Results 201 to 210 of about 14,068 (233)
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O-GlcNAcylation is a gatekeeper of porcine myogenesis
Journal of Animal Science, 2022Abstract Although it has long been known that growth media withdrawal is a prerequisite for myoblast differentiation and fusion, the underpinning molecular mechanism remains somewhat elusive. Using isolated porcine muscle satellite cells (SCs) as the model, we show elevated O-GlcNAcylation by O-GlcNAcase (OGA) inhibition impaired SC ...
Laila T Kirkpatrick +4 more
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Molecular mechanisms of O-GlcNAcylation
Current Opinion in Structural Biology, 2008Protein glycosylation with O-linked N-acetylglucosamine (O-GlcNAc) is a reversible post-translational modification of serines/threonines on metazoan proteins and occurring with similar time scales, dynamics and stoichiometry as protein phosphorylation.
Hurtado-Guerrero, Ramon +2 more
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O-GlcNAcylation in cancer development and immunotherapy
Cancer Letters, 2023O-linked β-D-N-acetylglucosamine (O-GlcNAc), as a posttranslational modification (PTM), is a reversible reaction that attaches β-N-GlcNAc to Ser/Thr residues on specific proteins by O-GlcNAc transferase (OGT). O-GlcNAcase (OGA) removes the O-GlcNAc from O-GlcNAcylated proteins.
Xue-Fen, He +4 more
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Regulation of cancer metabolism by O-GlcNAcylation
Glycoconjugate Journal, 2013Cancer cells exhibit increased uptake of glucose and glutamine, and rewire the metabolic flux toward anabolic pathways important for cell growth and proliferation. Understanding how this altered metabolism is regulated has recently emerged as an intense research focus in cancer biology.
Zhonghua, Li, Wen, Yi
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Regulation of keratinocyte differentiation by O-GlcNAcylation
Journal of Dermatological Science, 2014O-linked β-N-acetylglucosamine (O-GlcNAc) modification is one of the posttranslational modification, emerging as an important regulatory mechanism in various cellular events.We attempted to investigate whether O-GlcNAcylation is involved in keratinocyte differentiation.Immunohistochemistry and Western blot were performed to demonstrate O-GlcNAcylation ...
Kyung-Cheol, Sohn +12 more
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Identification and Characterization of GRASP55 O-GlcNAcylation
2022O-GlcNAcylation is a posttranslational modification of proteins that adds a single sugar, β-N-acetylglucosamine (GlcNAc), to Ser/Thr residues. Extensive studies have been conducted to identify and characterize substrates of this modification but mostly focused on cytosolic and nuclear proteins.
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Role of O-GlcNAcylation in cancer biology
Pathology - Research and PracticeOne of the general characteristics of cancer cells is the abnormal increase of O-GlcNAcylation. Recent studies have shown that it affects the basic functions of proteins and regulates multiple phenotypes of cancer cells through key signals and metabolic pathways.
Yuxuan, Li +4 more
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O‐GlcNAcylation of the Human Kinome
The FASEB Journal, 2017O‐GlcNAc, first characterized more than 30 years ago, is an O‐linked β‐N‐acetylglucosamine moiety attached to the side chain hydroxyl of a serine or threonine residue. O‐GlcNAc has been found on over 4,000 cytoplasmic and nuclear proteins. The addition of O‐GlcNAc to proteins is catalyzed by O‐GlcNAc transferase (OGT) while its removal is catalyzed by ...
Xin Liu +3 more
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