A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.
about
Structure and Mechanism of the Sphingopyxin I Lasso Peptide IsopeptidaseStructural basis for precursor protein-directed ribosomal peptide macrocyclizationThe Radical S-Adenosyl-l-methionine Enzyme MftC Catalyzes an Oxidative Decarboxylation of the C-Terminus of the MftA PeptideThe genomic landscape of ribosomal peptides containing thiazole and oxazole heterocycles.Construction of Lasso Peptide Fusion ProteinsThe enterococcal cytolysin synthetase has an unanticipated lipid kinase foldLeader Peptide-Free In Vitro Reconstitution of Microviridin Biosynthesis Enables Design of Synthetic Protease-Targeted Libraries.Initial Molecular Recognition Steps of McjA Precursor during Microcin J25 Lasso Peptide Maturation.Elucidating and engineering thiopeptide biosynthesis.Characterization of the macrocyclase involved in the biosynthesis of RiPP cyclic peptides in plants.New Insights into the Biosynthetic Logic of Ribosomally Synthesized and Post-translationally Modified Peptide Natural Products.Structure and tRNA Specificity of MibB, a Lantibiotic Dehydratase from Actinobacteria Involved in NAI-107 Biosynthesis.In Vitro Biosynthesis of the Core Scaffold of the Thiopeptide ThiomuracinDemonstration That the Radical S-Adenosylmethionine (SAM) Enzyme PqqE Catalyzes de Novo Carbon-Carbon Cross-linking within a Peptide Substrate PqqA in the Presence of the Peptide Chaperone PqqDStructure-Activity Analysis of Gram-positive Bacterium-producing Lasso Peptides with Anti-mycobacterial Activity.Capture of micrococcin biosynthetic intermediates reveals C-terminal processing as an obligatory step for in vivo maturation.At the confluence of ribosomally synthesized peptide modification and radical S-adenosylmethionine (SAM) enzymology.Nuclear Magnetic Resonance Structure and Binding Studies of PqqD, a Chaperone Required in the Biosynthesis of the Bacterial Dehydrogenase Cofactor Pyrroloquinoline Quinone.YcaO-Dependent Posttranslational Amide Activation: Biosynthesis, Structure, and Function.A new genome-mining tool redefines the lasso peptide biosynthetic landscape.Methanobactins: from genome to function.Employing the promiscuity of lantibiotic biosynthetic machineries to produce novel antimicrobials.Mechanisms of cyanobactin biosynthesisBiosynthesis: Leading the way to RiPPs.Mechanistic Understanding of Lanthipeptide Biosynthetic Enzymes.A Lanthipeptide-like N-Terminal Leader Region Guides Peptide Epimerization by Radical SAM Epimerases: Implications for RiPP Evolution.Reconstitution and Minimization of a Micrococcin Biosynthetic Pathway in Bacillus subtilis.Post-translational Claisen Condensation and Decarboxylation en Route to the Bicyclic Core of Pantocin APost-translational thioamidation of methyl-coenzyme M reductase, a key enzyme in methanogenic and methanotrophic Archaea.Chimeric Leader Peptides for the Generation of Non-Natural Hybrid RiPP Products.The B1 Protein Guides the Biosynthesis of a Lasso Peptide.In Vitro Biosynthesis and Substrate Tolerance of the Plantazolicin Family of Natural Products.Lasso Peptide Biosynthetic Protein LarB1 Binds Both Leader and Core Peptide Regions of the Precursor Protein LarA.Insights into the Unique Phosphorylation of the Lasso Peptide Paeninodin.Dissection of goadsporin biosynthesis by in vitro reconstitution leading to designer analogues expressed in vivo.The B12-Radical SAM Enzyme PoyC Catalyzes Valine Cβ-Methylation during Polytheonamide Biosynthesis.Mutagenesis of NosM Leader Peptide Reveals Important Elements in Nosiheptide BiosynthesisCharacterization of a dual function macrocyclase enables design and use of efficient macrocyclization substrates.Biosynthetic Timing and Substrate Specificity for the Thiopeptide Thiomuracin.Radical SAM Enzymes in the Biosynthesis of Ribosomally Synthesized and Post-translationally Modified Peptides (RiPPs).
P2860
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P2860
A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.
description
2015 nî lūn-bûn
@nan
2015年の論文
@ja
2015年論文
@yue
2015年論文
@zh-hant
2015年論文
@zh-hk
2015年論文
@zh-mo
2015年論文
@zh-tw
2015年论文
@wuu
2015年论文
@zh
2015年论文
@zh-cn
name
A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.
@ast
A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.
@en
type
label
A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.
@ast
A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.
@en
prefLabel
A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.
@ast
A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.
@en
P2860
P356
P1476
A prevalent peptide-binding domain guides ribosomal natural product biosynthesis.
@en
P2093
Brandon J Burkhart
Graham A Hudson
P2860
P2888
P304
P356
10.1038/NCHEMBIO.1856
P577
2015-07-13T00:00:00Z
P5875
P6179
1044995040