Sentence examples for mutant supported the from inspiring English sources

A second cryoEM reconstruction of a truncated VCC mutant supported the topology of our model in which the carboxyl-terminal lectin domain forms "spikes" around the toxin core with the putative carbohydrate receptor-binding site accessible on the surface of the oligomer.

This large deletion mutant supported the finding.

Since pentamers are required to close icosahedra built from hexamers, the phenotype of the mutant supports the proposed role of this protein in the carboxysome shell.

However, the observation that the notching phenotype can be enhanced by loss of dTcf and rescued by gain of Wg, as seen with the zw3+/− heterozygous mutant, supports the hypothesis that vg>Mad and vg>Med suppress Wg signaling activities, therefore leading to the terminal consequence: apoptosis in the wing margin.

Although our analysis of the cxcr3.2 mutant supports the role of Cxcr3.2 in macrophage chemotaxis to infections, the chemokine ligands that signal via this receptor are unknown.

Thus, expansion of ZCL2897 population in the mutant supports the idea that Ubc9 maintains proliferative quiescence in the progenitor population and prevents their aberrant and lamellocyte differentiation.

The conserved nature of this glycine and high level of FUDR resistance in this mutant supports the conclusion that this is a loss of function mutation.

Furthermore, mutation of dlk-1 suppressed a microtubule acetylation mutant supporting the idea that altering microtubule structures is an upstream signal for DLK-1 activation.

As shown in Figure 2B, the increase in transcript size observed in the rrp6-ts32 mutant was almost completely lost in the rrp6-ts32 pla1-ts37 double mutant, supporting the idea that the increase was caused by polyadenylation.

Current evidence based on Fhit mutants with impaired substrate binding (L25W and I10W/L25W mutants) or hydrolytic activity (H96D mutant) supports the notion that the formation and stability of the Fhit-Ap3A complex is crucial in growth inhibition and apoptosis [ 5- 7].

H49 is located in the active site; the observed moderate decrease in the salt dependence for the H49A mutant supports the previous finding that this residue carries a partial charge in the ground-state complex (26).