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Upon either deletion or mutation of the BP1 binding site, we observed an approximately 40%to50%0% decrease in bcl-2 promoter activity.
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Due to the nature of these families, their size is significantly larger than of those of the simple protein target families representing one binding site; we observe this to be a big influence on the results.
This region of the ribosome is known to play a role in the initiation of translation, and thus, the binding site we observe is consistent with evidence suggesting that thermorubin inhibits the initiation stage of protein synthesis.
However, it is interesting to mention that when computing the ratio between the total number of predictions along different conservation levels and the number of successfully identified ChIP-seq binding sites, we observed better predictive values for higher sequence conservation (see Additional file 8, bottom).
The enrichment of NF-Y binding sites we observed in the promoters of genes encoding proteins that peak in the G2&M fraction is consistent with previous reports linking NF-Y transcriptional activity to G2&M phase cell cycle functions (Hu et al., 2006).
Further studies are required to determine if the binding site specificity we observed is an intrinsic property of HLH-1 or reflects additional constraints, including required cooperativity with other factors or the limited accessibility to potential binding sites in the context of general or tissue-specific chromatin organization.
This extensive analysis revealed that the majority of PPARγ binding sites we mapped overlap with those previously reported although some differences in specific binding sites were observed, likely due to inherent differences between 3T3-L1 and C3H10T1/2 cells.
Moreover, the acetylcholinesterase (AChE) enzyme binding site was observed in the NRPS gene.
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.
Interestingly, several of the 2007 and 2009 isolates also exhibited reduced sensitivity to zanamivir, and accompanying HA mutations near the sialic acid binding site were observed.
Furthermore, no formation of hydrogen bonds between the ligand and protein binding site is observed.
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