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GlucosamineAcetylglucosamineN-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 ControlBone MatrixMuramic AcidsUridine DiphosphateUridine Diphosphate GlucoseGlucuronosyltransferaseTunicamycinPhosphotransferasesProton-Translocating ATPasesRotationProtein SubunitsIrritable Bowel SyndromeDefecationChinaConstipationBleomycinStreptomycesChromosome WalkingPhleomycinsStreptomyces coelicolorPeplomycinEndoplasmic ReticulumNorethindroneAbstracting and Indexing as TopicFace
GlucosamineAcetylglucosamine: The N-acetyl derivative of glucosamine.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 SugarsXenopsylla: A genus of fleas in the family Pulicidae which includes the species that serves as the primary vector of BUBONIC PLAGUE, Xenopsylla cheopis.Neuraminic AcidsAmidohydrolasesRodenticides: 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.Bone Matrix: Extracellular substance of bone tissue consisting of COLLAGEN fibers, ground substance, and inorganic crystalline minerals and salts.Muramic Acids: Compounds consisting of glucosamine and lactate joined by an ether linkage. They occur naturally as N-acetyl derivatives in peptidoglycan, the characteristic polysaccharide composing bacterial cell walls. (From Dorland, 28th ed)Uridine Diphosphate: A uracil nucleotide containing a pyrophosphate group esterified to C5 of the sugar moiety.Uridine Diphosphate Glucose: A key intermediate in carbohydrate metabolism. Serves as a precursor of glycogen, can be metabolized into UDPgalactose and UDPglucuronic acid which can then be incorporated into polysaccharides as galactose and glucuronic acid. Also serves as a precursor of sucrose lipopolysaccharides, and glycosphingolipids.Glucuronosyltransferase: A family of enzymes accepting a wide range of substrates, including phenols, alcohols, amines, and fatty acids. They function as drug-metabolizing enzymes that catalyze the conjugation of UDPglucuronic acid to a variety of endogenous and exogenous compounds. EC 2.4.1.17.Tunicamycin: An N-acetylglycosamine containing antiviral antibiotic obtained from Streptomyces lysosuperificus. It is also active against some bacteria and fungi, because it inhibits the glucosylation of proteins. Tunicamycin is used as tool in the study of microbial biosynthetic mechanisms.Phosphotransferases: A rather large group of enzymes comprising not only those transferring phosphate but also diphosphate, nucleotidyl residues, and others. These have also been subdivided according to the acceptor group. (From Enzyme Nomenclature, 1992) EC 2.7.Proton-Translocating ATPases: Multisubunit enzymes that reversibly synthesize ADENOSINE TRIPHOSPHATE. They are coupled to the transport of protons across a membrane.Rotation: Motion of an object in which either one or more points on a line are fixed. It is also the motion of a particle about a fixed point. (From McGraw-Hill Dictionary of Scientific and Technical Terms, 4th ed)Protein Subunits: Single chains of amino acids that are the units of multimeric PROTEINS. Multimeric proteins can be composed of identical or non-identical subunits. One or more monomeric subunits may compose a protomer which itself is a subunit structure of a larger assembly.Irritable Bowel Syndrome: A disorder with chronic or recurrent colonic symptoms without a clearcut etiology. This condition is characterized by chronic or recurrent ABDOMINAL PAIN, bloating, MUCUS in FECES, and an erratic disturbance of DEFECATION.Defecation: The normal process of elimination of fecal material from the RECTUM.China: A country spanning from central Asia to the Pacific Ocean.Constipation: Infrequent or difficult evacuation of FECES. These symptoms are associated with a variety of causes, including low DIETARY FIBER intake, emotional or nervous disturbances, systemic and structural disorders, drug-induced aggravation, and infections.Bleomycin: A complex of related glycopeptide antibiotics from Streptomyces verticillus consisting of bleomycin A2 and B2. It inhibits DNA metabolism and is used as an antineoplastic, especially for solid tumors.Streptomyces: A genus of bacteria that form a nonfragmented aerial mycelium. Many species have been identified with some being pathogenic. This genus is responsible for producing a majority of the ANTI-BACTERIAL AGENTS of practical value.Chromosome Walking: A technique with which an unknown region of a chromosome can be explored. It is generally used to isolate a locus of interest for which no probe is available but that is known to be linked to a gene which has been identified and cloned. A fragment containing a known gene is selected and used as a probe to identify other overlapping fragments which contain the same gene. The nucleotide sequences of these fragments can then be characterized. This process continues for the length of the chromosome.Phleomycins: Water-soluble, copper-containing low molecular weight polypeptides obtained from the culture medium of Streptomyces verticillus. They are specific inhibitors of DNA synthesis in bacteria and have been found to act as antitumor agents. They have also been used against rust fungi of plants.Streptomyces coelicolor: A soil-dwelling actinomycete with a complex lifecycle involving mycelial growth and spore formation. It is involved in the production of a number of medically important ANTIBIOTICS.Peplomycin: An antineoplastic agent derived from BLEOMYCIN.Endoplasmic Reticulum: A system of cisternae in the CYTOPLASM of many cells. In places the endoplasmic reticulum is continuous with the plasma membrane (CELL MEMBRANE) or outer membrane of the nuclear envelope. If the outer surfaces of the endoplasmic reticulum membranes are coated with ribosomes, the endoplasmic reticulum is said to be rough-surfaced (ENDOPLASMIC RETICULUM, ROUGH); otherwise it is said to be smooth-surfaced (ENDOPLASMIC RETICULUM, SMOOTH). (King & Stansfield, A Dictionary of Genetics, 4th ed)Norethindrone: A synthetic progestational hormone with actions similar to those of PROGESTERONE but functioning as a more potent inhibitor of ovulation. It has weak estrogenic and androgenic properties. The hormone has been used in treating amenorrhea, functional uterine bleeding, endometriosis, and for contraception.Abstracting and Indexing as Topic: Activities performed to identify concepts and aspects of published information and research reports.Face: The anterior portion of the head that includes the skin, muscles, and structures of the forehead, eyes, nose, mouth, cheeks, and jaw.

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. Goodwin"Expression 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
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 ...
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 ...
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 ...
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. ...
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.
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 ...
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.
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.. ...
Getting a handle on the O-GlcNAc modification - OReilly Science Art, LLCGetting a handle on the O-GlcNAc modification - O'Reilly 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 ...
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 ...
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.* ...
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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 ...
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.
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 - XI'AN 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...
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) ...
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% ...
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 ...
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 ...
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 ...
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...
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...
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.
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
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 ...
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)
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 ...
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 ...
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 ...
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.
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%)
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+.
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 ...
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 ...
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. ...
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.
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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 ...
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 ...
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
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
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 ...
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
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
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). ...
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
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...
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
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 ...
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.
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.
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsInformation ScienceHealth CareGeographicals
GlucosamineAcetylglucosamineN-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 ControlBone MatrixMuramic AcidsUridine DiphosphateUridine Diphosphate GlucoseGlucuronosyltransferaseTunicamycinPhosphotransferasesProton-Translocating ATPasesRotationProtein SubunitsIrritable Bowel SyndromeDefecationChinaConstipationBleomycinStreptomycesChromosome WalkingPhleomycinsStreptomyces coelicolorPeplomycinEndoplasmic ReticulumNorethindroneAbstracting and Indexing as TopicFace
GlycoproteinGlycoprotein
N-Acetylglucosamine Aminohexose GlcNAc N-Acetylneuraminic acid Aminononulosonic acid. (Sialic acid) NeuNAc ...
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, ...
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. doi:10.1038/ ... N-Acetylglucosamine, using x-ray diffraction, which she solved within a year. She then moved onto the study of the substrate ...
OligosaccharyltransferaseOligosaccharyltransferase
The sugar Glc3Man9GlcNAc2 (where Glc=Glucose, Man=Mannose, and GlcNAc=N-acetylglucosamine) is attached to an asparagine (Asn) ...
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 ...
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; ...
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 ...
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. ...
GlycosaminoglycanGlycosaminoglycan
The repeating unit (except for keratan) consists of an amino sugar (N-acetylglucosamine or N-acetylgalactosamine) along with a ...
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 ...
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 ...
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 ...
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. ...
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; ...
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 ...
UAP1UAP1
"The eukaryotic UDP-N-acetylglucosamine pyrophosphorylases. Gene cloning, protein expression, and catalytic mechanism". J Biol ...
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 ...
GNPTGGNPTG
... ("N-acetylglucosamine-1-phosphate transferase, gamma subunit.") is a gene in the human body. It is one of three genes ... "N-acetylglucosamine-1-phosphate transferase, gamma subunit". Gene Cards. Retrieved 2013-06-06. "GNPTG". Genetics Home Reference ... also called N-acetylglucosamine-1-phosphate transferase). This enzyme is made up of two alpha (α), two beta (β), and two gamma ...
SGSHSGSH
... and N-acetylglucosamine 6-sulfatase (type D; MIM 252940). The Sanfilippo syndrome is characterized by severe central nervous ...
N-AcetylgalactosamineN-Acetylgalactosamine
Galactosamine Globoside (N-Acetylglucosamine) GlcNAc Donald M. Marcus; Elvin A. Kabat; Gerald Schiffman (1964). "Immunochemical ...
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 ...
N-Acetylmuramic acidN-Acetylmuramic acid
... , or MurNAc, is the ether of lactic acid and N-acetylglucosamine with a chemical formula of C11H19NO8. It ... MurNAc is covalently linked to N-acetylglucosamine and may also be linked through the hydroxyl on carbon number 4 to the carbon ... MurNAc is a monosaccharide derivative of N-acetylglucosamine. N-Acetylmuramic acid (MurNAc) is part of the peptidoglycan ... is part of a biopolymer in the bacterial cell wall, which is built from alternating units of N-acetylglucosamine (GlcNAc) and N ...
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 ...
Paenibacillus tylopiliPaenibacillus tylopili
It lacks the ability to break down N-acetylglucosamine. Kuisiene N, Raugalas J, Spröer C, Kroppenstedt RM, Stuknyte M, ...
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 ...
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsInformation ScienceHealth CareGeographicals
GlucosamineAcetylglucosamineN-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 ControlBone MatrixMuramic AcidsUridine DiphosphateUridine Diphosphate GlucoseGlucuronosyltransferaseTunicamycinPhosphotransferasesProton-Translocating ATPasesRotationProtein SubunitsIrritable Bowel SyndromeDefecationChinaConstipationBleomycinStreptomycesChromosome WalkingPhleomycinsStreptomyces coelicolorPeplomycinEndoplasmic ReticulumNorethindroneAbstracting and Indexing as TopicFace
Uridine Diphosphate N-Acetylglucosamine Summary Report | CureHunterUridine Diphosphate N-Acetylglucosamine Summary Report | CureHunter
Uridine Diphosphate N-Acetylglucosamine: Serves as the biological precursor of insect chitin, of muramic acid in bacterial cell ... Acetylglucosamine, UDP; Diphosphate N-Acetylglucosamine, Uridine; Diphospho-N-Acetylglucosamine, Uridine; N-Acetylglucosamine, ... Uridine Diphosphate N-Acetylglucosamine: 13*2,3-dialdehydro-UDP-N-acetylglucosamine. *5-fluoro-2-deoxyuridine diphosphate-N- ... Uridine Diphosphate N-Acetylglucosamine: 13*2,3-dialdehydro-UDP-N-acetylglucosamine. *5-fluoro-2-deoxyuridine diphosphate-N- ...
curehunter.com
What does n-acetylglucosaminyltransferases stand for?What does n-acetylglucosaminyltransferases stand for?
Enzymes that catalyze the transfer of N-acetylglucosamine from a nucleoside diphosphate N-acetylglucosamine to an acceptor ...
abbreviations.com
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 ...
en.wikipedia.org
N-Acetyl Glucosamine - iHerb.comN-Acetyl Glucosamine - iHerb.com
Categories Supplements Amino Acids N-Acetyl Glucosamine N-Acetyl Glucosamine 2 Results (showing 1 - 2 ) ...
iherb.com
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 ...
ebi.ac.uk
N-Acetylglucosamine receptor - WikipediaN-Acetylglucosamine receptor - Wikipedia
The N-Acetylglucosamine receptor is a receptor which binds N-Acetylglucosamine. N-Acetylglucosamine Receptor at the US National ...
en.wikipedia.org
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 ...
freepatentsonline.com
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) ...
livestrong.com
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 ...
pnas.org
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: ...
ncbi.nlm.nih.gov
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. ...
mdpi.com
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 ...
primidi.com
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 ...
iherb.com
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: ...
ebi.ac.uk
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 ...
ncbi.nlm.nih.gov
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 ...
herbalremedies.com
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. ...
biocompare.com
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 ...
abcam.com
RCSB PDB - Protein Feature View - UDP-N-acetylglucosamine 1-carboxyvinyltransferase - B7M095 (MURA ECO8A)RCSB PDB - Protein Feature View - UDP-N-acetylglucosamine 1-carboxyvinyltransferase - B7M095 (MURA ECO8A)
The PDB archive contains information about experimentally-determined structures of proteins, nucleic acids, and complex assemblies. 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.
rcsb.org
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 ...
uniprot.org
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] ...
rcsb.org
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 ...
pubmed.ncbi.nlm.nih.gov
acetyl glucosamine | Cosmetic Ingredient Dictionary | Paulas Choiceacetyl glucosamine | Cosmetic Ingredient Dictionary | Paula's Choice
Acetyl glucosamine is a skin-replenishing ingredient that can have considerable value in cosmetic products aimed at diminishing ... Acetyl glucosamine also has research demonstrating that it can have skin-brightening benefits, particularly when combined with ... as their Olay brand uses acetyl glucosamine in select products. Still, the research is compelling and the protocols are sound, ... and both companies sell skincare products that contain acetyl glucosamine. ...
paulaschoice.com
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 ...
uniprot.org
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 ...
link.springer.com
AnatomyOrganismsDiseasesChemicals and DrugsAnalytical, Diagnostic and Therapeutic Techniques and EquipmentPhenomena and ProcessesDisciplines and OccupationsInformation ScienceHealth CareGeographicals
GlucosamineAcetylglucosamineN-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 ControlBone MatrixMuramic AcidsUridine DiphosphateUridine Diphosphate GlucoseGlucuronosyltransferaseTunicamycinPhosphotransferasesProton-Translocating ATPasesRotationProtein SubunitsIrritable Bowel SyndromeDefecationChinaConstipationBleomycinStreptomycesChromosome WalkingPhleomycinsStreptomyces coelicolorPeplomycinEndoplasmic ReticulumNorethindroneAbstracting and Indexing as TopicFace
ProteinsSubunitPyrophosphorylaseKinaseUridineBeta-N-acetylglucosaminePeptidoglycanThreonineAntibodyPhosphorylationGeneGalactoseEnolpyruvylProteinCandidaBacterialUptakePathwaysGlucosamineBindsMonosaccharideGlucoseSequenceSupplementActivitySide EffectsFormSingle
Proteins5
Subunit4
  • 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)
  • 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)
Pyrophosphorylase3
Kinase4
Uridine2
  • 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)
  • 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)
Beta-N-acetylglucosamine2
Peptidoglycan2
Threonine2
Antibody1
Phosphorylation1
  • Comparable to phosphorylation , addition or removal of N -acetylglucosamine is a means of activating or deactivating enzymes or transcription factors . (wikipedia.org)
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)
Galactose1
  • 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)
Enolpyruvyl1
Protein1
  • 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)
Candida1
  • 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)
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)
Uptake3
  • In pathogenic yeasts, two systems of different affinity for substrate were found to operate in the uptake of N-acetylglucosamine. (nih.gov)
  • Uranyl acetate (0.01 mM) which binds to cell membrane-associated polyphosphates, inhibited completely the inducible uptake of N-acetylglucosamine. (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)
Pathways1
Glucosamine1
  • N-acetylglucosamine (NAG) is a special sugar and a form of glucosamine, one of the main building blocks of joint tissue (areas where two or more bones meet) and other connective tissues. (yourhealthremedy.com)
Binds1
  • The N-Acetylglucosamine receptor is a receptor which binds N-Acetylglucosamine. (wikipedia.org)
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)
Glucose3
  • N-acetylglucosamine (NAG) is an amino sugar, a derivative of the simple sugar glucose. (livestrong.com)
  • 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)
Supplement1
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)
Side Effects1
Form1
  • Today I just got two jars of Ultimate Glubosamine (n-acetylglucosamine form) in the mail. (thisisms.com)
Single1
  • At each of these sites up to two N -acetylglucosamine 1-phosphate groups can be added to a single oligosaccharide. (biochemj.org)