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Methylation of adenosine on the N6 position (m6A) was first observed 40 years ago (4) and was recognized early as the most prevalent internal modification in eukaryotic mRNA.
The addition of glycosylphosphatidylinositol (GPI) anchors to proteins is an important posttranslational modification in eukaryotic cells.
Protein phosphorylation is the most widespread post-translational modification in eukaryotic cells [ 1].
Glycosylation is an important post-translational modification in eukaryotic and bacterial cells.
Glycosylation of proteins is the most common post-translational modification in eukaryotic cells: It has been estimated that up to 50% of human proteins are glycosylated.
Glycosylation is the attachment of a carbohydrate residue to a protein [ 23], and it is the most frequent post-translational modification in eukaryotic species [ 24].
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Glycosylation, the attachment of sugar moieties to proteins, is one of the important post-translational modifications in eukaryotic protein biosynthesis (Varki et al. 1995).
PPIs are often controlled by posttranslational modifications, with the most common modifications in eukaryotic proteomes being phosphorylation of Ser/Thr/Tyr residues [ 63].
Serine phosphorylation is among the most abundant posttranslational modifications in eukaryotic cells, and phosphorylated protein networks form the basis for regulating most physiological processes.
In this Review, we will discuss the properties and limitations of different designer endonuclease platforms for the developmental biologist, each of which can be adapted to introduce molecularly distinct site-specific modifications in eukaryotic genomes.
Pichia pastoris is a better host for larger scale recombinant protein production in biopharmaceutical industry than Escherichia coli as many human proteins are subject to specific posttranslational modifications in eukaryotic cells.
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