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Last Updated: 4 months ago

Possible Interaction: Acetylglucosamine and Serine



Research Papers that Mention the Interaction

The addition of O-linked N-acetylglucosamine (O-GlcNAc) on serine or threonine modifies a myriad of proteins and regulates their function, stability and localization.
Biochemical and biophysical research communications  •  2015  |  View Paper
Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions.
Proceedings of the National Academy of Sciences of the United States of America  •  2010  |  View Paper
O-linked attachment of GlcNAc to Ser and Thr residues regulates a variety of intracellular proteins, including transcription factors such as NFκB, c-myc and p53.
Scientifica  •  2012  |  View Paper
A very specific type of glycosylation, the addition of GlcNAc to serine or threonine (O-GlcNAc), is not only regulated by epigenetic mechanisms, but is an epigenetic modifier of histones and transcription factors.
International journal of molecular sciences  •  2017  |  View Paper
Elevating O-GlcNAc levels increased phosphorylation of Synapsin I/II at serine 9 (cAMP-dependent protein kinase substrate site), serine 62/67 (Erk 1/2 (MAPK 1/2) substrate site), and serine 603 (calmodulin kinase II site).
The Journal of biological chemistry  •  2009  |  View Paper
Intracellular attachment of O-linked N-acetylglucosamine to serine and threonine residues hinders phosphorylation, thereby regulating the activity of the proteins concerned.
Journal of neuroscience research  •  2008  |  View Paper
In addition to O-phosphorylation, O-linked modifications of serine and threonine by beta-N-acetyl-D-glucosamine (GlcNAc) may regulate muscle contractile function.
Circulation research  •  2008  |  View Paper