Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25.
about
Complete Structural Model of Escherichia coli RNA Polymerase from a Hybrid ApproachStructural basis for hijacking siderophore receptors by antimicrobial lasso peptidesThermolysin-linearized microcin J25 retains the structured core of the native macrocyclic peptide and displays antimicrobial activity.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.YojI of Escherichia coli functions as a microcin J25 efflux pumpStructure-activity analysis of microcinJ25: distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymeraseNovel approach to mapping of resistance mutations in whole genomes by using restriction enzyme modulation of transformation efficiencyStructures of naturally occurring circular proteins from bacteria.Novel peptide-protein assay for identification of antimicrobial peptides by fluorescence quenching.Ribosomally synthesized and post-translationally modified peptide natural products: overview and recommendations for a universal nomenclature.Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channelInhibition of lipopolysaccharide transport to the outer membrane in Pseudomonas aeruginosa by peptidomimetic antibiotics.Mutations in the proteolipid subunits of the vacuolar H+-ATPase provide resistance to indolotryptoline natural products.Computational design of the lasso peptide antibiotic microcin J25.Structural basis of transcription: role of the trigger loop in substrate specificity and catalysis.Genetic changes that correlate with reduced susceptibility to daptomycin in Staphylococcus aureus.Macrophage environment turns otherwise MccJ25-resistant Salmonella into sensitive.The antibacterial threaded-lasso peptide capistruin inhibits bacterial RNA polymerase.Collagen-like antimicrobial peptides.Identification and classification of known and putative antimicrobial compounds produced by a wide variety of Bacillales species.Structural perspective on mutations affecting the function of multisubunit RNA polymerases.Low-molecular-weight post-translationally modified microcins.Functional analysis of CedA based on its structure: residues important in binding of DNA and RNA polymerase and in the cell division regulation.Potential applicability of chymotrypsin-susceptible microcin J25 derivatives to food preservation.NMR as an effective tool for the structure determination of lasso peptides.Proline-rich antimicrobial peptides: potential therapeutics against antibiotic-resistant bacteria.Cell Wall-active Bacteriocins and Their Applications Beyond Antibiotic Activity.The proton channel is the minimal structure of ATP synthase necessary and sufficient for microcin h47 antibiotic action.Protective action of ppGpp in microcin J25-sensitive strains.Resistance to the Cyclotide Cycloviolacin O2 in Salmonella enterica Caused by Different Mutations That Often Confer Cross-Resistance or Collateral Sensitivity to Other Antimicrobial Peptides.Ribosome-controlled transcription termination is essential for the production of antibiotic microcin C.Sensitization of microcin J25-resistant strains by a membrane-permeabilizing peptide.Microcin J25 has dual and independent mechanisms of action in Escherichia coli: RNA polymerase inhibition and increased superoxide productionThe leucine-responsive regulatory protein, Lrp, modulates microcin J25 intrinsic resistance in Escherichia coli by regulating expression of the YojI microcin exporter.Mechanism of bactericidal activity of microcin L in Escherichia coli and Salmonella entericaMicrocin J25 uptake: His5 of the MccJ25 lariat ring is involved in interaction with the inner membrane MccJ25 transporter protein SbmA.Mutations of bacterial RNA polymerase leading to resistance to microcin j25.Genome analysis reveals insights of the endophytic Bacillus toyonensis BAC3151 as a potentially novel agent for biocontrol of plant pathogens.Cyclization of pyrrhocoricin retains structural elements crucial for the antimicrobial activity of the native peptide.Lasso-inspired peptides with distinct antibacterial mechanisms.
P2860
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P2860
Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25.
description
2001 nî lūn-bûn
@nan
2001 թուականի Օգոստոսին հրատարակուած գիտական յօդուած
@hyw
2001 թվականի օգոստոսին հրատարակված գիտական հոդված
@hy
2001年の論文
@ja
2001年論文
@yue
2001年論文
@zh-hant
2001年論文
@zh-hk
2001年論文
@zh-mo
2001年論文
@zh-tw
2001年论文
@wuu
name
Escherichia coli RNA polymeras ...... ptide antibiotic microcin J25.
@ast
Escherichia coli RNA polymeras ...... ptide antibiotic microcin J25.
@en
type
label
Escherichia coli RNA polymeras ...... ptide antibiotic microcin J25.
@ast
Escherichia coli RNA polymeras ...... ptide antibiotic microcin J25.
@en
prefLabel
Escherichia coli RNA polymeras ...... ptide antibiotic microcin J25.
@ast
Escherichia coli RNA polymeras ...... ptide antibiotic microcin J25.
@en
P2093
P2860
P1476
Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25
@en
P2093
P2860
P304
P356
10.1128/JB.183.15.4543-4550.2001
P407
P577
2001-08-01T00:00:00Z