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Discover Supplement-Drug Interactions

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Possible Interaction: Serine and Threonine





Research Papers that Mention the Interaction

The efficiency of μ‐opioid receptor signalling is tightly regulated and ultimately limited by the coordinated phosphorylation of intracellular serine and threonine residues.
British journal of pharmacology  •  2015  |  View Paper
Similarly, the hydroxyl group in the side chains of serine and threonine can also be used to covalently couple drugs for delivery into cells via ATB(0,+).
Current drug targets. Immune, endocrine and metabolic disorders  •  2005  |  View Paper
Strikingly, phosphorylation of threonine 18 is dependent upon prior phosphorylation of serine 15.
FEBS letters  •  1999  |  View Paper
Although the relative abundance of tyrosine phosphorylation as a percentage of total labeling was variable due to concomitant enhancement of serine and threonine phosphorylation, exogenous peptide substrate assays confirmed the increased tyrosine kinase activity quantitatively.
Journal of immunology  •  1985  |  View Paper
In some cases, phosphorylation of the cotransporter itself on serine and threonine (but not tyrosine) is associated with changes in transport rate, in others, phosphorylation of associated proteins has more influence.
Biochimica et biophysica acta  •  2002  |  View Paper
Thermal hysteresis data showed that substitution of Thr by Ser resulted in moderate to complete loss of antifreeze activity, depending on the number and position of the substituted Thr residue(s).
The Journal of Biological Chemistry  •  1998  |  View Paper
Whole-body glycine, proline, serine and cystine concentrations decreased (P < 0.05) as Thr was increased in the diet.
The British journal of nutrition  •  1997  |  View Paper
Substitution of threonine by serine , an amino acid that also carries a hydroxyl group, even improves cGMP sensitivity of the wild-type channels 2- to 5-fold.
Proceedings of the National Academy of Sciences of the United States of America  •  1991  |  View Paper
Expression of the mutagenized cDNA in COS-1 cells demonstrated that substitution of serine 194 with threonine or alanine abolished enzyme activity in hydrolyzing the water-soluble substrate, p-nitrophenyl butyrate, and the lipid substrates cholesteryl [14C]oleate and [14C] lysophosphatidylcholine.
The Journal of biological chemistry  •  1990  |  View Paper
These data suggest that the phosphorylation of threonine 18 in addition to serine 19 change the conformation of myosin and HMM and this is associated with altered biological properties.
The Journal of biological chemistry  •  1988  |  View Paper
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