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The Myc/Max heterodimer is a co-activator that recruits multiple histone acetyl transferase to maintain euchromatin status, whereas the Mad/Max a co-repressor that recruits histone deacetylase (HDAC) to repress transcription.
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For example gene activation can be associated with histone acetylation by histone acetyl transferase (HAT) [ 56], whereas histone deacetylation by histone deacetylase (HDAC) can suppress gene expression.
Histone acetylation is mediated by histone acetyl transferases (e.g., p300, CBP, and p/CAF in mammalian cells), while acetyl groups are removed by histone deacetylases [ 9].
For example, ethanol affects the activity of enzymes called histone acetyl transferases (HATs) that mediate histone acetylation.
9 In this sense, they work against histone acetyl transferases (HATs) that acetylate histones and activate gene expression.
c-ETS2 binding was facilitated by an active chromatin distinguished by acetylated histone H3 orchestrated by histone acetyl transferase GCN5 and followed by HBO1 mediated histone H4 acetylation.
Histone deacetylases (HDACs) and histone acetyl transferases catalyze the reversible acetylation of histones and nonhistone substrates to control the epigenetic and transcriptomic landscape of normal and tumor cells.
Histone deacetylases (HDACs) and histone acetyl transferases (HATs) determine the pattern of histone acetylation, and thus are involved in the regulation of gene expression.
HDACs and histone acetyl transferases play crucial roles in regulating histone acetylation to regulate gene transcription [9] [13].
Two histone acetyl transferases (HATs), Gcn5 and p300, responsible for the acetylation of multiple lysine residues within all four core histones, are implicated in the UV-induced DDR.
Histone acetylation and then gene transcription is controlled by histone acetyl transferases and histone deacetylases (HDACs) bringing and removing acetyl groups.
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