D15 mutant.

Overexpression of PmtA in the perR mutant is responsible for a higher resistance of up to 1.75 mM zinc, concentrations to which the wild-type and pmtA mutant were susceptible.

The introduction of this alanine mutation restored normal migration properties on polyacrylamide gels, suggesting that the arginine side chain in the mutant is responsible for the observed electrophoretic abnormalities.

Similar(54)

Single α-Spec lm88 mutants did not, suggesting that the dlt mutation in the double mutant was responsible for the suppression (Table 1, Rows 17−22).

Importantly, this result suggests that Pio protein is the critical target whose reduced secretion in γCOP mutants is responsible for the specific DB defects observed in γCOP mutants.

Our results suggest that the observed premature Wnt signaling in oto mutants is responsible for repressing hesx1 in the anterior neural plate.

These results indicate that the compound heterozygote pattern of these two functional-inactive mutants is responsible for complete lactose intolerance in the infant.

Accumulation of secondary, accessory mutants is responsible for the further increase in the level of the resistance and often restored replication capacity [ 20- 22].

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