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DOI: http://dx.doi.org/10.7554/eLife.02740.004 10.7554/eLiFigure40.005 Figure 1 figure supplement 2. The ATPase activity of BmrCD-WT (wild type BmrCD), BmrCD-WT* (Cysteine-less BmrCD) and its spin-labeled mutants is stimulated by Hoechst33342 (hereafter referred as Hoechst) (10 µM) and inhibited by vanadate (1 mM).
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However, when mutants were stimulated 24 hours prior to testing, the reversal frequency dropped to a level midway between that in wild type and in animals lacking GLR-1 altogether.
However, when pink1 mutants were stimulated at a higher and more intense frequency of 10 Hz, a small but significant progressive decline in synaptic transmission (Fig 1I) was observed.
Individual alanine mutation of Site-1 and Site-2, preventing phosphorylation at these sites, led to a moderate activation of KCC3A under isotonic conditions, and the activity of these mutants was stimulated further following exposure to hypotonic high K+ conditions.
In the acid soil, the root growth of WT plants was inhibited by 54 %, whereas that of the mutant was stimulated in comparison with its growth on the neutral soil (Fig. 2d).
Lastly, the sorted Ba/F3-EpoR cells expressing each mutant were stimulated or not with Epo, lysed and immunobloted in the presence of phosphospecific antibodies (Figure 3C).
Interestingly, the P509S mutant was stimulated robustly by DnaJC19, which is consistent with hTid-1 isoforms (P < 0.01; Fig. 1D).
The already enhanced levels of expression seen with the T435D mutant were stimulated somewhat further by TNFα treatment, as might be expected from the enhanced translocation of RelA to the nucleus under these conditions.
(G ) CLB-GAR cells harboring the ALK-R1275Q mutant were stimulated for 30 min with medium from HEK293 cells transfected with either vector control, FAM150A or FAM150B prior to analysis by immunoblot.
In contrast, translation of the 5mut1,2 double mutant RNA is stimulated by the mutated miR-122 mu more than three-fold.
DOI: http://dx.doi.org/10.7554/eLife.02740.014 10.7554/eLiFigure4 figureigure 4—figure supplement 2. The ATPase activity of BmrCD-WT (wild type BmrCD), BmrCD-WT* (Cysteine-less BmrCD) and its spin-labeled mutants in PC/PA nanodiscs is stimulated by Hoechst (10 µM) and inhibited by vanadate (5 mM).
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