Mutations of bacterial RNA polymerase leading to resistance to microcin j25. - Wikidata - awgldk - TriplyDB

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

http://www.wikidata.org/entity/Q44195387

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Inhibition of bacterial RNA polymerase by streptolydigin: stabilization of a straight-bridge-helix active-center conformation Structural basis for transcription inhibition by tagetitoxin New Insights into the Functions of Transcription Factors that Bind the RNA Polymerase Secondary Channel Complete Structural Model of Escherichia coli RNA Polymerase from a Hybrid Approach Xanthomonins I-III: a new class of lasso peptides with a seven-residue macrolactam ring 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.Stepwise mechanism for transcription fidelity YojI of Escherichia coli functions as a microcin J25 efflux pump Structure-activity analysis of microcinJ25: distinct parts of the threaded lasso molecule are responsible for interaction with bacterial RNA polymerase Central role of the RNA polymerase trigger loop in intrinsic RNA hydrolysis.Structures of naturally occurring circular proteins from bacteria.Alpha-amanitin blocks translocation by human RNA polymerase II.Antibacterial peptide microcin J25 inhibits transcription by binding within and obstructing the RNA polymerase secondary channel 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.Purification of bacterial RNA polymerase: tools and protocols.The antibacterial threaded-lasso peptide capistruin inhibits bacterial RNA polymerase.NTP-driven translocation and regulation of downstream template opening by multi-subunit RNA polymerases.Structural perspective on mutations affecting the function of multisubunit RNA polymerases.Low-molecular-weight post-translationally modified microcins.Potential applicability of chymotrypsin-susceptible microcin J25 derivatives to food preservation.NMR as an effective tool for the structure determination of lasso peptides.Antibiotic streptolydigin requires noncatalytic Mg2+ for binding to RNA polymerase.Aptamers to Escherichia coli core RNA polymerase that sense its interaction with rifampicin, sigma-subunit and GreB.The proteome targets of intracellular targeting antimicrobial peptides.Intracellular Targeting Mechanisms by Antimicrobial Peptides Protective action of ppGpp in microcin J25-sensitive strains.Involvement of the beta subunit of RNA polymerase in resistance to streptolydigin and streptovaricin in the producer organisms Streptomyces lydicus and Streptomyces spectabilis 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.Expanding the chemical diversity of lasso peptide MccJ25 with genetically encoded noncanonical amino acids.Sensitization of microcin J25-resistant strains by a membrane-permeabilizing peptide.Systematic structure-activity analysis of microcin J25.Microcin J25 has dual and independent mechanisms of action in Escherichia coli: RNA polymerase inhibition and increased superoxide production The 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 enterica Microcin J25 uptake: His5 of the MccJ25 lariat ring is involved in interaction with the inner membrane MccJ25 transporter protein SbmA.Lasso peptides from proteobacteria: Genome mining employing heterologous expression and mass spectrometry.Antibiotics from Gram-negative bacteria: a comprehensive overview and selected biosynthetic highlights.

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P2860

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

http://www.wikidata.org/entity/Q44195387

description

2002 nî lūn-bûn

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2002年の論文

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年学术文章

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2002年學術文章

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2002年學術文章

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name

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

@en

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

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type

label

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

@en

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

@nl

prefLabel

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

@en

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

@nl

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P1433

Journal of Biological Chemistry

P1476

Mutations of bacterial RNA polymerase leading to resistance to microcin j25.

@en

P2093

Dhruti Savalia

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

Irina Artsimovitch

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Julia Yuzenkova

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Konstantin Severinov

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

Monica Delgado

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Rachel A Mooney

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Raul Salomon

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Ricardo N Farias

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Robert Landick

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Sergei Nechaev

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P2860

Structural mechanism for rifampicin inhibition of bacterial rna polymerase

Crystal structure of a bacterial RNA polymerase holoenzyme at 2.6 A resolution

Structural basis of transcription initiation: RNA polymerase holoenzyme at 4 A resolution

Mapping and sequencing of mutations in the Escherichia colirpoB gene that lead to rifampicin resistance

Extensive homology among the largest subunits of eukaryotic and prokaryotic RNA polymerases

Solution structure of microcin J25, the single macrocyclic antimicrobial peptide from Escherichia coli.

Crystal structure of Thermus aquaticus core RNA polymerase at 3.3 A resolution.

RNA polymerase structure-function: insights into points of transcriptional regulation.

Escherichia coli RNA polymerase is the target of the cyclopeptide antibiotic microcin J25.

Localization of an alpha-amanitin resistance mutation in the gene encoding the largest subunit of mouse RNA polymerase II.

P304

50867-50875

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scholarly article

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10.1074/JBC.M209425200

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P433

52

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P478

277

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2002-10-24T00:00:00Z

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11061692

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12401787

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