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The growth repression recorded was rapid, being observed within 24 h after initiating drug exposure, and continuing in the presence of drug for up to 120 h.
It was concluded that the expulsion of water, Na+, and Cl− continuing in the presence of ouabain is driven by an energy-providing mechanism other than the Na+/K+-ATPase, clearly associated with the presence of round electron-clear vesicles.
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No apparent morphological changes were observed and cardiomyocyte beating continued in the presence of BI 2536.
Therefore the dnaC2 cells maintained at non-permissive temperature had been arrested at a late stage of initiation process where DnaA protein synthesis was no longer required, i.e., initiation had taken place, and replication could continue in the presence of rifampicin when DnaC was re-activated at permissive temperature.
Hence, signaling from the receptor form of HER2 continued in the presence of HER2 antibodies, indicating that HER2 ECD promoted resistance to HER2-targeted antibody therapy.
Deprotonation of the diphosphate-containing unit results in C1 C2 π bond formation, allowing chain elongation to continue in the presence of appropriate enzymes.
The authors say that the steroids may not have had much influence, so it is difficult to judge why they were continued in the presence of previous progression.
DA alone was applied for 40 minutes, and then, DA administration was continued in the presence of either EtOH or water for an additional 40 minutes.
After the first 24 h of transfection, cells were treated by addition of the required reagents, and incubation continued in the presence of both siRNA and treatment for the next 72 h.
Finally, sense RNA was transcribed in vitro using T7 RNA polymerase; reinitiation and elongation continued in the presence of limiting amounts of ribonucleotides to produce linear amplification of mRNA.
In contrast, sterol-induced binding of UBIAD1 to reductase continued in the presence of 20 µM farnesol, a 15-carbon nonsterol isoprenoid that does not augment sterol-accelerated ERAD of reductase (Sever et al., 2003a).
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