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“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
“As an illustration, we propose blocking of phosphorylation by O‐GlcNAc modification on Ser 10 , which may result in gene silencing in the presence of methylated Lys 9.”
Journal of cellular biochemistry • 2008 | 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 & bgr;-N-acetyl-d-glucosamine (GlcNAc) may regulate muscle contractile function.”
“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.”