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Most small molecular inhibitors are designed to block kinase activity via binding to the ATP pocket of the enzyme.
For this reason, most small molecular antitumor agents have a large volume of distribution after intravenous administration.
Most small molecular inhibitors are not specifically acting on different proteases and are not always effective [ 39, 48, 49].
This is not surprising, given the large and often shallow interaction areas of PPIs and the fact that most small molecular drugs target well-defined cavities of enzymes or receptors.
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Especially, compound 23 (IC50 = 104 nM) was the most potent small molecular, and about 3-times more potent than WDR5-47.
Moreover, most of the small molecular weight proteins in the range of 15-50 kDa, have significantly (p < 0.05) higher spot volume and intensity in ethanol supernatant rather than precipitate (Table 2 and Figures. 2A and 2A).
Since most of hormones are small molecular compounds which are called haptens (molecular weight less than 1000), they will not be able to stimulate the animals to produce specific antibodies directly.
The separation of acetone and ethanol binary mixture derived from the fermentation broth using pervaporation membranes is very challenging, most likely due to their small molecular size differences.
Low to moderate rejection values were most likely due to the small molecular sizes of the PhACs (i.e., MW << MWCO) and the divalent ions present in the raw water.
As such, there has been an intriguing interest in discovering and developing novel multi-targeted PTK inhibitors, and most of them focused on small molecular entities.
Most of TK inhibitors (TKIs) are small molecular and hydrophobic compounds, thus they can rapidly reach their specific intracellular targets and inhibit the activation of the related TKs.
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