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GlucosamineAcetylglucosamineProduct LabelingSkinFood LabelingProduct PackagingSpin LabelsSkin AgingCosmeticsCosmetic TechniquesDatabases, FactualSkin DiseasesN-AcetylglucosaminyltransferasesMolecular Sequence DataGlycosylationCarbohydrate SequenceUridine Diphosphate N-AcetylglucosamineAmino Acid SequenceNeodymiumDiagnosis, OralBiological ProductsChitinPeriodonticsSulfuric AcidsTamarindusDatura stramoniumHerbaspirillumPlant LectinsUDPglucose 4-EpimeraseCarbohydrate EpimerasesSalmonellaAlgorithmsSalmonella typhimuriumUridine Diphosphate SugarsXenopsyllaNeuraminic AcidsAmidohydrolasesRodenticidesTransferases (Other Substituted Phosphate Groups)Rodent ControlGlycomicsLectinsPolysaccharidesInternetGlycoconjugatesBone Matrix
Glucosamine
Acetylglucosamine
The N-acetyl derivative of glucosamine.
Product Labeling
Use of written, printed, or graphic materials upon or accompanying a product or its container or wrapper. It includes purpose, effect, description, directions, hazards, warnings, and other relevant information.
Skin
The outer covering of the body that protects it from the environment. It is composed of the DERMIS and the EPIDERMIS.
Food Labeling
Use of written, printed, or graphic materials upon or accompanying a food or its container or wrapper. The concept includes ingredients, NUTRITIONAL VALUE, directions, warnings, and other relevant information.
Product Packaging
Form in which product is processed or wrapped and labeled. PRODUCT LABELING is also available.
Spin Labels
Molecules which contain an atom or a group of atoms exhibiting an unpaired electron spin that can be detected by electron spin resonance spectroscopy and can be bonded to another molecule. (McGraw-Hill Dictionary of Chemical and Technical Terms, 4th ed)
Skin Aging
The process of aging due to changes in the structure and elasticity of the skin over time. It may be a part of physiological aging or it may be due to the effects of ultraviolet radiation, usually through exposure to sunlight.
Cosmetics
Substances intended to be applied to the human body for cleansing, beautifying, promoting attractiveness, or altering the appearance without affecting the body's structure or functions. Included in this definition are skin creams, lotions, perfumes, lipsticks, fingernail polishes, eye and facial makeup preparations, permanent waves, hair colors, toothpastes, and deodorants, as well as any material intended for use as a component of a cosmetic product. (U.S. Food & Drug Administration Center for Food Safety & Applied Nutrition Office of Cosmetics Fact Sheet (web page) Feb 1995)
Cosmetic Techniques
Procedures for the improvement or enhancement of the appearance of the visible parts of the body.
Databases, Factual
Extensive collections, reputedly complete, of facts and data garnered from material of a specialized subject area and made available for analysis and application. The collection can be automated by various contemporary methods for retrieval. The concept should be differentiated from DATABASES, BIBLIOGRAPHIC which is restricted to collections of bibliographic references.
Skin Diseases
N-Acetylglucosaminyltransferases
Enzymes that catalyze the transfer of N-acetylglucosamine from a nucleoside diphosphate N-acetylglucosamine to an acceptor molecule which is frequently another carbohydrate. EC 2.4.1.-.
Molecular Sequence Data
Descriptions of specific amino acid, carbohydrate, or nucleotide sequences which have appeared in the published literature and/or are deposited in and maintained by databanks such as GENBANK, European Molecular Biology Laboratory (EMBL), National Biomedical Research Foundation (NBRF), or other sequence repositories.
Glycosylation
The chemical or biochemical addition of carbohydrate or glycosyl groups to other chemicals, especially peptides or proteins. Glycosyl transferases are used in this biochemical reaction.
Carbohydrate Sequence
The sequence of carbohydrates within POLYSACCHARIDES; GLYCOPROTEINS; and GLYCOLIPIDS.
Uridine Diphosphate N-Acetylglucosamine
Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell walls, and of sialic acids in mammalian glycoproteins.
Amino Acid Sequence
The order of amino acids as they occur in a polypeptide chain. This is referred to as the primary structure of proteins. It is of fundamental importance in determining PROTEIN CONFORMATION.
Neodymium
Neodymium. An element of the rare earth family of metals. It has the atomic symbol Nd, atomic number 60, and atomic weight 144.24, and is used in industrial applications.
Diagnosis, Oral
Examination of the mouth and teeth toward the identification and diagnosis of intraoral disease or manifestation of non-oral conditions.
Biological Products
Complex pharmaceutical substances, preparations, or matter derived from organisms usually obtained by biological methods or assay.
Chitin
A linear polysaccharide of beta-1->4 linked units of ACETYLGLUCOSAMINE. It is the second most abundant biopolymer on earth, found especially in INSECTS and FUNGI. When deacetylated it is called CHITOSAN.
Periodontics
A dental specialty concerned with the histology, physiology, and pathology of the tissues that support, attach, and surround the teeth, and of the treatment and prevention of disease affecting these tissues.
Sulfuric Acids
Inorganic and organic derivatives of sulfuric acid (H2SO4). The salts and esters of sulfuric acid are known as SULFATES and SULFURIC ACID ESTERS respectively.
Tamarindus
A plant genus of the family FABACEAE known for its sour fruit.
Datura stramonium
A plant species of the genus DATURA, family SOLANACEAE, that contains TROPANES and other SOLANACEOUS ALKALOIDS.
Herbaspirillum
A genus of gram-negative bacteria in the family OXALOBACTERACEAE, comprised of vibrioid or sometimes helical cells. They are chemoorganotrophic nitrogen fixers and are found free-living in the soil or in association with the roots of members of the GRAMINEAE. (From Bergey's Manual of Determinative Bacteriology, 9th ed)
Plant Lectins
Protein or glycoprotein substances of plant origin that bind to sugar moieties in cell walls or membranes. Some carbohydrate-metabolizing proteins (ENZYMES) from PLANTS also bind to carbohydrates, however they are not considered lectins. Many plant lectins change the physiology of the membrane of BLOOD CELLS to cause agglutination, mitosis, or other biochemical changes. They may play a role in plant defense mechanisms.
UDPglucose 4-Epimerase
A necessary enzyme in the metabolism of galactose. It reversibly catalyzes the conversion of UDPglucose to UDPgalactose. NAD+ is an essential component for enzymatic activity. EC 5.1.3.2.
Carbohydrate Epimerases
Enzymes that catalyze the epimerization of chiral centers within carbohydrates or their derivatives. EC 5.1.3.
Salmonella
A genus of gram-negative, facultatively anaerobic, rod-shaped bacteria that utilizes citrate as a sole carbon source. It is pathogenic for humans, causing enteric fevers, gastroenteritis, and bacteremia. Food poisoning is the most common clinical manifestation. Organisms within this genus are separated on the basis of antigenic characteristics, sugar fermentation patterns, and bacteriophage susceptibility.
Algorithms
A procedure consisting of a sequence of algebraic formulas and/or logical steps to calculate or determine a given task.
Salmonella typhimurium
A serotype of Salmonella enterica that is a frequent agent of Salmonella gastroenteritis in humans. It also causes PARATYPHOID FEVER.
Uridine Diphosphate Sugars
Xenopsylla
A genus of fleas in the family Pulicidae which includes the species that serves as the primary vector of BUBONIC PLAGUE, Xenopsylla cheopis.
Neuraminic Acids
Amidohydrolases
Rodenticides
Substances used to destroy or inhibit the action of rats, mice, or other rodents.
Transferases (Other Substituted Phosphate Groups)
A class of enzymes that transfers substituted phosphate groups. EC 2.7.8.
Rodent Control
The reduction or regulation of the population of noxious, destructive, or dangerous rodents through chemical, biological, or other means.
Glycomics
The systematic study of the structure and function of the complete set of glycans (the glycome) produced in a single organism and identification of all the genes that encode glycoproteins.
Lectins
Proteins that share the common characteristic of binding to carbohydrates. Some ANTIBODIES and carbohydrate-metabolizing proteins (ENZYMES) also bind to carbohydrates, however they are not considered lectins. PLANT LECTINS are carbohydrate-binding proteins that have been primarily identified by their hemagglutinating activity (HEMAGGLUTININS). However, a variety of lectins occur in animal species where they serve diverse array of functions through specific carbohydrate recognition.
Polysaccharides
Internet
A loose confederation of computer communication networks around the world. The networks that make up the Internet are connected through several backbone networks. The Internet grew out of the US Government ARPAnet project and was designed to facilitate information exchange.
Glycoconjugates
Carbohydrates covalently linked to a nonsugar moiety (lipids or proteins). The major glycoconjugates are glycoproteins, glycopeptides, peptidoglycans, glycolipids, and lipopolysaccharides. (From Biochemical Nomenclature and Related Documents, 2d ed; From Principles of Biochemistry, 2d ed)
Bone Matrix
Extracellular substance of bone tissue consisting of COLLAGEN fibers, ground substance, and inorganic crystalline minerals and salts.

Crystal structures of two H-2Db/glycopeptide complexes suggest a molecular basis for CTL cross-reactivity. (1/1610)

Two synthetic O-GlcNAc-bearing peptides that elicit H-2Db-restricted glycopeptide-specific cytotoxic T cells (CTL) have been shown to display nonreciprocal patterns of cross-reactivity. Here, we present the crystal structures of the H-2Db glycopeptide complexes to 2.85 A resolution or better. In both cases, the glycan is solvent exposed and available for direct recognition by the T cell receptor (TCR). We have modeled the complex formed between the MHC-glycopeptide complexes and their respective TCRs, showing that a single saccharide residue can be accommodated in the standard TCR-MHC geometry. The models also reveal a possible molecular basis for the observed cross-reactivity patterns of the CTL clones, which appear to be influenced by the length of the CDR3 loop and the nature of the immunizing ligand.  (+info)

Gangliosides of human kidney. (2/1610)

Five gangliosides isolated from human kidney have been characterized. The two main fractions were shown to be typical extraneural gangliosides in having lactose as their neutral carbohydrate moiety. Their structures were identified as: AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-8)AcNeu(alpha2-3)Gal(beta1-4)Glc(beta1-1)Cer. The two main hexosamine-containing gangliosides are structurally related to human blood group substances of glycosphingolipid nature. The following structures are postulated: AcNeu(alpha2-3)Gal(beta1-4)GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1)Cer and AcNeu(alpha2-3)Gal(beta1-4)[Fuc(alpha1-3)]GlcNAc(beta1-3)Gal(beta1-4)Glc(beta1-1) Cer. The third hexosamine-containing ganglioside belongs to a different series of glycolipids and was shown to have the structure of a major ganglioside of human brain: AcNeu(alpha2-3)Gal(beta1-3)GalNAc(beta1-4)[AcNeu(alpha2-3)]Gal(beta1-4)Glc(beta1- 1)Cer. The fatty acid structure of different gangliosides was shown to resemble that of neutral glycolipids of human kidney with the nonhydroxy acids C16:0, C22:0, and C24:0 as major components.  (+info)

Participation of a trisaccharide-lipid in glycosylation of oviduct membrane glycoproteins. (3/1610)

Preincubation of a hen oviduct membrane preparation with UDP-Nactyl[14C]glucosamine and bacitracin, followed by incubation with GDP-mannose, leads to formation of a chloroform/methanol (2/1)-extractable glycolipid. Treatment of the lipid with mild acid results in the release of a trisaccharide shown to have the structure beta-mannosyl-N-acetylglucosamineyl-N-acetylglucosamine. Incubation of purified trisaccharide-lipid with oviduct membranes in the presence of sodium deoxycholate, Mn2+, and GDP-mannose leads to formation of a labeled glycoprotein with an apparent molecular weight of 25,000...  (+info)

Lectin receptor sites on rat liver cell nuclear membranes. (4/1610)

The presence and localization of lectin receptor sites on rat liver cell nuclear and other endomembranes was studied by light and electron microscopy using fluorescein and ferritin-coupled lectin conjugates. Isolated nuclei labelled with fluorescein-conjugated Concanavalin A (Con A) or wheat germ agglutinin (WGA) often showed membrane staining, which sometimes was especially bright on small stretches of the nuclear surface. Unlabelled nuclei and nuclei with a complete ring fluorescence were also seen. The nuclear fluorescence corresponded in intensity to that seen on the surface of isolated rat liver cells. Con A-ferritin particles were seldom detected on the cytoplasmic surface of the intact nuclear envelope. However, at places where the 2 leaflets of the envelope were widely separated or where the outer nuclear membrane was partly torn away, heavy labelling was seen on the cisternal surface of both the inner and outer nuclear membranes. Labelling with Con A-ferritin was also found on the cisternal side of rough endoplasmic reticulum present in the specimens. No labelling was seen on the cytoplasmic surface of mitochondrial outer membrane. The results demonstrate the presence of binding sites for Con A and WGA in nuclei and an asymmetric localization of these sites on the cisternal side of ribosome-carrying endomembranes in rat liver cells.  (+info)

Role of surface proteins in Vibrio cholerae attachment to chitin. (5/1610)

The role of surface proteins in Vibrio cholerae attachment to chitin particles in vitro was studied. Treatment of V. cholerae O1 ATCC 14034 and ATCC 14035 with pronase E reduced the attachment of bacteria to chitin particles by 57 to 77%. A statistically significant reduction was also observed when the attachment to chitin was evaluated in the presence of homologous Sarkosyl-insoluble membrane proteins (MPs) (67 to 84%), N-acetylglucosamine (GlcNAc) (62%), the sugar that makes up chitin, and wheat germ agglutinin (40 to 56%), a lectin that binds GlcNAc. The soluble oligomers N,N'-diacetylchitobiose or N,N', N"-triacetylchitotriose caused an inhibition of 14 to 23%. Sarkosyl-insoluble MPs able to bind chitin particles were isolated and visualized by sodium dodecyl sulfate-polyacrylamide gel electrophoresis; two of these peptides (molecular sizes, 36 and 53 kDa) specifically bind GlcNAc.  (+info)

Platelet high affinity low density lipoprotein binding and import of lipoprotein derived phospholipids. (6/1610)

The binding of low density lipoprotein (LDL) to the platelet cell membrane could facilitate the transfer of phospholipids from LDL to the platelets. A polyclonal antibody against the platelet glycoproteins IIb/IIIa inhibited the high affinity binding of 125I-LDL by up to 80%. The transfer of pyrene (py)-labeled sphingomyelin (SM), phosphatidylcholine and phosphatidylethanolamine from LDL to the platelets was unaffected by the antibody. The lectin wheat germ agglutinin (WGA) reduced the binding of 125I-LDL to the platelets by approximately 80%. In contrast, the lectin stimulated the transfer of SM from LDL into the platelets by about three-fold. WGA also specifically augmented the transfer of py-SM between lipid vesicles and the platelets, the stimulation being abolished in the presence of N-acetylglucosamine. Dextran sulfate (DS) increased the specific binding of 125I-LDL to the platelets by up to 2.8-fold. On the other hand, the import of LDL-derived py-phospholipids was unaffected by DS. Together, the results indicate that the phospholipid transfer from LDL to the platelets is independent of the high affinity LDL binding to the platelets and is specifically stimulated by WGA. Thus, the interactions of platelets with LDL phospholipids differ markedly from those with the apoprotein components of the lipoproteins.  (+info)

Mutations that confer resistance to 2-deoxyglucose reduce the specific activity of hexokinase from Myxococcus xanthus. (7/1610)

The glucose analog 2-deoxyglucose (2dGlc) inhibits the growth and multicellular development of Myxococcus xanthus. Mutants of M. xanthus resistant to 2dGlc, designated hex mutants, arise at a low spontaneous frequency. Expression of the Escherichia coli glk (glucokinase) gene in M. xanthus hex mutants restores 2dGlc sensitivity, suggesting that these mutants arise upon the loss of a soluble hexokinase function that phosphorylates 2dGlc to form the toxic intermediate, 2-deoxyglucose-6-phosphate. Enzyme assays of M. xanthus extracts reveal a soluble hexokinase (ATP:D-hexose-6-phosphotransferase; EC 2.7.1.1) activity but no phosphotransferase system activities. The hex mutants have lower levels of hexokinase activities than the wild type, and the levels of hexokinase activity exhibited by the hex mutants are inversely correlated with the ability of 2dGlc to inhibit their growth and sporulation. Both 2dGlc and N-acetylglucosamine act as inhibitors of glucose turnover by the M. xanthus hexokinase in vitro, consistent with the finding that glucose and N-acetylglucosamine can antagonize the toxic effects of 2dGlc in vivo.  (+info)

Quantitative determination of N-acetylglucosamine residues at the non-reducing ends of peptidoglycan chains by enzymic attachment of [14C]-D-galactose. (8/1610)

The ability of human milk galactosyltransferase to attach D-galactose residues quantitatively to the C-4 of N-acetylglucosamine moieties at the ends of oligosaccharides has been utilized for the specific labeling and quantitative determination of the chain length of the glycan moiety of the bacterial cell wall. The average polysaccharide chain length of the soluble, uncrosslinked peptidoglycan secreted by Micrococcus luteus cells on incubation with penicillin G was studied with this technique and found to be approximately 70 hexosamines long. Furthermore, the peptidoglycan chain length of Escherichia coli sacculi of different cell shapes and dimensions was determined both in rod-shaped cells and in filaments induced by temperature shift of a division mutant or by addition of cephalexin or nalidixic acid. The average chain length found in most of these sacculi was between 70 and 100 hexosamines long. Small spherical 'mini' cells had chain lengths similar to those of the isogenic rod-like cells.  (+info)

Expression of O-linked N-acetylglucosamine modified proteins and produ by Octavia Y. GoodwinExpression of O-linked N-acetylglucosamine modified proteins and produ by Octavia Y. Goodwin
O-linked â-N-acetylglucosamine is a regulatory post translational modification. This modification occurs on nearly all functional classes of proteins, in the nucleus and cytoplasm. O-GlcNAc is added to serine or threonine by O-GlcNAc transferase and removed by O-GlcNAcase. Previous attempts to study O-GlcNAc-modified proteins have resulted in low yields, making 3-dimensional structure determination impossible. In this dissertation O-GlcNAc transferase will be co-expressed with domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2) in E. coli, to produce O-GlcNAc-modified protein. The O-GlcNAc-modified protein was expressed in a variety of E. coli cell lines at a variety of conditions, but only small quantities of insoluble protein were produced. A glycosidase was suspected due to the disappearance of the O-GlcNAc modification from the protein. O-(2-acetamido-2-dexoy-dglucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), a â-N-acetylglucosaminidase
https://digitalcommons.lsu.edu/gradschool_dissertations/3325/
Dynamic Interplay between O-Linked N-Acetylglucosaminylation and Glycogen Synthase Kinase-3-dependent Phosphorylation |...Dynamic Interplay between O-Linked N-Acetylglucosaminylation and Glycogen Synthase Kinase-3-dependent Phosphorylation |...
O-GlcNAc1 is a dynamically regulated post-translational modification (PTM), in which a β-N-acetylglucosamine moiety is attached to hydroxyl side chains of serine or threonine residues of proteins by O-GlcNAc-transferase (1) and removed by β-N-acetylglucosaminidase (O-GlcNAcase) (2). O-GlcNAc is ubiquitous on nuclear and cytoplasmic proteins in all multicellular eukaryotes (3). Dynamic O-GlcNAcylation plays critical roles in signal transduction (4), transcriptional control (5, 6), cell cycle regulation (7), protein degradation (8), neurodegeneration (9), and stress responses (10). Abnormally regulated O-GlcNAcylation has been found in diseases such as diabetes (11) and Alzheimer disease (12).. The role of O-GlcNAcylation in signal transduction is at least in part related to its competitive interplay with O-phosphorylation. Some of the known O-GlcNAc sites are the same as or adjacent to phosphorylation sites. For example, O-GlcNAc is reciprocal to O-phosphorylation on the C-terminal domain of ...
https://www.mcponline.org/content/6/8/1365?ijkey=442d426eb944c24e0a9d5cc49866bb11037b5e09&keytype2=tf_ipsecsha
Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress: A survival response of mammalian cells -...Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress: A survival response of mammalian cells -...
Fingerprint Dive into the research topics of Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress: A survival response of mammalian cells. Together they form a unique fingerprint. ...
https://jhu.pure.elsevier.com/en/publications/dynamic-o-glcnac-modification-of-nucleocytoplasmic-proteins-in-re-4/fingerprints/
GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels<...GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels<...
TY - JOUR. T1 - GlcNAcstatin. T2 - a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels. AU - Dorfmueller, Helge C.. AU - Borodkin, Vladimir S.. AU - Schimpl, Marianne. AU - Shepherd, Sharon M.. AU - Shpiro, Natalia A.. AU - van Aalten, Daan M. F.. PY - 2006/12. Y1 - 2006/12. N2 - Many phosphorylation signal transduction pathways in the eukaryotic cell are modulated by posttranslational modification of specific serines/threonines with N-acetylglucosamine (O-GlcNAc). Levels of O-GlcNAc on key proteins regulate biological processes as diverse as the cell cycle, insulin signaling, and protein degradation. The two enzymes involved in this dynamic and abundant modification are the O-GlcNAc transferase and O-GlcNAcase. Structural data have recently revealed that the O-GlcNAcase possesses an active site with significant structural similarity to that of the human lysosomal hexosaminidases HexA/HexB. PUGNAc, an O-GlcNAcase inhibitor widely used to raise levels ...
https://discovery.dundee.ac.uk/en/publications/glcnacstatin-a-picomolar-selective-o-glcnacase-inhibitor-that-mod
Frontiers | FGF23 Induction of O-Linked N-Acetylglucosamine Regulates IL-6 Secretion in Human Bronchial Epithelial Cells |...Frontiers | FGF23 Induction of O-Linked N-Acetylglucosamine Regulates IL-6 Secretion in Human Bronchial Epithelial Cells |...
The hexosamine biosynthetic pathway (HBP) generates the substrate for the O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins. The HBP also serves as a stress sensor and has been reported to be involved with nuclear factor of activated T-cells (NFAT) activation, which can contribute to multiple cellular processes including cell metabolism, proliferation, and inflammation. In our previously published report, Fibroblast Growth Factor (FGF) 23, an important endocrine pro-inflammatory mediator, was shown to activate the FGFR4/phospholipase Cγ (PLCγ)/nuclear factor of activated T-cells (NFAT) signaling in chronic inflammatory airway diseases such as cystic fibrosis (CF) and chronic obstructive pulmonary disease (COPD). Here, we demonstrate that FGF23 increased the O-GlcNAc modification of proteins in HBECs. Furthermore, the increase in O-GlcNAc levels by FGF23 stimulation resulted in the downstream activation of NFAT and secretion of interleukin-6 (IL-6). Conversely, inhibition of FGF23
https://www.frontiersin.org/articles/10.3389/fendo.2018.00708/full
Diamond Publications - Search ResultsDiamond Publications - Search Results
Abstract: O-GlcNAc transferase (OGT) glycosylates a diverse range of intracellular proteins with O-linked N-acetylglucosamine (O-GlcNAc), an essential and dynamic post-translational modification in metazoans. Although this enzyme modifies hundreds of proteins with O-GlcNAc, it is not understood how OGT achieves substrate specificity. In this study, we describe the application of a high-throughput OGT assay to a library of peptides. We mapped sites of O-GlcNAc modification by electron transfer dissociation MS and found that they correlate with previously detected O-GlcNAc sites. Crystal structures of four acceptor peptides in complex with Homo sapiens OGT suggest that a combination of size and conformational restriction defines sequence specificity in the −3 to +2 subsites. This work reveals that although the N-terminal TPR repeats of OGT may have roles in substrate recognition, the sequence restriction imposed by the peptide-binding site makes a substantial contribution to O-GlcNAc site ...
https://publications.diamond.ac.uk/pubman/searchpublicationsadvanced?advancedsearch=1&authorId=37873&publicationStates%5B4%5D.selected=true
Protein O-GlcNAcylation Is Required for Fibroblast Growth Factor Signaling in Drosophila | Science SignalingProtein O-GlcNAcylation Is Required for Fibroblast Growth Factor Signaling in Drosophila | Science Signaling
Glycosylation is essential for growth factor signaling through N-glycosylation of ligands and receptors and the biosynthesis of proteoglycans as co-receptors. Here, we show that protein O-GlcNAcylation is crucial for fibroblast growth factor (FGF) signaling in Drosophila. We found that nesthocker (nst) encodes a phosphoacetylglucosamine mutase and that nst mutant embryos exhibited low amounts of intracellular uridine 5′-diphosphate-N-acetylglucosamine (UDP-GlcNAc), which disrupted protein O-GlcNAcylation. Nst was required for mitogen-activated protein kinase (MAPK) signaling downstream of FGF but not MAPK signaling activated by epidermal growth factor. nst was dispensable for the function of the FGF ligands and the FGF receptors extracellular domain but was essential in the signal-receiving cells downstream of the FGF receptor. We identified the adaptor protein Downstream of FGF receptor (Dof), which interacts with the FGF receptor, as the relevant target for O-GlcNAcylation in the FGF ...
https://stke.sciencemag.org/content/4/204/ra89
Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α...Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α...
TY - JOUR. T1 - Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4. AU - Akimoto, Yoshihiro. AU - Miura, Yuri. AU - Toda, Tosifusa. AU - Wolfert, Margreet A.. AU - Wells, Lance. AU - Boons, Geert Jan. AU - Hart, Gerald Warren. AU - Endo, Tamao. AU - Kawakami, Hayato. PY - 2011. Y1 - 2011. N2 - Purpose. The objective of the present study is to identify proteins that change in the extent of the modification with O-linked N-acetylglucosamine (O-GlcNAcylation) in the kidney from diabetic model Goto-Kakizaki (GK) rats, and to discuss the relation between O-GlcNAcylation and the pathological condition in diabetes. Methods. O-GlcNAcylated proteins were identified by two-dimensional gel electrophoresis, immunoblotting and peptide mass fingerprinting. The level of O-GlcNAcylation of these proteins was examined by immunoprecipitation, immunoblotting and in situ Proximity Ligation Assay (PLA). Results: O-GlcNAcylated ...
https://jhu.pure.elsevier.com/en/publications/morphological-changes-in-diabetic-kidney-are-associated-with-incr-5
Abstract 19733: Shear-Dependent Aortic Valve Endothelial Inflammation and Calcification Are Regulated by O-GlcNAc Modification...Abstract 19733: Shear-Dependent Aortic Valve Endothelial Inflammation and Calcification Are Regulated by O-GlcNAc Modification...
Introduction: Aortic valve (AV) disease is a significant contributor to cardiovascular mortality. AV calcification occurs preferentially on the fibrosa side, where endothelial cells (ECs) are subjected to characteristic oscillatory shear stress (OS), whereas the ventricularis ECs experience stable unidirectional laminar shear stress (LS). OS and LS differently regulate endothelial function via gene expression and protein modification. While the post-translational β-N-acetylglucosamine modification of amino acids (O-GlcNAcylation) has been shown to be important in the function of various cell types, its role in AV disease is unknown. We hypothesized that OS impairs EC O-GlcNAcylation, leading to AV inflammation and calcification.. Methods and Results: Immunostaining analysis showed that O-GlcNAcylation was decreased in fibrosa endothelium compared to ventricularis in human and porcine AVs, and human AV ECs (HAVECs) exhibited increased O-GlcNAcylation by LS (20 dyn/cm2) and decreased by OS (+5 ...
http://circ.ahajournals.org/content/134/Suppl_1/A19733
Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc | ScienceGlycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc | Science
In order for a protein modification to play an active role in signal transduction, it needs to have certain key features. First, the modification needs to be dynamic. For the proteins that have been examined to date, the O-GlcNAc half-life is much shorter than that of the modified polypeptide chain (8). Second, the removal or attachment of the modification should be inducible by certain stimuli. O-GlcNAc modification of certain proteins is known to change in response to T cell activation, insulin signaling, glucose metabolism, and cell cycle progression (6). Thus, O-GlcNAc displays features essential for a role in signal transduction.. Consistent with O-GlcNAc being dynamic and inducible, regulated nucleocytoplasmic enzymes for the attachment [O-GlcNAc transferase (OGT)] and for the removal (O-GlcNAcase) of the modification have been purified, characterized, and cloned (9-12). The OGT enzyme is modified by both O-GlcNAc and tyrosine phosphorylation and has 11 protein-protein interaction domains ...
https://science.sciencemag.org/content/291/5512/2376?ijkey=5e99fa5fb28fe2d0fe73c63d7cd4017a02fe4d88&keytype2=tf_ipsecsha
Human OGA binds substrates in a conserved peptide recognition groove | Biochemical JournalHuman OGA binds substrates in a conserved peptide recognition groove | Biochemical Journal
The O-GlcNAc (O-linked N-acetylglucosamine) modification is a dynamic and reversible form of protein glycosylation occurring on specific serine and threonine residues of intracellular proteins [1,2]. Since the initial discovery of O-GlcNAc [3], technological advances have greatly facilitated its detection, and proteomics studies [4-6] have shown that a significant proportion of cellular proteins are O-GlcNAcylated. However, the functional importance of O-GlcNAc is only just emerging, with evidence to suggest that it may regulate protein activity in a manner analogous (and complementary) to phosphorylation [7]. O-GlcNAc levels are known to respond dynamically to nutrient availability [1] and stress [8], and to undergo changes during the cell cycle [9] and development [10]. O-GlcNAc has been shown to be associated with a range of human diseases [2]. Strikingly, only two enzymes orchestrate the O-GlcNAc modification. Both the OGT (O-GlcNAc transferase) and its antagonistic OGA (O-GlcNAcase or ...
http://www.biochemj.org/content/432/1/1
The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation<...The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation<...
TY - JOUR. T1 - The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation. AU - Liu, Bing. AU - Salgado, Oscar C.. AU - Singh, Sangya. AU - Hippen, Keli L.. AU - Maynard, Jason C.. AU - Burlingame, Alma L.. AU - Ball, Lauren E.. AU - Blazar, Bruce R.. AU - Farrar, Michael A.. AU - Hogquist, Kristin A.. AU - Ruan, Hai Bin. PY - 2019/12/1. Y1 - 2019/12/1. N2 - Regulatory T (Treg) cells control self-tolerance, inflammatory responses and tissue homeostasis. In mature Treg cells, continued expression of FOXP3 maintains lineage identity, while T cell receptor (TCR) signaling and interleukin-2 (IL-2)/STAT5 activation support the suppressive effector function of Treg cells, but how these regulators synergize to control Treg cell homeostasis and function remains unclear. Here we show that TCR-activated posttranslational modification by O-linked N-Acetylglucosamine (O-GlcNAc) stabilizes FOXP3 and activates STAT5, thus integrating these critical signaling pathways. ...
https://experts.umn.edu/en/publications/the-lineage-stability-and-suppressive-program-of-regulatory-t-cel
N-Acetyl-Glucosamine Binding Lectins - GlycoMatrix™N-Acetyl-Glucosamine Binding Lectins - GlycoMatrix™
Several lectins recognize n-acetyl-glucosamine in a glycoprotein. Based on the linkage and specificity for binding, different N-Acetyl-Glucosamine-binding lectins are utilized to obtain optimum results.
https://www.glycomatrix.com/collections/n-acetyl-glucosamine-binding-lectins
OGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens (human)] - Gene - NCBIOGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens (human)] - Gene - NCBI
This gene encodes a glycosyltransferase that catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. Since both phosphorylation and glycosylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. The protein contains multiple tetratricopeptide repeats that are required for optimal recognition of substrates. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Oct 2009 ...
https://www.ncbi.nlm.nih.gov/gene/8473
Profiling of Protein O-GlcNAcylation in Murine CD8<sup>+</sup> Effector- and Memory-like T...Profiling of Protein O-GlcNAcylation in Murine CD8<sup>+</sup> Effector- and Memory-like T...
TY - JOUR. T1 - Profiling of Protein O-GlcNAcylation in Murine CD8+ Effector- and Memory-like T Cells. AU - Lopez Aguilar, Aime. AU - Gao, Yu. AU - Hou, Xiaomeng. AU - Lauvau, Gregoire. AU - Yates, John R.. AU - Wu, Peng. N1 - Funding Information: This work was performed at The Scripps Research Institute with the financial support from the National Institutes of Health to P.W. (GM093282, GM113046) and to J.R.Y. (MH067880, GM103533). We thank the Histology Core Facility at TSRI for providing access to their equipment and support.. PY - 2017/12/15. Y1 - 2017/12/15. N2 - During an acute infection, antigenic stimulation leads to activation, expansion, and differentiation of naïve CD8+ T cells, first into cytotoxic effector cells and eventually into long-lived memory cells. T cell antigen receptors (TCRs) detect antigens on antigen-presenting cells (APCs) in the form of antigenic peptides bound to major histocompatibility complex I (MHC-I)-encoded molecules and initiate TCR signal transduction ...
https://einstein.pure.elsevier.com/en/publications/profiling-of-protein-o-glcnacylation-in-murine-cd8supsup-effector
China N-Acetyl-D-Glucosamine - China N-Acetyl-D-Glucosamine, GlucosamineChina N-Acetyl-D-Glucosamine - China N-Acetyl-D-Glucosamine, Glucosamine
China N-Acetyl-D-Glucosamine, Find details about China N-Acetyl-D-Glucosamine, Glucosamine from N-Acetyl-D-Glucosamine - Yangzhou Rixing Bio-Tech Co., Ltd.
http://yzrixing.en.made-in-china.com/product/nKhEqSWVgfYc/China-N-Acetyl-D-Glucosamine.html
Nutrient Regulation of Immunity: O-GlcNAcylation Regulates Stimulus-Specific NF-κB-Dependent Transcription | Science SignalingNutrient Regulation of Immunity: O-GlcNAcylation Regulates Stimulus-Specific NF-κB-Dependent Transcription | Science Signaling
Nutrients regulate gene transcription by the dynamic cycling of O-linked N-acetylglucosamine (O-GlcNAc) on proteins that constitute the transcriptional machinery. A study shows that O-GlcNAcylation of the nuclear factor κB (NF-κB) subunit c-Rel is required for its binding to the promoters of some, but not all, key T cell receptor-dependent genes; however, O-GlcNAcylation is dispensable for the binding of c-Rel to the promoters of tumor necrosis factor-α-dependent genes. This study not only illustrates how specific stimuli that act on the same transcription factor can elicit the expression of particular sets of genes, it also suggests a possible mechanism for autoimmunity in diabetes.. ...
http://stke.sciencemag.org/content/6/290/pe26
Getting a handle on the O-GlcNAc modification - OReilly Science Art, LLCGetting a handle on the O-GlcNAc modification - OReilly Science Art, LLC
Protein glycosylation is usually relegated to the cell surface and intracellular compartments. In a fascinating exception to this rule that was first observed in the 1980s, A GlcNAc monosaccharide can be added to serine and threonine residues of cytosolic proteins. Many labs are trying to understand the dynamic regulation of the addition and removal of this sugar that seemingly has a hand in every cellular process and disease state known to man. More and more examples are being found to suggest that this modification and phosphorylation regulate each other, as if they werent already complicated enough on their own.. There are a handful of ways to detect O-GlcNAc, which have helped build the laundry list by telling us which proteins are modified. Now, in a recent Nature Chemical Biology paper from Linda Hsieh-Wilsons lab at CalTech, they show us a useful new method that reveals what proportion of any particular protein is modified (2%? 80%), and of those that are modified, exactly how many ...
http://oreillyscienceart.com/whats-new/2010/8/22/getting-a-handle-on-the-o-glcnac-modification.html
Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic diseaseCross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
O-GlcNAcylation is the addition of β-D-N-acetylglucosamine to serine or threonine residues of nuclear and cytoplasmic proteins. O-linked N-acetylglucosamine (O-GlcNAc) was not discovered until the early 1980s and still remains difficult to detect and quantify. Nonetheless, O-GlcNAc is highly abundan …
https://pubmed.ncbi.nlm.nih.gov/21391816/?dopt=Abstract
3pe4 - Proteopedia, life in 3D3pe4 - Proteopedia, life in 3D
OGT1_HUMAN] Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the Thr-308 phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating ...
http://proteopedia.org/wiki/index.php/3pe4
David Vocadlo - Department of Chemistry - Simon Fraser UniversityDavid Vocadlo - Department of Chemistry - Simon Fraser University
Cecioni, S., Vocadlo, D.J. Carbohydrate Bis-acetal-Based Substrates as Tunable Fluorescence-Quenched Probes for Monitoring exo-Glycosidase Activity. Journal of the American Chemical Society 2017, 139, 8392-8395. Liu T.-W., Myschyshyn M., Sinclair D.A., Cecioni S., Beja K., Honda B.M., Morin R.D., Vocadlo D.J. Genome-wide chemical mapping of O-GlcNAcylated proteins in Drosophila. Nature Chemical Biology 2017, 13, 161-7.. Perley-Robertson GE, Yadav AK, Winogrodzki JL, Stubbs KA, Mark BL, Vocadlo DJ.* A Fluorescent Transport Assay Enables Studying AmpG Permeases Involved in Peptidoglycan Recycling and Antibiotic Resistance. ACS Chem. Biol., 2016, 11, 2626-35.. Cekic N, Heinonen JE, Stubbs KA, Roth C, He Y, Bennet AJ, McEachern EJ, Davies GJ, Vocadlo DJ. Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O-GlcNAcase. Chem. Sci. 2016, 7, 3742-3750.. Zhu, Y., Liu, T., Eskandari, R., Zandberg, W., Cecioni, S., Vocadlo, D.J.* ...
https://www.sfu.ca/chemistry/people/profiles/dvocadlo.html
Plus itPlus it
Cancer cells increase nutrient consumption leading to the altered metabolic state known as the Warburg effect. One pathway dependent on glucose, glutamine and acetyl-CoA is the Hexosamine Biosynthetic Pathway (HBP). Increased flux through the HBP leads to elevated post-translation addition of O-linked-β-N-acetylglucosamine (O-GlcNAc) on a diverse population of nuclear and cytosolic proteins, many of which are implicated in cancer. Recently, our lab provided the first evidence that breast and prostate cancers increases total O-GlcNAcylation by increasing O-GlcNAc Transferase (OGT) levels. Importantly, reducing OGT activity inhibits cancer cell invasion in vitro and metastasis in vivo. OGT inhibition reduces breast and prostate cancer cell invasion through, in part, inhibition of the oncogenic transcription factor, FOXM1 and its transcriptional target matrix metalloproteinase 2 (MMP2). Here, we show that OGT regulation of FOXM1 and cancer cell invasion requires regulation of the NAD+-dependent ...
http://cancerres.aacrjournals.org/content/75/15_Supplement/518
anti-O-GlcNAc transferase antibody [GT2037] | GeneTexanti-O-GlcNAc transferase antibody [GT2037] | GeneTex
O-GlcNAc transferase antibody [GT2037] (O-linked N-acetylglucosamine (GlcNAc) transferase) for WB. Anti-O-GlcNAc transferase mAb (GTX629813) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
http://www.genetex.com/O-GlcNAc-transferase-antibody-GT2037-GTX629813.html
N-Acetyl-D-Glucosamine (CAS No.: 7512-17-6;134451-94-8); USP - XIAN VEDA CHEMICAL CO.,LTD - ecplaza.netN-Acetyl-D-Glucosamine (CAS No.: 7512-17-6;134451-94-8); USP - XIAN VEDA CHEMICAL CO.,LTD - ecplaza.net
Product Name:N-acetyl-D-(+)-Glucosamine Synonyms:N-Acetyl-Beta-D-Glucosamine; N-Acetyl-D-Glucosamine; 2-Acetamido-2-Deoxy-D-Glucopyranose; N-((1R,2R,3S,4R)-1-Formyl-2,3,4,5-Tetrahydroxy-Pentyl)-Acetamide; N-Acetyl-D-Glucosamine, Immobilized On...
https://www.ecplaza.net/products/n-acetyl-d-glucosamine-cas-no_4091810
Team:Northwestern/Project/Modeling - 2010.igem.orgTeam:Northwestern/Project/Modeling - 2010.igem.org
Iex: External Inducer, determined by diffusion through Ficks law (IPTG in our experiment) Iin: Internal Inducer (IPTG) Ii: Inducer bound to Repressor (IPTG bound to lacI) i: Repressor (lacI) Db: Repressor-bound DNA (lacI-bound DNA(CHS3) region in plasmid) Dunb: transcribe-able or Repressor-unbound DNA (lacI-unbound DNA(CHS3)) Re: mRNA for Enzyme (CHS3 mRNA) E: Enzyme (CHS3) S: Substrate (N-Acetyl Glucosamine) C: Enzyme Substrate Complex (CHS3-(N-Acetyl-Glucosamine)-Chitin or (NAG)n Complex) P: Protein Product (Chitin or (NAG)n+1) ...
http://2010.igem.org/wiki/index.php?title=Team:Northwestern/Project/Modeling&oldid=150687
Vegfa | High-Throughput Screen for the Chemical InhibitorsVegfa | High-Throughput Screen for the Chemical Inhibitors
Many neuronal cytosolic and nuclear proteins are post-translationally modified by the reversible addition of O-linked = 176), demonstrating that cotransfection is a reliable approach in our system. of culturing. Comparison of the staining intensity in neurons expressing dsRED alone (= 23) to that in nontransfected neurons from cultures transfected with either dsRED (= 23) or dsRED + O-GlcNAcase (= 25) did not reveal a difference (> 0.32 and > 0.21 respectively, 2-tailed Welch > 0.25, 2-tailed Welch = 23) to dsRED transfected neurons revealed a 61% decrease in O-GlcNAc staining intensity (< 0.00001, 2-tailed Welch = 140) of O-GlcNAcase over-expressing neurons exhibited one LY310762 supplier or more branches relative to 20% (= 60) of dsRED alone expressing control neurons [Fig. 2(E)]. Thus, decreases in O-GlcNAc levels induced by overexpression of O-GlcNAcase resulted in a 1.85-fold increase in the percentage of neurons that exhibited axon branching. O-GlcNAcase over-expression resulted in a 50% ...
http://acancerjourney.info/index.php/tag/vegfa/
Deciphering nucleoporin functions in nucleocytoplasmic protein transport in Drosophila.Deciphering nucleoporin functions in nucleocytoplasmic protein transport in Drosophila.
Part of urn:nbn:se:su:diva-968Available from: 2006-04-06 Created: 2006-04-06 Last updated: 2010-01-13Bibliographically approved ...
http://su.diva-portal.org/smash/record.jsf?pid=diva2:200745
SAUPAN002586000 - AureoWikiSAUPAN002586000 - AureoWiki
Staphylococcus aureus; pan ID: SAUPAN002586000; symbol: nagA; products: N-acetylglucosamine-6-phosphate deacetylase, putative N-acetylglucosamine-6-phosphatedeacetylase; orthologs: COL: SACOL0761 (nagA), N315: SA0656 (nagA), NCTC8325: SAOUHSC_00710, Newman: NWMN_0670 (nagA), USA300_FPR3757: SAUSA300_0686 (nagA), 04-02981: SA2981_0678 (nagA)
https://aureowiki.med.uni-greifswald.de/SAUPAN002586000
N-acetyl-D-glucosamineN-acetyl-D-glucosamine
Hyaluronic acid (HA), a polymer with elastic properties, is a polysaccharide formed from N-acetyl-D-glucosamine and glucuronic acid. HA belongs to a group of chemicals called glycosaminoglycans (GAGs). The activity of a specific form or polymer of HA depends on the size the molecule. HA forms an aggregation center for a large molecule of chondroitin sulfate […]. View Post ...
https://www.rainbow.coop/nutritional-library/miscellaneous/n-acetyl-d-glucosamine/
The Basics of Protein Structure Part 1: The Levels of StructureThe Basics of Protein Structure Part 1: The Levels of Structure
How protein structure is established is a fascinating question and a field that is actively studied by prominent labs around the world. Protein folding is the process of a chain of amino acids curling into its final shape, and how this process occurs is complex and not completely understood. In general proteins fold depending on their environment (exposed to water or not, for example) and with the help of other proteins, called chaperones. Protein chaperones help to establish a proteins structure as well as maintain it during times of stress. Further, modifications on proteins can change their structures, such as when p53, a protein that is involved in regulating many processes within the cell, is phosphorylated - its structure and, consequently, its function is altered slightly ...
http://poorhungrydrowsy.blogspot.com/2014/06/the-basics-of-protein-structure-part-1.html
O-GlcNAc (CTD110.6) | ALZFORUMO-GlcNAc (CTD110.6) | ALZFORUM
detects O-GlcNAc (ß-O-linked N- acetylglucosamine) and Thr-O-GlcNAc but shows no cross reactivity with peptide determinants or other closely-related carbohydrate antigens ...
https://www.alzforum.org/antibodies/o-glcnac-ctd1106
Targeted disruption the enzymes of O-GlcNAc cycling: Animal models of Disease - John HanoverTargeted disruption the enzymes of O-GlcNAc cycling: Animal models of Disease - John Hanover
The hexosamine signaling pathway terminating in O-GlcNAc cycling has been implicated in cellular signaling cascades and regulation of transcription and translat...
http://grantome.com/grant/NIH/ZIA-DK060101-07
Development of Research Reagents Specific for O-Glcnac (O-Glcnac Lectenz) - Lori YangDevelopment of Research Reagents Specific for O-Glcnac (O-Glcnac Lectenz) - Lori Yang
The long-term objectives of this proposal are to generate and commercialize a new class of high-specificity, high-affinity proteins called Lectenz?, as research...
http://grantome.com/grant/NIH/261201300048C-0-0-1
Kraeber & Co GmbH - N-Acetyl-D-GlucosamineKraeber & Co GmbH - N-Acetyl-D-Glucosamine
Kraeber & Co GmbH - Pharmazeutische Rohstoffe - Hersteller von Wirk- und Hilfsstoffen für die Pharmazie, Biotechnologie, Kosmetik und Fototechnik.
https://www.kraeber.de/products/cosmetic/n-acetyl-d-glucosamine
Early detection of diabetes - The Johns Hopkins UniversityEarly detection of diabetes - The Johns Hopkins University
The present invention is based on the discovery that hexosamine, and in particular the dynamic O-GlcNAcylation of proteins (modification of proteins by the sugar N-acetylglucosamine) both causes insul
http://www.freepatentsonline.com/9250248.html
KEGG ENZYME: 2.4.1.320KEGG ENZYME: 2.4.1.320
4-O-beta-D-mannopyranosyl-N-acetyl-D-glucosamine + phosphate = N-acetyl-D-glucosamine + alpha-D-mannose 1-phosphate [RN:R10829 ...
http://www.genome.jp/dbget-bin/www_bget?ec:2.4.1.320
Activation of AKT by O-linked N-Acetylglucosamine induces vascular calcification in diabetes mellitus<...Activation of AKT by O-linked N-Acetylglucosamine induces vascular calcification in diabetes mellitus<...
TY - JOUR. T1 - Activation of AKT by O-linked N-Acetylglucosamine induces vascular calcification in diabetes mellitus. AU - Heath, Jack M.. AU - Sun, Yong. AU - Yuan, Kaiyu. AU - Bradley, Wayne E.. AU - Litovsky, Silvio. AU - DellItalia, Louis J.. AU - Chatham, John C.. AU - Wu, Hui. AU - Chen, Yabing. N1 - Copyright: Copyright 2014 Elsevier B.V., All rights reserved.. PY - 2014/3/28. Y1 - 2014/3/28. N2 - RATIONALE:: Vascular calcification is a serious cardiovascular complication that contributes to the increased morbidity and mortality of patients with diabetes mellitus. Hyperglycemia, a hallmark of diabetes mellitus, is associated with increased vascular calcification and increased modification of proteins by O-linked N-acetylglucosamine (O-GlcNAcylation). OBJECTIVE:: We sought to determine the role of protein O-GlcNAcylation in regulating vascular calcification and the underlying mechanisms. METHODS AND RESULTS:: Low-dose streptozotocin-induced diabetic mice exhibited increased aortic ...
https://ohsu.pure.elsevier.com/en/publications/activation-of-akt-by-o-linked-n-acetylglucosamine-induces-vascula
Pomgnt2 (protein O-linked mannose N-acetylglucosaminyltransferase 2 (beta 1,4-)) - Chinchilla Research Resource DatabasePomgnt2 (protein O-linked mannose N-acetylglucosaminyltransferase 2 (beta 1,4-)) - Chinchilla Research Resource Database
ENCODES a protein that exhibits acetylglucosaminyltransferase activity (ortholog); protein O-GlcNAc transferase activity (ortholog); INVOLVED IN neuron migration (ortholog); protein O-linked glycosylation (ortholog); protein O-linked mannosylation (ortholog); ASSOCIATED WITH Autosomal Recessive Limb-Girdle Muscular Dystrophy Type 24 (ortholog); congenital muscular dystrophy-dystroglycanopathy type A8 (ortholog); Perinatal Death (ortholog); FOUND IN endoplasmic reticulum (ortholog); endoplasmic reticulum membrane (ortholog); integral component of membrane (ortholog)
https://crrd.mcw.edu/rgdweb/report/gene/main.html?id=9047503
Impact of O-GlcNAc on cardioprotection by remote ischaemic preconditioning in non-diabetic and diabetic patients. - CARDIO PEGImpact of O-GlcNAc on cardioprotection by remote ischaemic preconditioning in non-diabetic and diabetic patients. - CARDIO PEG
The cardioprotective capacity and the influence on myocardial O-GlcNAc levels of plasma dialysate from eight healthy volunteers and eight type 2 diabetic patients drawn before and after subjection to an rIPC stimulus were tested on human isolated atrial trabeculae subjected to ischaemia/reperfusion injury. Dialysate from healthy volunteers exposed to rIPC improved post-ischaemic haemodynamic recovery (40 ± 6 vs. 16 ± 2%; P , 0.01) and increased myocardial O-GlcNAc levels. Similar observations were made with dialysate from diabetic patients before exposure to rIPC (43 ± 3 vs. 16 ± 2%; P , 0.001) but no additional cardioprotection or further increase in O-GlcNAc levels was achieved by perfusion with dialysate after exposure to rIPC (44 ± 4 and 42 ± 5 vs. 43 ± 3%; P = 0.7). The glutamine:fructose-6-phosphate amidotransferase (GFAT) inhibitor azaserine abolished the cardioprotective effects and the increment in myocardial O-GlcNAc levels afforded by plasma from diabetic patients and healthy ...
http://pegnac.sdsc.edu/cardiopeg/pmc3584969/
Inhibition of O-GlcNAc transferase activity reprograms prostate cancer cell metabolism<...Inhibition of O-GlcNAc transferase activity reprograms prostate cancer cell metabolism<...
TY - JOUR. T1 - Inhibition of O-GlcNAc transferase activity reprograms prostate cancer cell metabolism. AU - Itkonen, Harri M. AU - Gorad, Saurabh S. AU - Duveau, Damien Y. AU - Martin, Sara E S. AU - Barkovskaya, Anna. AU - Bathen, Tone F. AU - Moestue, Siver A. AU - Mills, Ian G. PY - 2016/1/27. Y1 - 2016/1/27. N2 - Metabolic networks are highly connected and complex, but a single enzyme, O-GlcNAc transferase (OGT) can sense the availability of metabolites and also modify target proteins. We show that inhibition of OGT activity inhibits the proliferation of prostate cancer cells, leads to sustained loss of c-MYC and suppresses the expression of CDK1, elevated expression of which predicts prostate cancer recurrence (p=0.00179). Metabolic profiling revealed decreased glucose consumption and lactate production after OGT inhibition. This decreased glycolytic activity specifically sensitized prostate cancer cells, but not cells representing normal prostate epithelium, to inhibitors of oxidative ...
https://pure.qub.ac.uk/en/publications/inhibition-of-o-glcnac-transferase-activity-reprograms-prostate-c
Validity Study of Glutamine to Improve Cardiac Function in Cardiac Surgery - Tabular View - ClinicalTrials.govValidity Study of Glutamine to Improve Cardiac Function in Cardiac Surgery - Tabular View - ClinicalTrials.gov
Cardiosurgery is mostly done under cardiopulmonary bypass. However, the cardiopulmonary bypass and the later recovery of spontaneous circulation, a cardiac ischemia / reperfusion process, may cause myocardial damage and affect cardiac function as well as prognosis.. Glutamine, an amino acid abundant in the human body, plays an important role in the regulation of metabolism and immune cells and the protection of organs. Relative lack of glutamine is reported during stress or serious illness. Animal studies have confirmed that pretreatment with glutamine has a protective effect on the heart, liver, kidney and other organs post ischemia / reperfusion injury. It is also established that glutamine exerts myocardial protection mainly by activating hexosamine biosynthetic pathway, increasing intracellular O-GlcNAc protein modification and expression of heat shock protein 70 (HSP70), starting the protective reaction in the body, improving the function of myocardial cells, and inhibiting the release of ...
https://clinicaltrials.gov/ct2/show/record/NCT01794884?show_rss=Y&sel_rss=mod14
Pomgnt1 (untagged) - Mouse protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase (Pomgnt1), transcript variant 1, ...Pomgnt1 (untagged) - Mouse protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase (Pomgnt1), transcript variant 1, ...
Pomgnt1 (untagged) - Mouse protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase (Pomgnt1), transcript variant 1, (10ug), 10 µg.
https://www.acris-antibodies.com/cdna/mouse-cdna/pomgnt1-untagged-mouse-protein-o-linked-mannose-beta1-2-n-acetylglucosaminyltransferase-pomgnt1-transcript-variant-1-10ug-mc201045.htm
Enzymes of N-Acetylglucosamine Metabolism during Germ-tube Formation in Candida albicans | Microbiology SocietyEnzymes of N-Acetylglucosamine Metabolism during Germ-tube Formation in Candida albicans | Microbiology Society
SUMMARY: The enzymes of N-acetyl-D-glucosamine (GlcNAc) metabolism, GlcNAc-6-phosphate deacetylase and GlcN-6-phosphate deaminase were found to be inducible in Candida albicans. The pattern of induction for these enzymes was the same under conditions of germ-tube formation (37 °C) and where yeast cells metabolized GlcNAc with no change in morphology (28 °C); this indicates that these enzymes are not control points in the dimorphic development of C. albicans. During induction there was a 40- and 25-fold increase in specific activity for the deacetylase and the deaminase, respectively, and the maximum specific activity corresponded to the time when all the GlcNAc had been metabolized. The presence of lomofungin (an inhibitor of transcription) or trichodermin (an inhibitor of translation) in cell suspensions of C. albicans containing GlcNAc prevented the increase in specific activity of these enzymes. 2-Deoxyglucose inhibited germ-tube formation, partially inhibited the induction of the deacetylase (43%)
https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-128-10-2319
Analysis of nucleocytoplasmic protein shuttling by imaging flow cytometry<...Analysis of nucleocytoplasmic protein shuttling by imaging flow cytometry<...
TY - JOUR. T1 - Analysis of nucleocytoplasmic protein shuttling by imaging flow cytometry. AU - Fasler-Kan, Elizaveta. AU - Baiken, Yeldar. AU - Vorobjev, Ivan A.. AU - Barteneva, Natasha S.. PY - 2016. Y1 - 2016. N2 - Many intracellular signal transduction events involve the reversible shuttling of proteins between the cytoplasm and the nucleus. Study of these processes requires imaging information on the protein localization in a given cell and a large number of measurements to obtain sufficient statistics on the protein localization in the whole population. The protocol describes method for quantitative imaging flow cytometry analysis of intracellular distribution of NF-kappaB in ARPE-19 cells stained with specific fluorochrome-conjugated antibodies. The described technique alone or in combination with standard flow cytometry methods can be applied to study any protein undergoing translocation from cytoplasm into the nucleus in a variety of cell lines as well as in heterogeneous primary cell ...
https://research.nu.edu.kz/en/publications/analysis-of-nucleocytoplasmic-protein-shuttling-by-imaging-flow-c
N-Acetylglucosaminyltransferase III/MGAT3 Research Products: Novus BiologicalsN-Acetylglucosaminyltransferase III/MGAT3 Research Products: Novus Biologicals
N-Acetylglucosaminyltransferase III/MGAT3 products available through Novus Biologicals. Browse our N-Acetylglucosaminyltransferase III/MGAT3 product catalog backed by our Guarantee+.
https://www.novusbio.com/common-name/n-acetylglucosaminyltransferase-iii-mgat3
EGF domain-specific O-linked N-acetylglucosamine transferaseEGF domain-specific O-linked N-acetylglucosamine transferase
This gene encodes an enzyme that acts in the lumen of the endoplasmic reticulum to catalyze the transfer of N-acetylglucosamine to serine or threonine residues of extracellular-targeted proteins. This enzyme modifies proteins containing eukaryotic growth factor (EGF)-like domains, including the Notch receptor, thereby regulating developmental signalling. Mutations in this gene have been observed in individuals with Adams-Oliver syndrome 4. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2015 ...
https://pharos.nih.gov/idg/targets/Q5NDL2
Oligomannosides or oligosaccharide-lipids as potential substrates for rat liver cytosolic α-d-mannosidase | Biochemical JournalOligomannosides or oligosaccharide-lipids as potential substrates for rat liver cytosolic α-d-mannosidase | Biochemical Journal
We have previously reported the substrate specificity of the cytosolic α-D-mannosidase purified from rat liver using Man9GlcNAc, i.e. Manα1-2Manα1-3(Manα1-2Manα1-6)Man α1-6(Manα1-2Manα1-2Manα1-3)Manβ1-4GlcNAc, as substrate [Grard, Saint-Pol, Haeuw, Alonso, Wieruszeski, Strecker and Michalski (1994) Eur. J. Biochem. 223, 99-106]. Man9GlcNAc is hydrolysed giving Man5GlcNAc, i.e. Manα1-2Manα1-2Manα1-3(Manα1-6)Manβ1-4GlcNAc, possessing the same structure as the oligosaccharide of the dolichol pathway formed in the cytosolic compartment during the biosynthesis of N-glycosylprotein glycans. We study here the activity of the purified cytosolic α-D-mannosidase towards the oligosaccharide-diphosphodolichol intermediates formed during the biosynthesis of N-glycans, and also towards soluble oligosaccharides released from the endoplasmic reticulum which are glucosylated or not and possessing at their reducing end either a single N-acetylglucosamine residue or a di-N-acetylchitobiose ...
http://www.biochemj.org/content/316/3/787
c-Myc alters substrate utilization and O-GlcNAc protein posttranslational modifications without altering cardiac function...c-Myc alters substrate utilization and O-GlcNAc protein posttranslational modifications without altering cardiac function...
The protooncogene C-Myc (Myc) regulates cardiac hypertrophy. Myc promotes compensated cardiac function, suggesting that the operative mechanisms differ from those leading to heart failure. Myc regulation of substrate metabolism is a reasonable target, as Myc alters metabolism in other tissues. We hypothesize that Myc-induced shifts in substrate utilization signal and promote compensated hypertrophy. We used cardiac specific Myc-inducible C57/BL6 male mice between 4-6 months old that develop hypertrophy with tamoxifen (tam). Isolated working hearts and 13Carbon (13C )-NMR were used to measure function and fractional contributions (Fc) to the citric acid cycle by using perfusate containing 13C-labeled free fatty acids,more » acetoacetate, lactate, unlabeled glucose and insulin. Studies were performed at pre-hypertrophy (3-days tam, 3dMyc), established hypertrophy (7-days tam, 7dMyc) or vehicle control (cont). Non-transgenic siblings (NTG) received 7-days tam or vehicle to assess drug effect. ...
https://www.osti.gov/pages/biblio/1229960-myc-alters-substrate-utilization-glcnac-protein-posttranslational-modifications-without-altering-cardiac-function-during-early-aortic-constriction
nagJ - O-GlcNAcase NagJ precursor - Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 /...nagJ - O-GlcNAcase NagJ precursor - Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 /...
Binds carbohydrates (PubMed:16990278). Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals.
https://www.uniprot.org/uniprot/Q0TR53
Aging | The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of...Aging | The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of...
Full Text - Acyl-CoA ligase 4 (ACSL4) has been reported to be overexpressed in hepatocellular carcinoma (HCC) and to enhance cell proliferation. However, the molecular mechanisms underlying the role of ACSL4 in HCC progression remain largely unclear. Here, we aimed to investigate whether and how O-GlcNAcylation and ACSL4 regulate each other and HCC progression. The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis. CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis. IP technology was used to evaluate the relationship between ACSL4 and O-GlcNAc. ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients. ACSL4 overexpression significantly promoted cell proliferation and tumorigenesis and inhibited cell apoptosis, whereas these effects were all obviously impaired when mTOR signalling was repressed
https://www.aging-us.com/article/103092/text
Plus itPlus it
Type 2 diabetes mellitus (T2DM) is a well-recognized independent risk factor for heart failure (HF). T2DM is associated with altered cardiac energy metabolism, leading to ectopic lipid accumulation and glucose overload, the exact contribution of these two parameters remaining unclear. To provide new insight into the mechanism driving the development of diabetic cardiomyopathy, we studied a unique model of T2DM: lipodystrophic Bscl2-/- (seipin knockout (SKO)) mice. Echocardiography and cardiac magnetic resonance imaging revealed hypertrophic cardiomyopathy with left ventricular dysfunction in SKO mice and these two abnormalities were strongly correlated with hyperglycemia. Surprisingly, neither intramyocardial lipid accumulation nor lipotoxic hallmarks were detected in SKO mice. 18F-FDG positron emission tomography showed increased myocardial glucose uptake. Consistently, the O-GlcNAcylated protein levels were markedly increased in SKO heart, suggesting a glucose overload. To test this ...
http://diabetes.diabetesjournals.org/content/early/2017/01/04/db16-0733
GlucosamineGlucosamine
Certainly, N-acetylglucosamine appeared to accelerate the facilitated glucose uptake and boost each GAG and HA synthesis, suggesting that N-acetyl-glucosamine may perhaps be more efficient than native glucosamine. The American College of Rheumatology 2012 recommendations do not propose the use of glucosamine or chondroitin for the management of osteoarthritis. If there is advantage in terms of discomfort or function, it may well be continued. Sufferers nevertheless need to develop a comprehensive program with their physicians to treat osteoarthritis, which consists of diet plan, exercise, weight loss, and working with common, established drugs.. It is significant to point out that these research had been performed in various culture systems, with a variety of formulations and concentrations of glucosamine. The specifics of the culture systems and the formulations are provided in Table 2. Additionally, some of these studies compared the effects of two formulations of glucosamine in order to ...
https://www.letsmovebrooklyn.org/glucosamine/
Pomgnt1 MGI Mouse Gene Detail - MGI:1915523 - protein O-linked mannose beta 1,2-N-acetylglucosaminyltransferasePomgnt1 MGI Mouse Gene Detail - MGI:1915523 - protein O-linked mannose beta 1,2-N-acetylglucosaminyltransferase
View mouse Pomgnt1 Chr4:116123840-116159849 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
http://www.informatics.jax.org/marker/MGI:1915523
Pomgnt2 MGI Mouse Gene Detail - MGI:2143424 - protein O-linked mannose beta 1,4-N-acetylglucosaminyltransferase 2Pomgnt2 MGI Mouse Gene Detail - MGI:2143424 - protein O-linked mannose beta 1,4-N-acetylglucosaminyltransferase 2
View mouse Pomgnt2 Chr9:121981606-121996053 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
http://www.informatics.jax.org/marker/MGI:2143424
Dynamic Glycosylation in Neurons May Be Linked to Memory, Pathology | ALZFORUMDynamic Glycosylation in Neurons May Be Linked to Memory, Pathology | ALZFORUM
A new technique for detecting proteins modified by β-N-acetyl-D-glucosamine (i.e., O-GlcNAc glycosylation) reveals that the process is reversible and dynamic in neurons and may even play a role in memory. Linda Hsieh-Wilson, California Institute of Technology, Pasadena, and colleagues have developed a quantitative isotopic and chemoenzymatic tagging system (QUIC-Tag) to detect glycosylated proteins inside neurons. Unlike some other methodologies, QUIC-Tag does not require metabolic incorporation of isotopes or rounds of cell division. Cellular levels of O-GlcNAc-proteins are also unperturbed. The technique, which involves protection of the O-GlcNAc moieties by biotinylation followed by avidin-based purification and then mass spectrometry detection, is particularly suited to non-dividing cells, such as neurons.. The technique is explained in detail in the May 13 Nature Chemical Biology online. First author Nelly Khidekel and colleagues also describe how they used the QUIC-Tag method to detect ...
http://www.alzforum.org/news/research-news/dynamic-glycosylation-neurons-may-be-linked-memory-pathology
Keratan sulfate: an up-to-date review.Keratan sulfate: an up-to-date review.
Keratan sulfate (KS) is a glycosaminoglycan (GAG) type consisted of a sulfated poly-N-acetyl lactosamine chain. Besides acting as a constitutive molecule of the extracellular matrices, this GAG also plays a role as a hydrating and signaling agent in
http://www.biomedsearch.com/nih/Keratan-sulfate-up-to-date/25179279.html
Histone H2B (S112) PAb - GlycoScientificHistone H2B (S112) PAb - GlycoScientific
Rabbit polyclonal antibody to human Histone H2B (H2B, NP_001019770.1). GS0021 binds to histone H2B regardless of the presence of an O-GlcNAc on serine 112 (S112). Amino acid sequence of the region flanking S112 suggests cross-reactivity with histone H2B of multiple species including mouse, rat, chicken, hamster and pri
https://www.glycoscientific.com/products/histone-h2b-s112-pab
LectinLectin
Wheat germ agglutinin (WGA) is one of the most widely used lectins in cell biology. The receptor sugar for WGA is N-acetylglucosamine, with preferential binding to dimers and trimers of this sugar. WGA can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures which are common to many serum and membrane glycoproteins. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA has also been reported to interact with some glycoproteins via sialic acid residues (see succinylated WGA). ...
https://au.mpbio.com/life-sciences/immunology/proteins-enzymes/lectin
Global (US, EU, Japan & China) N-Acetyl-D-Glucosamine (CAS 7512-17-6) Industry Supply and Consumption 2016 to 2021 Market...Global (US, EU, Japan & China) N-Acetyl-D-Glucosamine (CAS 7512-17-6) Industry Supply and Consumption 2016 to 2021 Market...
Global (US, EU, Japan & China) N-Acetyl-D-Glucosamine (CAS 7512-17-6) Industry Supply and Consumption 2016 to 2021 Market Research Report
https://www.newsmaker.com.au/news/49714/global-us-eu-japan-china-nacetyldglucosamine-cas-7512176-industry-supply-and-consumption-2016-to-2021-market-research-report
Rapid myoglobin aggregation through... | ERARapid myoglobin aggregation through... | ERA
The extent of glycation and conformational changes of horse myoglobin (Mb) upon glycation with N-acetyl-glucosamine (GlcNAc), glucose...
https://era.library.ualberta.ca/items/86c27fd1-f581-440e-930c-27cd7ff1c81d
Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents...Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents...
X-MOL提供的期刊论文更新，Proceedings of the National Academy of Sciences of the United States of America--Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents hyperglycemia [Physiology]，Tandrika Chattopadhyay, Babukrishna Maniyadath, Hema P. Bagul, Arindam Chakraborty, Namrata Shukla, Srikanth Budnar, Abinaya Rajendran, Arushi Shukla, Siddhesh S. Kamat, Ullas Kolthur-Seetharam
https://www.x-mol.com/paper/1243046918234771456
RCSB PDB - 1W3B: The superhelical TPR domain of O-linked GlcNAc transferase reveals structural similarities to importin alpha.RCSB PDB - 1W3B: The superhelical TPR domain of O-linked GlcNAc transferase reveals structural similarities to importin alpha.
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
http://www.rcsb.org/structure/1W3B
Journal News: JBC: Probing beneath the surfaceJournal News: JBC: Probing beneath the surface
In 2014, Gerald Hart, an associate editor for the Journal of Biological Chemistry, organized a thematic minireview series on O-GlcNAcylation. O-GlcNAc is found on many different proteins throughout the cell. Its function varies dependent upon the protein to which it is attached. Much like phosphorylation, one known purpose of O-GlcNAc is to control signaling in response to nutrients. Holt, who is now the chief science officer at NorthShore Bio, describes O-GlcNAc as an orthogonal method of regulating the same proteins: Its like a rivet: If theres a carbohydrate at a phosphorylation site, then that phosphorylation site is no longer regulated by classical phosphorylation pathways. Instead, it becomes regulated by the O-GlcNAc regulatory pathways.. Methods for studying phosphorylation have advanced rapidly in recent years, thanks in part to the existence of site-specific antibodies, while methods for studying O-GlcNAc continue to lag behind. Researchers only recently have begun to recognize the ...
http://www.asbmb.org/asbmbtoday/201604/JournalNews/JBCHart/
O-GlcNAcase/OGA/MGEA5 Antibody (1C7) (H00010724-M02): Novus BiologicalsO-GlcNAcase/OGA/MGEA5 Antibody (1C7) (H00010724-M02): Novus Biologicals
Mouse Monoclonal Anti-O-GlcNAcase/OGA/MGEA5 Antibody (1C7). Validated: WB, ELISA, ICC/IF. Tested Reactivity: Human. 100% Guaranteed.
https://www.novusbio.com/products/o-glcnacase-oga-mgea5-antibody-1c7_h00010724-m02
Study finds low sugar metabolite associates with disability, neurodegeneration in MSStudy finds low sugar metabolite associates with disability, neurodegeneration in MS
Irvine, CA - May 13, 2021 - A new University of California, Irvine-led study finds low serum levels of the sugar N-acetylglucosamine (GlcNAc), is associated wit
https://clinicalnews.org/2021/05/13/study-finds-low-sugar-metabolite-associates-with-disability-neurodegeneration-in-ms/
GLC 2000 - ProgressiveHealth.comGLC 2000 - ProgressiveHealth.com
GLC 2000 uses high-strength and multiple forms of glucosamine. Find out what advantages this combination of the 4 forms of glucosamine give GLC 2000.
http://www.progressivehealth.com/glc-2000.htm
GlycoproteinGlycoprotein
N-Acetylglucosamine Aminohexose GlcNAc N-Acetylneuraminic acid Aminononulosonic acid. (Sialic acid) NeuNAc ...
https://en.wikipedia.org/wiki/Glycoprotein
N-acetyl-D-glucosamine kinaseN-acetyl-D-glucosamine kinase
N-acetylglucosamine kinase (NAGK; EC 2.7.1.59) converts endogenous N-acetylglucosamine (GlcNAc), a major component of complex ... "Structures of human N-Acetylglucosamine kinase in two complexes with N-Acetylglucosamine and with ADP/glucose: insights into ... "N-acetylglucosamine kinase and N-acetylglucosamine 6-phosphate deacetylase in normal human erythrocytes and Plasmodium ... "Entrez Gene: NAGK N-acetylglucosamine kinase". Ligos JM, de Lera TL, Hinderlich S, Guinea B, Sánchez L, Roca R, Valencia A, ...
https://en.wikipedia.org/wiki/N-acetyl-D-glucosamine_kinase
GlucosamineGlucosamine
"UDP-N-acetylglucosamine Biosynthesis". Recommendations of the Nomenclature Committee of the International Union of Biochemistry ... The end-product of this pathway is uridine diphosphate N-acetylglucosamine (UDP-GlcNAc), which is then used for making ... The intravenous use of a combination of N-acetylglucosamine, pentosan polysulfate and sodium hyaluronate in horses with ... and N-acetylglucosamine. Of the three commonly available forms of glucosamine, only glucosamine sulfate is given a "likely ...
https://en.wikipedia.org/wiki/Glucosamine
Louise JohnsonLouise Johnson
Johnson, Louise Napier (1965). An X-ray crystallographic study of N-acetylglucosamine and its relation to lysozyme. london.ac. ... Johnson, L. N.; Phillips, D. C. (1964). "Crystal Structure of N-Acetylglucosamine". Nature. 202 (4932): 588. Bibcode:1964Natur. ... N-Acetylglucosamine, using x-ray diffraction, which she solved within a year. She then moved onto the study of the substrate ...
https://en.wikipedia.org/wiki/Louise_Johnson
GlycanGlycan
First, two N-acetylglucosamine residues are attached to dolichol monophosphate, a lipid, on the external side of the ... A Core 2 structure is generated by the addition of N-acetyl-glucosamine to the N-acetyl-galactosamine of the Core 1 structure. ... Core 3 structures are generated by the addition of a single N-acetyl-glucosamine to the original N-acetyl-galactosamine. Core 4 ... These are formed by the repetitive addition of galactose and N-acetyl-glucosamine units. Polylactosamine chains on O-linked ...
https://en.wikipedia.org/wiki/Glycan
OligosaccharyltransferaseOligosaccharyltransferase
The sugar Glc3Man9GlcNAc2 (where Glc=Glucose, Man=Mannose, and GlcNAc=N-acetylglucosamine) is attached to an asparagine (Asn) ...
https://en.wikipedia.org/wiki/Oligosaccharyltransferase
P110αP110α
Phosphatidylinositol-4,5-bisphosphate 3-kinase (also called phosphatidylinositol 3-kinase (PI3K)) is composed of an 85 kDa regulatory subunit and a 110 kDa catalytic subunit. The protein encoded by this gene represents the catalytic subunit, which uses ATP to phosphorylate phosphatidylinositols (PtdIns), PtdIns4P and PtdIns(4,5)P2.[7] The involvement of p110α in human cancer has been hypothesized since 1995. Support for this hypothesis came from genetic and functional studies, including the discovery of common activating PIK3CA missense mutations in common human tumors.[8] It has been found to be oncogenic and is implicated in cervical cancers.[9] PIK3CA mutations are present in over one-third of breast cancers, with enrichment in the luminal and in human epidermal growth factor receptor 2-positive subtypes (HER2 +). The three hotspot mutation positions (GLU542, GLU545, and HIS1047) have been widely reported till date.[10] While substantial preclinical data show an association with robust ...
https://en.wikipedia.org/wiki/PIK3CA
Class II PI 3-kinasesClass II PI 3-kinases
... are a subgroup of the enzyme family, phosphoinositide 3-kinase that share a common protein domain structure, substrate specificity and method of activation. Class II PI 3-kinases were the most recently identified class of PI 3-kinases and little is currently known about these enzymes. There are three class II PI 3-kinase isoforms expressed in mammalian cells; ...
https://en.wikipedia.org/wiki/Class_II_PI_3-kinases
Polynucleotide phosphorylasePolynucleotide phosphorylase
... (PNPase) is a bifunctional enzyme with a phosphorolytic 3' to 5' exoribonuclease activity and a 3'-terminal oligonucleotide polymerase activity.[2] That is, it dismantles the RNA chain starting at the 3' end and working toward the 5' end.[1] It also synthesizes long, highly heteropolymeric tails in vivo. It accounts for all of the observed residual polyadenylation in strains of Escherichia coli missing the normal polyadenylation enzyme.[1] Discovered by Marianne Grunberg-Manago working in Severo Ochoa's lab in 1955, the RNA-polymerization activity of PNPase was initially believed to be responsible for DNA-dependent synthesis of messenger RNA, a notion that got disproved by the late 1950s.[3][4] It is involved in mRNA processing and degradation in bacteria, plants,[5] and in humans.[6] In humans, the enzyme is encoded by the PNPT1 gene. In its active form, the protein forms a ring structure consisting of three PNPase molecules. Each PNPase molecule consists of two ...
https://en.wikipedia.org/wiki/Polynucleotide_phosphorylase
Uridine kinaseUridine kinase
Thus, the two substrates of this enzyme are ATP and uridine, whereas its two products are ADP and UMP. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:uridine 5'-phosphotransferase. Other names in common use include pyrimidine ribonucleoside kinase, uridine-cytidine kinase, uridine kinase (phosphorylating), and uridine phosphokinase. This enzyme participates in pyrimidine metabolism. ...
https://en.wikipedia.org/wiki/Uridine_kinase
GalacturonokinaseGalacturonokinase
Thus, the two substrates of this enzyme are ATP and D-galacturonate, whereas its two products are ADP and 1-phospho-alpha-D-galacturonate. This enzyme belongs to the family of transferases, specifically those transferring phosphorus-containing groups (phosphotransferases) with an alcohol group as acceptor. The systematic name of this enzyme class is ATP:D-galacturonate 1-phosphotransferase. This enzyme is also called galacturonokinase (phosphorylating) D-galacturonic acid kinase. This enzyme participates in nucleotide sugars metabolism. ...
https://en.wikipedia.org/wiki/Galacturonokinase
GlycosaminoglycanGlycosaminoglycan
The repeating unit (except for keratan) consists of an amino sugar (N-acetylglucosamine or N-acetylgalactosamine) along with a ...
https://en.wikipedia.org/wiki/Glycosaminoglycan
Taq polymeraseTaq polymerase
ˈpɒlɪməreɪz/ is a thermostable DNA polymerase named after the thermophilic bacterium Thermus aquaticus from which it was originally isolated by Chien et al. in 1976.[1] Its name is often abbreviated to Taq Pol or simply Taq. It is frequently used in the polymerase chain reaction (PCR), a method for greatly amplifying the quantity of short segments of DNA. T. aquaticus is a bacterium that lives in hot springs and hydrothermal vents, and Taq polymerase was identified[1] as an enzyme able to withstand the protein-denaturing conditions (high temperature) required during PCR.[2] Therefore, it replaced the DNA polymerase from E. coli originally used in PCR.[3] Taq's optimum temperature for activity is 75-80 °C, with a half-life of greater than 2 hours at 92.5 °C, 40 minutes at 95 °C and 9 minutes at 97.5 °C, and can replicate a 1000 base pair strand of DNA in less than 10 seconds at 72 °C.[4] At 75-80 °C, Taq reaches its optimal polymerization rate of about 150 nucleotides per second per ...
https://en.wikipedia.org/wiki/Taq_polymerase
Creatine kinaseCreatine kinase
The mitochondrial creatine kinase (CKm) is present in the mitochondrial intermembrane space, where it regenerates phosphocreatine (PCr) from mitochondrially generated ATP and creatine (Cr) imported from the cytosol. Apart from the two mitochondrial CK isoenzyme forms, that is, ubiquitous mtCK (present in non-muscle tissues) and sarcomeric mtCK (present in sarcomeric muscle), there are three cytosolic CK isoforms present in the cytosol, depending on the tissue. Whereas MM-CK is expressed in sarcomeric muscle, that is, skeletal and cardiac muscle, MB-CK is expressed in cardiac muscle, and BB-CK is expressed in smooth muscle and in most non-muscle tissues. Mitochondrial mtCK and cytosolic CK are connected in a so-called PCr/Cr-shuttle or circuit. PCr generated by mtCK in mitochondria is shuttled to cytosolic CK that is coupled to ATP-dependent processes, e.g. ATPases, such as acto-myosin ATPase and calcium ATPase involved in muscle contraction, and sodium/potassium ATPase involved in sodium ...
https://en.wikipedia.org/wiki/Creatine_kinase
NeuraminidaseNeuraminidase
... inhibitors are useful for combating influenza infection: zanamivir, administered by inhalation; oseltamivir, administered orally; peramivir administered parenterally, that is through intravenous or intramuscular injection; and laninamivir which is in phase III clinical trials. There are two major proteins on the surface of influenza virus particles. One is the lectin haemagglutinin protein with three relatively shallow sialic acid-binding sites and the other is enzyme sialidase with the active site in a pocket. Because of the relative deep active site in which low-molecular-weight inhibitors can make multiple favorable interactions and approachable methods of designing transition-state analogues in the hydrolysis of sialosides, the sialidase becomes more attractive anti-influenza drug target than the haemagglutinin.[9] After the X-ray crystal structures of several influenza virus sialidases were available, the structure-based inhibitor design was applied to discover potent ...
https://en.wikipedia.org/wiki/Neuraminidase
RNA polymeraseRNA polymerase
... then starts to synthesize the initial DNA-RNA heteroduplex, with ribonucleotides base-paired to the template DNA strand according to Watson-Crick base-pairing interactions. As noted above, RNA polymerase makes contacts with the promoter region. However these stabilizing contacts inhibit the enzyme's ability to access DNA further downstream and thus the synthesis of the full-length product. In order to continue RNA synthesis, RNA polymerase must escape the promoter. It must maintain promoter contacts while unwinding more downstream DNA for synthesis, "scrunching" more downstream DNA into the initiation complex.[14] During the promoter escape transition, RNA polymerase is considered a "stressed intermediate." Thermodynamically the stress accumulates from the DNA-unwinding and DNA-compaction activities. Once the DNA-RNA heteroduplex is long enough (~10 bp), RNA polymerase releases its upstream contacts and effectively achieves the promoter escape transition into the elongation phase. ...
https://en.wikipedia.org/wiki/RNA_Polymerase
RNA polymerase II holoenzymeRNA polymerase II holoenzyme
RNAPII can exist in two forms: RNAPII0, with a highly phosphorylated CTD, and RNAPIIA, with a nonphosphorylated CTD.[16] Phosphorylation occurs principally on Ser2 and Ser5 of the repeats, although these positions are not equivalent. The phosphorylation state changes as RNAPII progresses through the transcription cycle: The initiating RNAPII is form IIA, and the elongating enzyme is form II0. While RNAPII0 does consist of RNAPs with hyperphosphorylated CTDs, the pattern of phosphorylation on individual CTDs can vary due to differential phosphorylation of Ser2 versus Ser5 residues and/or to differential phosphorylation of repeats along the length of the CTD.[16] The PCTD (phosphoCTD of an RNAPII0) physically links pre-mRNA processing to transcription by tethering processing factors to elongating RNAPII, e.g., 5′-end capping, 3′-end cleavage, and polyadenylation.[16] Ser5 phosphorylation (Ser5PO4) near the 5′ ends of genes depends principally on the kinase activity of TFIIH (Kin28 in yeast; ...
https://en.wikipedia.org/wiki/RNA_polymerase_II_holoenzyme
Serine/threonine-specific protein kinaseSerine/threonine-specific protein kinase
While serine/threonine kinases all phosphorylate serine or threonine residues in their substrates, they select specific residues to phosphorylate on the basis of residues that flank the phosphoacceptor site, which together comprise the consensus sequence. Since the consensus sequence residues of a target substrate only make contact with several key amino acids within the catalytic cleft of the kinase (usually through hydrophobic forces and ionic bonds), a kinase is usually not specific to a single substrate, but instead can phosphorylate a whole "substrate family" which share common recognition sequences. While the catalytic domain of these kinases is highly conserved, the sequence variation that is observed in the kinome (the subset of genes in the genome that encode kinases) provides for recognition of distinct substrates. Most kinases are inhibited by a pseudosubstrate that binds to the kinase like a real substrate but lacks the amino acid to be phosphorylated. When the pseudosubstrate is ...
https://en.wikipedia.org/wiki/Non-specific_serine/threonine_protein_kinase
UAP1UAP1
Mio T, Yabe T, Arisawa M, Yamada-Okabe H (Jul 1998). "The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, ...
https://en.wikipedia.org/wiki/UAP1
Glycoprotein 3-alpha-L-fucosyltransferaseGlycoprotein 3-alpha-L-fucosyltransferase
The systematic name of this enzyme class is GDP-L-fucose:glycoprotein (L-fucose to asparagine-linked N-acetylglucosamine of N4 ... The difucosylation of asparagine-bound N-acetylglucosamine". Eur. J. Biochem. 199 (3): 745-51. doi:10.1111/j.1432-1033.1991. ... N-acetylglucosamine of, 4-N-{N-acetyl-beta-D-glucosaminyl-(1->2)-alpha-D-mannosyl-(1->3)-[N-, acetyl-beta-D-glucosaminyl-(1->2 ... beta-N-acetylglucosamine (Fuc to (Fuc alpha 1--6GlcNAc)-Asn-peptide)alpha 1--3-fucosyltransferase activity in honeybee (Apis ...
https://en.wikipedia.org/wiki/Glycoprotein_3-alpha-L-fucosyltransferase
CollectinCollectin
MBL can recognize peptidoglykan via N-acetylglucosamine. This interaction leads to inhibition of ligand-induced inflammatory by ... "Mannose-binding lectin recognizes peptidoglycan via the N-acetyl glucosamine moiety, and inhibits ligand-induced ...
https://en.wikipedia.org/wiki/Collectin
SGSHSGSH
... and N-acetylglucosamine 6-sulfatase (type D; MIM 252940). The Sanfilippo syndrome is characterized by severe central nervous ...
https://en.wikipedia.org/wiki/SGSH
N-AcetylgalactosamineN-Acetylgalactosamine
Galactosamine Globoside (N-Acetylglucosamine) GlcNAc Donald M. Marcus; Elvin A. Kabat; Gerald Schiffman (1964). "Immunochemical ...
https://en.wikipedia.org/wiki/N-Acetylgalactosamine
N-AcetylmannosamineN-Acetylmannosamine
By base catalysed epimerization of N-acetyl glucosamine. By rhodium (II)-catalyzed oxidative cyclization of glucal 3-carbamates ... in a commercial process from N-acetylglucosamine. There is normally some level of glycan sialylation within a glycoprotein, but ...
https://en.wikipedia.org/wiki/N-Acetylmannosamine
GNPTGGNPTG
... ("N-acetylglucosamine-1-phosphate transferase, gamma subunit.") is a gene in the human body. It is one of three genes ... also called N-acetylglucosamine-1-phosphate transferase). This enzyme is made up of two alpha (α), two beta (β), and two gamma ...
https://en.wikipedia.org/wiki/GNPTG
N-Acetylmuramic acidN-Acetylmuramic acid
MurNAc is a monosaccharide derivative of N-acetylglucosamine. NAM is a combination of N-acetylglucosamine and ... MurNAc is covalently linked to N-acetylglucosamine and may also be linked through the hydroxyl on carbon number 4 to the carbon ... N-Acetylmuramic acid, "NAM" or MurNAc, is the addition of phosphoenolpyruvate and N-acetylglucosamine with the chemical formula ... which is built from alternating units of N-acetylglucosamine (GlcNAc) and N-acetylmuramic acid (MurNAc), cross-linked by ...
https://en.wikipedia.org/wiki/N-Acetylmuramic_acid
N-acetylgalactosamine-4-sulfataseN-acetylgalactosamine-4-sulfatase
This enzyme also acts on N-acetylglucosamine 4-sulfate. Arylsulfatase B Farooqui AA (October 1976). "The desulphation of ...
https://en.wikipedia.org/wiki/N-acetylgalactosamine-4-sulfatase
UDP-glucose 4-epimeraseUDP-glucose 4-epimerase
Accommodation of UDP-N-acetylglucosamine within the active site". J. Biol. Chem. 276 (18): 15131-6. doi:10.1074/jbc.M100220200 ... from UDP-N-acetylglucosamine (UDP-GlcNAc) in the presence of NAD+, an initial step in glycoprotein or glycolipid synthesis. Dr ...
https://en.wikipedia.org/wiki/UDP-glucose_4-epimerase
Paenibacillus tylopiliPaenibacillus tylopili
It lacks the ability to break down N-acetylglucosamine. Kuisiene N, Raugalas J, Spröer C, Kroppenstedt RM, Stuknyte M, ...
https://en.wikipedia.org/wiki/Paenibacillus_tylopili
Poly(ribitol-phosphate) N-acetylglucosaminyl-transferasePoly(ribitol-phosphate) N-acetylglucosaminyl-transferase
Other names in common use include UDP acetylglucosamine-poly(ribitol phosphate), acetylglucosaminyltransferase, uridine ... Nathenson SG, Ishimoto N, Strominger JL (1966). "UDP-N-acetylglucosamine:polyribitol phosphate N-acetylglucosaminyltransferases ...
https://en.wikipedia.org/wiki/Poly(ribitol-phosphate)_N-acetylglucosaminyl-transferase
N-Acetylglucosamine - WikipediaN-Acetylglucosamine - Wikipedia
N-Acetylglucosamine (GlcNAc) is an amide derivative of the monosaccharide glucose. It is a secondary amide between glucosamine ... O-GlcNAcylation is the process of adding a single N-acetylglucosamine sugar to the serine or threonine of a protein.[4] ... Comparable to phosphorylation, addition or removal of N-acetylglucosamine is a means of activating or deactivating enzymes or ... "Inhibition of elastase enzyme release from human polymorphonuclear leukocytes by N-acetyl-galactosamine and N-acetyl-glucosamine ...
https://en.wikipedia.org/wiki/N-acetylglucosamine
EWG Skin Deep® | What is ACETYL GLUCOSAMINEEWG Skin Deep® | What is ACETYL GLUCOSAMINE
2-ACETAMIDO-2-DEOXY-D-GLUCOSE; N-ACETYLGLUCOSAMINE, ACETAMIDO-2-DEOXY- ALPHA-D- GLUCOPYRANOSE, ACETAMIDO-2-DEOXYGLUCOSE, ACETYL ...
https://www.ewg.org/skindeep/ingredients/700084-ACETYL_GLUCOSAMINE/
N-Acetylglucosamine receptor - WikipediaN-Acetylglucosamine receptor - Wikipedia
The N-Acetylglucosamine receptor is a receptor which binds N-Acetylglucosamine. The N-Acetylglucosamine (GlcNAc) receptor has ... N-Acetylglucosamine+Receptor at the US National Library of Medicine Medical Subject Headings (MeSH) v t e. ... "Targeted gene delivery via N-acetylglucosamine receptor mediated endocytosis". Journal of Nanoscience and Nanotechnology. 14 ( ...
https://en.wikipedia.org/wiki/N-Acetylglucosamine_receptor
N-Acetyl Glucosamine - iHerb.comN-Acetyl Glucosamine - iHerb.com
Categories Supplements Amino Acids N-Acetyl Glucosamine N-Acetyl Glucosamine 2 Results (showing 1 - 2 ) ...
https://www.iherb.com/c/N-Acetyl-Glucosamine
Products That Contain ACETYL GLUCOSAMINE || Skin Deep® Cosmetics Database | EWGProducts That Contain ACETYL GLUCOSAMINE || Skin Deep® Cosmetics Database | EWG
Products Containing Acetyl Glucosamine by InstaNatural FILTERS Sort by. Best to worst. Worst to best. Alphabetical A-Z. ...
https://www.ewg.org/skindeep/browse/ingredients/700084ACETYL_GLUCOSAMINE/?brand=InstaNatural&category=&ingredient_id=700084ACETYL_GLUCOSAMINE
UDP-N-acetylglucosamine 2-epimerase domain (IPR003331) | InterPro | EMBL-EBIUDP-N-acetylglucosamine 2-epimerase domain (IPR003331) | InterPro | EMBL-EBI
UDP-N-acetylglucosamine 2-epimerase domain (IPR003331). Short name: UDP_GlcNAc_Epimerase_2_dom ... This entry represents a domain found in the bacterial UDP-N-acetylglucosamine 2-epimerase WecB, which is involved in the ... which has both the UDP-N-acetylglucosamine 2-epimerase and the N-acetylmannosamine kinase functions. GNE catalyses the first ...
http://www.ebi.ac.uk/interpro/entry/IPR003331
N-Acetyl Glucosamine (Nag): Uses, Side Effects, Interactions, Dosage, and WarningN-Acetyl Glucosamine (Nag): Uses, Side Effects, Interactions, Dosage, and Warning
Medications for cancer (Chemotherapy) interacts with N-ACETYL GLUCOSAMINE (NAG). There is some concern that N-acetyl ... Chitosan is a form of N-acetyl glucosamine that has been chemically altered.. N-acetyl glucosamine is used for osteoarthritis, ... N-ACETYL GLUCOSAMINE (NAG). OTHER NAME(S): 2-Acetamido-2-deoxyglucose, Acetylglucosamine, Acétylglucosamine, GlcNAc, ... When applied to the skin: N-acetyl glucosamine is POSSIBLY SAFE when used for up to 10 weeks.. When given as an enema (rectally ...
https://www.webmd.com/vitamins/ai/ingredientmono-619/n-acetyl-glucosamine-nag
Topical composition comprising n-acetyl glucosamine - YU RUEY JTopical composition comprising n-acetyl glucosamine - YU RUEY J
4. Effect of N-acetyl-glucosamine on skin. A female subject, age 74, applied topically twice daily 10% N-acetyl-glucosamine ... The white cream thus formulated contained 10% N-acetyl-glucosamine. N-Acetyl-glucosamine 1% or 5% cream was formulated in the ... A male subject, age 66, who had xerosis and dry skin on lower legs topically applied twice daily 5% N-acetyl-glucosamine cream ... 7. A water-containing composition comprising N-acetyl-glucosamine as isomeric or non-isomeric form thereof and a vitamin in a ...
https://www.freepatentsonline.com/EP2311452A1.html
Side Effects of N-Acetylglucosamine | Livestrong.comSide Effects of N-Acetylglucosamine | Livestrong.com
N-acetylglucosamine supplements are generally considered safe. Minor side effects occur uncommonly and serious side effects are ... N-acetylglucosamine (NAG) is an amino sugar, a derivative of the simple sugar glucose. Your body produces NAG, which serves as ... Side Effects of N-Acetylglucosamine Dr. Tina M. St. John , updated on April 29, 2018 ... N-Acetyl glucosamine is one of the forms of glucosamine. (Image: Farion_O/iStock/GettyImages) ...
https://www.livestrong.com/article/295135-the-side-effects-of-n-acetyl-glucosamine/
β-N-acetylglucosamine (O-GlcNAc) is part of the histone code | PNASβ-N-acetylglucosamine (O-GlcNAc) is part of the histone code | PNAS
β-N-acetylglucosamine (O-GlcNAc) is part of the histone code. Kaoru Sakabe, Zihao Wang, and Gerald W. Hart ... O-Linked N-Acetylglucosamine (O-GlcNAc) Transferase and O-GlcNAcase Interact with Mi2{beta} Protein at the A{gamma}-Globin ... O-Linked N-acetylglucosamine transferase 1 regulates global histone H4 acetylation via stabilization of the nonspecific lethal ... O-Linked N-Acetylglucosamine (O-GlcNAc) Expression Levels Epigenetically Regulate Colon Cancer Tumorigenesis by Affecting the ...
https://www.pnas.org/content/107/46/19915/tab-figures-data
OGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens (human)] - Gene - NCBIOGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens (human)] - Gene - NCBI
O-linked N-acetylglucosamine (GlcNAc) transferase (UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase). O- ... UDP-N-acetylglucosamine:polypeptide-N-acetylglucosaminyl transferase. uridinediphospho-N-acetylglucosamine:polypeptide beta-N- ... OGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens] OGT O-linked N-acetylglucosamine (GlcNAc) transferase [ ... O-linked N-acetylglucosamine (GlcNAc) transferaseprovided by HGNC. Primary source. HGNC:HGNC:8127 See related. Ensembl: ...
https://www.ncbi.nlm.nih.gov/gene/8473
Marine Drugs | Free Full-Text | N-Acetylglucosamine: Production and ApplicationsMarine Drugs | Free Full-Text | N-Acetylglucosamine: Production and Applications
N-Acetylglucosamine (GlcNAc) is a monosaccharide that usually polymerizes linearly through (1,4)-β-linkages. GlcNAc is the ... Keywords: N-acetylglucosamine; chitin; carbohydrateN-acetylglucosamine; chitin; carbohydrate N-acetylglucosamine; chitin; ... N-Acetylglucosamine (GlcNAc) is a monosaccharide that usually polymerizes linearly through (1,4)-β-linkages. GlcNAc is the ... Chen, J.-K.; Shen, C.-R.; Liu, C.-L. N-Acetylglucosamine: Production and Applications. Mar. Drugs 2010, 8, 2493-2516. ...
http://www.mdpi.com/1660-3397/8/9/2493
RCSB PDB - 2JF2: Nucleotide substrate binding by UDP-N-acetylglucosamine acyltransferaseRCSB PDB - 2JF2: Nucleotide substrate binding by UDP-N-acetylglucosamine acyltransferase
ACYL-[ACYL-CARRIER-PROTEIN]--UDP-N-ACETYLGLUCOSAMINE O-ACYLTRANSFERASE. A. 264. Escherichia coli. Mutation(s): 0 EC: 2.3.1.129 ... UDP-N-acetylglucosamine acyltransferase (LpxA) initiates lipid A biosynthesis by catalyzing the transfer of R-3-hydroxymyristic ... UDP-N-acetylglucosamine acyltransferase (LpxA) initiates lipid A biosynthesis by catalyzing the transfer of R-3-hydroxymyristic ... Nucleotide Substrate Recognition by Udp-N-Acetylglucosamine Acyltransferase (Lpxa) in the First Step of Lipid a Biosynthesis.. ...
https://www.rcsb.org/structure/2jf2
Acetyl Glucosamine | Technology TrendsAcetyl Glucosamine | Technology Trends
Acetyl Glucosamine. Some articles on acetyl, glucosamine:. Lactosylceramide 1,3-N-acetyl-beta-D-glucosaminyltransferase. ... ... acetyl-glucosamine to the N-acetyl-galactosamine of the Core 1 structure ... are generated by the addition of a single N-acetyl ...
http://www.primidi.com/acetyl_glucosamine
Nutricology, N-Acetyl Glucosamine, 90 Vegetarian Capsules - iHerb.comNutricology, N-Acetyl Glucosamine, 90 Vegetarian Capsules - iHerb.com
N-Acetyl Glucosamine (NAG). Although research suggests that glucosamine sulfate is better absorbed than NAG, individuals ...
https://www.iherb.com/pr/Nutricology-N-Acetyl-Glucosamine-90-Vegetarian-Capsules/24558
Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase (IPR005882) | InterPro |...Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase (IPR005882) | InterPro |...
N-Acetylglucosamine-1-PO(4) uridyltransferase (GlmU, EC:2.7.7.23) is a trimeric bifunctional enzyme that catalyzes the last two ... Bifunctional UDP-N-acetylglucosamine pyrophosphorylase/glucosamine-1-phosphate N-acetyltransferase (IPR005882). Short name: ... GO:0003977 UDP-N-acetylglucosamine diphosphorylase activity GO:0019134 glucosamine-1-phosphate N-acetyltransferase activity GO: ...
https://www.ebi.ac.uk/interpro/entry/IPR005882
Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase. - PubMed - NCBIAlloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase. - PubMed - NCBI
Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase.. Konrad RJ1, Zhang F, Hale JE, Knierman MD, ... We have previously shown that diabetogenic antibiotic streptozotocin (STZ), an analog of N-acetylglucosamine (GlcNAc), inhibits ...
https://www.ncbi.nlm.nih.gov/pubmed/12054585?dopt=Abstract
N-Acetyl Glucosamine, 90 capsN-Acetyl Glucosamine, 90 caps
N-Acetyl Glucosamine (NAG) differs from glucosamine sulfate in that it is attached to an acetic acid molecule, while ...
http://www.herbalremedies.com/n-acetyl-glucosamine.html
N-acetylglucosamine-1-phosphotransferase, gamma subunit Biomolecules | BiocompareN-acetylglucosamine-1-phosphotransferase, gamma subunit Biomolecules | Biocompare
Compare N-acetylglucosamine-1-phosphotransferase, gamma subunit Biomolecules from leading suppliers on Biocompare. View ... N-Acetylglucosamine-1-Phosphate Transferase, gamma Subunit (GNPTG) (AA 25-307) protein (His tag) ... Your search returned 5 N-acetylglucosamine-1-phosphotransferase, gamma subunit Biomolecules across 4 suppliers. ...
https://www.biocompare.com/pfu/110875/soids/2185116/Biomolecules/N-acetylglucosamine-1-phosphotransferase_gamma_subunit
Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739)Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739)
... to O-Linked N-Acetylglucosamine antibody. Validated in ChIP/Chip, Dot, ICC/IF, IHC-Fr, IP, WB. Clone RL2 referenced in 58 peer- ... Anti-O-Linked N-Acetylglucosamine antibody [RL2] (Alexa Fluor® 488) (ab201993) *Anti-O-Linked N-Acetylglucosamine antibody [RL2 ... Anti-O-Linked N-Acetylglucosamine antibody [RL2]. See all O-Linked N-Acetylglucosamine primary antibodies. ... All lanes : Anti-O-Linked N-Acetylglucosamine antibody [RL2] (ab2739) at 1 µg/ml. Lanes 1 & 3 : Jurkat cells treated with 0 uM ...
https://www.abcam.com/o-linked-n-acetylglucosamine-antibody-rl2-ab2739.html
rfbC - UDP-N-acetylglucosamine 2-epimerase - Salmonella borreze - rfbC gene & proteinrfbC - UDP-N-acetylglucosamine 2-epimerase - Salmonella borreze - rfbC gene & protein
UDP-N-acetylglucosamine 2-epimerase (EC:5.1.3.14*Search proteins in UniProtKB for this EC number. ... Belongs to the UDP-N-acetylglucosamine 2-epimerase family.Curated. Family and domain databases. Integrated resource of protein ... sp,P52642,RFBC_SALBO UDP-N-acetylglucosamine 2-epimerase OS=Salmonella borreze OX=55400 GN=rfbC PE=3 SV=1 ...
https://www.uniprot.org/uniprot/P52642
RCSB PDB - 1FXJ: CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE Macromolecule Annotations PageRCSB PDB - 1FXJ: CRYSTAL STRUCTURE OF N-ACETYLGLUCOSAMINE 1-PHOSPHATE URIDYLTRANSFERASE Macromolecule Annotations Page
Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for ... UDP-N-ACETYLGLUCOSAMINE PYROPHOSPHORYLASE (1FXJ:A,B) * Magnesium Ion Binding * Udp N Acetylglucosamine Diphosphorylase Activity ... UDP N-Acetylglucosamine Acyltransferase; domain 1 Hexapeptide repeat proteins B1. 1fxjB01. Alpha Beta Alpha-Beta Complex Spore ... N-acetylglucosamine 1-phosphate uridyltransferase GlmU, C- terminal domain Escherichia coli [TaxId: 562] ...
http://www.rcsb.org/pdb/explore/derivedData.do?structureId=1FXJ
Regulation of N-acetylglucosamine Uptake in YeastRegulation of N-acetylglucosamine Uptake in Yeast
The yeasts unable to grow on N-acetylglucosamine lacked the capacity to transport the aminosugar … ... Various yeasts have been investigated for their ability to grow on N-acetylglucosamine as the sole carbon source and only those ... Regulation of N-acetylglucosamine Uptake in Yeast Biochim Biophys Acta. 1979 Oct 19;557(1):248-58. doi: 10.1016/0005-2736(79) ... Various yeasts have been investigated for their ability to grow on N-acetylglucosamine as the sole carbon source and only those ...
https://pubmed.ncbi.nlm.nih.gov/398716/?dopt=Abstract
acetyl glucosamine | Cosmetic Ingredient Dictionary | Paulas Choiceacetyl glucosamine | Cosmetic Ingredient Dictionary | Paula's Choice
Although pure acetyl glucosamine is considered unstable, a synthetic or bio-fermented derivative known as n-acetyl glucosamine ... Acetyl glucosamine is an amino-monosaccharide (simple sugar) and a precursor of hyaluronic acid (meaning it helps skin make ... Acetyl glucosamine has also been shown to be effective in reducing visible discolorations when paired with the B vitamin ... pure acetyl glucosamine is typically derived from shellfish). ...
https://www.paulaschoice.com/ingredient-dictionary/skin-replenishing/acetyl-glucosamine.html
Amdhd2 - N-acetylglucosamine-6-phosphate deacetylase - Rattus norvegicus (Rat) - Amdhd2 gene & proteinAmdhd2 - N-acetylglucosamine-6-phosphate deacetylase - Rattus norvegicus (Rat) - Amdhd2 gene & protein
N-acetylglucosamine-6-phosphate deacetylaseAdd BLAST. 409. Proteomic databases. jPOST - Japan Proteome Standard Repository/ ... N-acetylglucosamine catabolic process Source: GO_Central ,p>Inferred from Biological aspect of Ancestor,/p> ,p>A type of ... N-acetylglucosamine-6-phosphate deacetylaseBy similarity. Manual assertion inferred from sequence similarity toi ... sp,Q5BJY6,NAGA_RAT N-acetylglucosamine-6-phosphate deacetylase OS=Rattus norvegicus OX=10116 GN=Amdhd2 PE=3 SV=2 ...
https://www.uniprot.org/uniprot/Q5BJY6
N-Acetylglucosamine - Lectins - Lectins & Glycobiology Reagents - All ProductsN-Acetylglucosamine - Lectins - Lectins & Glycobiology Reagents - All Products
JavaScript seems to be disabled in your browser. For the best experience on our site, be sure to turn on Javascript in your browser. ...
https://vectorlabs.com/all-products/lectins-glycobiology-reagents/lectins/n-acetylglucosamine.html
Targeting N-acetylglucosamine-bearing polymer-coated liposomes to vascular smooth muscle cells | SpringerLinkTargeting N-acetylglucosamine-bearing polymer-coated liposomes to vascular smooth muscle cells | SpringerLink
Drug delivery system N-acetylglucosamine Lectin Restenosis Vascular smooth muscle cells This is a preview of subscription ... Kobayashi S, Ise H, Takahashi M, Goto M, Akaike T, Ikeda U. Surface coating of bone marrow cells with N-acetylglucosamine for ... Aso S, Ise H, Takahashi M, Kobayashi S, Morimoto H, Izawa A, Goto M, Ikeda U. Effective uptake of N-acetylglucosamine- ... To develop a drug delivery system targeted to injured blood vessels, we examined whether N-acetylglucosamine (GlcNAc)-bearing ...
https://link.springer.com/article/10.1007/s10047-011-0595-3
Source Naturals N-A-G, N-Acetyl Glucosamine at Netrition.com.Source Naturals N-A-G, N-Acetyl Glucosamine at Netrition.com.
Source Naturals N-A-G, N-Acetyl Glucosamine, is an amino sugar (a building block of mucopolysaccharides). It is formed from L- ...
https://www.netrition.com/source_naturals_nag.html
Fred Meyer - Source Naturals N-A-G™ N-Acetyl Glucosamine, 500 mg - 120 TabletsFred Meyer - Source Naturals N-A-G™ N-Acetyl Glucosamine, 500 mg - 120 Tablets
N-A-G, N-acetyl glucosamine, is an amino sugar (the building blocks of mucopolysaccharides). It is formed from L-glutamine and ...
https://www.fredmeyer.com/p/source-naturals-n-a-g-n-acetyl-glucosamine/0002107800222
GlcNAcProteinsSubunitUridine diphosphate N-acetylglucosamineResiduesEnzymeKinaseBeta-N-acetylglucosaminePeptidoglycanPyrophosphorylaseThreonineAntibodyGeneProteinPhosphorylationBindsBacterialBiosynthetic pathwayPathwaysEnolpyruvylUptakeReceptorDerivativePhosphate groupsEscherichiaMonosaccharideGlucoseSequenceActivityProductionForm
GlcNAc33
  • N -Acetylglucosamine (GlcNAc) is an amide derivative of the monosaccharide glucose . (wikipedia.org)
  • The N-Acetylglucosamine (GlcNAc) receptor has been recently found to interact and bind with vimentins at the cell surface. (wikipedia.org)
  • Uridine diphosphate release mechanism in O-N-acetylglucosamine (O-GlcNAc) transferase catalysis. (nih.gov)
  • N -Acetylglucosamine (GlcNAc) is a monosaccharide that usually polymerizes linearly through (1,4)-β-linkages. (mdpi.com)
  • N-Acetylglucosamine-1-PO(4) uridyltransferase (GlmU, EC:2.7.7.23 ) is a trimeric bifunctional enzyme that catalyzes the last two sequential reactions in the de novo biosynthetic pathway for UDP-GlcNAc. (ebi.ac.uk)
  • We have previously shown that diabetogenic antibiotic streptozotocin (STZ), an analog of N-acetylglucosamine (GlcNAc), inhibits the enzyme O-GlcNAc-selective N-acetyl-beta-d-glucosaminidase (O-GlcNAcase) which is responsible for the removal of O-GlcNAc from proteins. (nih.gov)
  • Many cellular proteins, including nuclear pore, oncogene, cytoskeletal, heat shock, viral and transcription regulatory proteins contain single O-linked N-acetylglucosamine (O-GlcNAc) residues attached to serine or threonine residues. (abcam.com)
  • To develop a drug delivery system targeted to injured blood vessels, we examined whether N -acetylglucosamine (GlcNAc)-bearing polymer-coated liposomes (GlcNAc-Ls) are specifically taken up by vascular smooth muscle cells (VSMCs). (springer.com)
  • Your search returned 3 O-linked N-acetylglucosamine (GlcNAc) transferase L homeolog ELISA Kit across 1 supplier. (biocompare.com)
  • N -acetylglucosamine (GlcNAc), the vital signaling molecule controlling the onset of development and antibiotic synthesis in Streptomyces , was found to increase the yields of bleomycins significantly in chemically defined medium. (springer.com)
  • O -Linked N -acetylglucosaminylation ( O -GlcNAcylation) (or O -linked N -acetylglucosamine ( O -GlcNAc)) is an abundant and reversible glycosylation type found within the cytosolic and the nuclear compartments. (mcponline.org)
  • The hexosamine biosynthetic pathway (HBP) generates the substrate for the O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins. (frontiersin.org)
  • Once activated, the HBP generates the sugar nucleotide UDP-N-acetyl-glucosamine (UDP-GlcNAc), which is a substrate for hyaluronan (HA), N-linked glycosylation, and for the O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins ( 17 ). (frontiersin.org)
  • Uridine diphosphate-N-acetylglucosamine (uridine 5'-diphosphate-GlcNAc, or UDP-Glc-NAc) is an acetylated aminosugar nucleotide. (hmdb.ca)
  • UDP-GlcNAc is the donor substrate for modification of nucleocytoplasmic proteins at serine and threonine residues with N-acetylglucosamine (O-GlcNAc). (hmdb.ca)
  • The aim of the present study was to evaluate the anti‑inflammatory effects of citrulline (Cit), glucosamine (GlcN) and N‑acetylglucosamine (GlcNAc) on synovial cells, which are primarily involved in inflammatory joint diseases. (spandidos-publications.com)
  • N-acetylglucosamine (GlcNAc), a derivative of GlcN, exhibits anti-inflammatory and chondroprotective effects in a rat model of OA by reducing IL-6 production, cyclooxygenase expression and type II collagen degradation ( 12-15 ). (spandidos-publications.com)
  • Immunoblot analysis using an antibody generated against human IRS-1 Ser 1011 GlcNAc further confirmed the site of attachment and the identity of the +203.2-Da mass shift as β- N -acetylglucosamine. (mcponline.org)
  • Our study investigated the effect of N-acetylglucosamine (GlcNAc) on the intestinal mucosal barrier function in rats. (banglajol.info)
  • O-linked N -acetylglucosamine (O-GlcNAc) modification has been described in many proteins, including nuclear pore glycoproteins. (portlandpress.com)
  • Uridine diphosphate N-acetylglucosamine (GlcNAc) is the product of the hexosamine biosynthetic pathway and the substrate for O-linked GlcNAc (O-GlcNAc) modification. (molvis.org)
  • As an initial step to identify plant NPC proteins, we examined whether NPC proteins from tobacco are modified by N-acetylglucosamine (GlcNAc). (plantcell.org)
  • Beta-N-acetylglucosamine (O-GlcNAc) is part of the histone code. (semanticscholar.org)
  • Dynamic posttranslational modification of serine and threonine residues of nucleocytoplasmic proteins by β-N-acetylglucosamine (O-GlcNAc) is a regulator of cellular processes such as transcription, signaling, and protein-protein interactions. (semanticscholar.org)
  • In studies on mice, Dr. Michael Demetriou and colleagues with the UC Irvine Center for Immunology found that N-acetylglucosamine (GlcNAc), which is similar but more effective than the widely available glucosamine, inhibited the growth and function of abnormal T-cells that incorrectly direct the immune system to attack specific tissues in the body, such as brain myelin in MS and insulin-producing cells of the pancreas in diabetes. (thisisms.com)
  • To study the effect of short N -acetylglucosamine (GlcNAc) oligosaccharides on the physiology of plants, N-ACETYLGLUCOSAMINYLTRANSFERASE ( NodC ) of Azorhizobium caulinodans was expressed in Arabidopsis ( Arabidopsis thaliana ). (plantphysiol.org)
  • Catalyzes the ATP-dependent phosphorylation of both cell wall (peptidoglycan) amino sugars, N-acetylmuramic acid (MurNAc) and N-acetylglucosamine (GlcNAc), at the 6-hydroxyl group. (mybiosource.com)
  • Also known as N-acetylmuramic acid/N-acetylglucosamine kinase (MurNAc/GlcNAc kinase) (Murein sugar kinase). (mybiosource.com)
  • Antiporter transporting nucleotide sugars such as UDP-N-acetylglucosamine (UDP-GlcNAc), UDP-glucose (UDP-Glc) and GDP-mannose (GDP-Man) pooled in the cytosol into the lumen of the Golgi in exchange for the corresponding nucleosides monophosphates (UMP for UDP-sugars and GMP for GDP-sugars). (mybiosource.com)
  • Structures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA). (escholarship.org)
  • Uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (LpxA) catalyzes a reversible reaction for adding an O-acyl group to the GlcNAc in UDP-GlcNAc in the first step of lipid A biosynthesis. (escholarship.org)
  • O-linked N-acetylglucosamine transferase (OGT), an enzyme used for addition of O-GlcNAc during O-GlcNAcylation, is identified as a key regulator to promote oncogenesis in a feedback mechanism through the stabilization of c-Myc. (peerj.com)
  • Objective: There is increasing evidence that the addition of O-linked N-acetylglucosamine (O-GlcNAc) to proteins plays an important role in cell signaling pathways. (elsevier.com)
Proteins5
  • In Western blot many bands are expected as the O-Linked N-Acetylglucosamine modification can occur on proteins of different sizes. (abcam.com)
  • Hart GW, Housley MP, Slawson C. Cycling of O-linked beta-N-acetylglucosamine on nucleocytoplasmic proteins. (banglajol.info)
  • Plant nuclear pore complex proteins are modified by novel oligosaccharides with terminal N-acetylglucosamine. (plantcell.org)
  • Hyperglycemia, a hallmark of diabetes mellitus, is associated with increased vascular calcification and increased modification of proteins by O-linked N-acetylglucosamine (O-GlcNAcylation). (ahajournals.org)
  • O-Linked beta-N-acetylglucosamine transferase (OGT) levels are highest in the brain, and neurodegenerative disorders such as Alzheimer disease have been shown to involve abnormally phosphorylated key proteins, probably as a result of hypoglycosylation. (antibody-antibodies.com)
Subunit5
  • Your search returned 5 N-acetylglucosamine-1-phosphotransferase, gamma subunit Biomolecules across 4 suppliers. (biocompare.com)
  • 9 We have previously ascribed ML III type C to mutations in the UDP -N- acetylglucosamine-1-phosphotransferase gamma subunit gene (GNPTAG) on chromosome 16p. (bmj.com)
  • We suggest that, although the exact relative frequency of each ML III type is not known, the UDP -N- acetylglucosamine-1-phosphotransferase gamma subunit gene apparently plays a major role in mucolipidosis type III. (bmj.com)
  • A gene on chromosome 12q23.2 that encodes two of three subunit types of the membrane-bound enzyme N-acetylglucosamine-1-phosphotransferase, a heterohexameric complex composed of 2 alpha, 2 beta and 2 gamma subunits. (thefreedictionary.com)
  • This is mostly due to the stabilyty of the standard of the Rat UDP-N-acetylglucosamine--peptide N-acetylglucosaminyltransferase 110 kDa subunit(OGT) ELISA kit. (antibody-antibodies.com)
Uridine diphosphate N-acetylglucosamine1
  • Toxin ζ expression triggers a reversible state of dormancy, diminishes the pool of purine nucleotides, promotes (p)ppGpp synthesis, phosphorylates a fraction of the peptidoglycan precursor uridine diphosphate-N-acetylglucosamine (UNAG), leading to unreactive UNAG-P, induces persistence in a reduced subpopulation, and sensitizes cells to different antibiotics. (mdpi.com)
Residues3
  • This gene encodes a glycosyltransferase that catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. (nih.gov)
  • When developing cotyledons are labeled with [3H]glucosamine and glycopeptides of PHA present in the Golgi complex isolated, the radioactivity can be released as [3H]N-acetylglucosamine by digestion of the glycopeptides with beta-N-acetylglucosaminidase, indicating that the residues are in a terminal position. (rupress.org)
  • Arrival of PHA in the protein bodies is followed by the slow removal of these terminal N-acetylglucosamine residues, resulting in a decrease in the Mr of the modified sidechains. (rupress.org)
Enzyme6
  • Alloxan is an inhibitor of the enzyme O-linked N-acetylglucosamine transferase. (nih.gov)
  • Here we present that stable knock-down of UDP- N -acetylglucosamine 2-epimerase / N -acetylmannosamine kinase ( GNE ), the key enzyme in the sialic acid biosynthetic pathway, dramatically increases incorporation of N -acetylmannosamine analogues into glycoproteins of HEK293 cells . (rsc.org)
  • Detection and characterization of a phospholactoyl-enzyme adduct in the reaction catalyzed by UDP-N-acetylglucosamine enolpyruvoyl transferase, MurZ. (harvard.edu)
  • 3, 4 The UDP -N- acetylglucosamine-1-phosphotransferase enzyme activity is defective in ML III 6 and three complementation groups (A, B, C) have been reported suggesting genetic heterogeneity. (bmj.com)
  • 6, 8 In 1996, Bao et al 9 showed that UDP -N- acetylglucosamine-1-phosphotransferase is a multimeric enzyme made up of three different subunits. (bmj.com)
  • Further, it was demonstrated that the activity of the precursor-producing enzyme UDP-N-acetylglucosamine 4-epimerase, converting UDP-N-acetylglucosamine into UDP-N-acetylgalactosamine, is responsible for the presence of N-acetylgalactosamine in the EPS repeating units of both strains. (hud.ac.uk)
Kinase4
  • It can also be found in the N-terminal region of the mammalian bifunctional protein GNE, which has both the UDP-N-acetylglucosamine 2-epimerase and the N-acetylmannosamine kinase functions. (ebi.ac.uk)
  • Similar results were obtained with Saccharomyces cerevisiae 3059 and some other yeasts which are devoid of N-acetylglucosamine kinase in both uninduced and induced conditions. (nih.gov)
  • Below are the list of possible N-acetylmuramic acid/N-acetylglucosamine kinase products. (mybiosource.com)
  • N-acetylglucosamine kinase [Source:HGNC Sym. (broadinstitute.org)
Beta-N-acetylglucosamine2
  • GENTAUR antibody-antibodies.com The Marketplace for Antibodies : Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain. (antibody-antibodies.com)
  • Ataxin-10 interacts with O-linked beta-N-acetylglucosamine transferase in the brain. (antibody-antibodies.com)
Peptidoglycan2
  • Six of these homologues have been proposed to be peptidoglycan N-acetylglucosamine deacetylases. (pasteur.fr)
  • This is the first biochemical study of bacterial peptidoglycan N-acetylglucosamine deacetylases. (pasteur.fr)
Pyrophosphorylase3
  • A search of the yeast data base for a protein homologous to Escherichia coli UDP-N-acetylglucosamine pyrophosphorylase yielded UAP1 (UDP-N-acetylglucosamine pyrophosphorylase), the Saccharomyces cerevisiae gene for UDP-N-acetylglucosamine pyrophosphorylase. (semanticscholar.org)
  • Crystal structure of the bifunctional N-acetylglucosamine 1-phosphate uridyltransferase from Escherichia coli: a paradigm for the related pyrophosphorylase superfamily. (semanticscholar.org)
  • UDP-N-acetylglucosamine pyrophosphorylase 1. (broadinstitute.org)
Threonine1
  • O-GlcNAcylation is the process of adding a single N -acetylglucosamine sugar to the serine or threonine of a protein. (wikipedia.org)
Antibody1
  • N-Acetylglucosamine antibody LS-C505218 is an AP-conjugated mouse monoclonal antibody to human N-Acetylglucosamine. (lsbio.com)
Gene1
  • Kim SJ, Ise H, Goto M, Komura K, Cho CS, Akaike T. Gene delivery system based on highly specific recognition of surface-vimentin with N -acetylglucosamine immobilized polyethylenimine. (springer.com)
Protein3
  • Also known as UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter (Homolog of Fringe connection protein 1) (HFRC1) (SQV7-like protein) (SQV7L) (Solute carrier family 35 member D2) (UDP-galactose transporter-related protein 8) (UGTrel8). (mybiosource.com)
  • UDP-acetylglucosamine acts as a donor for the first two steps of the N-glycan precursor biosynthesis pathway, and is later used as a substrate for further modifications after the precursor has been attached to the protein. (reactome.org)
  • Transient N-acetylglucosamine in the biosynthesis of phytohemagglutinin: attachment in the Golgi apparatus and removal in protein bodies. (rupress.org)
Phosphorylation1
  • [4] Comparable to phosphorylation , addition or removal of N -acetylglucosamine is a means of activating or deactivating enzymes or transcription factors . (wikipedia.org)
Binds2
  • The N-Acetylglucosamine receptor is a receptor which binds N-Acetylglucosamine. (wikipedia.org)
  • Uranyl acetate (0.01 mM) which binds to cell membrane-associated polyphosphates, inhibited completely the inducible uptake of N-acetylglucosamine. (nih.gov)
Bacterial1
  • This entry represents a domain found in the bacterial UDP-N-acetylglucosamine 2-epimerase WecB, which is involved in the enterobacterial common antigen biosynthesis [ PMID: 2166030 ]. (ebi.ac.uk)
Biosynthetic pathway1
  • Nutrient sensing in mammals is done through the hexosamine biosynthetic pathway (HSP), which produces uridine 5'-diphospho-N-acetylglucosamine (UDP-Glc-NAc) as its end product. (hmdb.ca)
Pathways1
Enolpyruvyl1
  • Adds enolpyruvyl to UDP-N-acetylglucosamine. (rcsb.org)
Uptake3
  • In pathogenic yeasts, two systems of different affinity for substrate were found to operate in the uptake of N-acetylglucosamine. (nih.gov)
  • In glucose-grown Candida albicans cells which are devoid of N-acetylglucosamine enters into the cells as phosphorylated form using a constitutive uptake system. (nih.gov)
  • Furthermore, inhibitors of energy metabolism (arsenate, azide and cyanide), proton conductor (m-chlorocarbonylcyanide phenylhydrazine) and dibenzyl diammonium ion (membrane permeable cation) inhibited the inducible N-acetylglucosamine uptake in C. albicans. (nih.gov)
Receptor2
  • Return to N-Acetylglucosamine receptor . (wikidoc.org)
  • Thus, ASA receives N -acetylglucosamine 1-phosphate groups in a sequential manner at two or more sites located within the secretory route proximal and distal to the site where ASA is retrieved by the KDEL receptor, i.e. proximal to the trans -Golgi. (biochemj.org)
Derivative1
  • N-acetylglucosamine (NAG) is an amino sugar, a derivative of the simple sugar glucose. (livestrong.com)
Phosphate groups2
  • At each of these sites up to two N -acetylglucosamine 1-phosphate groups can be added to a single oligosaccharide. (biochemj.org)
  • The biosynthetic intermediates of the glycoproteins destined for the lysosomal compartments of animal cells contain high-mannose sidechains modified by phosphate groups covered by N-acetylglucosamine that is labile to mild acid treatment. (rupress.org)
Escherichia1
  • A Poly-N-acetylglucosamine-Shiga toxin broad-spectrum conjugate vaccine for Shiga toxin-producing Escherichia coli. (surrey.ac.uk)
Monosaccharide1
  • Structural studies including monosaccharide and phosphate analysis, glycosidase and phosphatase treatments, methylation analysis, and periodate treatment indicated the structure of this compound to be NeuAc alpha 2-6Gal beta 1-4GlcNAc-6-P. This provides the first evidence for the occurrence of N-acetylglucosamine 6-phosphate as an integral component in complex carbohydrates. (nih.gov)
Glucose2
  • Ciszewicz M, Wu G, Tam P, Polubinska A, Breborowicz A. Changes in peritoneal mesothelial cells phenotype after chronic exposure to glucose or N-acetylglucosamine. (banglajol.info)
  • Below are the list of possible UDP-N-acetylglucosamine/UDP-glucose/GDP-mannose transporter products. (mybiosource.com)
Sequence1
  • Labelling experiments, designed to determine the temporal sequence of appearance of N-acetylglucosamine in intracellular free sugar and sugar-phosphate pools, indicated that N-acetylglucosamine first appeared in the cells as pohosphorylated form. (nih.gov)
Activity1
  • The activity of UDP-N-acetylglucosamine 4-epimerase was higher in both S. thermophilus strains than in a non-EPS-producing control strain. (hud.ac.uk)
Production2
  • Liu, C.-L. N -Acetylglucosamine: Production and Applications. (mdpi.com)
  • Chen J-K, Shen C-R, Liu C-L. N -Acetylglucosamine: Production and Applications. (mdpi.com)
Form1
  • Today I just got two jars of Ultimate Glubosamine (n-acetylglucosamine form) in the mail. (thisisms.com)
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