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histidine and udp-3-o-(3-hydroxymyristoyl)-n-acetylglucosamine

histidine has been researched along with udp-3-o-(3-hydroxymyristoyl)-n-acetylglucosamine in 1 studies

Research

Studies (1)

TimeframeStudies, this research(%)All Research%
pre-19900 (0.00)18.7374
1990's0 (0.00)18.2507
2000's1 (100.00)29.6817
2010's0 (0.00)24.3611
2020's0 (0.00)2.80

Authors

AuthorsStudies
Christianson, DW; Fierke, CA; Gennadios, HA; Hernick, M; Rusche, KM; Whittington, DA1

Other Studies

1 other study(ies) available for histidine and udp-3-o-(3-hydroxymyristoyl)-n-acetylglucosamine

ArticleYear
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