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Ablation of the terminal loop of pre-let-7a-1 also reduced the binding frequency, indicating that TUT7 recognizes both the overhang and the terminal loop.
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Among all functional categories, targets involved in nuclear components occupied the highest frequency, followed by targets participating in DNA-dependent transcription, DNA-dependent regulation of transcription, and DNA binding, respectively, indicating that most targets were transcription factors.
R111A mutant almost completely loses the c-di-GMP binding affinity, indicating that R111 is the most important residue for c-di-GMP binding.
Furthermore, our results show that the binding is reversible, indicating that LA is an exchangeable ligand.
Molecular docking studies and competitive binding assay indicated that 5m effectively bind at the colchicine binding site of the tubulin.
Competitive binding experiments indicate that these three compounds bind significantly stronger to warfarin compared to diazepam binding site.
A single binding site was observed in the BSA rivaroxaban complex and the binding constants indicated that their binding is quite strong to be highly bound in plasma.
In addition, the methylation of H3K9 does not notably inhibit this binding, which indicates that H3K9 does not participate in the binding.
The in vitro binding assay indicated that several compounds are potent selective V2 receptor antagonists.
The frequency spectra indicated that the pO2 fluctuated at very low frequencies, that is, at frequencies lower than 1.5 2.0 mHz, corresponding to less than 0.1 cycle min−1.
However, MrkH116-end loses the c-di-GMP binding affinity, which indicates that the connecting loop between two β-barrels is crucial for c-di-GMP binding.
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