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Adr1 promoter-binding may be stabilized by interactions with coactivators [32], and post-translational modification may regulate this interaction.
Therefore, the modification may regulate the apoptotic activity in our model.
This suggested that epigenetic modification may regulate BnFLC.A10 expression by changing the Monkey King DNA methylation status.
These results support the idea that histone modification may regulate the associated enhancer activities in scale- and feather-forming skin [ 55].
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Epigenetic modifications, such as hypermethylation of promoter regions or histone modifications may regulate the expression of MHC class I and II, and APM molecules in human pluripotent stem cells.
Our data supports the hypotheses that histone modifications may regulate chromatin accessibility and Pol II movement during transcription and co-transcriptional splicing, and may also "prime" exon-intron structures prior to transcription.
Because nvp63 itself is transcribed from a strong constitutively active expression plasmid, it is likely that post-translational modifications may regulate its activity by inactivation of the putative C-terminal TID.
Furthermore, post-translational modifications may regulate kinetochore formation.
These results suggest that the absence (in the case of pan-H4ac) or presence (in the case of H3K36me2) of these histone modifications may regulate the recruitment of Hmt1 as opposed to Hmt1 regulating their levels in ORF gene bodies.
These data support the idea that post translational modification events may regulate the stability of NICD that could then directly affect the pace of the segmentation clock.
Results from our directed ChIP experiments, however, suggests that these histone modification marks may regulate the recruitment of Hmt1 to ORF-containing gene bodies instead, at least for pan-H4 acetylation and the majority of H4K36me2 tested.
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