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For the IKKα-controlled pathway, phosphorylation of p65 at ser536 may control DNA binding activity or release from IκB.
Studies in fungi and plant, and, to a lesser degree, in mammals indicate that methyl-H3K9 may control DNA methylation in heterochromatin [ 6- 8].
The enhancer of zeste homolog 2 (EZH2) gene encodes a polycomb group (PcG) protein which acts as a histone methyltransferase [ 3, 4] and also may control DNA methylation [ 5].
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Based on this knowledge, in addition to our current findings, it is intriguing to speculate that nuclear bFGF may control DNA-PKCS expression/activity in a manner dependent on a nuclear bFGF receptor, a topic of current investigation.
Li et al (2015) hypothesised that PRMT5 may control the DNA damage response through alternative RNA splicing in PGCs by the methylation of Sm spliceosomal proteins.
These data suggest that mutations in other components of the p53 pathway, or in separate pathways that control DNA damage checkpoints, may create a permissive environment for chromosomal rearrangements.
Interestingly, Bandyopadhyay et al (1998) have shown that EGFR-mediated signalling may control the activity of DNA-PK, an enzyme directly involved in DNA damage repair; more precisely, from their work, high EGFR expression could maintain a high level of signalling, which would be associated with high basal levels of DNA repair capacity.
In prokaryotes, factors that package DNA, such as HU proteins, may control supercoiling by binding to DNA and trapping the free energy of supercoiling as writhe and subsequently releasing it through controlled dissociation [ 3,4].
These results suggest that DNA methylation may control the phenotypic changes observed in cancer cells.
This implies that a post-transcriptional method of regulation may control the transition from the DNA synthesis and growth phenotype of 24hr liver stage parasites to the cytokinesis and merozoite formation phenotype of 48hr liver stage parasites.
Taken together with repair propensities, our data suggest that the bending kinetics of MutS mismatched DNA complexes may control the entry into functional pathways for downstream signaling of repair.
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