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Based on previous studies, a possible explanation is that these mutants increase the inflammatory response by signaling through TLR4.
Studies have shown that pre-existing minority drug-resistant mutants increase the risk of virological failure to first-line antiretroviral therapy with non-nucleoside reverse transcriptase inhibitors (NNRTIs) [3], [4], [5], [6], [7].
Here, we report that the osu1 mutants increase the sensitivity to both high C/low N and low C/high N, suggesting that the OSU1-encoded putative methyltransferase acts as a negative modulator of the C/N nutrient imbalance response.
Temperature sensitive recB and recC mutants individually, or in combination, exhibit a temperature (42°C) induced drop in the cell viability, and additional rep inactivation in these thermo-sensitive mutants increase the accumulation of linear DNA fragments at high temperature [15], [16].
In addition, GTPase cycling rates in fast cycling mutants increase the transforming capacity of the Rho GTPases [ 45, 46].
Moreover, these mutants increase the degradation and turnover rate of DJ-1, which explains the lower protein levels detected in these experiments.
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Combination of three of these mutants increased the thermal stability of the molecule to 86 °C.
However, as the frequency of the dhps double mutants increased the estimates of the relationship between dhfr triple and protective efficacy became less precise.
The results (Figure 5A) indicate that the presence of R55W in 2C of the FMDV mutants increased the amount of extracellular viral RNA without any significant increase in the total viral RNA levels (intracellular plus extracellular).
All γ-2 Ex1 mutants increased the weighted-mean channel conductance of GluA2i to the same extent as γ-2 WT.
At several food levels, daf-7 mutants increased the variance of tph-1 expression compared to the wildtype or the tph-1 single mutant, whilst the daf-7 mutation reduced the variance of daf-7 expressinn in ASI.
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