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Further analysis of the YopJ binding site revealed that the face of the G α-helix that binds YopJ opposes the APE loop in the kinase domain (Figure 6D).
Moreover, the results of a docking study of compound 5n into the COX-2 binding site revealed that its mechanism was possibly similar to that of naproxen, a COX-2 inhibitor.
Using the available X-ray crystal structure of APE1 complexed with substrate DNA (PDB code: 1DE9), docking of 6-hydroxy-DL-DOPA into the APE1 binding site revealed that the sugar phosphate pocket can easily accommodate the aromatic moiety of the compound (Figure 9).
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Pharmacological treatment of the hemoglobin oxygen binding site reveals that hemoglobin-induced cellular injury is more prominent in red blood cells that are partially hydrated (about 5.5 to 3.5 g H2O/g dry wt) than in cells that are relatively dry (≤ 2 g H2O/g dry weight).
Further analysis of this binding site reveals that the YopJ binding site is conserved in other MKKs.
Analysis of the locations of the HSF binding sites revealed that 57% were contained within genes with approximately 2/3rds of these sites being in introns.
Closer inspection of these binding sites revealed that 3420 83.7%%) of the non-CTCF bound binding sites contained the CTCF motif, indicating that they are either not bound by CTCF in ESCs, even though the binding motif is present or that these sites were not detected during ChIP-sequencing.
A search for putative binding sites revealed that the CDH1 163+37235 position lies within a recognition motif of the human nuclear factor I/X (NFIX, OMIM #164005).
Analysis of the TR4 binding sites revealed that less than 30% of the peaks from any of the cell types contained the DR1 motif previously derived from in vitro studies, suggesting that TR4 may be recruited to the genome via interaction with other proteins.
Calculating the statistical significance of the estimated number of binding sites revealed that in mouse for all three genes the promoter regions were enriched for motifs associated with transcription factor NFY, as well as Sp1 (Table 3).> -wrap-foot> *Denotesignificantnt values.
A close inspection of the area of the peptide-binding site reveals that it is next to a cavity formed by the 3 neighboring molecules (Figure 4D).
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Since I tried Ludwig back in 2017, I have been constantly using it in both editing and translation. Ever since, I suggest it to my translators at ProSciEditing.

Justyna Jupowicz-Kozak
CEO of Professional Science Editing for Scientists @ prosciediting.com