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It is well known that the covalent modifications in the N-terminal tails of histones represent a key mechanism of transcriptional control in all eukaryotic cells, and that the functional link between chromatin structure and transcriptional activation is determined by the histone "code".
A synthetic view of the biological role of histone modifications is provided by the histone code hypothesis [ 1].
Histone modifications have been hypothesized to mark chromatin as active or inactive for gene transcription by affecting chromatin accessibility, as described by the "histone code hypothesis" (29, 30).
Our work previously demonstrated the enrichment of a wide range of histone PTMs across discrete developmental stages in living frog embryos and in adult cultured cells, demonstrating the remarkable discrimination of cell type by the histone code.
Either way, association of DNAm changes with the histone code confirms that both mechanisms interact and may even be dependent on each other: either the DNAm pattern affects activity of histone modifiers or changes in heterochromatin evoked by the histone code impact on DNAm.
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Estrogen induces transient cyclical DNA methylation of active promoters that leads to transcription inhibition by changing the histone code [ 51, 52].
In addition, we show that KRAB suppressed gene expression by altering the histone code, but not DNA methylation in the gene promoter.
Reconstitution of recombinant nucleosomes bearing mutations in these lysine residues revealed the cascade of gene activation via a point-by-point interpretation of the histone code through the ordered recruitment of bromodomain-containing transcription complexes.
3, 4 All the modifications incurred by histones form the "histone code".
These results suggest that differential PARylation of histone proteins by ARTD1 can indirectly influence histone methylation and thus the histone code by determining which target proteins are modified.
CbfA is a multidomain protein that belongs to the large family of "jumonji-type transcription regulators", which contribute to the deciphering of the histone code by removing methyl groups from methyllysine or methylarginine residues in histone tails [10], [11].
More suggestions(16)
by the histone evidence
by the histone acetylase
by the dress code
by the histone methylation
by the histone methyl
by the histone demethylase
by the design code
by the histone deactylase
by the histone variant
by the histone mRNA
by the histone octamer
by the histone modification
by the histone chaperone
by the histone acetyltransferase
by the histone acetylation
by the histone mark
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