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For each identified peptide with observed mass-to-charge m/z, charge z,O modification state s, and user-defined purity of H2O p, the abundance of the peptide from the light sample A (light) and the heavy sample A (heavy) was calculated.
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The goal was to determine the impacts of electrospun conduit composition and hyaluronan oligomer (HA-o) modification on the recruitment of peritoneal cells, and their phenotype and ability to synthesize elastic matrix.
Dynamic changes of the post-translational O-GlcNAc modification (O-GlcNAcylation) are controlled by O-linked β-N-acetylglucosamine (O-GlcNAc) transferase (OGT) and the glycoside hydrolase O-GlcNAcase (OGA) in cells.
In the absence of a protective group on the exocyclic amino group, the regioselective 5′- O-phosphorylation reaction of ddA and d4A was performed at −40 °C to enhance the O- versus N-alkylation (8 1 in favor of the 5′- O-modification, Scheme 52).
O-Methylation and probably also other O-modifications of the flavonoid OH substitutions inactivate both the antioxidant and the prooxidant activities of the flavonoids.
Taken together, these results suggest that tyrosine phosphorylation enhances O-GlcNAc modification whereas O-GlcNAc modification attenuates tyrosine phosphorylation at least in these peptides.
O Posttranslational modification, protein turnover, chaperones.
Open image in new window Figure 1 The process of O -GlcNAc modification and the molecular structure of OGT isoforms.
O-GlcNAc modification is reversibly regulated by O-linked β-N-acetylgulcosamine transferase (OGT) and β-D-N-acetylgulcosaminase (O-GlcNAcase).
O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins mediates stress response and cellular motility in animal cells.
O-GlcNAc modification of biotinylated peptide spanning potential O-GlcNAc modification sites by OGT (Fig. 2A) suggested that it could be O-GlcNAc sites in vivo too.
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