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您的检索式：作者名="David S.Rubenstein"
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| 1 | The role of intracellular protein O-glycosylation in cell adhesion and disease显示文摘Post-translational protein modification,including phosphorylation,is generally quick and reversible,facilitating rapid biologic adjustments to altered cellular physiologic demands.In addition to protein phosphorylation,other post-translational modifications have been identified.Intracellular protein O-glycosylation,the addition of the simple sugar O-linked N-acetylglucosamine (O-GlcNAc) to serine/threonine residues,is a relatively recently identified post-translational modification that has added to the complexity by which protein function is regulated.Two intracellular enzymes,O-GlcNAc transferase and O-GlcNAcase,catalyze the addition and removal,respectively,of O-GlcNAc to serine and threonine side-chain hydroxyl groups.Numerous proteins,including enzymes,transcription factors,receptors and structural proteins have been shown to be modified by intracellular O-glycosylation.In this review,the mechanism and relevance of O-GlcNAc protein modification are discussed in the context of cell adhesion and several representative diseases. | Meryem Bektas David S.Rubenstein | 2011 | The Journal of Biomedical Research2011，25，4： | 2 |
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