• This mechanism proceeds with starting materials Uridine diphosphate N-acetylglucosamine, and a peptide chain with a reactive serine or threonine hydroxyl group. (wikipedia.org)
  • In recent years, due to the crucial role that protein post-translational modifications (PTMs) play in maintaining protein function and regulating signaling pathways, and the growing recognition of the extensive cross-talk that can occur between PTMs, simultaneous analysis of different types of PTMs represents a requirement of a new generation of enrichment materials. (bvsalud.org)
  • HOF is set to become an active research direction in the development of highly efficient simultaneous protein enrichment materials, and offers a new approach for comprehensive PTMs analysis. (bvsalud.org)
  • Other names include: O-GlcNAc transferase OGTase O-linked N-acetylglucosaminyltransferase Uridine diphospho-N-acetylglucosamine:polypeptide β-N-acetylglucosaminyltransferase Systematic name: UDP-N-α-acetyl-d-glucosamine:[protein]-3-O-N-acetyl-β-d-glucosaminyl transferase OGT catalyzes the addition of a single N-acetylglucosamine through an O-glycosidic linkage to serine or threonine and an S-glycosidic linkage to cysteine residues of nucleocytoplasmic proteins. (wikipedia.org)
  • Additionally, O-GlcNAc transferase catalyzes intracellular glycosylation of serine and threonine residues with the addition of N-acetylglucosamine. (wikipedia.org)
  • Post-translational modification on protein Ser/Thr residues by O-linked attachment of ß-N-acetyl-glucosamine (O-GlcNAcylation) is a key mechanism integrating redox signaling, metabolism and stress responses. (biomedcentral.com)
  • O-linked beta-N-acetylglucosamine ( O -GlcNAc) is a widespread modification of serine/threonine residues of nucleocytoplasmic proteins. (mcw.edu)
  • This post-translational modification on lysine residues of proteins plays a crucial role in a number of cellular processes such as nuclear transport, DNA replication and repair, mitosis and signal transduction. (nih.gov)
  • O-Linked GlcNAc addition and phosphorylation may compete for sites on nuclear pore proteins and transcription factors. (nih.gov)
  • The addition of the monosaccharide beta-N-acetyl-D-glucosamine to proteins ( O -GlcNAc glycosylation) is an intracellular, post-translational modification that shares features with phosphorylation. (mcw.edu)
  • 10. Identification of O-GlcNAc sites within peptides of the Tau protein and their impact on phosphorylation. (nih.gov)
  • Protein O-GlcNAc transferase also known as OGT or O-linked N-acetylglucosaminyltransferase is an enzyme (EC 2.4.1.255) that in humans is encoded by the OGT gene. (wikipedia.org)
  • The molecular mechanism of O-linked N-acetylglucosamine transferase has not been extensively studied either, since there is not a confirmed crystal structure of the enzyme. (wikipedia.org)
  • 1. Tandem mass spectrometry identifies many mouse brain O-GlcNAcylated proteins including EGF domain-specific O-GlcNAc transferase targets. (nih.gov)
  • 2. Cross-talk between two essential nutrient-sensitive enzymes: O-GlcNAc transferase (OGT) and AMP-activated protein kinase (AMPK). (nih.gov)
  • 4. O-linked-N-acetylglucosamine modification of mammalian Notch receptors by an atypical O-GlcNAc transferase Eogt1. (nih.gov)
  • 5. Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in Adams-Oliver syndrome. (nih.gov)
  • 11. Developmental regulation of protein O-GlcNAcylation, O-GlcNAc transferase, and O-GlcNAcase in mammalian brain. (nih.gov)
  • 18. A two-layered machine learning method to identify protein O-GlcNAcylation sites with O-GlcNAc transferase substrate motifs. (nih.gov)
  • Hédou J, Bastide B, Page A, Michalski JC, Morelle W. Mapping of O-linked beta-N-acetylglucosamine modification sites in key contractile proteins of rat skeletal muscle. (mcw.edu)
  • Recently, several key contractile proteins in rat skeletal muscle (i.e., myosin heavy and light chains and actin) were identified as O -GlcNAc modified. (mcw.edu)
  • Thus, the results suggest that this PTM might be involved in protein-protein interactions but could also modulate the contractile properties of skeletal muscle. (mcw.edu)
  • 13. O-GlcNAcylation site mapping by (azide-alkyne) click chemistry and mass spectrometry following intensive fractionation of skeletal muscle cells proteins. (nih.gov)
  • OGT catalyzes the addition of the O-GlcNAc post-translational modification to proteins. (wikipedia.org)
  • 12. Intracellular and extracellular O-linked N-acetylglucosamine in the nervous system. (nih.gov)
  • This mechanism proceeds with starting materials Uridine diphosphate N-acetylglucosamine, and a peptide chain with a reactive serine or threonine hydroxyl group. (wikipedia.org)
  • Serine-threonine/tyrosine-protein kinase, catalytic domain [Interproscan]. (ntu.edu.sg)
  • We demonstrate that this approach can be used for direct in-gel detection and mass spectrometric identification of O -GlcNAc proteins, identifying 146 novel glycoproteins from the mammalian brain. (mcw.edu)
  • Dynamic glycosylation of nuclear and cytosolic proteins. (nih.gov)
  • Using the method, we detect changes in O -GlcNAc glycosylation on several proteins involved in the regulation of transcription and mRNA translocation. (mcw.edu)
  • 6. Nucleocytoplasmic O-glycosylation: O-GlcNAc and functional proteomics. (nih.gov)
  • 7. Antibodies that detect O-linked β-D-N-acetylglucosamine on the extracellular domain of cell surface glycoproteins. (nih.gov)
  • To determine whether increased O-GlcNAcylation affects neuronal function and survival, we exposed rat primary cortical neurons to thiamet G, a highly selective inhibitor of the enzyme which removes the O-GlcNAc modification from target proteins, O-GlcNAcase (OGA). (biomedcentral.com)
  • The impact of O-GlcNAcylation has been studied in the context of neurodegenerative diseases, focusing mainly on O-GlcNAc modification of aggregation-prone proteins [ 18 ]. (biomedcentral.com)
  • In order to better understand how O -GlcNAc can modulate the contractile activity of muscle fibers, we decided to identify the sites of O -GlcNAc modification in purified contractile protein homogenates. (mcw.edu)
  • Microvesicles loaded with MCs encoding a thymidine kinase (TK)/nitroreductase (NTR) fusion protein produced prolonged TK-NTR expression in mammary carcinoma cells. (regenerativemedicine.net)
  • Coatomer complex is required for budding from Golgi membranes, and is essential for the retrograde Golgi-to-ER transport of dilysine-tagged proteins. (nih.gov)
  • Depolymerization of microtubules inhibits the export of a newly synthesized transmembrane protein from the Golgi apparatus to the plasma membrane and simultaneously blocks membrane growth. (rupress.org)
  • protein_coding" "Cz01g23140.t1","No alias","Chromochloris zofingiensis","Nuclear pore protein 84/107 [Interproscan]. (ntu.edu.sg)
  • Exploring the O -GlcNAc proteome: direct identification of O -GlcNAc-modified proteins from the brain. (mcw.edu)
  • 8. Identification of O-linked N-acetylglucosamine (O-GlcNAc)-modified osteoblast proteins by electron transfer dissociation tandem mass spectrometry reveals proteins critical for bone formation. (nih.gov)
  • Direct in-gel fluorescence detection and cellular imaging of O -GlcNAc-modified proteins. (mcw.edu)
  • We report an advanced chemoenzymatic strategy for the direct fluorescence detection, proteomic analysis, and cellular imaging of O -GlcNAc-modified proteins. (mcw.edu)
  • Furthermore, we show that the method can be exploited to quantify dynamic changes in cellular O -GlcNAc levels and to image O -GlcNAc-glycosylated proteins within cells. (mcw.edu)
  • To determine whether abnormal O-GlcNAcylation occurs in Parkinson's disease, we analyzed lysates from the postmortem temporal cortex of Parkinson's disease patients and compared them to age matched controls and found increased protein O-GlcNAcylation levels. (biomedcentral.com)
  • We found that inhibition of OGA by thiamet G at nanomolar concentrations significantly increased protein O-GlcNAcylation, activated MTOR, decreased autophagic flux, and increased α-synuclein accumulation, while sparing proteasomal activities. (biomedcentral.com)
  • Using an MS-based method that relies on mild beta-elimination followed by Michael addition of DTT (BEMAD), we determined the localization of one O -GlcNAc site in the subdomain four of actin and four O -GlcNAc sites in the light meromyosin region of myosin heavy chains (MHC). (mcw.edu)
  • According to previous reports concerning the role of these regions, our data suggest that O -GlcNAc sites might modulate the actin-tropomyosin interaction, and be involved in MHC polymerization or interactions between MHC and other contractile proteins. (mcw.edu)
  • protein_coding" "Cz02g21410.t1","No alias","Chromochloris zofingiensis","Domain of unknown function DUF1990 [Interproscan]. (ntu.edu.sg)
  • The ternary complex containing UFD1L, VCP and NPLOC4 binds ubiquitinated proteins and is necessary for the export of misfolded proteins from the ER to the cytoplasm, where they are degraded by the proteasome. (nih.gov)
  • These observations suggest that changes in protein O-GlcNAcylation are an important contributor to the pathogenesis of neurodegenerative diseases but its effects are highly context-dependent [ 27 ]. (biomedcentral.com)
  • Probe Set ID Ref Seq Protein ID Signal Strength Name Gene Symbol Species Function Swiss-Prot ID Amino Acid Sequence 1367452_at NP_598278 16.8 small ubiquitin-related modifier 2 precursor Sumo2 Rattus norvegicus " Ubiquitin-like protein that can be covalently attached to proteins as a monomer or as a lysine-linked polymer. (nih.gov)
  • Inhibition of MTOR by rapamycin decreased basal levels of protein O-GlcNAcylation, decreased AKT activation and partially reversed the effect of thiamet G on α-synuclein monomer accumulation. (biomedcentral.com)
  • Our method, which we have termed quantitative isotopic and chemoenzymatic tagging (QUIC-Tag), combines selective, chemoenzymatic tagging of O -GlcNAc proteins with an efficient isotopic labeling strategy. (mcw.edu)
  • Moreover, it was demonstrated that O -GlcNAc moieties involved in contractile protein interactions could modulate Ca(2+) activation parameters of contraction. (mcw.edu)