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RNA binding analysis indicated that the single-nucleotide change reduced the ability of 3′UAR-PPMO to block the RNA/RNA interaction required for genome cyclization.
Importantly, the results of this binding analysis indicated that maximum zipper heterodimer formation occurs with the corresponding zipper-scFv when the R-R34 and EE12RR345L zipper domains are located on the C-terminus of either the 566FF fiber or the fiber-fibritin knob deleted fibers (Table 1).
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Therefore, the binding analysis indicates that the YWHAH binding site for PIG-2 is located between residues 61 80, which constructively include in the α helix C-α helix D linker, may play an important role in this intracellular interaction.
The binding mode analysis indicated that all of these inhibitors are well accommodated in the active site and interact with the key amino acid residues of Catalytic anionic site (CAS) and peripheral anionic site (PAS).
Transcription factor binding site analysis indicated that increased HIF-1α activity, a transcription factor induced by either hypoxia or oxidative stress, is responsible for this aberrant metabolic profile in peripheral blood cells from T2DM patients.
Although one E2F1 binding site was predicted in the MMP-9 promoter, luciferase analysis indicated that this binding site was not functionally required.
Sequence analysis indicated that binding sites of miRNA and tasiRNA sequences are highly conserved in N. attenuata and A. thaliana.
This analysis indicated that binding affinity of compound 33RE to C- and N-domains, and therefore N-selectivity, is in the same range as that of the parent molecule.
GO analysis indicated that histone binding-related and RNA binding-related genes were significantly associated with ac-Htz1 when chz1 was deleted.
X-Ray photoelectron spectroscopy (XPS) analysis indicated that the binding energies of C 1s and N 1s are 286.43 and 399.08 eV, respectively.
However, Two-Hybrid analysis indicated that this binding was not direct (data not shown), suggesting the participation of intermediates in this interaction.
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