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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.
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Lastly, the interplay between O-GlcNAc modification and phosphorylation may not be limited to serine/threonine phosphorylation, but may also include tyrosine phosphorylation.
In other words, the interplay between O-GlcNAc modification and phosphorylation is not limited to serine/threonine phosphorylation but also includes tyrosine phosphorylation.
Enzyme specificity was set to trypsin with one missed cleavage using carbamidomethylcysteine as fixed modification and phosphorylation of S/T/Y as variable modification.
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.
SCG10 activity is known to be controlled by two post-translational modifications: palmitoylation and phosphorylation [20].
Oxidative modifications, nitration, and phosphorylation of proteins were also suggested to be involved in the aggregation of pathogenic proteins [ 1].
The majority of differentially abundant proteins were those regulated by PTMs (post-translational modifications, acetylation and phosphorylation) or with specific subcellular localization (cytosolic and mitochondrial) (Table 2).
This leads to a model whereby Pkc1 promotes the coordinate modification of these two chromatin modifications and H3T45 phosphorylation is functionally coupled to H3K56 acetylation.
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.
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