@article{oai:repo.qst.go.jp:00075663,
 author = {三浦, 太一 and 西原, 祥子 and Miura, Taichi},
 issue = {180},
 journal = {Trends in Glycoscience and Glycotechnology},
 month = {May},
 note = {O-linked N-acetylglucosaminylation (O-GlcNAcylation) is a glycosylation characterized by the attachment of a single N-acetylglucosamine (GlcNAc) to the serine/threonine residues of nuclear, mitochondrial, and cytoplasmic proteins. Proteins modified by O-GlcNAc include signaling components, transcription factors, epigenetic regulators, and histones. O-GlcNAc has various functions such as inhibition of phosphorylation, regulation of transcriptional activity, stabilization of proteins, and regulation of intracellular localization. In recent years, O-GlcNAc has been drawing attention as a key factor for regulating the undifferentiated/differentiated state in mouse/human pluripotent stem cells, and the functions of O-GlcNAc have been gradually clarified.},
 pages = {E69--E75},
 title = {The Functions of O-GlcNAc in Pluripotent Stem Cells},
 volume = {31},
 year = {2019}
}