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The scanning activity of the ribosome may impair the interaction of the miRNA-RISC with the 5' UTR, suggesting there would be inefficient inhibition of gene expression.
Mutations at the E-cadherin extracellular domain may impair the interaction of E-cadherin and EGFR, lead to activation of EGFR, and further enhance cell motility through activation of RhoA [ 34].
In these cells, inactivation of the nuclear pool of Rac1 may impair the interaction of Rac1 with nuclear proteins such as TCF4 and beta-catenin, resulting in a reduction in the expression of proliferation-related genes and therefore the reduction in cell proliferation.
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As expected (Sauter et al., 2012), mutation of the serine phosphorylation sites impaired the interaction of Vpu with β-TrCP.
Similarly, presaturation of HSP70 with PET-16 also impairs the interaction of this protein with PES (data not shown).
Phosphorylation of Ser impairs the interaction of eEF2K with CaM [ 33], whereas phosphorylation of Ser impairs its activation by Ca2+ ions [ 15].
Moreover, the same authors demonstrated that the T allele significantly impairs the interaction of miR-1827 withethe 3′UTR of MYCL1, reducing miR-1827 dependent inhibition of MYCL1 expression.
The R620W polymorphism is located in the critical PRS1 domain of Pep, and impairs the interaction of Pep with Csk [ 50, 55].
Co-immunoprecipitation of HDAC6 with RanBPM Δ360 was markedly reduced compared to RanBPM WT and Δ212, suggesting that deletion of the LisH/CTLH domain severely impairs the interaction of RanBPM with HDAC6 (Fig. 7D).
Second, VP35 is phosphorylated by κB kinase epsilon (IKK-ε) and TANK-binding kinase 1 (TBK-1), thereby impairing the interaction of these kinases with their substrates IRF-3 and IRF-7 and preventing their phosphorylation [ 37].
Importantly, abrogating the RVxF and SILK domains in the context of the rif1-7A allele (rif1-7APP1 allele) both restored the suppression of hsk1-89 and impaired the interaction of Sds21 with chromatin, indicating that the synthetic lethality conferred by these alanine substitutions requires the ability of Rif1 to interact with PP1.
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