uridine diphosphate n-acetylgalactosamine and arginine

uridine diphosphate n-acetylgalactosamine has been researched along with arginine in 3 studies

Research

Studies (3)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's1 (33.33)29.6817
2010's2 (66.67)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Creuzenet, C; Obhi, RK1
Feldman, MF; Hug, I; Lowary, TL; Nothaft, H; Poulin, MB; Szymanski, CM1
Dalrymple, SA; Lowary, TL; Pinto, BM; Poulin, MB; Protsko, C; Sanders, DA; Shi, Y1

Other Studies

3 other study(ies) available for uridine diphosphate n-acetylgalactosamine and arginine

ArticleYear
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
Characterization of a bifunctional pyranose-furanose mutase from Campylobacter jejuni 11168.
    The Journal of biological chemistry, 2010, Jan-01, Volume: 285, Issue:1

    Topics: Alleles; Arginine; Biocatalysis; Biological Assay; Campylobacter jejuni; Carbohydrate Sequence; Catalytic Domain; Escherichia coli; Genetic Complementation Test; Intramolecular Transferases; Kinetics; Magnetic Resonance Spectroscopy; Models, Molecular; Molecular Sequence Data; Mutagenesis; Mutant Proteins; Oxazoles; Polysaccharides, Bacterial; Protein Structure, Secondary; Structural Homology, Protein; Uridine Diphosphate N-Acetylgalactosamine

2010
Specificity of a UDP-GalNAc pyranose-furanose mutase: a potential therapeutic target for Campylobacter jejuni infections.
    Chembiochem : a European journal of chemical biology, 2014, Jan-03, Volume: 15, Issue:1

    Topics: Arginine; Bacterial Proteins; Binding Sites; Biocatalysis; Campylobacter Infections; Campylobacter jejuni; Crystallography, X-Ray; Escherichia coli; Humans; Intramolecular Transferases; Molecular Dynamics Simulation; Protein Binding; Protein Structure, Tertiary; Substrate Specificity; Uridine Diphosphate Galactose; Uridine Diphosphate N-Acetylgalactosamine

2014