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Epigenetic modifications can either activate on inactivate genes and are tightly modulated by metabolic inputs [ 38– 45].
These modifications can either be associated with activation or repression of corresponding genes in different cell types [ 22].
In addition, the introduction of arginine modifications can either create or compromise a substrate recognition site for other histone-modifying enzymes even spanning different histone tails.
Different kinds of histone modifications can either activate or inactivate the nearby genes, and can also be passed on to new cells.
Finally, the observation that different interfacial modifications can either eliminate or enhance ultrastability suggests that native ultrastability is an evolved trait that provides an optimal, rather than the maximal, level of kinetic durability.
Accordingly, histones within chromosomes are subjected to several forms of post translational modifications such as phosphorylation, ubiquitination, methylation, and acetylation and these modifications can either create or eliminate binding sites for non-histone proteins that mediate DNA repair or modify chromatin structure [ 2].
Similar(54)
Usually, DNA methylation is associated with reduced gene expression (Bird 1984; Razin and Cedar 1991; Lim and Maher 2010) and histone modification can either enhance or repress expression, according to different modification targets (e.g., which amino acids are at the histone tail) and modification types (e.g., methylation or acetylation) (Berger 2002; Cheung and Lau 2005).
These modifications can be either activating or inactivating.
Cross talk between posttranslational modifications can be either positive or negative [ 2].
These modifications can be either added or removed to create dynamic changes in protein binding properties, thus enabling rapid cellular responses to both external and internal stimuli.
This is the case in lysine modification, which can either be acetylated or methylated on the same nitrogen atom.
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