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Citrated platelet rich plasma was incubated with the NO-donor SIN-1 (10 μM), an active metabolite of molsidomine, prior to activation with 10 μM adenosine-diphosphate (ADP) or 0.05 U/ml human α-thrombin (both ED50), or with agonists or buffer only.
Spectroscopy was then used to compare how holoenzyme structure and function changes in response to activation with CaM in the dimeric mutant, WT-holoenzyme, and a monomeric CaMKII oligomerization-domain deletion mutant control.
This shift is hypothesized to be due to the introduction of two bulkier residues, suggesting that the addition of these bulkier residues introduces molecular interactions between the ligand and receptor, leading to activation with cholecalciferol.
Following EdC activation with lactose/urea or lactose/ammonia, the intracellular acidification rate was increased compared to activation with lactose alone (Figure 1E).
B cell treatment with IFN-α prior to activation with SAC triggered higher mRNA expression and IFN-γ production (Fig. 2D, 2E).
Therefore, we pre-treated monocytes with I3MO (5 µM) prior to activation with A23187 and AA.
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Hence, we investigated the clinical relevance of common genetic polymorphisms in the TLR-mediated IL-12/IFN-γ loop to macrophage activation with regard to susceptibility to development of IA in ASCT recipients.
However, platelets of dogs with infection failed to respond to platelet activation with PAR 4 agonist.
In contrast, hormone-sensing cells require Wip1 to respond to HER2/neu activation with either ERK or STAT5 activation, highlighting the importance of cell context in signal transduction.
It also shows that persons respond differently to PPARα activation with respect to their gene expression changes, indicating a possible person-specific nutrient response.
hCG stimulation led to ERK1/2 activation with a similar profile to that induced by 8Br-cAMP (Fig. 2, lower panels of A, B, and C).
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