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Similar to their regulatory role in transcription, histone modifications could regulate the access of replication factors to replication origins and therefore determine the time of origin activation.
Nonetheless, cell cycle-specific histone modifications could regulate the association of non-histone factors with chromatin.
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Thus, the complement of genes that undergo altered regulation as a consequence of physiological state and epigenetic modifications that could regulate their expression provides only a partial view of the genetic architectures that regulate physiological state-induced regulation of gene expression.
Altogether, these data might pinpoint a common post-translational modification that could regulate the activity of the entire ARID family proteins.
The post-translational modification of Srs2 could regulate the availability of specific DNA substrates that either favor homologous recombination or promote the use of alternate pathway to bypass the damage, such as template switching.
Because the thiol modifications reported here occur on known phosphorylation sites, these age-related modifications could influence the structure and function of the modified proteins, particularly protein– protein interactions and perhaps cell signaling events that are regulated by phosphorylation.
Although LBR can interact directly with histones and with other chromatin-associated proteins (reviewed in Olins et al. 2010), the regulation of HP1 binding by cell cycle-dependent modifications of histone H3 could regulate the post-mitotic association of the INM protein with chromatin.
In our present study, we show that NDRG2 could regulate GLUT1 posttranslational modification without affecting other glucose transporters, including GLUT2, GLUT3 and GLUT4.
In the 'MiRNA Regulates Epigenetic Modification' section, users can separately or synergistically select interested miRNA and epigenetic modifications to find out which epigenetic modifications could be regulated by the miRNA or which miRNAs could affect the epigenetics.
Alternatively, it has been reported that HSP90 could regulate IKK receptiveness to post-translational modification or even the activity of enzymes that carry out such modifications [ 31].
Since TFE3 post-translational modifications were affected by FLCN, we examined whether FLCN expression could regulate TFE3 subcellular localization after cellular fractionation to yield cytoplasmic, soluble and insoluble nuclear fractions.
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