Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis. - sprookjes - yvandenbroek - TriplyDB

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

http://www.wikidata.org/entity/Q34207315

about

Biosynthesis of oxygen and nitrogen-containing heterocycles in polyketides Cyclisation mechanisms in the biosynthesis of ribosomally synthesised and post-translationally modified peptides Enzyme Function Initiative-Enzyme Similarity Tool (EFI-EST): A web tool for generating protein sequence similarity networks Identification of an Auxiliary Leader Peptide-Binding Protein Required for Azoline Formation in Ribosomal Natural Products.Structural analysis of leader peptide binding enables leader-free cyanobactin processing Identification of the minimal cytolytic unit for streptolysin S and an expansion of the toxin family.Expanded natural product diversity revealed by analysis of lanthipeptide-like gene clusters in actinobacteria The genomic landscape of ribosomal peptides containing thiazole and oxazole heterocycles.A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.Elucidating and engineering thiopeptide biosynthesis.New Insights into the Biosynthetic Logic of Ribosomally Synthesized and Post-translationally Modified Peptide Natural Products.In Vitro Biosynthesis of the Core Scaffold of the Thiopeptide Thiomuracin Capture of micrococcin biosynthetic intermediates reveals C-terminal processing as an obligatory step for in vivo maturation.The structural biology of patellamide biosynthesis Klebsazolicin inhibits 70S ribosome by obstructing the peptide exit tunnel.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.Mechanisms of cyanobactin biosynthesis Iterative Mechanism of Macrodiolide Formation in the Anticancer Compound Conglobatin.Oxidative Cyclization in Natural Product Biosynthesis Post-translational modifications involved in the biosynthesis of thiopeptide antibiotics.Post-translational thioamidation of methyl-coenzyme M reductase, a key enzyme in methanogenic and methanotrophic Archaea.In Vitro Biosynthesis and Substrate Tolerance of the Plantazolicin Family of Natural Products.Dissection of goadsporin biosynthesis by in vitro reconstitution leading to designer analogues expressed in vivo.Rational design of substrate binding pockets in polyphosphate kinase for use in cost-effective ATP-dependent cascade reactions.In Vitro Biosynthetic Studies of Bottromycin Expand the Enzymatic Capabilities of the YcaO Superfamily.Structure of the Lasso Peptide Isopeptidase Identifies a Topology for Processing Threaded Substrates.Chalkophores.Enzymatic reconstitution of ribosomal peptide backbone thioamidation.

P2860

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P2860

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

http://www.wikidata.org/entity/Q34207315

description

2014 nî lūn-bûn

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2014 թուականի Օգոստոսին հրատարակուած գիտական յօդուած

@hyw

2014 թվականի օգոստոսին հրատարակված գիտական հոդված

@hy

2014年の論文

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2014年論文

@yue

2014年論文

@zh-hant

2014年論文

@zh-hk

2014年論文

@zh-mo

2014年論文

@zh-tw

2014年论文

@wuu

name

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@ast

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@en

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@nl

type

label

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@ast

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@en

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@nl

prefLabel

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@ast

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@en

Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@nl

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Nature Chemical Biology

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Discovery of a new ATP-binding motif involved in peptidic azoline biosynthesis.

@en

P2093

Brandon J Burkhart

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

Courtney L Cox

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Satish K Nair

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P2860

Cytoscape: a software environment for integrated models of biomolecular interaction networks

Patellamide A and C biosynthesis by a microcin-like pathway in Prochloron didemni, the cyanobacterial symbiont of Lissoclinum patella

InterPro in 2011: new developments in the family and domain prediction database

Structure and biosynthesis of the antibiotic bottromycin D

Ubiquitin-like protein activation by E1 enzymes: the apex for downstream signalling pathways

PHENIX: a comprehensive Python-based system for macromolecular structure solution

PROCHECK: a program to check the stereochemical quality of protein structures

Evolution of enzymatic activities in the enolase superfamily: D-Mannonate dehydratase from Novosphingobium aromaticivorans

How the MccB bacterial ancestor of ubiquitin E1 initiates biosynthesis of the microcin C7 antibiotic

Unusual regioversatility of acetyltransferase Eis, a cause of drug resistance in XDR-TB

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823-829

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scholarly article

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10.1038/NCHEMBIO.1608

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10

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10

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Douglas A Mitchell

Jonathan R Chekan

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2014-08-17T00:00:00Z

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264830491

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4167974

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