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A complete list of binding partners is shown in Figure 5A and the number of peptides detected in each biological sample is shown in Additional file 9: Table S4.
In Figure 3 a number of S. cerevisiae ion transporters and their binding partners is shown and the effect of potassium starvation on their transcript levels is indicated in a color scale, with down-regulation in green and up-regulation in red.
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The interaction between Plk1 and its binding partners was shown to be phosphorylation-dependent which often requires priming by Cyclin-dependent kinases [50], [51].
It is important to note that many of the binding partners were shown to exist as homodimers therefore DYNLL most likely forms dimer-dimer complexes with its partners [24], [30], [35].
This was particularly relevant as it has been suggested that CDK4 and CDK6 may phosphorylate as yet unidentified substrates (Ruas et al., 2007), and we have now shown that these binding partners are critical for p16INK4a-induced senescence.
As shown in Additional file 3, expression of BRCA1/2 binding partners was deregulated [ 33, 34].
The Eps15 binding partner intersectin was shown to activate the Elk-1 transcription factor [ 21].
All isoforms regulate complement in an equivalent manner, and no binding partner has been shown to modulate C4bp complement regulatory activity.
Compared to the absence of a binding partner, it was shown that the existence of a complex which is broken down within the tissue, releasing free IGF, may lead to a substantial increase in the free IGF concentration within the tissue, even to concentrations well above those at the tissue boundary.
Another typical case is that binding partners are phosphorylated on binding sites and bind other effectors.
It is clear that the RNA levels of some binding partners are increased and of some binding partners decreased.
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