We found that C. gattii calcineurin mutants from R265 and WM276 and C. neoformans H99 exhibited multiple vesicle phenotypes at 37°, whereas these mutants exhibited a normal wild-type morphology at 24°.
Instead, the mutants exhibited a dosage-dependent dominance over wild-type poliovirus.
During recovery from sleep loss, Afh mutants exhibited a significant reduction of the power density in the delta band for NREMs.
Both mutants exhibited a better cyclodextrin-forming ability and a faster turnover rate (kcat) than the parental CGTase.
The lax1-1 fzp2 double mutants exhibited a novel, basically additive, phenotype, which suggests that LAX1 and FZP2 function in genetically independent pathways.
Both ST1 mutants exhibited a loss of dopamine affinity but similar binding properties for inverse agonists compared to their parent receptors.
However, the W139A and W53A mutants exhibited a 67%and4%4% relative increase in their specific activity with a specific substrate (CMC), respectively.
However, most investigated desmin mutants exhibited a distinct reduction in strain stiffening compared to wild-type desmin and promoted nonaffine network deformation.
It was discovered that the mutants exhibited a variable range of resistance to killing by gentamicin, suggesting that the presence of the kanamycin-resistance cassette or the particular insertion mutation did in many cases affect the bactericidal potency of gentamicin.
The remaining mutants exhibited a range of replication efficiencies; however, each mutant was capable of replicating in the presence of concentrations of DSB that effectively inhibited wild-type HIV-1.
It is worth of noting that one of the five tested mutants exhibited a 30% improvement in bioconversion yields compared to the wild-type enzyme, despite the absence of the CBM in this variant.
