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These results imply that Jvl microtubule binding activity is repressed by its N-terminal region, and that binding Spn-F could relieve this inhibition.
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Taken collectively, HNF4α and HNF1α expression and DNA-binding activity was repressed after cyclosporine treatment as was transcription of genes in the glucose and insulin signaling pathways targeted by HNF4α and HNF1α.
Previous studies have established the Cyclin A promoter to contain E2F-binding site and the promoter activity is repressed by the RB-E2F complex [24].
According to current understanding, under basal conditions, Nrf2 transactivational activity is repressed by binding to Kelch-like erythroid cell-derived protein with CNC homology-associated protein 1 (Keap1).
The absence of changes in torsinA protein expression upon up- or down-regulation of Thap1 in our system was unexpected, given the evidence demonstrating that the Tor1A promoter contains Thap1 binding sites and that Tor1A promoter activity is repressed by Thap1 [ 15, 17].
In the resting state, phosphopeptide binding is inhibited by interaction with the kinase domain and the kinase activity is repressed by the association of the PBD[42].
This Ppc and Mez pathways can effectively bypass the Pyk reaction, where its activity is repressed under light condition [77].
Previously, we showed that β-catenin transcriptional activity is repressed by nuclear-targeted PTK6 [23].
Its activity is repressed by ligand-bound PPARs [ 37, 38].
When the 3′ UTR region of Mlck/ Telokin containing the predicted miR-1 binding site was cloned downstream of a luciferase reporter, luciferase activity was repressed in the presence of a miR-1 mimic.
Catalase activity was repressed by 65%to82%2% in bCu and CuCl2 treatments.
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