Compounds > glucuronic acid
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glucuronic acid and histidine

glucuronic acid has been researched along with histidine in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's1 (20.00)18.2507
2000's3 (60.00)29.6817
2010's1 (20.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Chakrabarty, AM; Roychoudhury, S; Sakai, K1
He, HS; Wang, SB; Weng, LJ; Xu, FH1
Rehm, BH; Remminghorst, U1
Barré, L; Fournel-Gigleux, S; Li, D; Magdalou, J; Mulliert, G; Netter, P; Ouzzine, M1
Hashimoto, W; Mikami, B; Murata, K; Ochiai, A; Yamasaki, M1

Other Studies

5 other study(ies) available for glucuronic acid and histidine

ArticleYear
AlgR2 is an ATP/GTP-dependent protein kinase involved in alginate synthesis by Pseudomonas aeruginosa.
    Proceedings of the National Academy of Sciences of the United States of America, 1992, Apr-01, Volume: 89, Issue:7

    Topics: Adenosine Triphosphate; Alginates; Bacterial Proteins; Binding Sites; Escherichia coli; Gene Expression Regulation, Bacterial; Genes, Bacterial; Glucuronic Acid; Guanosine Triphosphate; Hexuronic Acids; Histidine; Hydrogen-Ion Concentration; Phosphoproteins; Phosphorylation; Promoter Regions, Genetic; Protein Kinases; Pseudomonas aeruginosa

1992
Novel alginate-poly(L-histidine) microcapsules as drug carriers: in vitro protein release and short term stability.
    Macromolecular bioscience, 2005, May-23, Volume: 5, Issue:5

    Topics: Alginates; Capsules; Drug Carriers; Drug Delivery Systems; Drug Stability; Glucuronic Acid; Hexuronic Acids; Histidine; Proteins; Time Factors

2005
Alg44, a unique protein required for alginate biosynthesis in Pseudomonas aeruginosa.
    FEBS letters, 2006, Jul-10, Volume: 580, Issue:16

    Topics: Alginates; Bacterial Proteins; Glucuronic Acid; Hexuronic Acids; Histidine; Membrane Proteins; Models, Biological; Mutation; Oligopeptides; Open Reading Frames; Plasmids; Protein Biosynthesis; Pseudomonas aeruginosa; Recombinant Fusion Proteins; Recombination, Genetic

2006
Identification of aspartic acid and histidine residues mediating the reaction mechanism and the substrate specificity of the human UDP-glucuronosyltransferases 1A.
    The Journal of biological chemistry, 2007, Dec-14, Volume: 282, Issue:50

    Topics: Aspartic Acid; Catalysis; Glucuronic Acid; Glucuronosyltransferase; Histidine; Humans; Mutagenesis, Site-Directed; Phenols; Substrate Specificity; Xenobiotics

2007
Crystal structure of exotype alginate lyase Atu3025 from Agrobacterium tumefaciens.
    The Journal of biological chemistry, 2010, Aug-06, Volume: 285, Issue:32

    Topics: Agrobacterium tumefaciens; Alginates; Amino Acid Sequence; Base Sequence; Catalysis; Catalytic Domain; Crystallography, X-Ray; Glucuronic Acid; Hexuronic Acids; Histidine; Molecular Sequence Data; Mutagenesis, Site-Directed; Polysaccharide-Lyases; Protein Structure, Secondary; Protein Structure, Tertiary; Selenomethionine; Sequence Homology, Amino Acid; Tyrosine

2010