uridine diphosphate n-acetylglucosamine has been researched along with asparagine in 4 studies
| Timeframe | Studies, this research(%) | All Research% |
|---|---|---|
| pre-1990 | 2 (50.00) | 18.7374 |
| 1990's | 0 (0.00) | 18.2507 |
| 2000's | 2 (50.00) | 29.6817 |
| 2010's | 0 (0.00) | 24.3611 |
| 2020's | 0 (0.00) | 2.80 |
| Authors | Studies |
|---|---|
| Khalkhali, Z; Marshall, RD; Serafini-Cessi, F | 1 |
| Khalkhali, Z; Marshall, RD | 1 |
| Amrhein, N; Etezady-Esfarjani, T; Macheroux, P; Samland, AK | 1 |
| Dong, J; Kitagawa, H; Krahn, JM; Negishi, M; Pedersen, LC; Pedersen, LG; Sugahara, K; Taniguchi, F | 1 |
4 other study(ies) available for uridine diphosphate n-acetylglucosamine and asparagine
| Article | Year |
|---|---|
Properties of membrane-bound uridine diphosphate N-acetylglucosamine-asparagine sequon N-acetylglucosaminyltransferase in preparations of endoplasmic reticulum from rabbit liver and from regenerating rat liver [proceedings].
Topics: Acetylglucosamine; Animals; Asparagine; Cell Membrane; Endoplasmic Reticulum; Hexosyltransferases; Kinetics; Liver; Liver Regeneration; Phospholipases; Rabbits; Rats; Temperature; Uridine Diphosphate N-Acetylglucosamine | 1977 |
UDP-N-acetyl-D-glucosamine-asparagine sequon N-acetyl-beta-D-glucosaminyl-transferase-activity in human serum.
Topics: Acetylglucosamine; Amino Acids; Animals; Asparagine; Cattle; Chromatography, Affinity; Cytidine Diphosphate Choline; Hexosyltransferases; Humans; Kinetics; Manganese; Pancreas; Polyamines; Protein Binding; Ribonucleases; Uridine Diphosphate N-Acetylglucosamine | 1976 |
Asparagine 23 and aspartate 305 are essential residues in the active site of UDP-N-acetylglucosamine enolpyruvyl transferase from Enterobacter cloacae.
Topics: Alkyl and Aryl Transferases; Amino Acid Substitution; Asparagine; Aspartic Acid; Binding Sites; Catalysis; Cysteine; Enterobacter cloacae; Enzyme Inhibitors; Fosfomycin; Mutagenesis, Site-Directed; Phosphates; Phosphoenolpyruvate; Recombinant Proteins; Uridine Diphosphate N-Acetylglucosamine | 2001 |
Crystal structure of an alpha 1,4-N-acetylhexosaminyltransferase (EXTL2), a member of the exostosin gene family involved in heparan sulfate biosynthesis.
Topics: Amino Acid Sequence; Animals; Arginine; Asparagine; Aspartic Acid; Binding Sites; Catalytic Domain; COS Cells; Crystallography, X-Ray; Heparitin Sulfate; Hydrogen Bonding; Membrane Proteins; Mice; Models, Molecular; Molecular Sequence Data; Mutagenesis, Site-Directed; N-Acetylgalactosaminyltransferases; N-Acetylglucosaminyltransferases; Protein Conformation; Protein Structure, Tertiary; Sequence Homology, Amino Acid; Transfection; Uridine Diphosphate N-Acetylglucosamine | 2003 |