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SET domain-containing methyltransferases seem to be particularly sensitive to the sequence and posttranslational modifications surrounding the target lysine site.
False negatives due to epitope occlusion by additional modifications surrounding the targeted residues were also frequently observed.
The molecular interactions between lysine methyltransferases and their substrates appear to be regulated by posttranslational modifications surrounding the lysine methyl acceptor.
SET domain containing methyltransferases seems to be particularly sensitive to the sequence and posttranslational modifications surrounding the target lysine site [ 32].
However, upon further characterization of these promoters, they were discovered to be expressed, and have high levels of active histone modifications surrounding the promoter (Additional file 10B, PHF8 shown).
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In the case of the PPARγ agonist cellular system, the key structural modifications surrounding ligand binding were successfully detected and the tendencies of impact were examined.
Our results imply that this method can provide novel information about transcription factor organization at enhancers and core promoters as well as about the histone modifications surrounding regulatory regions in any immune or other cell types.
Taken together, these correspondences clearly point out that the top-ranked ES symbols are the key structural modifications surrounding molecular binding.
Recently, it has been shown that genes within specific functional groups can be distinguished by the pattern of histone modifications surrounding them.
In a ligand-dependent receptor-mediated cellular system (or ligand cellular system), key structural modifications surrounding ligand binding are expected to cause outliers.
To analyze the relationship between histone modifications and gene expression, histone modification profiles surrounding the TSS and gene body were plotted for genes ranked by their expression level (Additional file 1: Figures 1B-E and S3-5).
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