Chemicals and Drugs
GlucosamineAcetylglucosamine
Glucosamine
Acetylglucosamine
The N-acetyl derivative of glucosamine.

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

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

Gangliosides of human kidney. (2/1610)

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

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

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

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

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

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

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

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

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

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

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

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

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

Expression of O-linked N-acetylglucosamine modified proteins and produ by Octavia Y. GoodwinExpression of O-linked N-acetylglucosamine modified proteins and produ by Octavia Y. Goodwin
O-linked â-N-acetylglucosamine is a regulatory post translational modification. This modification occurs on nearly all functional classes of proteins, in the nucleus and cytoplasm. O-GlcNAc is added to serine or threonine by O-GlcNAc transferase and removed by O-GlcNAcase. Previous attempts to study O-GlcNAc-modified proteins have resulted in low yields, making 3-dimensional structure determination impossible. In this dissertation O-GlcNAc transferase will be co-expressed with domains of human cAMP responsive element-binding protein (CREB1) and Abelson tyrosine-kinase 2 (ABL2) in E. coli, to produce O-GlcNAc-modified protein. The O-GlcNAc-modified protein was expressed in a variety of E. coli cell lines at a variety of conditions, but only small quantities of insoluble protein were produced. A glycosidase was suspected due to the disappearance of the O-GlcNAc modification from the protein. O-(2-acetamido-2-dexoy-dglucopyranosylidene) amino-N-phenylcarbamate (PUGNAc), a â-N-acetylglucosaminidase
https://digitalcommons.lsu.edu/gradschool_dissertations/3325/
Dynamic Interplay between O-Linked N-Acetylglucosaminylation and Glycogen Synthase Kinase-3-dependent Phosphorylation |...Dynamic Interplay between O-Linked N-Acetylglucosaminylation and Glycogen Synthase Kinase-3-dependent Phosphorylation |...
O-GlcNAc1 is a dynamically regulated post-translational modification (PTM), in which a β-N-acetylglucosamine moiety is attached to hydroxyl side chains of serine or threonine residues of proteins by O-GlcNAc-transferase (1) and removed by β-N-acetylglucosaminidase (O-GlcNAcase) (2). O-GlcNAc is ubiquitous on nuclear and cytoplasmic proteins in all multicellular eukaryotes (3). Dynamic O-GlcNAcylation plays critical roles in signal transduction (4), transcriptional control (5, 6), cell cycle regulation (7), protein degradation (8), neurodegeneration (9), and stress responses (10). Abnormally regulated O-GlcNAcylation has been found in diseases such as diabetes (11) and Alzheimer disease (12).. The role of O-GlcNAcylation in signal transduction is at least in part related to its competitive interplay with O-phosphorylation. Some of the known O-GlcNAc sites are the same as or adjacent to phosphorylation sites. For example, O-GlcNAc is reciprocal to O-phosphorylation on the C-terminal domain of ...
https://www.mcponline.org/content/6/8/1365?ijkey=442d426eb944c24e0a9d5cc49866bb11037b5e09&keytype2=tf_ipsecsha
Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress: A survival response of mammalian cells -...
Fingerprint Dive into the research topics of Dynamic O-GlcNAc modification of nucleocytoplasmic proteins in response to stress: A survival response of mammalian cells. Together they form a unique fingerprint. ...
https://jhu.pure.elsevier.com/en/publications/dynamic-o-glcnac-modification-of-nucleocytoplasmic-proteins-in-re-4/fingerprints/
GlcNAcstatin: a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels<...
TY - JOUR. T1 - GlcNAcstatin. T2 - a picomolar, selective O-GlcNAcase inhibitor that modulates intracellular O-glcNAcylation levels. AU - Dorfmueller, Helge C.. AU - Borodkin, Vladimir S.. AU - Schimpl, Marianne. AU - Shepherd, Sharon M.. AU - Shpiro, Natalia A.. AU - van Aalten, Daan M. F.. PY - 2006/12. Y1 - 2006/12. N2 - Many phosphorylation signal transduction pathways in the eukaryotic cell are modulated by posttranslational modification of specific serines/threonines with N-acetylglucosamine (O-GlcNAc). Levels of O-GlcNAc on key proteins regulate biological processes as diverse as the cell cycle, insulin signaling, and protein degradation. The two enzymes involved in this dynamic and abundant modification are the O-GlcNAc transferase and O-GlcNAcase. Structural data have recently revealed that the O-GlcNAcase possesses an active site with significant structural similarity to that of the human lysosomal hexosaminidases HexA/HexB. PUGNAc, an O-GlcNAcase inhibitor widely used to raise levels ...
https://discovery.dundee.ac.uk/en/publications/glcnacstatin-a-picomolar-selective-o-glcnacase-inhibitor-that-mod
Frontiers | FGF23 Induction of O-Linked N-Acetylglucosamine Regulates IL-6 Secretion in Human Bronchial Epithelial Cells |...Frontiers | FGF23 Induction of O-Linked N-Acetylglucosamine Regulates IL-6 Secretion in Human Bronchial Epithelial Cells |...
The hexosamine biosynthetic pathway (HBP) generates the substrate for the O-linked β-N-acetylglucosamine (O-GlcNAc) modification of proteins. The HBP also serves as a stress sensor and has been reported to be involved with nuclear factor of activated T-cells (NFAT) activation, which can contribute to multiple cellular processes including cell metabolism, proliferation, and inflammation. In our previously published report, Fibroblast Growth Factor (FGF) 23, an important endocrine pro-inflammatory mediator, was shown to activate the FGFR4/phospholipase Cγ (PLCγ)/nuclear factor of activated T-cells (NFAT) signaling in chronic inflammatory airway diseases such as cystic fibrosis (CF) and chronic obstructive pulmonary disease (COPD). Here, we demonstrate that FGF23 increased the O-GlcNAc modification of proteins in HBECs. Furthermore, the increase in O-GlcNAc levels by FGF23 stimulation resulted in the downstream activation of NFAT and secretion of interleukin-6 (IL-6). Conversely, inhibition of FGF23
https://www.frontiersin.org/articles/10.3389/fendo.2018.00708/full
Diamond Publications - Search Results
Abstract: O-GlcNAc transferase (OGT) glycosylates a diverse range of intracellular proteins with O-linked N-acetylglucosamine (O-GlcNAc), an essential and dynamic post-translational modification in metazoans. Although this enzyme modifies hundreds of proteins with O-GlcNAc, it is not understood how OGT achieves substrate specificity. In this study, we describe the application of a high-throughput OGT assay to a library of peptides. We mapped sites of O-GlcNAc modification by electron transfer dissociation MS and found that they correlate with previously detected O-GlcNAc sites. Crystal structures of four acceptor peptides in complex with Homo sapiens OGT suggest that a combination of size and conformational restriction defines sequence specificity in the −3 to +2 subsites. This work reveals that although the N-terminal TPR repeats of OGT may have roles in substrate recognition, the sequence restriction imposed by the peptide-binding site makes a substantial contribution to O-GlcNAc site ...
https://publications.diamond.ac.uk/pubman/searchpublicationsadvanced?advancedsearch=1&authorId=37873&publicationStates%5B4%5D.selected=true
Protein O-GlcNAcylation Is Required for Fibroblast Growth Factor Signaling in Drosophila | Science SignalingProtein O-GlcNAcylation Is Required for Fibroblast Growth Factor Signaling in Drosophila | Science Signaling
Glycosylation is essential for growth factor signaling through N-glycosylation of ligands and receptors and the biosynthesis of proteoglycans as co-receptors. Here, we show that protein O-GlcNAcylation is crucial for fibroblast growth factor (FGF) signaling in Drosophila. We found that nesthocker (nst) encodes a phosphoacetylglucosamine mutase and that nst mutant embryos exhibited low amounts of intracellular uridine 5′-diphosphate-N-acetylglucosamine (UDP-GlcNAc), which disrupted protein O-GlcNAcylation. Nst was required for mitogen-activated protein kinase (MAPK) signaling downstream of FGF but not MAPK signaling activated by epidermal growth factor. nst was dispensable for the function of the FGF ligands and the FGF receptors extracellular domain but was essential in the signal-receiving cells downstream of the FGF receptor. We identified the adaptor protein Downstream of FGF receptor (Dof), which interacts with the FGF receptor, as the relevant target for O-GlcNAcylation in the FGF ...
https://stke.sciencemag.org/content/4/204/ra89
Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α...
TY - JOUR. T1 - Morphological changes in diabetic kidney are associated with increased O-GlcNAcylation of cytoskeletal proteins including α-actinin 4. AU - Akimoto, Yoshihiro. AU - Miura, Yuri. AU - Toda, Tosifusa. AU - Wolfert, Margreet A.. AU - Wells, Lance. AU - Boons, Geert Jan. AU - Hart, Gerald Warren. AU - Endo, Tamao. AU - Kawakami, Hayato. PY - 2011. Y1 - 2011. N2 - Purpose. The objective of the present study is to identify proteins that change in the extent of the modification with O-linked N-acetylglucosamine (O-GlcNAcylation) in the kidney from diabetic model Goto-Kakizaki (GK) rats, and to discuss the relation between O-GlcNAcylation and the pathological condition in diabetes. Methods. O-GlcNAcylated proteins were identified by two-dimensional gel electrophoresis, immunoblotting and peptide mass fingerprinting. The level of O-GlcNAcylation of these proteins was examined by immunoprecipitation, immunoblotting and in situ Proximity Ligation Assay (PLA). Results: O-GlcNAcylated ...
https://jhu.pure.elsevier.com/en/publications/morphological-changes-in-diabetic-kidney-are-associated-with-incr-5
Abstract 19733: Shear-Dependent Aortic Valve Endothelial Inflammation and Calcification Are Regulated by O-GlcNAc Modification...Abstract 19733: Shear-Dependent Aortic Valve Endothelial Inflammation and Calcification Are Regulated by O-GlcNAc Modification...
Introduction: Aortic valve (AV) disease is a significant contributor to cardiovascular mortality. AV calcification occurs preferentially on the fibrosa side, where endothelial cells (ECs) are subjected to characteristic oscillatory shear stress (OS), whereas the ventricularis ECs experience stable unidirectional laminar shear stress (LS). OS and LS differently regulate endothelial function via gene expression and protein modification. While the post-translational β-N-acetylglucosamine modification of amino acids (O-GlcNAcylation) has been shown to be important in the function of various cell types, its role in AV disease is unknown. We hypothesized that OS impairs EC O-GlcNAcylation, leading to AV inflammation and calcification.. Methods and Results: Immunostaining analysis showed that O-GlcNAcylation was decreased in fibrosa endothelium compared to ventricularis in human and porcine AVs, and human AV ECs (HAVECs) exhibited increased O-GlcNAcylation by LS (20 dyn/cm2) and decreased by OS (+5 ...
http://circ.ahajournals.org/content/134/Suppl_1/A19733
Glycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc | ScienceGlycosylation of Nucleocytoplasmic Proteins: Signal Transduction and O-GlcNAc | Science
In order for a protein modification to play an active role in signal transduction, it needs to have certain key features. First, the modification needs to be dynamic. For the proteins that have been examined to date, the O-GlcNAc half-life is much shorter than that of the modified polypeptide chain (8). Second, the removal or attachment of the modification should be inducible by certain stimuli. O-GlcNAc modification of certain proteins is known to change in response to T cell activation, insulin signaling, glucose metabolism, and cell cycle progression (6). Thus, O-GlcNAc displays features essential for a role in signal transduction.. Consistent with O-GlcNAc being dynamic and inducible, regulated nucleocytoplasmic enzymes for the attachment [O-GlcNAc transferase (OGT)] and for the removal (O-GlcNAcase) of the modification have been purified, characterized, and cloned (9-12). The OGT enzyme is modified by both O-GlcNAc and tyrosine phosphorylation and has 11 protein-protein interaction domains ...
https://science.sciencemag.org/content/291/5512/2376?ijkey=5e99fa5fb28fe2d0fe73c63d7cd4017a02fe4d88&keytype2=tf_ipsecsha
Human OGA binds substrates in a conserved peptide recognition groove | Biochemical JournalHuman OGA binds substrates in a conserved peptide recognition groove | Biochemical Journal
The O-GlcNAc (O-linked N-acetylglucosamine) modification is a dynamic and reversible form of protein glycosylation occurring on specific serine and threonine residues of intracellular proteins [1,2]. Since the initial discovery of O-GlcNAc [3], technological advances have greatly facilitated its detection, and proteomics studies [4-6] have shown that a significant proportion of cellular proteins are O-GlcNAcylated. However, the functional importance of O-GlcNAc is only just emerging, with evidence to suggest that it may regulate protein activity in a manner analogous (and complementary) to phosphorylation [7]. O-GlcNAc levels are known to respond dynamically to nutrient availability [1] and stress [8], and to undergo changes during the cell cycle [9] and development [10]. O-GlcNAc has been shown to be associated with a range of human diseases [2]. Strikingly, only two enzymes orchestrate the O-GlcNAc modification. Both the OGT (O-GlcNAc transferase) and its antagonistic OGA (O-GlcNAcase or ...
http://www.biochemj.org/content/432/1/1
The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation<...The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation<...
TY - JOUR. T1 - The lineage stability and suppressive program of regulatory T cells require protein O-GlcNAcylation. AU - Liu, Bing. AU - Salgado, Oscar C.. AU - Singh, Sangya. AU - Hippen, Keli L.. AU - Maynard, Jason C.. AU - Burlingame, Alma L.. AU - Ball, Lauren E.. AU - Blazar, Bruce R.. AU - Farrar, Michael A.. AU - Hogquist, Kristin A.. AU - Ruan, Hai Bin. PY - 2019/12/1. Y1 - 2019/12/1. N2 - Regulatory T (Treg) cells control self-tolerance, inflammatory responses and tissue homeostasis. In mature Treg cells, continued expression of FOXP3 maintains lineage identity, while T cell receptor (TCR) signaling and interleukin-2 (IL-2)/STAT5 activation support the suppressive effector function of Treg cells, but how these regulators synergize to control Treg cell homeostasis and function remains unclear. Here we show that TCR-activated posttranslational modification by O-linked N-Acetylglucosamine (O-GlcNAc) stabilizes FOXP3 and activates STAT5, thus integrating these critical signaling pathways. ...
https://experts.umn.edu/en/publications/the-lineage-stability-and-suppressive-program-of-regulatory-t-cel
N-Acetyl-Glucosamine Binding Lectins - GlycoMatrix™N-Acetyl-Glucosamine Binding Lectins - GlycoMatrix™
Several lectins recognize n-acetyl-glucosamine in a glycoprotein. Based on the linkage and specificity for binding, different N-Acetyl-Glucosamine-binding lectins are utilized to obtain optimum results.
https://www.glycomatrix.com/collections/n-acetyl-glucosamine-binding-lectins
OGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens (human)] - Gene - NCBIOGT O-linked N-acetylglucosamine (GlcNAc) transferase [Homo sapiens (human)] - Gene - NCBI
This gene encodes a glycosyltransferase that catalyzes the addition of a single N-acetylglucosamine in O-glycosidic linkage to serine or threonine residues. Since both phosphorylation and glycosylation compete for similar serine or threonine residues, the two processes may compete for sites, or they may alter the substrate specificity of nearby sites by steric or electrostatic effects. The protein contains multiple tetratricopeptide repeats that are required for optimal recognition of substrates. Alternatively spliced transcript variants encoding distinct isoforms have been found for this gene. [provided by RefSeq, Oct 2009 ...
https://www.ncbi.nlm.nih.gov/gene/8473
Profiling of Protein O-GlcNAcylation in Murine CD8<sup>+</sup> Effector- and Memory-like T...Profiling of Protein O-GlcNAcylation in Murine CD8<sup>+</sup> Effector- and Memory-like T...
TY - JOUR. T1 - Profiling of Protein O-GlcNAcylation in Murine CD8+ Effector- and Memory-like T Cells. AU - Lopez Aguilar, Aime. AU - Gao, Yu. AU - Hou, Xiaomeng. AU - Lauvau, Gregoire. AU - Yates, John R.. AU - Wu, Peng. N1 - Funding Information: This work was performed at The Scripps Research Institute with the financial support from the National Institutes of Health to P.W. (GM093282, GM113046) and to J.R.Y. (MH067880, GM103533). We thank the Histology Core Facility at TSRI for providing access to their equipment and support.. PY - 2017/12/15. Y1 - 2017/12/15. N2 - During an acute infection, antigenic stimulation leads to activation, expansion, and differentiation of naïve CD8+ T cells, first into cytotoxic effector cells and eventually into long-lived memory cells. T cell antigen receptors (TCRs) detect antigens on antigen-presenting cells (APCs) in the form of antigenic peptides bound to major histocompatibility complex I (MHC-I)-encoded molecules and initiate TCR signal transduction ...
https://einstein.pure.elsevier.com/en/publications/profiling-of-protein-o-glcnacylation-in-murine-cd8supsup-effector
China N-Acetyl-D-Glucosamine - China N-Acetyl-D-Glucosamine, GlucosamineChina N-Acetyl-D-Glucosamine - China N-Acetyl-D-Glucosamine, Glucosamine
China N-Acetyl-D-Glucosamine, Find details about China N-Acetyl-D-Glucosamine, Glucosamine from N-Acetyl-D-Glucosamine - Yangzhou Rixing Bio-Tech Co., Ltd.
http://yzrixing.en.made-in-china.com/product/nKhEqSWVgfYc/China-N-Acetyl-D-Glucosamine.html
Nutrient Regulation of Immunity: O-GlcNAcylation Regulates Stimulus-Specific NF-κB-Dependent Transcription | Science SignalingNutrient Regulation of Immunity: O-GlcNAcylation Regulates Stimulus-Specific NF-κB-Dependent Transcription | Science Signaling
Nutrients regulate gene transcription by the dynamic cycling of O-linked N-acetylglucosamine (O-GlcNAc) on proteins that constitute the transcriptional machinery. A study shows that O-GlcNAcylation of the nuclear factor κB (NF-κB) subunit c-Rel is required for its binding to the promoters of some, but not all, key T cell receptor-dependent genes; however, O-GlcNAcylation is dispensable for the binding of c-Rel to the promoters of tumor necrosis factor-α-dependent genes. This study not only illustrates how specific stimuli that act on the same transcription factor can elicit the expression of particular sets of genes, it also suggests a possible mechanism for autoimmunity in diabetes.. ...
http://stke.sciencemag.org/content/6/290/pe26
Getting a handle on the O-GlcNAc modification - OReilly Science Art, LLCGetting a handle on the O-GlcNAc modification - OReilly Science Art, LLC
Protein glycosylation is usually relegated to the cell surface and intracellular compartments. In a fascinating exception to this rule that was first observed in the 1980s, A GlcNAc monosaccharide can be added to serine and threonine residues of cytosolic proteins. Many labs are trying to understand the dynamic regulation of the addition and removal of this sugar that seemingly has a hand in every cellular process and disease state known to man. More and more examples are being found to suggest that this modification and phosphorylation regulate each other, as if they werent already complicated enough on their own.. There are a handful of ways to detect O-GlcNAc, which have helped build the laundry list by telling us which proteins are modified. Now, in a recent Nature Chemical Biology paper from Linda Hsieh-Wilsons lab at CalTech, they show us a useful new method that reveals what proportion of any particular protein is modified (2%? 80%), and of those that are modified, exactly how many ...
http://oreillyscienceart.com/whats-new/2010/8/22/getting-a-handle-on-the-o-glcnac-modification.html
Cross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic diseaseCross talk between O-GlcNAcylation and phosphorylation: roles in signaling, transcription, and chronic disease
O-GlcNAcylation is the addition of β-D-N-acetylglucosamine to serine or threonine residues of nuclear and cytoplasmic proteins. O-linked N-acetylglucosamine (O-GlcNAc) was not discovered until the early 1980s and still remains difficult to detect and quantify. Nonetheless, O-GlcNAc is highly abundan …
https://pubmed.ncbi.nlm.nih.gov/21391816/?dopt=Abstract
3pe4 - Proteopedia, life in 3D3pe4 - Proteopedia, life in 3D
OGT1_HUMAN] Catalyzes the transfer of a single N-acetylglucosamine from UDP-GlcNAc to a serine or threonine residue in cytoplasmic and nuclear proteins resulting in their modification with a beta-linked N-acetylglucosamine (O-GlcNAc). Glycosylates a large and diverse number of proteins including histone H2B, AKT1, PFKL, KMT2E/MLL5, MAPT/TAU and HCFC1. Can regulate their cellular processes via cross-talk between glycosylation and phosphorylation or by affecting proteolytic processing. Involved in insulin resistance in muscle and adipocyte cells via glycosylating insulin signaling components and inhibiting the Thr-308 phosphorylation of AKT1, enhancing IRS1 phosphorylation and attenuating insulin signaling. Involved in glycolysis regulation by mediating glycosylation of 6-phosphofructokinase PFKL, inhibiting its activity. Component of a THAP1/THAP3-HCFC1-OGT complex that is required for the regulation of the transcriptional activity of RRM1. Plays a key role in chromatin structure by mediating ...
http://proteopedia.org/wiki/index.php/3pe4
David Vocadlo - Department of Chemistry - Simon Fraser UniversityDavid Vocadlo - Department of Chemistry - Simon Fraser University
Cecioni, S., Vocadlo, D.J. Carbohydrate Bis-acetal-Based Substrates as Tunable Fluorescence-Quenched Probes for Monitoring exo-Glycosidase Activity. Journal of the American Chemical Society 2017, 139, 8392-8395. Liu T.-W., Myschyshyn M., Sinclair D.A., Cecioni S., Beja K., Honda B.M., Morin R.D., Vocadlo D.J. Genome-wide chemical mapping of O-GlcNAcylated proteins in Drosophila. Nature Chemical Biology 2017, 13, 161-7.. Perley-Robertson GE, Yadav AK, Winogrodzki JL, Stubbs KA, Mark BL, Vocadlo DJ.* A Fluorescent Transport Assay Enables Studying AmpG Permeases Involved in Peptidoglycan Recycling and Antibiotic Resistance. ACS Chem. Biol., 2016, 11, 2626-35.. Cekic N, Heinonen JE, Stubbs KA, Roth C, He Y, Bennet AJ, McEachern EJ, Davies GJ, Vocadlo DJ. Analysis of transition state mimicry by tight binding aminothiazoline inhibitors provides insight into catalysis by human O-GlcNAcase. Chem. Sci. 2016, 7, 3742-3750.. Zhu, Y., Liu, T., Eskandari, R., Zandberg, W., Cecioni, S., Vocadlo, D.J.* ...
https://www.sfu.ca/chemistry/people/profiles/dvocadlo.html
Plus itPlus it
Cancer cells increase nutrient consumption leading to the altered metabolic state known as the Warburg effect. One pathway dependent on glucose, glutamine and acetyl-CoA is the Hexosamine Biosynthetic Pathway (HBP). Increased flux through the HBP leads to elevated post-translation addition of O-linked-β-N-acetylglucosamine (O-GlcNAc) on a diverse population of nuclear and cytosolic proteins, many of which are implicated in cancer. Recently, our lab provided the first evidence that breast and prostate cancers increases total O-GlcNAcylation by increasing O-GlcNAc Transferase (OGT) levels. Importantly, reducing OGT activity inhibits cancer cell invasion in vitro and metastasis in vivo. OGT inhibition reduces breast and prostate cancer cell invasion through, in part, inhibition of the oncogenic transcription factor, FOXM1 and its transcriptional target matrix metalloproteinase 2 (MMP2). Here, we show that OGT regulation of FOXM1 and cancer cell invasion requires regulation of the NAD+-dependent ...
http://cancerres.aacrjournals.org/content/75/15_Supplement/518
anti-O-GlcNAc transferase antibody [GT2037] | GeneTexanti-O-GlcNAc transferase antibody [GT2037] | GeneTex
O-GlcNAc transferase antibody [GT2037] (O-linked N-acetylglucosamine (GlcNAc) transferase) for WB. Anti-O-GlcNAc transferase mAb (GTX629813) is tested in Human, Mouse, Rat samples. 100% Ab-Assurance.
http://www.genetex.com/O-GlcNAc-transferase-antibody-GT2037-GTX629813.html
N-Acetyl-D-Glucosamine (CAS No.: 7512-17-6;134451-94-8); USP - XIAN VEDA CHEMICAL CO.,LTD - ecplaza.netN-Acetyl-D-Glucosamine (CAS No.: 7512-17-6;134451-94-8); USP - XIAN VEDA CHEMICAL CO.,LTD - ecplaza.net
Product Name:N-acetyl-D-(+)-Glucosamine Synonyms:N-Acetyl-Beta-D-Glucosamine; N-Acetyl-D-Glucosamine; 2-Acetamido-2-Deoxy-D-Glucopyranose; N-((1R,2R,3S,4R)-1-Formyl-2,3,4,5-Tetrahydroxy-Pentyl)-Acetamide; N-Acetyl-D-Glucosamine, Immobilized On...
https://www.ecplaza.net/products/n-acetyl-d-glucosamine-cas-no_4091810
Team:Northwestern/Project/Modeling - 2010.igem.orgTeam:Northwestern/Project/Modeling - 2010.igem.org
Iex: External Inducer, determined by diffusion through Ficks law (IPTG in our experiment) Iin: Internal Inducer (IPTG) Ii: Inducer bound to Repressor (IPTG bound to lacI) i: Repressor (lacI) Db: Repressor-bound DNA (lacI-bound DNA(CHS3) region in plasmid) Dunb: transcribe-able or Repressor-unbound DNA (lacI-unbound DNA(CHS3)) Re: mRNA for Enzyme (CHS3 mRNA) E: Enzyme (CHS3) S: Substrate (N-Acetyl Glucosamine) C: Enzyme Substrate Complex (CHS3-(N-Acetyl-Glucosamine)-Chitin or (NAG)n Complex) P: Protein Product (Chitin or (NAG)n+1) ...
http://2010.igem.org/wiki/index.php?title=Team:Northwestern/Project/Modeling&oldid=150687
Vegfa | High-Throughput Screen for the Chemical Inhibitors
Many neuronal cytosolic and nuclear proteins are post-translationally modified by the reversible addition of O-linked = 176), demonstrating that cotransfection is a reliable approach in our system. of culturing. Comparison of the staining intensity in neurons expressing dsRED alone (= 23) to that in nontransfected neurons from cultures transfected with either dsRED (= 23) or dsRED + O-GlcNAcase (= 25) did not reveal a difference (> 0.32 and > 0.21 respectively, 2-tailed Welch > 0.25, 2-tailed Welch = 23) to dsRED transfected neurons revealed a 61% decrease in O-GlcNAc staining intensity (< 0.00001, 2-tailed Welch = 140) of O-GlcNAcase over-expressing neurons exhibited one LY310762 supplier or more branches relative to 20% (= 60) of dsRED alone expressing control neurons [Fig. 2(E)]. Thus, decreases in O-GlcNAc levels induced by overexpression of O-GlcNAcase resulted in a 1.85-fold increase in the percentage of neurons that exhibited axon branching. O-GlcNAcase over-expression resulted in a 50% ...
http://acancerjourney.info/index.php/tag/vegfa/
Deciphering nucleoporin functions in nucleocytoplasmic protein transport in Drosophila.Deciphering nucleoporin functions in nucleocytoplasmic protein transport in Drosophila.
Part of urn:nbn:se:su:diva-968Available from: 2006-04-06 Created: 2006-04-06 Last updated: 2010-01-13Bibliographically approved ...
http://su.diva-portal.org/smash/record.jsf?pid=diva2:200745
SAUPAN002586000 - AureoWikiSAUPAN002586000 - AureoWiki
Staphylococcus aureus; pan ID: SAUPAN002586000; symbol: nagA; products: N-acetylglucosamine-6-phosphate deacetylase, putative N-acetylglucosamine-6-phosphatedeacetylase; orthologs: COL: SACOL0761 (nagA), N315: SA0656 (nagA), NCTC8325: SAOUHSC_00710, Newman: NWMN_0670 (nagA), USA300_FPR3757: SAUSA300_0686 (nagA), 04-02981: SA2981_0678 (nagA)
https://aureowiki.med.uni-greifswald.de/SAUPAN002586000
N-acetyl-D-glucosamineN-acetyl-D-glucosamine
Hyaluronic acid (HA), a polymer with elastic properties, is a polysaccharide formed from N-acetyl-D-glucosamine and glucuronic acid. HA belongs to a group of chemicals called glycosaminoglycans (GAGs). The activity of a specific form or polymer of HA depends on the size the molecule. HA forms an aggregation center for a large molecule of chondroitin sulfate […]. View Post ...
https://www.rainbow.coop/nutritional-library/miscellaneous/n-acetyl-d-glucosamine/
The Basics of Protein Structure Part 1: The Levels of StructureThe Basics of Protein Structure Part 1: The Levels of Structure
How protein structure is established is a fascinating question and a field that is actively studied by prominent labs around the world. Protein folding is the process of a chain of amino acids curling into its final shape, and how this process occurs is complex and not completely understood. In general proteins fold depending on their environment (exposed to water or not, for example) and with the help of other proteins, called chaperones. Protein chaperones help to establish a proteins structure as well as maintain it during times of stress. Further, modifications on proteins can change their structures, such as when p53, a protein that is involved in regulating many processes within the cell, is phosphorylated - its structure and, consequently, its function is altered slightly ...
http://poorhungrydrowsy.blogspot.com/2014/06/the-basics-of-protein-structure-part-1.html
O-GlcNAc (CTD110.6) | ALZFORUMO-GlcNAc (CTD110.6) | ALZFORUM
detects O-GlcNAc (ß-O-linked N- acetylglucosamine) and Thr-O-GlcNAc but shows no cross reactivity with peptide determinants or other closely-related carbohydrate antigens ...
https://www.alzforum.org/antibodies/o-glcnac-ctd1106
Targeted disruption the enzymes of O-GlcNAc cycling: Animal models of Disease - John HanoverTargeted disruption the enzymes of O-GlcNAc cycling: Animal models of Disease - John Hanover
The hexosamine signaling pathway terminating in O-GlcNAc cycling has been implicated in cellular signaling cascades and regulation of transcription and translat...
http://grantome.com/grant/NIH/ZIA-DK060101-07
Development of Research Reagents Specific for O-Glcnac (O-Glcnac Lectenz) - Lori YangDevelopment of Research Reagents Specific for O-Glcnac (O-Glcnac Lectenz) - Lori Yang
The long-term objectives of this proposal are to generate and commercialize a new class of high-specificity, high-affinity proteins called Lectenz?, as research...
http://grantome.com/grant/NIH/261201300048C-0-0-1
Kraeber & Co GmbH - N-Acetyl-D-Glucosamine
Kraeber & Co GmbH - Pharmazeutische Rohstoffe - Hersteller von Wirk- und Hilfsstoffen für die Pharmazie, Biotechnologie, Kosmetik und Fototechnik.
https://www.kraeber.de/products/cosmetic/n-acetyl-d-glucosamine
Early detection of diabetes - The Johns Hopkins UniversityEarly detection of diabetes - The Johns Hopkins University
The present invention is based on the discovery that hexosamine, and in particular the dynamic O-GlcNAcylation of proteins (modification of proteins by the sugar N-acetylglucosamine) both causes insul
http://www.freepatentsonline.com/9250248.html
KEGG ENZYME: 2.4.1.320
4-O-beta-D-mannopyranosyl-N-acetyl-D-glucosamine + phosphate = N-acetyl-D-glucosamine + alpha-D-mannose 1-phosphate [RN:R10829 ...
http://www.genome.jp/dbget-bin/www_bget?ec:2.4.1.320
Activation of AKT by O-linked N-Acetylglucosamine induces vascular calcification in diabetes mellitus<...Activation of AKT by O-linked N-Acetylglucosamine induces vascular calcification in diabetes mellitus<...
TY - JOUR. T1 - Activation of AKT by O-linked N-Acetylglucosamine induces vascular calcification in diabetes mellitus. AU - Heath, Jack M.. AU - Sun, Yong. AU - Yuan, Kaiyu. AU - Bradley, Wayne E.. AU - Litovsky, Silvio. AU - DellItalia, Louis J.. AU - Chatham, John C.. AU - Wu, Hui. AU - Chen, Yabing. N1 - Copyright: Copyright 2014 Elsevier B.V., All rights reserved.. PY - 2014/3/28. Y1 - 2014/3/28. N2 - RATIONALE:: Vascular calcification is a serious cardiovascular complication that contributes to the increased morbidity and mortality of patients with diabetes mellitus. Hyperglycemia, a hallmark of diabetes mellitus, is associated with increased vascular calcification and increased modification of proteins by O-linked N-acetylglucosamine (O-GlcNAcylation). OBJECTIVE:: We sought to determine the role of protein O-GlcNAcylation in regulating vascular calcification and the underlying mechanisms. METHODS AND RESULTS:: Low-dose streptozotocin-induced diabetic mice exhibited increased aortic ...
https://ohsu.pure.elsevier.com/en/publications/activation-of-akt-by-o-linked-n-acetylglucosamine-induces-vascula
Pomgnt2 (protein O-linked mannose N-acetylglucosaminyltransferase 2 (beta 1,4-)) - Chinchilla Research Resource Database
ENCODES a protein that exhibits acetylglucosaminyltransferase activity (ortholog); protein O-GlcNAc transferase activity (ortholog); INVOLVED IN neuron migration (ortholog); protein O-linked glycosylation (ortholog); protein O-linked mannosylation (ortholog); ASSOCIATED WITH Autosomal Recessive Limb-Girdle Muscular Dystrophy Type 24 (ortholog); congenital muscular dystrophy-dystroglycanopathy type A8 (ortholog); Perinatal Death (ortholog); FOUND IN endoplasmic reticulum (ortholog); endoplasmic reticulum membrane (ortholog); integral component of membrane (ortholog)
https://crrd.mcw.edu/rgdweb/report/gene/main.html?id=9047503
Impact of O-GlcNAc on cardioprotection by remote ischaemic preconditioning in non-diabetic and diabetic patients. - CARDIO PEG
The cardioprotective capacity and the influence on myocardial O-GlcNAc levels of plasma dialysate from eight healthy volunteers and eight type 2 diabetic patients drawn before and after subjection to an rIPC stimulus were tested on human isolated atrial trabeculae subjected to ischaemia/reperfusion injury. Dialysate from healthy volunteers exposed to rIPC improved post-ischaemic haemodynamic recovery (40 ± 6 vs. 16 ± 2%; P , 0.01) and increased myocardial O-GlcNAc levels. Similar observations were made with dialysate from diabetic patients before exposure to rIPC (43 ± 3 vs. 16 ± 2%; P , 0.001) but no additional cardioprotection or further increase in O-GlcNAc levels was achieved by perfusion with dialysate after exposure to rIPC (44 ± 4 and 42 ± 5 vs. 43 ± 3%; P = 0.7). The glutamine:fructose-6-phosphate amidotransferase (GFAT) inhibitor azaserine abolished the cardioprotective effects and the increment in myocardial O-GlcNAc levels afforded by plasma from diabetic patients and healthy ...
http://pegnac.sdsc.edu/cardiopeg/pmc3584969/
Inhibition of O-GlcNAc transferase activity reprograms prostate cancer cell metabolism<...
TY - JOUR. T1 - Inhibition of O-GlcNAc transferase activity reprograms prostate cancer cell metabolism. AU - Itkonen, Harri M. AU - Gorad, Saurabh S. AU - Duveau, Damien Y. AU - Martin, Sara E S. AU - Barkovskaya, Anna. AU - Bathen, Tone F. AU - Moestue, Siver A. AU - Mills, Ian G. PY - 2016/1/27. Y1 - 2016/1/27. N2 - Metabolic networks are highly connected and complex, but a single enzyme, O-GlcNAc transferase (OGT) can sense the availability of metabolites and also modify target proteins. We show that inhibition of OGT activity inhibits the proliferation of prostate cancer cells, leads to sustained loss of c-MYC and suppresses the expression of CDK1, elevated expression of which predicts prostate cancer recurrence (p=0.00179). Metabolic profiling revealed decreased glucose consumption and lactate production after OGT inhibition. This decreased glycolytic activity specifically sensitized prostate cancer cells, but not cells representing normal prostate epithelium, to inhibitors of oxidative ...
https://pure.qub.ac.uk/en/publications/inhibition-of-o-glcnac-transferase-activity-reprograms-prostate-c
Validity Study of Glutamine to Improve Cardiac Function in Cardiac Surgery - Tabular View - ClinicalTrials.govValidity Study of Glutamine to Improve Cardiac Function in Cardiac Surgery - Tabular View - ClinicalTrials.gov
Cardiosurgery is mostly done under cardiopulmonary bypass. However, the cardiopulmonary bypass and the later recovery of spontaneous circulation, a cardiac ischemia / reperfusion process, may cause myocardial damage and affect cardiac function as well as prognosis.. Glutamine, an amino acid abundant in the human body, plays an important role in the regulation of metabolism and immune cells and the protection of organs. Relative lack of glutamine is reported during stress or serious illness. Animal studies have confirmed that pretreatment with glutamine has a protective effect on the heart, liver, kidney and other organs post ischemia / reperfusion injury. It is also established that glutamine exerts myocardial protection mainly by activating hexosamine biosynthetic pathway, increasing intracellular O-GlcNAc protein modification and expression of heat shock protein 70 (HSP70), starting the protective reaction in the body, improving the function of myocardial cells, and inhibiting the release of ...
https://clinicaltrials.gov/ct2/show/record/NCT01794884?show_rss=Y&sel_rss=mod14
Pomgnt1 (untagged) - Mouse protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase (Pomgnt1), transcript variant 1, ...
Pomgnt1 (untagged) - Mouse protein O-linked mannose beta1,2-N-acetylglucosaminyltransferase (Pomgnt1), transcript variant 1, (10ug), 10 µg.
https://www.acris-antibodies.com/cdna/mouse-cdna/pomgnt1-untagged-mouse-protein-o-linked-mannose-beta1-2-n-acetylglucosaminyltransferase-pomgnt1-transcript-variant-1-10ug-mc201045.htm
Enzymes of N-Acetylglucosamine Metabolism during Germ-tube Formation in Candida albicans | Microbiology SocietyEnzymes of N-Acetylglucosamine Metabolism during Germ-tube Formation in Candida albicans | Microbiology Society
SUMMARY: The enzymes of N-acetyl-D-glucosamine (GlcNAc) metabolism, GlcNAc-6-phosphate deacetylase and GlcN-6-phosphate deaminase were found to be inducible in Candida albicans. The pattern of induction for these enzymes was the same under conditions of germ-tube formation (37 °C) and where yeast cells metabolized GlcNAc with no change in morphology (28 °C); this indicates that these enzymes are not control points in the dimorphic development of C. albicans. During induction there was a 40- and 25-fold increase in specific activity for the deacetylase and the deaminase, respectively, and the maximum specific activity corresponded to the time when all the GlcNAc had been metabolized. The presence of lomofungin (an inhibitor of transcription) or trichodermin (an inhibitor of translation) in cell suspensions of C. albicans containing GlcNAc prevented the increase in specific activity of these enzymes. 2-Deoxyglucose inhibited germ-tube formation, partially inhibited the induction of the deacetylase (43%)
https://www.microbiologyresearch.org/content/journal/micro/10.1099/00221287-128-10-2319
Analysis of nucleocytoplasmic protein shuttling by imaging flow cytometry<...Analysis of nucleocytoplasmic protein shuttling by imaging flow cytometry<...
TY - JOUR. T1 - Analysis of nucleocytoplasmic protein shuttling by imaging flow cytometry. AU - Fasler-Kan, Elizaveta. AU - Baiken, Yeldar. AU - Vorobjev, Ivan A.. AU - Barteneva, Natasha S.. PY - 2016. Y1 - 2016. N2 - Many intracellular signal transduction events involve the reversible shuttling of proteins between the cytoplasm and the nucleus. Study of these processes requires imaging information on the protein localization in a given cell and a large number of measurements to obtain sufficient statistics on the protein localization in the whole population. The protocol describes method for quantitative imaging flow cytometry analysis of intracellular distribution of NF-kappaB in ARPE-19 cells stained with specific fluorochrome-conjugated antibodies. The described technique alone or in combination with standard flow cytometry methods can be applied to study any protein undergoing translocation from cytoplasm into the nucleus in a variety of cell lines as well as in heterogeneous primary cell ...
https://research.nu.edu.kz/en/publications/analysis-of-nucleocytoplasmic-protein-shuttling-by-imaging-flow-c
N-Acetylglucosaminyltransferase III/MGAT3 Research Products: Novus BiologicalsN-Acetylglucosaminyltransferase III/MGAT3 Research Products: Novus Biologicals
N-Acetylglucosaminyltransferase III/MGAT3 products available through Novus Biologicals. Browse our N-Acetylglucosaminyltransferase III/MGAT3 product catalog backed by our Guarantee+.
https://www.novusbio.com/common-name/n-acetylglucosaminyltransferase-iii-mgat3
EGF domain-specific O-linked N-acetylglucosamine transferaseEGF domain-specific O-linked N-acetylglucosamine transferase
This gene encodes an enzyme that acts in the lumen of the endoplasmic reticulum to catalyze the transfer of N-acetylglucosamine to serine or threonine residues of extracellular-targeted proteins. This enzyme modifies proteins containing eukaryotic growth factor (EGF)-like domains, including the Notch receptor, thereby regulating developmental signalling. Mutations in this gene have been observed in individuals with Adams-Oliver syndrome 4. Alternative splicing results in multiple transcript variants. [provided by RefSeq, Aug 2015 ...
https://pharos.nih.gov/idg/targets/Q5NDL2
Oligomannosides or oligosaccharide-lipids as potential substrates for rat liver cytosolic α-d-mannosidase | Biochemical JournalOligomannosides or oligosaccharide-lipids as potential substrates for rat liver cytosolic α-d-mannosidase | Biochemical Journal
We have previously reported the substrate specificity of the cytosolic α-D-mannosidase purified from rat liver using Man9GlcNAc, i.e. Manα1-2Manα1-3(Manα1-2Manα1-6)Man α1-6(Manα1-2Manα1-2Manα1-3)Manβ1-4GlcNAc, as substrate [Grard, Saint-Pol, Haeuw, Alonso, Wieruszeski, Strecker and Michalski (1994) Eur. J. Biochem. 223, 99-106]. Man9GlcNAc is hydrolysed giving Man5GlcNAc, i.e. Manα1-2Manα1-2Manα1-3(Manα1-6)Manβ1-4GlcNAc, possessing the same structure as the oligosaccharide of the dolichol pathway formed in the cytosolic compartment during the biosynthesis of N-glycosylprotein glycans. We study here the activity of the purified cytosolic α-D-mannosidase towards the oligosaccharide-diphosphodolichol intermediates formed during the biosynthesis of N-glycans, and also towards soluble oligosaccharides released from the endoplasmic reticulum which are glucosylated or not and possessing at their reducing end either a single N-acetylglucosamine residue or a di-N-acetylchitobiose ...
http://www.biochemj.org/content/316/3/787
c-Myc alters substrate utilization and O-GlcNAc protein posttranslational modifications without altering cardiac function...c-Myc alters substrate utilization and O-GlcNAc protein posttranslational modifications without altering cardiac function...
The protooncogene C-Myc (Myc) regulates cardiac hypertrophy. Myc promotes compensated cardiac function, suggesting that the operative mechanisms differ from those leading to heart failure. Myc regulation of substrate metabolism is a reasonable target, as Myc alters metabolism in other tissues. We hypothesize that Myc-induced shifts in substrate utilization signal and promote compensated hypertrophy. We used cardiac specific Myc-inducible C57/BL6 male mice between 4-6 months old that develop hypertrophy with tamoxifen (tam). Isolated working hearts and 13Carbon (13C )-NMR were used to measure function and fractional contributions (Fc) to the citric acid cycle by using perfusate containing 13C-labeled free fatty acids,more » acetoacetate, lactate, unlabeled glucose and insulin. Studies were performed at pre-hypertrophy (3-days tam, 3dMyc), established hypertrophy (7-days tam, 7dMyc) or vehicle control (cont). Non-transgenic siblings (NTG) received 7-days tam or vehicle to assess drug effect. ...
https://www.osti.gov/pages/biblio/1229960-myc-alters-substrate-utilization-glcnac-protein-posttranslational-modifications-without-altering-cardiac-function-during-early-aortic-constriction
nagJ - O-GlcNAcase NagJ precursor - Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 /...nagJ - O-GlcNAcase NagJ precursor - Clostridium perfringens (strain ATCC 13124 / DSM 756 / JCM 1290 / NCIMB 6125 / NCTC 8237 /...
Binds carbohydrates (PubMed:16990278). Capable of hydrolyzing the glycosidic link of O-GlcNAcylated proteins. Can bind and deglycosylate O-glycosylated peptides from mammals.
https://www.uniprot.org/uniprot/Q0TR53
Aging | The positive feedback between ACSL4 expression and O-GlcNAcylation contributes to the growth and survival of...
Full Text - Acyl-CoA ligase 4 (ACSL4) has been reported to be overexpressed in hepatocellular carcinoma (HCC) and to enhance cell proliferation. However, the molecular mechanisms underlying the role of ACSL4 in HCC progression remain largely unclear. Here, we aimed to investigate whether and how O-GlcNAcylation and ACSL4 regulate each other and HCC progression. The clinical significance of ACSL4, O-GlcNAc and GLUT1 in HCC was determined by Pearson chi-squared test and Kaplan-Meier analysis. CCK-8, flow cytometry and in vivo tumour formation assays were performed to detect cell proliferation, apoptosis and tumorigenesis. IP technology was used to evaluate the relationship between ACSL4 and O-GlcNAc. ACSL4, GLUT1 and O-GlcNAc levels were elevated in HCC tissues and predicted poor prognosis in HCC patients. ACSL4 overexpression significantly promoted cell proliferation and tumorigenesis and inhibited cell apoptosis, whereas these effects were all obviously impaired when mTOR signalling was repressed
https://www.aging-us.com/article/103092/text
Plus itPlus it
Type 2 diabetes mellitus (T2DM) is a well-recognized independent risk factor for heart failure (HF). T2DM is associated with altered cardiac energy metabolism, leading to ectopic lipid accumulation and glucose overload, the exact contribution of these two parameters remaining unclear. To provide new insight into the mechanism driving the development of diabetic cardiomyopathy, we studied a unique model of T2DM: lipodystrophic Bscl2-/- (seipin knockout (SKO)) mice. Echocardiography and cardiac magnetic resonance imaging revealed hypertrophic cardiomyopathy with left ventricular dysfunction in SKO mice and these two abnormalities were strongly correlated with hyperglycemia. Surprisingly, neither intramyocardial lipid accumulation nor lipotoxic hallmarks were detected in SKO mice. 18F-FDG positron emission tomography showed increased myocardial glucose uptake. Consistently, the O-GlcNAcylated protein levels were markedly increased in SKO heart, suggesting a glucose overload. To test this ...
http://diabetes.diabetesjournals.org/content/early/2017/01/04/db16-0733
GlucosamineGlucosamine
Certainly, N-acetylglucosamine appeared to accelerate the facilitated glucose uptake and boost each GAG and HA synthesis, suggesting that N-acetyl-glucosamine may perhaps be more efficient than native glucosamine. The American College of Rheumatology 2012 recommendations do not propose the use of glucosamine or chondroitin for the management of osteoarthritis. If there is advantage in terms of discomfort or function, it may well be continued. Sufferers nevertheless need to develop a comprehensive program with their physicians to treat osteoarthritis, which consists of diet plan, exercise, weight loss, and working with common, established drugs.. It is significant to point out that these research had been performed in various culture systems, with a variety of formulations and concentrations of glucosamine. The specifics of the culture systems and the formulations are provided in Table 2. Additionally, some of these studies compared the effects of two formulations of glucosamine in order to ...
https://www.letsmovebrooklyn.org/glucosamine/
Pomgnt1 MGI Mouse Gene Detail - MGI:1915523 - protein O-linked mannose beta 1,2-N-acetylglucosaminyltransferasePomgnt1 MGI Mouse Gene Detail - MGI:1915523 - protein O-linked mannose beta 1,2-N-acetylglucosaminyltransferase
View mouse Pomgnt1 Chr4:116123840-116159849 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
http://www.informatics.jax.org/marker/MGI:1915523
Pomgnt2 MGI Mouse Gene Detail - MGI:2143424 - protein O-linked mannose beta 1,4-N-acetylglucosaminyltransferase 2Pomgnt2 MGI Mouse Gene Detail - MGI:2143424 - protein O-linked mannose beta 1,4-N-acetylglucosaminyltransferase 2
View mouse Pomgnt2 Chr9:121981606-121996053 with: phenotypes, sequences, polymorphisms, proteins, references, function, expression
http://www.informatics.jax.org/marker/MGI:2143424
Dynamic Glycosylation in Neurons May Be Linked to Memory, Pathology | ALZFORUMDynamic Glycosylation in Neurons May Be Linked to Memory, Pathology | ALZFORUM
A new technique for detecting proteins modified by β-N-acetyl-D-glucosamine (i.e., O-GlcNAc glycosylation) reveals that the process is reversible and dynamic in neurons and may even play a role in memory. Linda Hsieh-Wilson, California Institute of Technology, Pasadena, and colleagues have developed a quantitative isotopic and chemoenzymatic tagging system (QUIC-Tag) to detect glycosylated proteins inside neurons. Unlike some other methodologies, QUIC-Tag does not require metabolic incorporation of isotopes or rounds of cell division. Cellular levels of O-GlcNAc-proteins are also unperturbed. The technique, which involves protection of the O-GlcNAc moieties by biotinylation followed by avidin-based purification and then mass spectrometry detection, is particularly suited to non-dividing cells, such as neurons.. The technique is explained in detail in the May 13 Nature Chemical Biology online. First author Nelly Khidekel and colleagues also describe how they used the QUIC-Tag method to detect ...
http://www.alzforum.org/news/research-news/dynamic-glycosylation-neurons-may-be-linked-memory-pathology
Keratan sulfate: an up-to-date review.
Keratan sulfate (KS) is a glycosaminoglycan (GAG) type consisted of a sulfated poly-N-acetyl lactosamine chain. Besides acting as a constitutive molecule of the extracellular matrices, this GAG also plays a role as a hydrating and signaling agent in
http://www.biomedsearch.com/nih/Keratan-sulfate-up-to-date/25179279.html
Histone H2B (S112) PAb - GlycoScientific
Rabbit polyclonal antibody to human Histone H2B (H2B, NP_001019770.1). GS0021 binds to histone H2B regardless of the presence of an O-GlcNAc on serine 112 (S112). Amino acid sequence of the region flanking S112 suggests cross-reactivity with histone H2B of multiple species including mouse, rat, chicken, hamster and pri
https://www.glycoscientific.com/products/histone-h2b-s112-pab
Lectin
Wheat germ agglutinin (WGA) is one of the most widely used lectins in cell biology. The receptor sugar for WGA is N-acetylglucosamine, with preferential binding to dimers and trimers of this sugar. WGA can bind oligosaccharides containing terminal N-acetylglucosamine or chitobiose, structures which are common to many serum and membrane glycoproteins. Bacterial cell wall peptidoglycans, chitin, cartilage glycosaminoglycans, and glycolipids can also bind WGA. Native WGA has also been reported to interact with some glycoproteins via sialic acid residues (see succinylated WGA). ...
https://au.mpbio.com/life-sciences/immunology/proteins-enzymes/lectin
Global (US, EU, Japan & China) N-Acetyl-D-Glucosamine (CAS 7512-17-6) Industry Supply and Consumption 2016 to 2021 Market...Global (US, EU, Japan & China) N-Acetyl-D-Glucosamine (CAS 7512-17-6) Industry Supply and Consumption 2016 to 2021 Market...
Global (US, EU, Japan & China) N-Acetyl-D-Glucosamine (CAS 7512-17-6) Industry Supply and Consumption 2016 to 2021 Market Research Report
https://www.newsmaker.com.au/news/49714/global-us-eu-japan-china-nacetyldglucosamine-cas-7512176-industry-supply-and-consumption-2016-to-2021-market-research-report
Rapid myoglobin aggregation through... | ERARapid myoglobin aggregation through... | ERA
The extent of glycation and conformational changes of horse myoglobin (Mb) upon glycation with N-acetyl-glucosamine (GlcNAc), glucose...
https://era.library.ualberta.ca/items/86c27fd1-f581-440e-930c-27cd7ff1c81d
Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents...Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents...
X-MOL提供的期刊论文更新，Proceedings of the National Academy of Sciences of the United States of America--Spatiotemporal gating of SIRT1 functions by O-GlcNAcylation is essential for liver metabolic switching and prevents hyperglycemia [Physiology]，Tandrika Chattopadhyay, Babukrishna Maniyadath, Hema P. Bagul, Arindam Chakraborty, Namrata Shukla, Srikanth Budnar, Abinaya Rajendran, Arushi Shukla, Siddhesh S. Kamat, Ullas Kolthur-Seetharam
https://www.x-mol.com/paper/1243046918234771456
RCSB PDB - 1W3B: The superhelical TPR domain of O-linked GlcNAc transferase reveals structural similarities to importin alpha.RCSB PDB - 1W3B: The superhelical TPR domain of O-linked GlcNAc transferase reveals structural similarities to importin alpha.
As a member of the wwPDB, the RCSB PDB curates and annotates PDB data according to agreed upon standards. The RCSB PDB also provides a variety of tools and resources. Users can perform simple and advanced searches based on annotations relating to sequence, structure and function. These molecules are visualized, downloaded, and analyzed by users who range from students to specialized scientists.
http://www.rcsb.org/structure/1W3B
Journal News: JBC: Probing beneath the surfaceJournal News: JBC: Probing beneath the surface
In 2014, Gerald Hart, an associate editor for the Journal of Biological Chemistry, organized a thematic minireview series on O-GlcNAcylation. O-GlcNAc is found on many different proteins throughout the cell. Its function varies dependent upon the protein to which it is attached. Much like phosphorylation, one known purpose of O-GlcNAc is to control signaling in response to nutrients. Holt, who is now the chief science officer at NorthShore Bio, describes O-GlcNAc as an orthogonal method of regulating the same proteins: Its like a rivet: If theres a carbohydrate at a phosphorylation site, then that phosphorylation site is no longer regulated by classical phosphorylation pathways. Instead, it becomes regulated by the O-GlcNAc regulatory pathways.. Methods for studying phosphorylation have advanced rapidly in recent years, thanks in part to the existence of site-specific antibodies, while methods for studying O-GlcNAc continue to lag behind. Researchers only recently have begun to recognize the ...
http://www.asbmb.org/asbmbtoday/201604/JournalNews/JBCHart/
O-GlcNAcase/OGA/MGEA5 Antibody (1C7) (H00010724-M02): Novus BiologicalsO-GlcNAcase/OGA/MGEA5 Antibody (1C7) (H00010724-M02): Novus Biologicals
Mouse Monoclonal Anti-O-GlcNAcase/OGA/MGEA5 Antibody (1C7). Validated: WB, ELISA, ICC/IF. Tested Reactivity: Human. 100% Guaranteed.
https://www.novusbio.com/products/o-glcnacase-oga-mgea5-antibody-1c7_h00010724-m02
Study finds low sugar metabolite associates with disability, neurodegeneration in MSStudy finds low sugar metabolite associates with disability, neurodegeneration in MS
Irvine, CA - May 13, 2021 - A new University of California, Irvine-led study finds low serum levels of the sugar N-acetylglucosamine (GlcNAc), is associated wit
https://clinicalnews.org/2021/05/13/study-finds-low-sugar-metabolite-associates-with-disability-neurodegeneration-in-ms/
GLC 2000 - ProgressiveHealth.comGLC 2000 - ProgressiveHealth.com
GLC 2000 uses high-strength and multiple forms of glucosamine. Find out what advantages this combination of the 4 forms of glucosamine give GLC 2000.
http://www.progressivehealth.com/glc-2000.htm
N-AcetylglucosamineN-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. Comparable ... Grigorian A, Araujo L, Naidu NN, Place DJ, Choudhury B, Demetriou M (2011). "N-Acetylglucosamine Inhibits T-helper 1 (Th1)/T- ... "Inhibition of elastase enzyme release from human polymorphonuclear leukocytes by N-acetyl-galactosamine and N-acetyl-glucosamine ...
https://en.wikipedia.org/wiki/N-Acetylglucosamine
N-Acetylglucosamine receptorN-Acetylglucosamine receptor
The N-Acetylglucosamine receptor is a receptor which binds N-Acetylglucosamine. The N-Acetylglucosamine (GlcNAc) receptor has ... N-Acetylglucosamine+Receptor at the US National Library of Medicine Medical Subject Headings (MeSH) v t e (Articles with short ... "Targeted gene delivery via N-acetylglucosamine receptor mediated endocytosis". Journal of Nanoscience and Nanotechnology. 14 ( ...
https://en.wikipedia.org/wiki/N-Acetylglucosamine_receptor
N-acetylglucosamine kinaseN-acetylglucosamine kinase
In enzymology, a N-acetylglucosamine kinase (EC 2.7.1.59) is an enzyme that catalyzes the chemical reaction ATP + N-acetyl-D- ... doi:10.1016/0076-6879(66)09085-2. Datta A (October 1970). "Studies on hog spleen N-acetylglucosamine kinase. I. Purification ... Other names in common use include acetylglucosamine kinase (phosphorylating), ATP:2-acetylamino-2-deoxy-D-glucose 6- ... and properties of N-acetylglucosamine kinase". Biochimica et Biophysica Acta. 220 (1): 51-60. doi:10.1016/0005-2744(70)90228-7 ...
https://en.wikipedia.org/wiki/N-acetylglucosamine_kinase
N-acetylglucosamine deacetylaseN-acetylglucosamine deacetylase
I. N-acetylglucosamine deacetylase". The Journal of Biological Chemistry. 226 (1): 115-24. PMID 13428742. Portal: Biology v t e ... In enzymology, a N-acetylglucosamine deacetylase (EC 3.5.1.33) is an enzyme that catalyzes the chemical reaction N-acetyl-D- ...
https://en.wikipedia.org/wiki/N-acetylglucosamine_deacetylase
Uridine diphosphate N-acetylglucosamineUridine diphosphate N-acetylglucosamine
... or UDP-GlcNAc is a nucleotide sugar and a coenzyme in metabolism. It is used by ... UDP-GlcNAc is extensively involved in intracellular signaling as a substrate for O-linked N-acetylglucosamine transferases ( ... Hanover, J. A. (2001). "Glycan-dependent signaling: O-linked N-acetylglucosamine". The FASEB Journal. 15 (11): 1865-1876. ... glycosyltransferases to transfer N-acetylglucosamine residues to substrates. D-Glucosamine is made naturally in the form of ...
https://en.wikipedia.org/wiki/Uridine_diphosphate_N-acetylglucosamine
UDP-N-acetylglucosamine diphosphorylaseUDP-N-acetylglucosamine diphosphorylase
Acetylglucosamine 1-phosphate uridylyltransferase, UDP-acetylglucosamine pyrophosphorylase, uridine diphosphate-N- ... acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine phosphorylase, and acetylglucosamine 1-phosphate ... In enzymology, an UDP-N-acetylglucosamine diphosphorylase (EC 2.7.7.23) is an enzyme that catalyzes the chemical reaction UTP ... Other names in common use include UDP-N-acetylglucosamine pyrophosphorylase, uridine diphosphoacetylglucosamine ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_diphosphorylase
Peptidoglycan-N-acetylglucosamine deacetylasePeptidoglycan-N-acetylglucosamine deacetylase
N-acetylglucosamine deacetylase, peptidoglycan GlcNAc deacetylase, peptidoglycan N-acetylglucosamine deacetylase, PG N- ... Peptidoglycan-N-acetylglucosamine+deacetylase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: ... Peptidoglycan-N-acetylglucosamine deacetylase (EC 3.5.1.104, HP310, PgdA, SpPgdA, BC1960, peptidoglycan deacetylase, ... "Peptidoglycan N-acetylglucosamine deacetylases from Bacillus cereus, highly conserved proteins in Bacillus anthracis". The ...
https://en.wikipedia.org/wiki/Peptidoglycan-N-acetylglucosamine_deacetylase
UDP-N-acetylglucosamine kinaseUDP-N-acetylglucosamine kinase
... (EC 2.7.1.176, UNAG kinase, zeta toxin, toxin PezT, ATP:UDP-N-acetyl-D-glucosamine 3'- ... UDP-N-acetylglucosamine+kinase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: Biology (EC 2.7.1 ... UDP-N-acetylglucosamine 1-carboxyvinyltransferase. These enzymes are found as part of plasmid-encoded and chromosomal bacterial ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_kinase
N-acetylglucosamine-6-sulfataseN-acetylglucosamine-6-sulfatase
N-acetylglucosamine 6-sulfate sulfatase, O,N-disulfate O-sulfohydrolase, acetylglucosamine 6-sulfatase, chondroitinsulfatase, ... N-acetylglucosamine-6-sulfatase (EC 3.1.6.14, glucosamine (N-acetyl)-6-sulfatase, systematic name N-acetyl-D-glucosamine-6- ... N-acetylglucosamine-6-sulfatase at the US National Library of Medicine Medical Subject Headings (MeSH) This article ... Kresse H, Fuchs W, Glössl J, Holtfrerich D, Gilberg W (December 1981). "N-acetylglucosamine-6-sulfate by human β-N- ...
https://en.wikipedia.org/wiki/N-acetylglucosamine-6-sulfatase
UDP-N-acetylglucosamine 4-epimeraseUDP-N-acetylglucosamine 4-epimerase
... uridine diphosphate N-acetylglucosamine-4-epimerase, and uridine 5'-diphospho-N-acetylglucosamine-4-epimerase. This enzyme ... In enzymology, an UDP-N-acetylglucosamine 4-epimerase (EC 5.1.3.7) is an enzyme that catalyzes the chemical reaction UDP-N- ... Other names in common use include UDP acetylglucosamine epimerase, uridine diphosphoacetylglucosamine epimerase, ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_4-epimerase
UDP-N-acetylglucosamine 2-epimeraseUDP-N-acetylglucosamine 2-epimerase
... uridine diphospho-N-acetylglucosamine 2'-epimerase, and uridine diphosphate-N-acetylglucosamine-2'-epimerase. This enzyme ... The UDP-N-acetylglucosamine 2-epimerase from rat liver displays both epimerase and kinase activity. As of late 2007, 4 ... In enzymology, an UDP-N-acetylglucosamine 2-epimerase (EC 5.1.3.14) is an enzyme that catalyzes the chemical reaction UDP-N- ... Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase". J. Biol. Chem ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_2-epimerase
N-acetylglucosamine-6-phosphate deacetylaseN-acetylglucosamine-6-phosphate deacetylase
"N-acetylglucosamine 6-phosphate deacetylase (nagA) is required for N-acetyl glucosamine assimilation in Gluconacetobacter ... "An alternative route for recycling of N-acetylglucosamine from peptidoglycan involves the N-acetylglucosamine ... "Purification and characterization of N-acetylglucosamine 6-phosphate deacetylase with activity against N-acetylglucosamine from ... N-acetylglucosamine (GlcNAc) enters the cell as part of the breakdown of the cell wall. GlcNAc, a monosaccharide and derivative ...
https://en.wikipedia.org/wiki/N-acetylglucosamine-6-phosphate_deacetylase
N-acetylglucosamine-1-phosphate transferaseN-acetylglucosamine-1-phosphate transferase
... is a transferase enzyme. It is made up of two alpha (α), two betas (β), and two ... GeneReviews/NIH/NCBI/UW entry on Mucolipidosis II GeneReviews/NIH/NCBI/UW entry on Mucolipidosis III Gamma N-acetylglucosamine- ...
https://en.wikipedia.org/wiki/N-acetylglucosamine-1-phosphate_transferase
UDP-N-acetylglucosamine 1-carboxyvinyltransferaseUDP-N-acetylglucosamine 1-carboxyvinyltransferase
... pyruvate-UDP-acetylglucosamine transferase, pyruvate-uridine diphospho-N-acetylglucosamine transferase, pyruvate-uridine ... UDP-N-acetylglucosamine enoylpyruvyltransferase, enoylpyruvate transferase, phosphoenolpyruvate-UDP-acetylglucosamine-3- ... In enzymology, an UDP-N-acetylglucosamine 1-carboxyvinyltransferase (EC 2.5.1.7) is an enzyme that catalyzes the first ... ISBN 0-07-144578-1. Other names in common use include MurA transferase, UDP-N-acetylglucosamine 1-carboxyvinyl-transferase, ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_1-carboxyvinyltransferase
UDP-N-acetylglucosamine 6-dehydrogenaseUDP-N-acetylglucosamine 6-dehydrogenase
In enzymology, an UDP-N-acetylglucosamine 6-dehydrogenase (EC 1.1.1.136) is an enzyme that catalyzes the chemical reaction UDP- ... Other names in common use include uridine diphosphoacetylglucosamine dehydrogenase, UDP-acetylglucosamine dehydrogenase, UDP-2- ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_6-dehydrogenase
UDP-N-acetylglucosamine 2-epimerase (hydrolysing)UDP-N-acetylglucosamine 2-epimerase (hydrolysing)
... (EC 3.2.1.183, UDP-N-acetylglucosamine 2-epimerase, GNE (gene), siaA (gene), ... UDP-N-acetylglucosamine+2-epimerase+(hydrolysing) at the US National Library of Medicine Medical Subject Headings (MeSH) Portal ... Blume A, Ghaderi D, Liebich V, Hinderlich S, Donner P, Reutter W, Lucka L (June 2004). "UDP-N-acetylglucosamine 2-epimerase/N- ... Molecular cloning and functional expression of UDP-N-acetyl-glucosamine 2-epimerase/N-acetylmannosamine kinase". The Journal of ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_2-epimerase_(hydrolysing)
UDP-3-O-N-acetylglucosamine deacetylaseUDP-3-O-N-acetylglucosamine deacetylase
In molecular biology, UDP-3-O-N-acetylglucosamine deacetylase (also known as UDP-3-O-[3-hydroxymyristoyl] N-acetylglucosamine ... The structure of UDP-3-O-N-acetylglucosamine deacetylase (LpxC) from Aquifex aeolicus has a two-layer alpha/beta structure ...
https://en.wikipedia.org/wiki/UDP-3-O-N-acetylglucosamine_deacetylase
UDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferaseUDP-N-acetylglucosamine-undecaprenyl-phosphate N-acetylglucosaminephosphotransferase
... (EC 2.7.8.33, UDP-N-acetylglucosamine: ... UDP-N-acetylglucosamine---undecaprenyl-phosphate+N-acetylglucosaminephosphotransferase at the US National Library of Medicine ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine—undecaprenyl-phosphate_N-acetylglucosaminephosphotransferase
UDP-3-O-acyl-N-acetylglucosamine deacetylaseUDP-3-O-acyl-N-acetylglucosamine deacetylase
N-acetylglucosamine deacetylase) is an enzyme with systematic name UDP-3-O-((3R)-3-hydroxymyristoyl)-N-acetylglucosamine ... N-acetylglucosamine deacetylase, UDP-(3-O-acyl)-N-acetylglucosamine deacetylase, UDP-3-O-(R-3-hydroxymyristoyl)-N- ... UDP-3-O-acyl-N-acetylglucosamine deacetylase (EC 3.5.1.108, LpxC protein, LpxC enzyme, LpxC deacetylase, deacetylase LpxC, UDP- ... UDP-3-O-acyl-N-acetylglucosamine+deacetylase at the US National Library of Medicine Medical Subject Headings (MeSH) Portal: ...
https://en.wikipedia.org/wiki/UDP-3-O-acyl-N-acetylglucosamine_deacetylase
UDP-galactose-UDP-N-acetylglucosamine galactose phosphotransferaseUDP-galactose-UDP-N-acetylglucosamine galactose phosphotransferase
In enzymology, an UDP-galactose-UDP-N-acetylglucosamine galactose phosphotransferase (EC 2.7.8.18) is an enzyme that catalyzes ... "Enzymatic transfer of galactosyl phosphate from UDP-galactose to UDP-N-acetylglucosamine". FEBS Lett. 151 (1): 15-8. doi: ...
https://en.wikipedia.org/wiki/UDP-galactose—UDP-N-acetylglucosamine_galactose_phosphotransferase
UDP-N-acetylglucosamine-decaprenyl-phosphate N-acetylglucosaminephosphotransferaseUDP-N-acetylglucosamine-decaprenyl-phosphate N-acetylglucosaminephosphotransferase
UDP-N-acetylglucosamine---decaprenyl-phosphate+N-acetylglucosaminephosphotransferase at the US National Library of Medicine ... UDP-N-acetylglucosamine---decaprenyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.35, GlcNAc-1-phosphate ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine—decaprenyl-phosphate_N-acetylglucosaminephosphotransferase
UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferaseUDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase
UDP-acetylglucosamine-dolichol phosphate acetylglucosamine phosphotransferase, and UDP-acetylglucosamine-dolichol phosphate ... Other names in common use include UDP-D-N-acetylglucosamine N-acetylglucosamine 1-phosphate transferase, UDP-GlcNAc:dolichyl- ... Villemez CL, Carlo PL (1980). "Properties of a soluble polyprenyl phosphate UDP-D-N-acetylglucosamine N-acetylglucosamine-1- ... In enzymology, an UDP-N-acetylglucosamine-dolichyl-phosphate N-acetylglucosaminephosphotransferase (EC 2.7.8.15) is an enzyme ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine—dolichyl-phosphate_N-acetylglucosaminephosphotransferase
UDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferaseUDP-N-acetylglucosamine-lysosomal-enzyme N-acetylglucosaminephosphotransferase
UDP-N-acetylglucosamine:glycoprotein N-acetylglucosamine-1-phosphotransferase, and UDP-N-acetylglucosamine:glycoprotein N- ... lysosomal enzyme precursor acetylglucosamine-1-phosphotransferase, UDP-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1 ... Other names in common use include UDP-N-acetylglucosamine:lysosomal enzyme N-acetylglucosamine-1-phosphotransferase, UDP-GlcNAc ... Waheed A, Hasilik A, von Figura K (1982). "UDP-N-acetylglucosamine:lysosomal enzyme precursor N-acetylglucosamine-1- ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine—lysosomal-enzyme_N-acetylglucosaminephosphotransferase
UDP-xylose and UDP-N-acetylglucosamine transporterUDP-xylose and UDP-N-acetylglucosamine transporter
... is a protein that in humans is encoded by the SLC35B4 gene. Solute carrier ... gene SLC35B4 encodes a bifunctional nucleotide sugar transporter with specificity for UDP-xylose and UDP-N-acetylglucosamine". ...
https://en.wikipedia.org/wiki/UDP-xylose_and_UDP-N-acetylglucosamine_transporter
N-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidaseN-acetylglucosamine-1-phosphodiester alpha-N-acetylglucosaminidase
The enzyme N-acetylglucosamine-1-phosphodiester α-N-acetylglucosaminidase (EC 3.1.4.45) catalyzes the reaction glycoprotein N- ...
https://en.wikipedia.org/wiki/N-acetylglucosamine-1-phosphodiester_alpha-N-acetylglucosaminidase
Uridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferaseUridine diphospho-N-acetylglucosamine:polypeptide beta-N-acetylglucosaminyltransferase
UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining)UDP-N-acetylglucosamine 4,6-dehydratase (configuration-retaining)
... (EC 4.2.1.135, PglF) is an enzyme with systematic name UDP-N- ... UDP-N-acetylglucosamine+4,6-dehydratase+(configuration-retaining) at the US National Library of Medicine Medical Subject ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_4,6-dehydratase_(configuration-retaining)
UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)UDP-N-acetylglucosamine 4,6-dehydratase (configuration-inverting)
... (EC 4.2.1.115, FlaA1, UDP-N-acetylglucosamine 5-inverting 4,6 ... UDP-N-acetylglucosamine+4,6-dehydratase+(configuration-inverting) at the US National Library of Medicine Medical Subject ... PseB, UDP-N-acetylglucosamine hydro-lyase (inverting, UDP-2-acetamido-2,6-dideoxy-β-L)arabino-hex-4-ulose-forming)) is an ... synthesis from UDP-N-acetylglucosamine by a single enzymatic reaction". Glycobiology. 16 (9): 8C-14C. doi:10.1093/glycob/cwl010 ...
https://en.wikipedia.org/wiki/UDP-N-acetylglucosamine_4,6-dehydratase_(configuration-inverting)
Acyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine O-acyltransferaseAcyl-(acyl-carrier-protein)-UDP-N-acetylglucosamine O-acyltransferase
In enzymology, an acyl-[acyl-carrier-protein]-UDP-N-acetylglucosamine O-acyltransferase (EC 2.3.1.129) is an enzyme that ... The systematic name of this enzyme class is (R)-3-hydroxytetradecanoyl-[acyl-carrier-protein]:UDP-N-acetylglucosamine 3-O-(3- ... Other names in common use include UDP-N-acetylglucosamine acyltransferase and uridine diphosphoacetylglucosamine ... N-acetylglucosamine Thus, the two substrates of this enzyme are (R)-3-hydroxytetradecanoyl-acyl-carrier-protein and UDP-N- ...
https://en.wikipedia.org/wiki/Acyl-(acyl-carrier-protein)—UDP-N-acetylglucosamine_O-acyltransferase
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine...N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine...
N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine: ... N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine: ... octacis-undecaprenyl-N-acetylglucosamine + 2 tRNA This Staphylococcus aureus enzyme catalyses the successive transfer of two ... octacis-undecaprenyl-N-acetylglucosamine + 2 glycyl-tRNA ⇌ {\displaystyle \rightleftharpoons } N-acetylmuramoyl-L-alanyl-D- ...
https://en.wikipedia.org/wiki/N-acetylmuramoyl-L-alanyl-D-glutamyl-L-lysyl-(N6-triglycine)-D-alanyl-D-alanine-diphosphoundecaprenyl-N-acetylglucosamine:glycine_glycyltransferase
Side Effects of N-Acetylglucosamine | livestrongSide Effects of N-Acetylglucosamine | livestrong
N-acetylglucosamine supplements are generally considered safe. Minor side effects occur uncommonly and serious side effects are ... Side Effects of N-Acetylglucosamine By Tina M. St. John, MD Updated April 29, 2018 ... N-acetylglucosamine (NAG) is an amino sugar, a derivative of the simple sugar glucose. Your body produces NAG, which serves as ... Experimental and Therapeutic Medicine: Effect of N-Acetylglucosamine Administration on Cartilage Metabolism and Safety in ...
https://www.livestrong.com/article/295135-the-side-effects-of-n-acetyl-glucosamine/
Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectinsAntinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins
Incorporation of N-acetylglucosamine-specific agglutinins from wheat germ (Triticum aestivum; WGA), thorn apple (Datura ... Antinutritive effects of wheat-germ agglutinin and other N-acetylglucosamine-specific lectins Br J Nutr. 1993 Jul;70(1):313-21. ... Incorporation of N-acetylglucosamine-specific agglutinins from wheat germ (Triticum aestivum; WGA), thorn apple (Datura ...
https://pubmed.ncbi.nlm.nih.gov/8399111/?dopt=AbstractPlus
N-acetylglucosamine - InnvistaN-acetylglucosamine - Innvista
Home › Health › Nutrition › Essential Sugars › N-acetylglucosamine. N-acetylglucosamine. Note: See also Economical Alternatives ... N-acetylglucosamine is another member of the group of eight essential sugars. It is best known by its derivative, Glucosamine, ... N-acetylglucosamine concentrations were also found in mammalian brains, suggesting a role in nerve function. This would also ... The thyroid gland is known to have N-acetylglucosamine receptors on its surface which are believed to play a role in the ...
https://innvista.com/health/nutrition/essential-sugars/n-acetylglucosamine/
4U0W: Crystal Structure Of Yvoa From Bacillus Subtilis In Complex With N- Acetylglucosamine-6-phosphate4U0W: Crystal Structure Of Yvoa From Bacillus Subtilis In Complex With N- Acetylglucosamine-6-phosphate
Molecules | Free Full-Text | Intracellular Hydrolysis of Small-Molecule O-Linked N-Acetylglucosamine Transferase Inhibitors...Molecules | Free Full-Text | Intracellular Hydrolysis of Small-Molecule O-Linked N-Acetylglucosamine Transferase Inhibitors...
UDP: uridine diphosphate; GlcNAc: N-Acetylglucosamine; UDP-GlcNAc: uridine diphosphate N-acetylglucosamine; DMSO: dimethyl ... "Intracellular Hydrolysis of Small-Molecule O-Linked N-Acetylglucosamine Transferase Inhibitors Differs among Cells and Is Not ... "Intracellular Hydrolysis of Small-Molecule O-Linked N-Acetylglucosamine Transferase Inhibitors Differs among Cells and Is Not ... Intracellular Hydrolysis of Small-Molecule O-Linked N-Acetylglucosamine Transferase Inhibitors Differs among Cells and Is Not ...
https://www.mdpi.com/1420-3049/25/15/3381
Relaxed acyl chain specificity of Bordetella UDP-N-acetylglucosamine acyltransferases<...
Relaxed acyl chain specificity of Bordetella UDP-N-acetylglucosamine acyltransferases. Charles R Sweet, Andrew Preston, Elinor ... Relaxed acyl chain specificity of Bordetella UDP-N-acetylglucosamine acyltransferases. / Sweet, Charles R; Preston, Andrew; ... Relaxed acyl chain specificity of Bordetella UDP-N-acetylglucosamine acyltransferases. In: Journal of Biological Chemistry. ... These acyl chains are attached by UDP-N-acetylglucosamine acyltransferase (LpxA). To determine the origin of the acyl ...
https://researchportal.bath.ac.uk/en/publications/relaxed-acyl-chain-specificity-of-bordetella-udp-n-acetylglucosam
An acidic, thermostable exochitinase with β-N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin...An acidic, thermostable exochitinase with β-N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin...
N-acetylglucosaminidase activity from Paenibacillus barengoltzii converting chitin to N-acetyl glucosamine ...
https://biotechnologyforbiofuels.biomedcentral.com/articles/10.1186/s13068-014-0174-y/tables/1
Fragmentation of negative ions from N-linked carbohydrates: Part 6. Glycans containing one N-acetylglucosamine in the core<...Fragmentation of negative ions from N-linked carbohydrates: Part 6. Glycans containing one N-acetylglucosamine in the core<...
Fragmentation of negative ions from N-linked carbohydrates: Part 6. Glycans containing one N-acetylglucosamine in the core. ... Fragmentation of negative ions from N-linked carbohydrates: Part 6. Glycans containing one N-acetylglucosamine in the core. In ... Fragmentation of negative ions from N-linked carbohydrates: Part 6. Glycans containing one N-acetylglucosamine in the core. / ... Fragmentation of negative ions from N-linked carbohydrates: Part 6. Glycans containing one N-acetylglucosamine in the core. ...
https://research.tees.ac.uk/en/publications/fragmentation-of-negative-ions-from-n-linked-carbohydrates-part-6-3
Induction of PNAd and N-acetylglucosamine 6-O-sulfotransferases 1 and 2 in mouse collagen-induced arthritis | BMC Immunology |...Induction of PNAd and N-acetylglucosamine 6-O-sulfotransferases 1 and 2 in mouse collagen-induced arthritis | BMC Immunology |...
The sulfation of these ligands depends on the action of two HEV-expressed N-acetylglucosamine 6-O-sulfotransferases: GlcNAc6ST- ... Yang, J., Rosen, S.D., Bendele, P. et al. Induction of PNAd and N-acetylglucosamine 6-O-sulfotransferases 1 and 2 in mouse ... Induction of PNAd and N-acetylglucosamine 6-O-sulfotransferases 1 and 2 in mouse collagen-induced arthritis. *Jiwei Yang1,4, ... The sulfation of these ligands depends on the action of two HEV-expressed N-acetylglucosamine 6-O-sulfotransferases: GlcNAc6ST- ...
https://bmcimmunol.biomedcentral.com/articles/10.1186/1471-2172-7-12
N Acetyl Glucosamine - UPC Food SearchN Acetyl Glucosamine - UPC Food Search
N Acetyl Glucosamine. What is N-Acetyl-Glucosamine?. N-Acetyl-Glucosamine (NAG) is a monosaccharide derivative of glucose. It ... Products containing N Acetyl Glucosamine. The percentage represents the approximate total number of food products from UPC Food ... Searchs data that contain the ingredient, "N Acetyl Glucosamine".. The data is calculated from UPC Food Searchs product data ...
https://upcfoodsearch.com/food-ingredients/n-acetyl-glucosamine/
N-Acetyl Glucosamine (NAG) - Humblebee & MeN-Acetyl Glucosamine (NAG) - Humblebee & Me
N-Acetyl Glucosamine (NAG) is a compound that is found in our skin. In skin care products it improves barrier function, boosts ... I like to save N-Acetyl Glucosamine (NAG) for facial products, where it can work its magic and be appreciated. NAG does so many ... Otherwise you could replace N-Acetyl Glucosamine (NAG) with a humectant, like glycerine or sodium lactate, or just use more ... Stored somewhere cool, dark, and dry, N-Acetyl Glucosamine (NAG) should last two years.. ...
https://www.humblebeeandme.com/project/n-acetyl-glucosamine-nag/
N. Acetylglucosamine pack of 60 capsules - EpigeneticsN. Acetylglucosamine pack of 60 capsules - Epigenetics
Acetylglucosamine pack of 60 capsules are a pure food supplement, manufactured in a high quality production facility in the UK. ... N. Acetylglucosamine pack of 60 capsules. £15.94. Sorry we cant ship this product to you while youre location is set to Error ... Be the first to review "N. Acetylglucosamine pack of 60 capsules" Cancel reply. You must be logged in to post a review. ... N. Acetylglucosamine is an amino sugar (the building blocks of mucopolysaccharides. It is formed from L-glutamine and glucose ...
https://www.epigenetics-international.com/product/n-acetylglucosamine-pack-of-60-capsules/
IMSEAR at SEARO: Turnover of inducible N-acetylglucosamine catabolic enzymes in Candida albicans.
Turnover of inducible N-acetylglucosamine catabolic enzymes in Candida albicans.. Authors: Biswas, M. Singh, B. Rai, Y P. Datta ... Biswas M, Singh B, Rai YP, Datta A. Turnover of inducible N-acetylglucosamine catabolic enzymes in Candida albicans. Indian ...
https://imsear.searo.who.int/handle/123456789/57178
Organika NAG (N-ACETYL GLUCOSAMINE) 500 mg 60 CapsulesOrganika NAG (N-ACETYL GLUCOSAMINE) 500 mg 60 Capsules
NAG (N-Acetyl Glucosamine) helps to reduce inflammation and joint pain for easier movement and better joint health. ... N-Acetylglucosamine (Crab (Exoskeleton)). 500 mg. Glucosamine Sulfate (Glucosamine Sulfate Potassium Chloride from shrimp, ...
https://healtha.ca/products/organika-nag-n-acetyl-glucosamine-500-mg-60-capsules
N-Acetyl Glucosamine (NAG) by Allergy Research Group 90ctN-Acetyl Glucosamine (NAG) by Allergy Research Group 90ct
... .product-template__content{ background-color: #ffffff; } .sidebar- ...
https://digestivewarrior.com/products/n-acetyl-glucosamine-nag-by-allergy-research-group
JoF | Free Full-Text | Candida spp./Bacteria Mixed BiofilmsJoF | Free Full-Text | Candida spp./Bacteria Mixed Biofilms
Frank, K.L.; Patel, R. Poly-N-acetylglucosamine is not a major component of the extracellular matrix in biofilms formed by ... Reduction of S. aureus poly-β-(1,6)-N-acetylglucosamine. [151]. Staphylococcus aureus, Pseudomonas aeruginosa, Acinetobacter ... Also, the abundance of S. aureus poly-β-(1,6)-N-acetylglucosamine was also cut with anidulafungin. ...
https://www.mdpi.com/2309-608X/6/1/5
Studies on hog spleen N-acetylglucosamine kinase : II. Allosteric regulation of the activity of N-acetylglucosamine kinase -...Studies on hog spleen N-acetylglucosamine kinase : II. Allosteric regulation of the activity of N-acetylglucosamine kinase -...
Studies on hog spleen N-acetylglucosamine kinase : II. Allosteric regulation of the activity of N-acetylglucosamine kinase ... Kinetic studies of hog spleen N-acetylglucosamine kinase indicate that N-acetylglucosamine-6-phosphate (GlcNAc-6-p), the ... All of these results strongly suggest that the hog spleen N-acetylglucosamine kinase is a regulatory enzyme, and the end ... Datta, Asis (1971) Studies on hog spleen N-acetylglucosamine kinase : II. Allosteric regulation of the activity of N- ...
http://repository.ias.ac.in/9315/
PGM3 gene: MedlinePlus GeneticsPGM3 gene: MedlinePlus Genetics
The PGM3 enzyme converts a molecule called N-acetylglucosamine-6-phosphate into a different molecule called N-acetylglucosamine ... This conversion is required to make a sugar called uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), which is needed to ...
https://medlineplus.gov/genetics/gene/pgm3/
OGT / O-Linked N-Acetylglucosamine Transferase抗体(ab96718)| Abcam中文官网OGT / O-Linked N-Acetylglucosamine Transferase抗体(ab96718)| Abcam中文官网
O-Linked N-Acetylglucosamine Transferase抗体经WB,IP验证，可与人,小鼠,大鼠样本反 ... O-Linked N-Acetylglucosamine Transferase兔多克隆抗体(ab96718)，OGT / ... O linked N acetylglucosamine (GlcNAc) transferase antibody. *O linked N acetylglucosamine transferase 110 kDa subunit antibody ... UDP N acetylglucosamine peptide N acetylglucosaminyltransferase 110 kDa subunit antibody. *UDP N acetylglucosamine peptide
https://www.abcam.cn/ogt--o-linked-n-acetylglucosamine-transferase-antibody-ab96718.html
Anti-aging: Why You Should Look Out For Acetyl Glucosamine. - The Dermatology ReviewAnti-aging: Why You Should Look Out For Acetyl Glucosamine. - The Dermatology Review
Acetyl glucosamine, or N-acetyl glucosamine, is a monosaccharide derivative of glucose, yes the sugar. Acetyl glucosamine has ... How Does Acetyl Glucosamine Benefit The Skin?. Acetyl glucosamine functions as an anti-aging skin care ingredient based on its ... Is Acetyl Glucosamine Safe?. There is limited data available on the safety of acetyl glucosamine as used in cosmetics and ... What Is Acetyl Glucosamine?. Acetyl glucosamine is a skin-replenishing ingredient that helps to reduce signs of aging. ...
https://thedermreview.com/acetyl-glucosamine
Table 2 - Environmental Source of Candida dubliniensis - Volume 13, Number 5-May 2007 - Emerging Infectious Diseases journal -...
N-acetylglucosamine. +. +. Identification. C. dubliniensis. C. albicans. API 20C AUX profile code. 6172134. 2566174. ...
https://wwwnc.cdc.gov/eid/article/13/5/06-1179-t2
Interaction of Neisseria meningitidis group X N-acetylglucosamine-1-phosphotransferase with its donor substrate
... which transfers N-acetylglucosamine-1-phosphate from UDP-N-acetylglucosamine to the 4-hydroxyl of the N-acetylglucosamine on ... The capsular polysaccharide of Group X is a homopolymer of N-acetylglucosamine α(1-4) phosphate and is a vaccine target for ... Interaction of Neisseria meningitidis group X N-acetylglucosamine-1-phosphotransferase with its donor substrate. dc.rights. ... Moreover, our survey of analogs with modifications on the N-acetylglucosamine residue of the sugar nucleotide donor highlights ...
https://dspace.rpi.edu/handle/20.500.13015/5019?show=full
EWG Skin Deep® | CoverGirl Clean Fresh Skin Milk Foundation, Deep 620 RatingEWG Skin Deep® | CoverGirl Clean Fresh Skin Milk Foundation, Deep 620 Rating
Aqua/Water/Eau, Cyclopentasiloxane, Glycerin, Phenyl Trimethicone, Trimethylsiloxysilicate, Acetyl Glucosamine, Niacinamide, ...
https://www.ewg.org/skindeep/products/927379-CoverGirl_Clean_Fresh_Skin_Milk_Foundation_Deep_620/
Reviews and MinireviewsReviews and Minireviews
The post-translational modification of intracellular proteins by O-linked N-acetylglucosamine (O-GlcNAc) regulates essential ... Methods for Enrichment and Assignment of N-Acetylglucosamine Modification Sites. Molecular & Cellular Proteomics ...
https://www.mcponline.org/reviews?startPage=0&pageSize=100
TotalSeq-C0205 anti-human CD206 MMR Antibody, CD206, 15-2TotalSeq-C0205 anti-human CD206 MMR Antibody, CD206, 15-2
Mannose, fucose, N-acetyl glucosamine Cell Type Dendritic cells, Endothelial cells, Macrophages Biology Area Cell Biology, ... MMR recognizes a range of microbial carbohydrates bearing mannose, fucose, or N-acetyl glucosamine. MMR mediates endocytosis ...
https://www.biolegend.com/en-gb/products/totalseq-c0205-anti-human-cd206-mmr-antibody-18090
Françoise Van Bambeke | UCLouvainFrançoise Van Bambeke | UCLouvain
... caspofungin increases fluoroquinolone activity against Staphylococcus aureus biofilms by inhibiting N-acetylglucosamine ...
https://uclouvain.be/en/directories/francoise.vanbambeke
Homoserine kinase - WikipediaHomoserine kinase - Wikipedia
Thus, the two substrates of this enzyme are ATP and L-homoserine, whereas its two products are ADP and O-phospho-L-homoserine. 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:L-homoserine O-phosphotransferase. Other names in common use include homoserine kinase (phosphorylating), and HSK. This enzyme participates in glycine, serine and threonine metabolism. ...
https://en.wikipedia.org/wiki/Homoserine_kinase
Antibiotic Resistance in Dermatology: Mechanisms of ResistanceAntibiotic Resistance in Dermatology: Mechanisms of Resistance
Bactericidal; Inhibition of UDP-N-acetylglucosamine-3- enolpyruvyltransferase (MurA). Destruction of antibiotic. Escherichia ...
https://www.medscape.com/viewarticle/989182
Glycobiology and Extracellular MatricesGlycobiology and Extracellular Matrices
O-Linked N-Acetylglucosamine (O-GlcNAc) Transferase and O-GlcNAcase Interact with Mi2β Protein at the Aγ-Globin Promoter. ... O-GlcNAcylation is the covalent addition of an O-linked β-N-acetylglucosamine (O-GlcNAc) sugar moiety to hydroxyl groups of ... The role of O-linked N-acetylglucosamine (O-GlcNAc) modification in the cell cycle has been enigmatic. Previously, both O- ... Here, we identified O-linked β-N-acetylglucosamine (O-GlcNAc)-transferase (OGT) as one of Chk1s substrates. We found that Chk1 ...
https://www.jbc.org/Glycobiology-Extracellular-Matrices?startPage=&KeywordRaw=O-GlcNAcylation
An in vitro assay for enzymatic studies on human ALG13/14 heterodimeric UDP- N-acetylglucosamine transferase | CDG HubAn in vitro assay for enzymatic studies on human ALG13/14 heterodimeric UDP- N-acetylglucosamine transferase | CDG Hub
Publications / An in vitro assay for enzymatic studies on human ALG13/14 heterodimeric UDP- N-acetylglucosamine transferase ... An in vitro assay for enzymatic studies on human ALG13/14 heterodimeric UDP- N-acetylglucosamine transferase. ... biosynthesis is catalyzed by the conserved ALG13/ALG14 heterodimeric UDP-N-acetylglucosamine transferase (GnTase). In humans, ...
https://www.cdghub.com/publication/an-in-vitro-assay-for-enzymatic-studies-on-human-alg13-14-heterodimeric-udp-n-acetylglucosamine-transferase/
TransferaseUridine Diphosphate N-AcetylglucosamineGlcNAcKinaseEnzymeMoleculeAmino sugarGlucosamineSugarsPolymerTurnoverPolysaccharideIngredientsFormSugarCommonTransferaseSingle N-acetylglucosamineModified with O-linked N-acetylglucosamineENZYMEDeacetylaseChitinMannoseProteinsSubunitsMetabolicModificationProteinGlycoproteinsReceptorsCatalyzesSynthesisStructuralTransferAlphaGrowthCellDomainDataFamilyCurrentStudyDevelopmentAbilityProduction
Transferase3
  • Recombinant fragment corresponding to Human OGT/ O-Linked N-Acetylglucosamine Transferase aa 213-462. (abcam.cn)
  • The second step of eukaryotic lipid-linked oligosaccharide (LLO) biosynthesis is catalyzed by the conserved ALG13/ALG14 heterodimeric UDP-N-acetylglucosamine transferase (GnTase). (cdghub.com)
  • Mutations in N -acetylglucosamine ( O -GlcNAc) transferase in patients with X-linked intellectual disability. (bvsalud.org)
Uridine Diphosphate N-Acetylglucosamine1
  • This conversion is required to make a sugar called uridine diphosphate-N-acetylglucosamine (UDP-GlcNAc), which is needed to transfer sugars to growing oligosaccharides during glycosylation. (medlineplus.gov)
GlcNAc6
  • Kinetic studies of hog spleen N-acetylglucosamine kinase indicate that N-acetylglucosamine-6-phosphate (GlcNAc-6-p), the product of the reaction and UDP-N-acetylglycosamine (UDP-GlcNAc), the end product of the pathway of N-acetylglucosamine (GlcNAc) metabolism, are noncompetitive inhibitors. (ias.ac.in)
  • All of these results strongly suggest that the hog spleen N-acetylglucosamine kinase is a regulatory enzyme, and the end product UDP-GlcNAc and the reaction product GlcNac-6-p both act on the enzyme as feedback inhibitor. (ias.ac.in)
  • Chaney, W & Stanley, P 1985, ' A lectin-resistant glycosylation mutant with partially inactive UDP-N-acetylglucosamine: α1,3 mannoside β1,2 N-acetylglucosaminyltransferase I(GlcNAc-TI) ', Federation Proceedings , vol. 44, no. 5, pp. (elsevier.com)
  • In E. coli , AmpG is specific for the import of N -acetylglucosamine (GlcNAc)-anhydroMurNAc(−peptides) which are common PGN turnover products, with the disaccharide portion as a minimal requirement. (biomedcentral.com)
  • Gnt-VB is predominantly expressed in brain and catalyses the transfer of N-acetylglucosamine (GlcNAc) to the beta 1-6 linkage of the mannose residue of GlcNAcbeta1,2-Manalpha on both the alpha1,3- and alpha1,6-linked mannose arms in the core structure of N-glycan. (embl.de)
  • The 45-kDa form was pulled down by lectin concanavalin A (Con A) and Galant husnivalis lectin (GNL), indicating an immature glycan with a high amount of mannose (Man), whereas the 65-kDa form is a mature glycan composed of acetylglucosamine (GlcNAc) and poly-N-acetyllactosame (poly-LacNAc) that was pulled down by wheat germ agglutinin (WGA) and tomato lectin, respectively. (emory.edu)
Kinase1
  • Studies on hog spleen N-acetylglucosamine kinase : II. (ias.ac.in)
Enzyme3
  • The PGM3 enzyme converts a molecule called N-acetylglucosamine-6-phosphate into a different molecule called N-acetylglucosamine-1-phosphate. (medlineplus.gov)
  • This enzyme catalyses the addition of N-acetylglucosamine in beta 1-6 linkage to the alpha-linked mannose of biantennary N-linked oligosaccharides. (embl.de)
  • 1994. N-acetylglucosamine dynamics in freshwater environment: concentration of amino-sugars, extracellular enzyme activities, and microbial uptake . (jcu.cz)
Molecule2
  • The structural difference is this: N-acetylglucosamine has a portion of an acetic acid molecule attached to it, causing the body to handle the two compounds differently. (innvista.com)
  • Chitin is a molecule made up of bound units of acetylglucosamine, which is joined in such a way as to allow for increased points at which hydrogen bonding can occur. (cdc.gov)
Amino sugar2
  • N-acetylglucosamine (NAG) is an amino sugar, a derivative of the simple sugar glucose. (livestrong.com)
  • N. Acetylglucosamine is an amino sugar (the building blocks of mucopolysaccharides. (epigenetics-international.com)
Glucosamine2
  • There are three common commercial forms of Glucosamine: N-acetylglucosamine, hydrochloride, and sulfate. (innvista.com)
  • In fact, N-acetylglucosamine and Glucosamine sulfate are two entirely different molecules. (innvista.com)
Sugars1
  • N-acetylglucosamine is another member of the group of eight essential sugars. (innvista.com)
Polymer2
  • We have demonstrated previously that the formation of the polymer is catalyzed by a phosphotransferase which transfers N-acetylglucosamine-1-phosphate from UDP-N-acetylglucosamine to the 4-hydroxyl of the N-acetylglucosamine on the nonreducing end of the growing chain. (rpi.edu)
  • The GH18 (glycosyl hydrolases, family 18) type II chitinases hydrolyze chitin, an abundant polymer of N-acetylglucosamine and have been identified in bacteria, fungi, insects, plants, viruses, and protozoan parasites. (unl.edu)
Turnover2
  • IMSEAR at SEARO: Turnover of inducible N-acetylglucosamine catabolic enzymes in Candida albicans. (who.int)
  • Biswas M, Singh B, Rai YP, Datta A. Turnover of inducible N-acetylglucosamine catabolic enzymes in Candida albicans. (who.int)
Polysaccharide2
  • The capsular polysaccharide of Group X is a homopolymer of N-acetylglucosamine α(1-4) phosphate and is a vaccine target for prevention of disease associated with this meningococcal serogroup. (rpi.edu)
  • A linear polysaccharide of beta-1->4 linked units of ACETYLGLUCOSAMINE. (semanticscholar.org)
Ingredients1
  • We respect nature and as such we do our part and only use vegan-friendly ingredients in our N. Acetylglucosamine. (epigenetics-international.com)
Form1
  • Scientific literature does not support the use of N-acetylglucosamine or the hydrochloride form. (innvista.com)
Sugar2
  • Moreover, our survey of analogs with modifications on the N-acetylglucosamine residue of the sugar nucleotide donor highlights the importance of substituents at C2 and C4 of the sugar residue. (rpi.edu)
  • The receptor sugar for WGA is N -acetylglucosamine, with preferential binding to dimers and trimers of this sugar. (vectorlabs.com)
Common1
  • WGA can bind oligosaccharides containing terminal N -acetylglucosamine or chitobiose, structures which are common to many serum and membrane glycoproteins. (vectorlabs.com)
Transferase11
  • O-linked β-N-acetylglucosamine (O-GlcNAc) modification of epidermal growth factor (EGF) domains catalyzed by EGF domain O-GlcNAc transferase (EOGT) is the first example of GlcNAc modification in the lumen of the endoplasmic reticulum (ER). (nih.gov)
  • Nutrient levels dictate the activity of O-linked N-acetylglucosamine transferase (OGT) to regulate O-GlcNAcylation, a post-translational modification mechanism to "fine-tune" intracellular signaling and metabolic status. (umn.edu)
  • This technology includes the development and use of small molecules that inhibit O-linked beta-N-acetylglucosamine (O-GlcNAc) transferase (OGT) for a variety of pathologies, including Alzheimer's disease, cancer, cancer, diabetes, and neurodegenerative disorders the treatment of cancer and as a potential antiviral. (nih.gov)
  • Further work with O-linked beta-N-acetylglucosamine transferase (OGT) inhibitors will permit the further study of the biological role of OGT in cell homeostasis. (nih.gov)
  • The series of O-linked beta-N-acetylglucosamine transferase (OGT) inhibitors described in this technology exhibit improved binding properties and OGT inhibition. (nih.gov)
  • Part of UDP-N-acetylglucosamine transferase complex. (nih.gov)
  • Ogawa M, Sawaguchi S, Kawai T, Nadano D, Matsuda T, Yagi H, Kato K, Furukawa K, Okajima T. Impaired O-linked N-acetylglucosaminylation in the endoplasmic reticulum by mutated epidermal growth factor (EGF) domain-specific O-linked N-acetylglucosamine transferase found in Adams-Oliver syndrome. (nih.gov)
  • Phosphorylation of TET Proteins Is Regulated via O-GlcNAcylation by the O-Linked N-Acetylglucosamine Transferase (OGT). (mpg.de)
  • UDP-N-acetylglucosamine (GlcNAc):hydroxyproline polypeptide GlcNAc- transferase. (expasy.org)
  • A suite of tools that enable small molecular regulation (Trimethoprim/Shield) of the expression of the O-GlcNAc transferase (OGT), O-GlcNAcase (OGT), Glutamine Fructose-6phophate aminotransferase 1, 2 (GFAT1,2), and UDP-N-Acetylglucosamine Pyrophosphorylase (UAP1/2). (nih.gov)
  • Marquardt, J. L., E. D. Brown, C. T. Walsh, and K. S. Anderson, Isolation and Structural Elucidation of a Tetrahedral Intermediate in the UDP-N-acetylglucosamine Enolpyruvoyl Transferase Enzymatic Pathway, Journal of the American Chemical Society, Vol. 115, 1993, p. 10398-9. (nih.gov)
Single N-acetylglucosamine2
  • The chemical structures of the O-glycosylations were determined to be single N-acetylglucosamine residues. (nih.gov)
  • In opposition to N- and O-glycosylations, O-GlcNAcylation only consists in the transfer of a single N-acetylglucosamine moiety through a beta-linkage onto serine and threonine residues of proteins confined within the cytosol, the nucleus and the mitochondria. (doabooks.org)
Modified with O-linked N-acetylglucosamine1
  • 1996. The microtubule-associated protein tau is extensively modified with O-linked N-acetylglucosamine. (cosmobio.co.jp)
ENZYME2
  • Patients with type D lack the enzyme N- acetylglucosamine-6-sulfatase. (medscape.com)
  • Phosphoacetylglucosamine mutase (PAGM) is a human enzyme that is the key to the formation of the essential metabolite UDP-N-acetylglucosamine. (umsystem.edu)
Deacetylase1
  • Quaternary variations in the structural assembly of N-acetylglucosamine-6-phosphate deacetylase from Pasteurella multocida. (ncbs.res.in)
Chitin3
  • N-Acetylglucosamine is the basic unit of the biopolymer chitin, which forms the outer coverings of insects and crustaceans (shrimp, crab, etc. (greenmedinfo.com)
  • Chitin is a molecule made up of bound units of acetylglucosamine, which is joined in such a way as to allow for increased points at which hydrogen bonding can occur. (cdc.gov)
  • Investigation of the successional dynamics of a soil microbiome during 21-weeks of enrichment on chitin and its monomer, N-acetylglucosamine (NAG). (pnnl.gov)
Mannose2
  • Following transfer of mannose (Man) to Ser or Thr by protein O-mannosyltransferase (POMT), either POMT1 or POMT2, the O-Man can be further modified with N -acetylglucosamine, galactose, sialic acid, PO 4 , N -acetylgalactosamine, glucuronic acid, and xylose to generate structures, such as those illustrated in Fig. 1 . (pnas.org)
  • Binding properties of the N-acetylglucosamine and high-mannose N-glycan PP2-A1 phloem lectin in Arabidopsis. (archives-ouvertes.fr)
Proteins1
  • The EOGT gene provides instructions for making a protein that modifies certain other proteins by transferring a molecule called N-acetylglucosamine to them. (nih.gov)
Subunits1
  • Earlier studies had linked mutations in a gene called Gnptab (for N-acetylglucosamine-1-phosphotransferase subunits alpha/beta) to stuttering in some people. (nih.gov)
Metabolic2
  • Predicted to act upstream of or within UDP-N-acetylglucosamine metabolic process and protein glycosylation. (mcw.edu)
  • Hypertrophied hearts accumulated lactate, pyruvate and glycogen, and displayed increased protein O-linked N-acetylglucosamine, which was prevented by increasing availability of non-glucose substrates in vivo by a ketogenic diet (KD) or a high-fat diet, which reversed the structural, metabolic and functional remodelling of non-stressed cMPC1-/- hearts. (internalmedicineiowa.org)
Modification1
  • Modification of RelA by O-linked N-Acetylglucosamine links glucose metabolism to NF-B acetylation and transcription. (mskcc.org)
Protein2
  • α1,4-linked N-acetylglucosamine (αGlcNAc), a unique O-glycan specific to gastric gland mucus, is biosynthesized by α1,4-N-acetylglucosaminyltransferase (α4GnT) and primarily bound at the terminal glycosylated residue to scaffold protein MUC6. (elsevier.com)
  • Glucosamine inhibits angiotensin II-induced cytoplasmic Ca2+ elevation in neonatal cardiomyocytes via protein-associated O-linked N-acetylglucosamine. (doktori.hu)
Glycoproteins1
  • 10. Mild alkaline borohydride treatment liberates N-acetylglucosamine linked oligosaccharide chains of glycoproteins. (nih.gov)
Receptors1
  • Cell surface receptors that bind to ACETYLGLUCOSAMINE . (bvsalud.org)
Catalyzes1
  • Catalyzes the hydrolysis of UDP-3-O-myristoyl-N-acetylglucosamine to form UDP-3-O-myristoylglucosamine and acetate, the committed step in lipid A biosynthesis. (uniprot.org)
Synthesis1
  • Alternatively POMGnT2 can add N -acetylglucosamine in β1,4-linkage ( Near Left ) leading to the synthesis of a complex structure that is still under investigation. (pnas.org)
Structural1
  • The production of cartilage, tendons, and joints depend on the structural integrity of N-Acetylglucosamine. (greenmedinfo.com)
Transfer1
  • Research suggests that the EOGT gene mutations reduce or eliminate the protein's ability to transfer N-acetylglucosamine. (nih.gov)
Alpha3
  • Acetylglucosamine is being promoted in skin care products as a new AHA (Alpha Hydroxy Acid) alternative. (valuemarketresearch.com)
  • Bovine colostrum UDP-N- acetylglucosamine: .alpha. (genome.jp)
  • D-mannoside .beta.2-N-acetylglucosaminyltransferase I. Separation from UDP-N-acetylglucosamine: .alpha. (genome.jp)
Growth2
  • Acetylglucosamine is widely used to treat various disorders due to its health-promoting features, which will boost its market growth. (valuemarketresearch.com)
  • The growth and trends of Acetylglucosamine Industry provide a holistic approach to this study. (valuemarketresearch.com)
Cell1
  • Fungi have cell walls composed of a polymer of N-Acetylglucosamine. (greenmedinfo.com)
Domain1
  • Energy landscape of the domain movement in Staphylococcus aureus UDP-N-acetylglucosamine 2-epimerase. (nih.gov)
Data1
  • This section of the acetylglucosamine market report provides detailed data on the segments by analyzing them at country and regional level, thereby assisting the strategist in identifying the target demographics for the respective product or services with the upcoming opportunities. (valuemarketresearch.com)
Family1
  • We assess the model on the UDP-N-acetylglucosamine acyltransferase (LPXA) family, as in our previous report, and we extend this study to all other members of the left-handed parallel beta helix fold (LβH) superfamily whose structure has been determined. (biomedcentral.com)
Current1
  • This section covers the regional outlook, which accentuates current and future demand for the Acetylglucosamine market across North America, Europe, Asia-Pacific, Latin America, and Middle East & Africa. (valuemarketresearch.com)
Study1
  • The global demand for Acetylglucosamine Market is presumed to reach the market size of nearly USD XX MN by 2027 from USD XX MN in 2020 with a CAGR of XX% under the study period of 2021 - 2027. (valuemarketresearch.com)
Development1
  • Acetylglucosamine has also been related to skin advantages such as wrinkle reduction, hydration, and decreasing the development of the skin pigment melanin. (valuemarketresearch.com)
Ability1
  • N-acetylglucosamine is being studied for its ability to brighten the skin's complexion and its anti-aging characteristics, which may help reduce age spots caused by cumulative skin damage caused by excessive UV (ultraviolet) radiation over time. (valuemarketresearch.com)
Production2
  • A non-sticky lightweight formula containing Niacinamide 10% and N-acetylglucosamine 2% to balance oil production, minimize the appearance of enlarged pores, calm acne prone skin and effectively target hyperpigmentation and post acne marks. (theformularx.com)
  • 4. Choi AH, Slamti L, Avci FY, Pier GB, Maira-Litrán T. The pgaABCD locus of Acinetobacter baumannii encodes the production of poly-β-1-6-N-acetylglucosamine, which is critical for biofilm formation. (southernbiotech.com)
JoF | Free Full-Text | Candida spp./Bacteria Mixed Biofilms
JoF | Free Full-Text | Candida spp./Bacteria Mixed Biofilms (mdpi.com)
Side Effects of N-Acetylglucosamine | livestrong
Side Effects of N-Acetylglucosamine | livestrong (livestrong.com)
PGM3 gene: MedlinePlus Genetics
PGM3 gene: MedlinePlus Genetics (medlineplus.gov)
Unconventional metabolites in chromatin regulation | Bioscience Reports | Portland Press
Unconventional metabolites in chromatin regulation | Bioscience Reports | Portland Press (portlandpress.com)
Glucosamina: MedlinePlus suplementos
Glucosamina: MedlinePlus suplementos (medlineplus.gov)
EWG Skin Deep® | CoverGirl Clean Fresh Skin Milk Foundation, Deep 620 Rating
EWG Skin Deep® | CoverGirl Clean Fresh Skin Milk Foundation, Deep 620 Rating (ewg.org)
TotalSeq-C0205 anti-human CD206 MMR Antibody, CD206, 15-2
TotalSeq-C0205 anti-human CD206 MMR Antibody, CD206, 15-2 (biolegend.com)
PGM3-congenital disorder of glycosylation: MedlinePlus Genetics
PGM3-congenital disorder of glycosylation: MedlinePlus Genetics (medlineplus.gov)
Homoserine kinase - Wikipedia
Homoserine kinase - Wikipedia (en.wikipedia.org)
Marine Drugs | Free Full-Text | Isolation and Characterization of a Heparin-Like Compound with Potent Anticoagulant and...
Marine Drugs | Free Full-Text | Isolation and Characterization of a Heparin-Like Compound with Potent Anticoagulant and... (mdpi.com)
Composition WELLA Sp reverse - Regenerating hair spray conditionner - UFC-Que Choisir
Composition WELLA Sp reverse - Regenerating hair spray conditionner - UFC-Que Choisir (quechoisir.org)
Mucopolysaccharidosis type III: MedlinePlus Medical Encyclopedia
Mucopolysaccharidosis type III: MedlinePlus Medical Encyclopedia (medlineplus.gov)
KEGG REACTION: R05647
KEGG REACTION: R05647 (genome.jp)
Molecules | Free Full-Text | Intracellular Hydrolysis of Small-Molecule O-Linked N-Acetylglucosamine Transferase Inhibitors...
Molecules | Free Full-Text | Intracellular Hydrolysis of Small-Molecule O-Linked N-Acetylglucosamine Transferase Inhibitors... (mdpi.com)
Lectins: Wheat Germ Agglutinin (WGA), Agarose bound
Lectins: Wheat Germ Agglutinin (WGA), Agarose bound (vectorlabs.com)
60. [Glutamine & Alanine: The Urea Cycle II] | Biochemistry | Educator.com
60. [Glutamine & Alanine: The Urea Cycle II] | Biochemistry | Educator.com (educator.com)
(researchgate.net)
Biomolecules | Free Full-Text | Targeting α-Synuclein for PD Therapeutics: A Pursuit on All Fronts
Biomolecules | Free Full-Text | Targeting α-Synuclein for PD Therapeutics: A Pursuit on All Fronts (mdpi.com)
Limb-Girdle Muscular Dystrophy Clinical Presentation: History, Causes
Limb-Girdle Muscular Dystrophy Clinical Presentation: History, Causes (medscape.com)
Limb-Girdle Muscular Dystrophy Clinical Presentation: History, Causes
Limb-Girdle Muscular Dystrophy Clinical Presentation: History, Causes (medscape.com)
Engineering Nanomedicines for Improved Melanoma Therapy
Engineering Nanomedicines for Improved Melanoma Therapy (medscape.com)
DailyMed - ACNE SOLUTIONS OIL CONTROL CLEANSING MASK ACNE MEDICATION ALL SKIN TYPES- salicylic acid cream
DailyMed - ACNE SOLUTIONS OIL CONTROL CLEANSING MASK ACNE MEDICATION ALL SKIN TYPES- salicylic acid cream (dailymed.nlm.nih.gov)
Specialty Archives - Breakspear Medical
Specialty Archives - Breakspear Medical (breakspearmedical.com)