An efficient method for the in vitro production of azol(in)e-based cyclic peptides.
about
Structure and Substrate Recognition of the Bottromycin Maturation Enzyme BotPSynthesis of Hybrid Cyclopeptides through Enzymatic MacrocyclizationStructural analysis of leader peptide binding enables leader-free cyanobactin processingFacile Removal of Leader Peptides from Lanthipeptides by Incorporation of a Hydroxy AcidCyanobactins from Cyanobacteria: Current Genetic and Chemical State of Knowledge.Metabolic model for diversity-generating biosynthesisNew 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 ThiomuracinA Unique Tryptophan C-Prenyltransferase from the Kawaguchipeptin Biosynthetic PathwayThe structural biology of patellamide biosynthesisNew Modalities for Challenging Targets in Drug Discovery.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.A Blind Test of Computational Technique for Predicting the Likelihood of Peptide Sequences to Cyclize.Mechanisms of cyanobactin biosynthesisDirecting Biosynthesis: Practical Supply of Natural and Unnatural Cyanobactins.Modularity of RiPP Enzymes Enables Designed Synthesis of Decorated Peptides.Bistratamides M and N, Oxazole-Thiazole Containing Cyclic Hexapeptides Isolated from Lissoclinum bistratum Interaction of Zinc (II) with Bistratamide K.In Vitro Biosynthesis and Substrate Tolerance of the Plantazolicin Family of Natural Products.Characterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates.Cyclic peptide production using a macrocyclase with enhanced substrate promiscuity and relaxed recognition determinants.Characterization of the Fast and Promiscuous Macrocyclase from Plant PCY1 Enables the Use of Simple Substrates.Parallel lives of symbionts and hosts: chemical mutualism in marine animals.A lanthipeptide library used to identify a protein-protein interaction inhibitor.Dinuclear ZnII and mixed CuII-ZnII complexes of artificial patellamides as phosphatase models.
P2860
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P2860
An efficient method for the in vitro production of azol(in)e-based cyclic peptides.
description
2014 nî lūn-bûn
@nan
2014年の論文
@ja
2014年学术文章
@wuu
2014年学术文章
@zh
2014年学术文章
@zh-cn
2014年学术文章
@zh-hans
2014年学术文章
@zh-my
2014年学术文章
@zh-sg
2014年學術文章
@yue
2014年學術文章
@zh-hant
name
An efficient method for the in vitro production of azol
@nl
An efficient method for the in vitro production of azol(in)e-based cyclic peptides.
@en
type
label
An efficient method for the in vitro production of azol
@nl
An efficient method for the in vitro production of azol(in)e-based cyclic peptides.
@en
prefLabel
An efficient method for the in vitro production of azol
@nl
An efficient method for the in vitro production of azol(in)e-based cyclic peptides.
@en
P2093
P2860
P50
P356
P1476
An efficient method for the in vitro production of azol(in)e-based cyclic peptides
@en
P2093
Andrew F Bent
Andrew R McEwan
Huanting Liu
Jesko Koehnke
Louise Thomas
Marcel Jaspars
Nathalie Pieiller
Rosemary I Adaba
P2860
P304
14171-14174
P356
10.1002/ANIE.201408082
P407
P577
2014-10-21T00:00:00Z