Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu. - Test2 - elhamkhani - TriplyDB

Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

http://www.wikidata.org/entity/Q34972804

about

Radical-mediated enzymatic carbon chain fragmentation-recombination Thiopeptide antibiotics: retrospective and recent advances Lessons learned from the transformation of natural product discovery to a genome-driven endeavor Radical SAM-mediated methylation reactions Radical-mediated enzymatic methylation: a tale of two SAMS Targeting Antibiotic Resistance ThioFinder: a web-based tool for the identification of thiopeptide gene clusters in DNA sequences Identification and Functional Analysis of the Nocardithiocin Gene Cluster in Nocardia pseudobrasiliensis Expansion of ribosomally produced natural products: a nitrile hydratase- and Nif11-related precursor family Two heterologously expressed Planobispora rosea proteins cooperatively induce Streptomyces lividans thiostrepton uptake and storage from the extracellular medium Plantazolicin, a novel microcin B17/streptolysin S-like natural product from Bacillus amyloliquefaciens FZB42.A simple reverse genetics approach to elucidating the biosynthetic pathway of nocathiacin.Biosynthesis and regulation of grisemycin, a new member of the linaridin family of ribosomally synthesized peptides produced by Streptomyces griseus IFO 13350.Recent trends and observations in the design of high-quality screening collections.Manipulation of thiocillin variants by prepeptide gene replacement: structure, conformation, and activity of heterocycle substitution mutants.Natural products version 2.0: connecting genes to molecules.Thiazolyl peptide antibiotic biosynthesis: a cascade of post-translational modifications on ribosomal nascent proteins.Clostridiolysin S, a post-translationally modified biotoxin from Clostridium botulinum.Antibiotic discovery in the twenty-first century: current trends and future perspectives.Production of a new thiopeptide antibiotic, TP-1161, by a marine Nocardiopsis species.Genome mining for ribosomally synthesized natural products Thiazole/oxazole-modified microcins: complex natural products from ribosomal templates YcaO domains use ATP to activate amide backbones during peptide cyclodehydrations.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Codon randomization for rapid exploration of chemical space in thiopeptide antibiotic variants.In vitro activity of the nisin dehydratase NisB.Genomic basis for natural product biosynthetic diversity in the actinomycetes Structure and mechanism of lanthipeptide biosynthetic enzymes.Progress in the discovery of treatments for C. difficile infection: A clinical and medicinal chemistry review.Heterologous expression of the thiopeptide antibiotic GE2270 from Planobispora rosea ATCC 53733 in Streptomyces coelicolor requires deletion of ribosomal genes from the expression construct.Identification of the thiazolyl peptide GE37468 gene cluster from Streptomyces ATCC 55365 and heterologous expression in Streptomyces lividans.Complex biotransformations catalyzed by radical S-adenosylmethionine enzymes.In vitro and in vivo activities of novel, semisynthetic thiopeptide inhibitors of bacterial elongation factor Tu.Genome mining for ribosomally synthesized and post-translationally modified peptides (RiPPs) in anaerobic bacteria.A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.Structure-based Mechanistic Insights into Terminal Amide Synthase in Nosiheptide-Represented Thiopeptides Biosynthesis Elucidating and engineering thiopeptide biosynthesis.In Vitro Biosynthesis of the Core Scaffold of the Thiopeptide Thiomuracin Saturation mutagenesis of TsrA Ala4 unveils a highly mutable residue of thiostrepton A.Thiostrepton Variants Containing a Contracted Quinaldic Acid Macrocycle Result from Mutagenesis of the Second Residue.

P2860

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P2860

Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

http://www.wikidata.org/entity/Q34972804

description

2009 nî lūn-bûn

@nan

2009 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2009 թվականի ապրիլին հրատարակված գիտական հոդված

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2009年の論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年論文

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2009年论文

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name

Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

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Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

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Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

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type

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Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

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Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

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Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

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prefLabel

Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

@ast

Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

@en

Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

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Journal of the American Chemical Society

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Ribosomally synthesized thiopeptide antibiotics targeting elongation factor Tu.

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P2093

Andreas E Hein

http://www.w3.org/2001/XMLSchema#string

Christian N Parker

http://www.w3.org/2001/XMLSchema#string

Eric Weber

http://www.w3.org/2001/XMLSchema#string

Esther K Schmitt

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Hans Ulrich Naegeli

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Jennifer A Leeds

http://www.w3.org/2001/XMLSchema#string

Klaus Memmert

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Lukas Oberer

http://www.w3.org/2001/XMLSchema#string

Matthew J LaMarche

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Nathalie Burrer

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5946-5955

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scholarly article

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10.1021/JA900488A

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16

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131

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2009-04-01T00:00:00Z

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24250078

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19338336

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