Characterization of substrate binding and catalysis in the potential antibacterial targetN-acetylglucosamine-1-phosphate uridyltransferase (GlmU)

Characterization of substrate binding and catalysis in the potential antibacterial targetN-acetylglucosamine-1-phosphate uridyltransferase (GlmU)

Item
http://www.wikidata.org/entity/Q27649118
NMR solution structure of poliovirus uridylyated peptide linked to the genome (VPgpU)The structural biology of enzymes involved in natural product glycosylationStructure of a small-molecule inhibitor complexed with GlmU from Haemophilus influenzae reveals an allosteric binding siteStructure and function of GlmU fromMycobacterium tuberculosisAn aminoquinazoline inhibitor of the essential bacterial cell wall synthetic enzyme GlmU has a unique non-protein-kinase-like binding modeStructure of uridine diphosphate N-acetylglucosamine pyrophosphorylase from Entamoeba histolyticaStructures of Bacteroides fragilis uridine 5'-diphosphate-N-acetylglucosamine (UDP-GlcNAc) acyltransferase (BfLpxA)Identification and characterization of novel small molecule inhibitors of the acetyltransferase activity of Escherichia coli N-acetylglucosamine-1-phosphate-uridyltransferase/glucosamine-1-phosphate-acetyltransferase (GlmU).Purification and biochemical characterisation of GlmU from Yersinia pestis.Expression, purification and preliminary crystallographic analysis of N-acetylglucosamine-1-phosphate uridylyltransferase from Mycobacterium tuberculosis.Self-association studies of the bifunctional N-acetylglucosamine-1-phosphate uridyltransferase from Escherichia coliStructure elucidation and in silico docking studies of a novel furopyrimidine antibiotics synthesized by endolithic bacterium Actinomadura sp. AL2.Structure-based design of diverse inhibitors of Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase: combined molecular docking, dynamic simulation, and biological activity.Inhibition studies on Mycobacterium tuberculosis N-acetylglucosamine-1-phosphate uridyltransferase (GlmU).
P2860

Characterization of substrate binding and catalysis in the potential antibacterial targetN-acetylglucosamine-1-phosphate uridyltransferase (GlmU)

Item
http://www.wikidata.org/entity/Q27649118
description
2007 nî lūn-bûn
@nan
2007 թուականի Դեկտեմբերին հրատարակուած գիտական յօդուած
@hyw
2007 թվականի դեկտեմբերին հրատարակված գիտական հոդված
@hy
2007年の論文
@ja
2007年論文
@yue
2007年論文
@zh-hant
2007年論文
@zh-hk
2007年論文
@zh-mo
2007年論文
@zh-tw
2007年论文
@wuu
name
Characterization of substrate ...... phate uridyltransferase (GlmU)
@ast
Characterization of substrate ...... phate uridyltransferase (GlmU)
@en
Characterization of substrate ...... phate uridyltransferase (GlmU)
@nl
type
label
Characterization of substrate ...... phate uridyltransferase (GlmU)
@ast
Characterization of substrate ...... phate uridyltransferase (GlmU)
@en
Characterization of substrate ...... phate uridyltransferase (GlmU)
@nl
prefLabel
Characterization of substrate ...... phate uridyltransferase (GlmU)
@ast
Characterization of substrate ...... phate uridyltransferase (GlmU)
@en
Characterization of substrate ...... phate uridyltransferase (GlmU)
@nl
P1433
P1476
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P932
P356
P1433
P1476
Characterization of substrate ...... phate uridyltransferase (GlmU)
@en
P2093
P2860
P304
P31
P356
P433
P478
P50
P577
P5875
P698
P932