Sentence examples for modifications of serine from inspiring English sources

Phosphorylation and OGlcNAcylation are the major reversible intracellular post-translational modifications of serine and threonine residues.

OGlcNAcylation and phosphorylation are the major competing intracellular post-translational modifications of serine and threonine residues.

Mucin-type O-glycan biosynthesis is associated with modifications of serine or threonine residues of certain proteins.

Phosphorylation and OGlcNAcylation are the major intracellular post-translational modifications of serine and threonine, occurring via regulated enzymatic responses to a multitude of intracellular and extracellular signals and resulting in diverse downstream intracellular responses.

The results herein, in combination with our previous results on the effects of phosphorylation and OGlcNAcylation in disordered regions of proteins, should provide a broad context for interpreting structural and potentially functional effects of post-translational modifications of serine and threonine in intracellular proteins.

Modification of serine and threonine residues in proteins by O-linked β-N-acetylgulcosamine (O-GlcNAc) glycosylation is a feature of many cellular responses to the nutritional state and to stress.

The first example of covalent modification of serine by pentavalent arsenic was observed with X-ray crystallography.

This may be altered in type 2 diabetes mellitus (T2DM), where autophagy is diminished, and where PGC1alpha is also downregulated through modification of serine residues by N-acetyl-glucosamine (O-GlcNAc) [ 23].

While these clickable galactose analogues were originally introduced to detect the presence of GlcNAc as a post-translational modification of serine and threonine residues, Qasba's group showed that the technology could also be used in conjunction with nonreducing GlcNAc residues for site-specific conjugations to antibodies.

In contrast, in humans, OGlcNAcylation (β- O-GlcNAc modification of serine or threonine, via addition of β- d- N-acetylglucosamine) is controlled by only one OGlcNAc transferase (OGT), with three isoforms in humans, which adds OGlcNAc, and only one OGlcNAcase (OGA), which removes OGlcNAc.

O-linked β- N-Acetylglucosamine (O-GlcNAc), the monosaccharide modification of serines and threonines in nuclear and cytosolic proteins, was first reported more than 30 years ago (Torres and Hart 1984).