Sentence examples for mutant located in from inspiring English sources

Plasmid rescue showed that the p-element of this mutant located in the first intron of the gene silver (svr) (Fig. 1A).

Finally, the G439D mutant, located in domain II loop 3, also showed an oligomeric structure that was mainly found inserted into the membrane.

The I35T mutant, located in β3 strand, showed a fast increase in ThT fluorescence (figure 2), and therefore in the rate of oligomerization, as also evidenced by the gel chromatographic analysis (data not shown), while the other mutant here investigated, L67V, ologomerizes with a slower rate, similarly to WT SOD1.

However, when we used the previously described non-toxic Cry11Aa-E97A mutant, located in helix α-3 that is affected in oligomerization [26], we found that this mutant did not show a DN phenotype since it was unable to inhibit the toxicity of the wildtype toxin when tested at 0.5∶1 or 1∶1 ratios.

These genetic links are specific to the conserved N-terminal region of the Sac3 PCI domain because a K467D/K468D double mutant located in the Sac3 winged helix domain did not exhibit a synthetic growth defect with cdk8Δ.

This mutant (located in TM1-EC1 junction) has been found to have similar intracellular trafficking consequences as V44E; it also inhibited coexpressed WT Cx50 and Cx46 in a dominant negative fashion [ 27].

At the same time, the integrity of F595 was also key to several other JAK2 mutants located in different locations of the protein, JAK2 K539L, JAK2 T875N and JAK2 R683G.

Experiments with alanine mutants, located in the complex interfaces, yielded an energy map for the contact areas of the Ras/effector complexes, which could be differentiated into enthalpy and entropy contributions.

FV des B C2 mutants located in the region between Lys2060 and Glu2069 were resistant to inhibition by three IgG preparations including the bovine thrombin-induced antibody in both prothrombinase and phospholipid-binding assays.

Figure 3A shows that some mutants located in helix α-4 completely blocked toxin action even at sub-stoichiometric ratios.

The analysis of additional point mutants located in and around the cap-binding pocket has allowed us to address this question in more depth.