Compounds > uridine diphosphate n-acetylglucosamine
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uridine diphosphate n-acetylglucosamine and udp-3-o-(3-hydroxymyristoyl)-n-acetylglucosamine

uridine diphosphate n-acetylglucosamine has been researched along with udp-3-o-(3-hydroxymyristoyl)-n-acetylglucosamine in 5 studies

Research

Studies (5)

TimeframeStudies, this research(%)All Research%
pre-19902 (40.00)18.7374
1990's0 (0.00)18.2507
2000's1 (20.00)29.6817
2010's2 (40.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Anderson, MS; Macher, I; Raetz, CR; Robertson, AD1
Anderson, MS; Raetz, CR1
Christianson, DW; Fierke, CA; Gennadios, HA; Hernick, M; Rusche, KM; Whittington, DA1
Andrews, B; Gao, N; Kern, G; Livchak, S; Ross, PL; Shapiro, AB; Thresher, J; Yang, W1
Clayton, GM; Klein, DJ; Kornienko, M; Lumb, KJ; Miesel, L; Patel, SB; Reid, JC; Rickert, KW; Sharma, S; Singh, SB; Soisson, SM; Tummala, S; Zugay-Murphy, J1

Other Studies

5 other study(ies) available for uridine diphosphate n-acetylglucosamine and udp-3-o-(3-hydroxymyristoyl)-n-acetylglucosamine

ArticleYear
Biosynthesis of lipid A in Escherichia coli: identification of UDP-3-O-[(R)-3-hydroxymyristoyl]-alpha-D-glucosamine as a precursor of UDP-N2,O3-bis[(R)-3-hydroxymyristoyl]-alpha-D-glucosamine.
    Biochemistry, 1988, Mar-22, Volume: 27, Issue:6

    Topics: Acetic Anhydrides; Acyl Carrier Protein; Adenosine Triphosphate; Escherichia coli; Indicators and Reagents; Lipid A; Magnetic Resonance Spectroscopy; Myristic Acids; Uridine Diphosphate N-Acetylglucosamine; Uridine Diphosphate Sugars

1988
Biosynthesis of lipid A precursors in Escherichia coli. A cytoplasmic acyltransferase that converts UDP-N-acetylglucosamine to UDP-3-O-(R-3-hydroxymyristoyl)-N-acetylglucosamine.
    The Journal of biological chemistry, 1987, Apr-15, Volume: 262, Issue:11

    Topics: Acyltransferases; Cytoplasm; Escherichia coli; Lipid A; Magnetic Resonance Spectroscopy; Myristic Acids; Protein Precursors; Spectrophotometry, Atomic; Uridine Diphosphate N-Acetylglucosamine; Uridine Diphosphate Sugars

1987
UDP-3-O-((R)-3-hydroxymyristoyl)-N-acetylglucosamine deacetylase functions through a general acid-base catalyst pair mechanism.
    The Journal of biological chemistry, 2005, Apr-29, Volume: 280, Issue:17

    Topics: Amidohydrolases; Bacteria; Binding Sites; Cacodylic Acid; Catalysis; Crystallography, X-Ray; Electrons; Escherichia coli; Histidine; Hydrogen-Ion Concentration; Ions; Kinetics; Models, Chemical; Models, Molecular; Mutagenesis; Mutagenesis, Site-Directed; Mutation; Myristic Acids; Oxygen; Palmitic Acid; Substrate Specificity; Uridine Diphosphate N-Acetylglucosamine; Zinc

2005
A high-throughput-compatible fluorescence anisotropy-based assay for competitive inhibitors of Escherichia coli UDP-N-acetylglucosamine acyltransferase (LpxA).
    Journal of biomolecular screening, 2013, Volume: 18, Issue:3

    Topics: Acyl Carrier Protein; Acyltransferases; Binding, Competitive; Catalytic Domain; Drug Evaluation, Preclinical; Enzyme Inhibitors; Escherichia coli; Fluorescence Polarization; High-Throughput Screening Assays; Inhibitory Concentration 50; Ligands; Lipid A; Myristic Acids; Peptides; Uridine Diphosphate N-Acetylglucosamine

2013
Structure of the bacterial deacetylase LpxC bound to the nucleotide reaction product reveals mechanisms of oxyanion stabilization and proton transfer.
    The Journal of biological chemistry, 2013, Nov-22, Volume: 288, Issue:47

    Topics: Amidohydrolases; Crystallography, X-Ray; Escherichia coli; Lipopolysaccharides; Myristic Acids; Protein Structure, Tertiary; Protons; Uridine Diphosphate N-Acetylglucosamine

2013