Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: atomic basis for GE2270A inhibition of EF-Tu
about
tRNAs as antibiotic targetsThiopeptide antibiotics: retrospective and recent advancesConformational change of elongation factor Tu (EF-Tu) induced by antibiotic binding. Crystal structure of the complex between EF-Tu.GDP and aurodoxAntimicrobial evaluation of nocathiacins, a thiazole peptide class of antibiotics.Identification of novel inhibitors of bacterial translation elongation factorsManipulation of thiocillin variants by prepeptide gene replacement: structure, conformation, and activity of heterocycle substitution mutants.Thiazolyl peptide antibiotic biosynthesis: a cascade of post-translational modifications on ribosomal nascent proteins.The function and synthesis of ribosomes.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Inhibition of translation by cytotrienin A--a member of the ansamycin familyCodon randomization for rapid exploration of chemical space in thiopeptide antibiotic variants.Elongation factor Tu-targeted antibiotics: four different structures, two mechanisms of action.New Frontiers in DruggabilityElucidating and engineering thiopeptide biosynthesis.Thiostrepton Variants Containing a Contracted Quinaldic Acid Macrocycle Result from Mutagenesis of the Second Residue.The posttranslational modification cascade to the thiopeptide berninamycin generates linear forms and altered macrocyclic scaffoldsRecent advances in the chemistry and biology of naturally occurring antibiotics.Generation of thiocillin variants by prepeptide gene replacement and in vivo processing by Bacillus cereus.Recent advances in thiopeptide antibiotic biosynthesis.Biosynthesis of thiopeptide antibiotics and their pathway engineering.Antibacterials Developed to Target a Single Organism: Mechanisms and Frequencies of Reduced Susceptibility to the Novel Anti-Clostridium difficile Compounds Fidaxomicin and LFF571.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.Rapid evolution in conformational space: a study of loop regions in a ubiquitous GTP binding domain.Elongation factor Tu3 (EF-Tu3) from the kirromycin producer Streptomyces ramocissimus Is resistant to three classes of EF-Tu-specific inhibitors.Characterization of a novel plasmid-borne thiopeptide gene cluster in Staphylococcus epidermidis strain 115.In vitro antibacterial activities of a thiazolyl peptide antibiotic PM2409.
P2860
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P2860
Structure of an EF-Tu complex with a thiazolyl peptide antibiotic determined at 2.35 A resolution: atomic basis for GE2270A inhibition of EF-Tu
description
2000 nî lūn-bûn
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2000 թուականի Յունուարին հրատարակուած գիտական յօդուած
@hyw
2000 թվականի հունվարին հրատարակված գիտական հոդված
@hy
2000年の論文
@ja
2000年論文
@yue
2000年論文
@zh-hant
2000年論文
@zh-hk
2000年論文
@zh-mo
2000年論文
@zh-tw
2000年论文
@wuu
name
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@ast
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@en
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@nl
type
label
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@ast
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@en
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@nl
prefLabel
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@ast
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@en
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@nl
P356
P1433
P1476
Structure of an EF-Tu complex ...... or GE2270A inhibition of EF-Tu
@en
P2093
P356
10.1021/BI9913597
P407
P577
2000-01-11T00:00:00Z