glucuronic acid has been researched along with aspartic acid in 4 studies
Timeframe | Studies, this research(%) | All Research% |
---|---|---|
pre-1990 | 1 (25.00) | 18.7374 |
1990's | 0 (0.00) | 18.2507 |
2000's | 3 (75.00) | 29.6817 |
2010's | 0 (0.00) | 24.3611 |
2020's | 0 (0.00) | 2.80 |
Authors | Studies |
---|---|
Emery, JA; Erova, TE; Harris, JM; Mattick, JS; Sargent, JL; Semmler, AB; Whitchurch, CB; Wozniak, DJ; Young, MD | 1 |
Ando, M; Hanioka, N; Jinno, H; Kaniwa, N; Minami, H; Ohtsu, A; Ozawa, S; Saeki, M; Sai, K; Saijo, N; Saito, Y; Sawada, J; Shirao, K; Tanaka-Kagawa, T; Yoshida, T | 1 |
EADES, CH; POLLACK, RL | 1 |
Barré, L; Fournel-Gigleux, S; Li, D; Magdalou, J; Mulliert, G; Netter, P; Ouzzine, M | 1 |
4 other study(ies) available for glucuronic acid and aspartic acid
Article | Year |
---|---|
Phosphorylation of the Pseudomonas aeruginosa response regulator AlgR is essential for type IV fimbria-mediated twitching motility.
Topics: Alginates; Amino Acid Sequence; Aspartic Acid; Bacterial Proteins; Biofilms; Electrochemistry; Fimbriae, Bacterial; Glucuronic Acid; Hexuronic Acids; Membrane Proteins; Methyl-Accepting Chemotaxis Proteins; Molecular Sequence Data; Mutation; Phenotype; Phosphorylation; Protein Structure, Secondary; Protein Structure, Tertiary; Pseudomonas aeruginosa; Trans-Activators | 2002 |
Functional characterization of human UDP-glucuronosyltransferase 1A9 variant, D256N, found in Japanese cancer patients.
Topics: Amino Acid Substitution; Animals; Antineoplastic Agents; Asparagine; Aspartic Acid; Camptothecin; COS Cells; Exons; Genetic Variation; Glucuronates; Glucuronic Acid; Glucuronosyltransferase; Humans; Irinotecan; Japan; Mutation; Neoplasms; Polymorphism, Single Nucleotide; Transfection; UDP-Glucuronosyltransferase 1A9 | 2003 |
Glucuronic acid conjugates of aspartic and glutamic acids in urine.
Topics: Aspartic Acid; Body Fluids; Glucuronates; Glucuronic Acid; Glutamates; Humans; Urine | 1954 |
Identification of aspartic acid and histidine residues mediating the reaction mechanism and the substrate specificity of the human UDP-glucuronosyltransferases 1A.
Topics: Aspartic Acid; Catalysis; Glucuronic Acid; Glucuronosyltransferase; Histidine; Humans; Mutagenesis, Site-Directed; Phenols; Substrate Specificity; Xenobiotics | 2007 |