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Due to the acid lability of N-phosphorylated histidine, direct detection of this posttranslational modification in proteins is still a challenge.
This would imply that there must be fundamental differences in the way O-GlcNAc modification in proteins is regulated in relation to phosphorylation.
Although proteomic methods[ 8] are increasingly able to identify this modification in proteins, no general function for it has been identified.
The mode of molecular evolution presented here may be relevant to various cases of adaptive modification in proteins, such as hydrophobic properties, molecular size, and electric charge.
However, relative development in this field has remained sluggish for almost two decades, mainly due to the lack of tools and techniques for the identification and quantification of O-GlcNAc modification in proteins.
Moreover, SNPs potentially can have stronger effects than one might imagine by hitting a splice site or a site of post-translational modification in proteins; e.g. a splice SNP could result in removal of an entire exon.
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We also assessed the purinergic receptor P2Y2 used as a negative control for the specificity of modification in protein distribution induced by PHE.
This allows to better investigate cellular processes including their modification in protein design and synthetic biology.
As O-GlcNAc modification in protein occurs at serine/threonine residues, the potential for interplay between serine/threonine phosphorylation and O-GlcNAc modification has been realized very early on [ 4].
Quantitative assessment of post-translational modifications in proteins by mass spectrometry often requires the consideration of the alteration in ionization efficiency of peptides induced by the modification.
MGO is known to induce aggregation and structural modifications in proteins through cross-linking and formation of chemical adducts [7], [8].
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