uridine diphosphate n-acetylgalactosamine and acetylglucosamine

uridine diphosphate n-acetylgalactosamine has been researched along with acetylglucosamine in 10 studies

Research

Studies (10)

TimeframeStudies, this research(%)All Research%
pre-19903 (30.00)18.7374
1990's1 (10.00)18.2507
2000's3 (30.00)29.6817
2010's2 (20.00)24.3611
2020's1 (10.00)2.80

Authors

AuthorsStudies
Filer, D; Kindler, SH; Rosenberg, E1
Gałasiński, W; Kopacz-Jodczyk, T; Paszkiewicz-Gadek, A1
Jamieson, JC; Kaplan, HA; Woloski, BM1
Elbein, AD; Pastuszak, I; Wang-Gillam, A1
Ihara, H; Ikeda, Y; Korekane, H; Koyota, S; Sasai, K; Taniguchi, N; Tsuda, T; Yamaguchi, Y1
Jarroll, EL; Newburg, DS; Sener, K; Shen, Z1
Creuzenet, C; Obhi, RK1
Furo, K; Murashige, H; Nozaki, M; Sato, Y1
Hart, GW; Hunt, DF; Li, Z; Ma, J; Shabanowitz, J; Wang, WH1
Arumugam, TV; Jo, DG; Lai, MKP; Park, J1

Reviews

1 review(s) available for uridine diphosphate n-acetylgalactosamine and acetylglucosamine

ArticleYear
O-GlcNAcylation as a Therapeutic Target for Alzheimer's Disease.
    Neuromolecular medicine, 2020, Volume: 22, Issue:2

    Topics: Acetylglucosamine; Aged; Alzheimer Disease; Amyloid beta-Protein Precursor; Animals; Antigens, Neoplasm; Brain; Diabetes Mellitus, Type 2; Disease Models, Animal; Glucose; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); Glycosylation; Hexosamines; Histone Acetyltransferases; Humans; Hyaluronoglucosaminidase; Insulin Resistance; Molecular Structure; Nerve Tissue Proteins; Neurodegenerative Diseases; Neuroprotective Agents; Phosphorylation; Protein Isoforms; Protein Processing, Post-Translational; Stroke; tau Proteins; Uridine Diphosphate; Uridine Diphosphate N-Acetylgalactosamine

2020

Other Studies

9 other study(ies) available for uridine diphosphate n-acetylgalactosamine and acetylglucosamine

ArticleYear
Myxospore coat synthesis in Myxococcus xanthus: enzymes associated with uridine 5'-diphosphate-N-acetylgalactosamine formation during myxospore development.
    Journal of bacteriology, 1977, Volume: 131, Issue:3

    Topics: Acetylglucosamine; Acyltransferases; Alkaline Phosphatase; Carbohydrate Epimerases; Cell Wall; Cell-Free System; Glucosamine; Glutamate-Ammonia Ligase; Glutamine-Fructose-6-Phosphate Transaminase (Isomerizing); Hydrolases; Isomerases; Malate Dehydrogenase; Myxococcales; Nucleotidyltransferases; Spores, Bacterial; Transferases; Uridine Diphosphate N-Acetylgalactosamine; Uridine Diphosphate N-Acetylglucosamine; Uridine Diphosphate Sugars

1977
The attachment of UDP-hexosamines to the ribosomes isolated from rat liver.
    Biochemical medicine and metabolic biology, 1988, Volume: 39, Issue:3

    Topics: Acetylglucosamine; Animals; Carbon Radioisotopes; Kinetics; Liver; Male; Nucleoside Diphosphate Sugars; Rats; Rats, Inbred Strains; Ribosomes; Uridine Diphosphate N-Acetylgalactosamine; Uridine Diphosphate N-Acetylglucosamine; Uridine Diphosphate Sugars

1988
Studies of the effect of experimental inflammation on rat liver nucleotide sugar pools.
    Comparative biochemistry and physiology. A, Comparative physiology, 1984, Volume: 77, Issue:2

    Topics: Acetylgalactosamine; Acetylglucosamine; Amino Acids; Animals; Cytidine Monophosphate N-Acetylneuraminic Acid; Guanosine Diphosphate Mannose; In Vitro Techniques; Inflammation; Liver; Mannose; Nucleotides; Rats; Uridine Diphosphate N-Acetylgalactosamine; Uridine Diphosphate N-Acetylglucosamine

1984
A 17-amino acid insert changes UDP-N-acetylhexosamine pyrophosphorylase specificity from UDP-GalNAc to UDP-GlcNAc.
    The Journal of biological chemistry, 1998, Oct-16, Volume: 273, Issue:42

    Topics: Acetylgalactosamine; Acetylglucosamine; Amino Acid Sequence; Animals; Dimerization; Humans; Liver; Molecular Sequence Data; Nucleotidyltransferases; Substrate Specificity; Swine; Uridine Diphosphate N-Acetylgalactosamine; Uridine Diphosphate N-Acetylglucosamine

1998
Kinetic basis for the donor nucleotide-sugar specificity of beta1, 4-N-acetylglucosaminyltransferase III.
    Journal of biochemistry, 2000, Volume: 128, Issue:4

    Topics: Acetylgalactosamine; Acetylglucosamine; Animals; Cell Line; Enzyme Inhibitors; Kinetics; Mutagenesis, Site-Directed; N-Acetylglucosaminyltransferases; Oligosaccharides; Protein Binding; Rats; Recombinant Fusion Proteins; Spectrometry, Mass, Electrospray Ionization; Substrate Specificity; Uridine Diphosphate Glucose; Uridine Diphosphate N-Acetylgalactosamine; Uridine Diphosphate N-Acetylglucosamine; Uridine Diphosphate Sugars

2000
Amino sugar phosphate levels in Giardia change during cyst wall formation.
    Microbiology (Reading, England), 2004, Volume: 150, Issue:Pt 5

    Topics: Acetylgalactosamine; Acetylglucosamine; Animals; Cell Wall; Electrophoresis, Capillary; Galactosamine; Giardia lamblia; Glucosamine; Glucose-6-Phosphate; Nucleotidyltransferases; Substrate Specificity; Up-Regulation; Uridine Diphosphate N-Acetylgalactosamine; Uridine Diphosphate N-Acetylglucosamine

2004
Biochemical characterization of the Campylobacter jejuni Cj1294, a novel UDP-4-keto-6-deoxy-GlcNAc aminotransferase that generates UDP-4-amino-4,6-dideoxy-GalNAc.
    The Journal of biological chemistry, 2005, May-27, Volume: 280, Issue:21

    Topics: Acetylglucosamine; Arginine; Bacterial Proteins; Campylobacter jejuni; Cloning, Molecular; Dimerization; Enzyme Stability; Escherichia coli; Gene Expression; Hydrogen-Ion Concentration; Lysine; Magnetic Resonance Spectroscopy; Mass Spectrometry; Molecular Sequence Data; Mutagenesis, Site-Directed; Pyridoxal Phosphate; Recombinant Proteins; Structure-Activity Relationship; Substrate Specificity; Transaminases; Uridine Diphosphate N-Acetylgalactosamine

2005
Identification of an N-acetylglucosamine kinase essential for UDP-N-acetylglucosamine salvage synthesis in Arabidopsis.
    FEBS letters, 2015, Oct-24, Volume: 589, Issue:21

    Topics: Acetylglucosamine; Arabidopsis; Arabidopsis Proteins; Gene Knockout Techniques; Humans; Mutation; Phosphotransferases (Alcohol Group Acceptor); Sequence Homology, Amino Acid; Signal Transduction; Substrate Specificity; Uridine Diphosphate N-Acetylgalactosamine

2015
O-GlcNAc Site Mapping by Using a Combination of Chemoenzymatic Labeling, Copper-Free Click Chemistry, Reductive Cleavage, and Electron-Transfer Dissociation Mass Spectrometry.
    Analytical chemistry, 2019, 02-19, Volume: 91, Issue:4

    Topics: Acetylglucosamine; Adaptor Proteins, Signal Transducing; Alkynes; alpha-Crystallins; Azides; Click Chemistry; Cycloaddition Reaction; Glycosylation; HEK293 Cells; Humans; Oxidation-Reduction; Peptides; Protein Processing, Post-Translational; Tandem Mass Spectrometry; Uridine Diphosphate N-Acetylgalactosamine

2019