Sentence examples for modification and tyrosine from inspiring English sources

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

We speculate that O-GlcNAc modification and tyrosine phosphorylation of PHB play an important role in tyrosine kinase signaling pathways including insulin, growth factors and immune receptors signaling.

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.

Using biotinylated peptides spanning potential O-GlcNAc modification and tyrosine phosphorylation sites we showed that they indeed affect each other (Fig. 2B).

In addition, we provide data which suggests that O-GlcNAc modification and tyrosine phosphorylation in a protein interact with 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.

Substitution of Ser121 and Thr258 with alanine and isoleucine respectively resulted in attenuation of O-GlcNAc modification and increased tyrosine phosphorylation of PHB suggesting an association between these two dynamic modifications.

Apart from phosphorylation, PHB is also regulated by several other post-transcriptional modifications, such as O-GlcNAc modifications, palmitoylation, transamidation, and tyrosine nitrosylation [ 114].

Britton et al. present their findings on a novel class of histone posttranslational modifications: serine, threonine and tyrosine O-acetylation.

The search parameters include a static cysteine modification of 57.02146 amu and differential modification on serine, threonine and tyrosine residues of 79.9663 amu.

The FP-biotin modification on serine, threonine, and tyrosine was introduced according to the instructions found on the Web site http://www.unimod.org.org