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Acetylation of lysine residues is the best-characterized modification shown to affect higher-order chromatin structure, where this mark neutralizes the basic charge of the residue on which it occurs, thereby inhibiting histone-histone or histone-DNA interaction and thus chromatin compaction [9], [10], [11].
Acetylation has the most potential to unfold chromatin, because it neutralizes the basic charge of the lysine residual and loosens the interaction between histone and DNA.
Of all HPTMs, acetylation has the most potential to unfold chromatin since it neutralizes the basic charge of the lysine [ 2].
Different lysines in both histones H3 and H4 are targets for this modification, which neutralizes the basic charge of the lysine, thereby potentially altering the interaction between adjacent histones and between histones and DNA [ 41].
Histone acetylation, one of the most thoroughly studied histone modifications to date, occurs on the N-termini of the protein octamers and neutralizes the basic charge of the affected lysine.
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Massive acetylation of lysine residues may activate transcription through neutralization of the basic charge of these residues and through the recruitment of bromodomain-containing protein complexes, which may include other HATs and chromatin remodeling enzymes [ 25].
Acetylation of histone lysine residues results in the neutralisation of the basic charge of this amino acid and is believed to open up chromatin present at promoters of active genes (reviewed in Kouzarides 2007).
Histone acetylation occurs on the N-terminal tails of histones, reducing the basic charge of histones to promote an open, trancription-promoting conformation of chromatin.
This modification often occurs along with transcriptional activation via stabilising the basic charge of lysine residues and reducing their affinity for DNA and finally preventing the formation of highly condensed chromatin in some cases [ 74– 76].
Owing to the highly basic charge of histone proteins, DNA charges are neutralized, allowing a compaction up to a factor of 10 000 (Jiang and Pugh, 2009).
This region is composed of four cryptic repeats and substantially contributes to the overall basic charge of TALE proteins [ 12, 15].
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