Identification of active-site inhibitors of MurG using a generalizable, high-throughput glycosyltransferase screen.
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The Membrane Steps of Bacterial Cell Wall Synthesis as Antibiotic TargetsVirtual Screening for UDP-Galactopyranose Mutase Ligands Identifies a New Class of Antimycobacterial AgentsA neutral diphosphate mimic crosslinks the active site of human O-GlcNAc transferaseIdentifying essential genes in bacterial metabolic networks with machine learning methodsSystematic error detection in experimental high-throughput screening.Antimicrobial activity and cytotoxicity of some 2-amino-5-alkylidene-thiazol-4-ones.A small molecule that inhibits OGT activity in cells.Chemoenzymatic syntheses of water-soluble lipid I fluorescent probes.Synthesis of ureidomuraymycidine derivatives for structure-activity relationship studies of muraymycins.Fluorescence-based assay for polyprenyl phosphate-GlcNAc-1-phosphate transferase (WecA) and identification of novel antimycobacterial WecA inhibitors.Lipid intermediates in the biosynthesis of bacterial peptidoglycanNon-carbohydrate inhibitors of the lectin DC-SIGN.The biosynthesis of peptidoglycan lipid-linked intermediates.First small molecular inhibitors of T. brucei dolicholphosphate mannose synthase (DPMS), a validated drug target in African sleeping sickness.Specific labeling of peptidoglycan precursors as a tool for bacterial cell wall studies.Improved synthesis of capuramycin and its analogues.Peptidoglycan biosynthesis machinery: a rich source of drug targets.Viable screening targets related to the bacterial cell wall.Detecting and overcoming systematic bias in high-throughput screening technologies: a comprehensive review of practical issues and methodological solutions.Concise synthesis of capuramycin.High-throughput screening for inhibitors of sialyl- and fucosyltransferases.Acceptor substrate selectivity and kinetic mechanism of Bacillus subtilis TagA.Scintillation proximity assay for inhibitors of Escherichia coli MurG and, optionally, MraY.The essential peptidoglycan glycosyltransferase MurG forms a complex with proteins involved in lateral envelope growth as well as with proteins involved in cell division in Escherichia coli.Exploring the role of the 5-substituent for the intrinsic fluorescence of 5-aryl and 5-heteroaryl uracil nucleotides: a systematic study.Discovery of novel inhibitors of Mycobacterium tuberculosis MurG: homology modelling, structure based pharmacophore, molecular docking, and molecular dynamics simulations.Rapid screening of sugar-nucleotide donor specificities of putative glycosyltransferases.Statistical analysis of systematic errors in high-throughput screening.
P2860
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P2860
Identification of active-site inhibitors of MurG using a generalizable, high-throughput glycosyltransferase screen.
description
2003 nî lūn-bûn
@nan
2003 թուականի Սեպտեմբերին հրատարակուած գիտական յօդուած
@hyw
2003 թվականի սեպտեմբերին հրատարակված գիտական հոդված
@hy
2003年の論文
@ja
2003年論文
@yue
2003年論文
@zh-hant
2003年論文
@zh-hk
2003年論文
@zh-mo
2003年論文
@zh-tw
2003年论文
@wuu
name
Identification of active-site ...... ut glycosyltransferase screen.
@ast
Identification of active-site ...... ut glycosyltransferase screen.
@en
type
label
Identification of active-site ...... ut glycosyltransferase screen.
@ast
Identification of active-site ...... ut glycosyltransferase screen.
@en
prefLabel
Identification of active-site ...... ut glycosyltransferase screen.
@ast
Identification of active-site ...... ut glycosyltransferase screen.
@en
P2093
P356
P1476
Identification of active-site ...... ut glycosyltransferase screen.
@en
P2093
Jeremiah S Helm
Suzanne Walker
P304
11168-11169
P356
10.1021/JA036494S
P407
P577
2003-09-01T00:00:00Z