Sentence examples for modification and phosphorylation from inspiring English sources

Enzyme specificity was set to trypsin with one missed cleavage using carbamidomethylcysteine as fixed modification and phosphorylation of S/T/Y as variable modification.

In other words, the interplay between O-GlcNAc modification and phosphorylation is not limited to serine/threonine phosphorylation but also includes tyrosine phosphorylation.

Lastly, the interplay between O-GlcNAc modification and phosphorylation may not be limited to serine/threonine phosphorylation, but may also include tyrosine phosphorylation.

The resulting PMF mass spectra were searched against the E2F1 protein sequence with carbamidomethylation of cysteine as a fixed modification and phosphorylation of serine residues as variable modification.

Taken together, these evidences would suggest that the interaction between O-GlcNAc modification and phosphorylation is not limited to serine/threonine phosphorylation (as initially thought) though rather also includes tyrosine phosphorylation.

Although shown to bind Ca2+ directly [47], the F1 FO ATP synthase is likely to be regulated via post-translational modifications and phosphorylation of the γ-subunit was sensitive to mitochondrial Ca2+ [48] with a K0.5 in the μM range.

We hypothesize that phosphorylation may be a requisite for O-GlcNAc modification and tyrosine phosphorylation plays a role in the interplay between O-GlcNAc modification and serine/threonine phosphorylation in proteins.

Such a high prevalence of O-GlcNAc modification and tyrosine phosphorylation together strongly support our hypothesis of a dynamic relationship between tyrosine phosphorylation and O-GlcNAc modification and a potential role of tyrosine phosphorylation in the interaction between O-GlcNAc modification and serine/threonine phosphorylation which warrants further investigation.

It is possible that O-GlcNAc modification and tyrosine phosphorylation in PHB2 interact in the same way as in PHB.

Because PHB undergoes both O-GlcNAc modification and tyrosine phosphorylation, we asked the question whether these modifications occur in neighboring residues and affect each other.

Because PHB (as well as few other insulin signaling intermediates such as IRS, Akt, GLUT4 etc) undergoes both O-GlcNAc modification and tyrosine phosphorylation and these modification sites are either adjacent or in the close proximity to each other we hypothesize that O-GlcNAc modification and tyrosine phosphorylation may be a previously unidentified novel binary switch.