The iron-siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11-Pro16 beta-hairpin region in the recognition mechanism.
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Structural basis for hijacking siderophore receptors by antimicrobial lasso peptidesStructure of an antibacterial peptide ATP-binding cassette transporter in a novel outward occluded stateFirst insights on organic cosolvent effects on FhuA wildtype and FhuA Δ1-159.Redesign of a plugged beta-barrel membrane protein.Adrenaline modulates the global transcriptional profile of Salmonella revealing a role in the antimicrobial peptide and oxidative stress resistance responses.Topoisomer differentiation of molecular knots by FTICR MS: lessons from class II lasso peptides.Sequence determinants governing the topology and biological activity of a lasso peptide, microcin J25.Dissecting the maturation steps of the lasso peptide microcin J25 in vitro.Microcins in action: amazing defence strategies of Enterobacteria.Beyond iron: non-classical biological functions of bacterial siderophoresGenome-Wide Screening Identifies Six Genes That Are Associated with Susceptibility to Escherichia coli Microcin PDILow-molecular-weight post-translationally modified microcins.Isothermal titration calorimetry of membrane proteins - progress and challenges.pMPES: A Modular Peptide Expression System for the Delivery of Antimicrobial Peptides to the Site of Gastrointestinal Infections Using Probiotics.Microcin PDI regulation and proteolytic cleavage are unique among known microcins.A Natural Chimeric Pseudomonas Bacteriocin with Novel Pore-Forming Activity Parasitizes the Ferrichrome Transporter.The role of bacterial membrane proteins in the internalization of microcin MccJ25 and MccB17.Lasso peptide, a highly stable structure and designable multifunctional backbone.Gemmata species: Planctomycetes of medical interest.Expanding the chemical diversity of lasso peptide MccJ25 with genetically encoded noncanonical amino acids.Characterization of Class IIa Bacteriocin Resistance in Enterococcus faeciumMicrocin J25 has dual and independent mechanisms of action in Escherichia coli: RNA polymerase inhibition and increased superoxide productionMicrocin J25 uptake: His5 of the MccJ25 lariat ring is involved in interaction with the inner membrane MccJ25 transporter protein SbmA.Thermodynamic studies of ligand binding to the human homopentameric glycine receptor using isothermal titration calorimetry.Virulence-targeted Antibacterials: Concept, Promise, and Susceptibility to Resistance Mechanisms.Lasso-inspired peptides with distinct antibacterial mechanisms.CRISPR-based herd immunity can limit phage epidemics in bacterial populations.A pH-sensitive peptide-containing lasso molecular switch.Bacteria-Phage Antagonistic Coevolution and the Implications for Phage TherapyResistance Development to Bacteriophages Occurring during Bacteriophage Therapy
P2860
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P2860
The iron-siderophore transporter FhuA is the receptor for the antimicrobial peptide microcin J25: role of the microcin Val11-Pro16 beta-hairpin region in the recognition mechanism.
description
2005 nî lūn-bûn
@nan
2005 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2005 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2005年の論文
@ja
2005年論文
@yue
2005年論文
@zh-hant
2005年論文
@zh-hk
2005年論文
@zh-mo
2005年論文
@zh-tw
2005年论文
@wuu
name
The iron-siderophore transport ...... in the recognition mechanism.
@ast
The iron-siderophore transport ...... in the recognition mechanism.
@en
type
label
The iron-siderophore transport ...... in the recognition mechanism.
@ast
The iron-siderophore transport ...... in the recognition mechanism.
@en
prefLabel
The iron-siderophore transport ...... in the recognition mechanism.
@ast
The iron-siderophore transport ...... in the recognition mechanism.
@en
P2093
P2860
P356
P1433
P1476
The iron-siderophore transport ...... in the recognition mechanism.
@en
P2093
Christophe Goulard
Jean Peduzzi
Lucienne Letellier
Michel Desmadril
Pascale Boulanger
Sophie Duquesne
P2860
P304
P356
10.1042/BJ20042107
P407
P577
2005-08-01T00:00:00Z