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Artificial activation of toxin-antitoxin systems as an antibacterial strategy

Artificial activation of toxin-antitoxin systems as an antibacterial strategy

http://www.wikidata.org/entity/Q37634568

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Toxin-Antitoxin Modules Are Pliable Switches Activated by Multiple Protease Pathways Toxin-Antitoxin Systems of Staphylococcus aureus Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems Toxin-antitoxin systems: Biology, identification, and application YoeB-ribosome structure: a canonical RNase that requires the ribosome for its specific activity Structure of the Proteus vulgaris HigB-(HigA)2-HigB Toxin-Antitoxin Complex Structural basis of Bacillus anthracis MoxXT disruption and the modulation of MoxT ribonuclease activity by rationally designed peptides Structure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic Bacteria Die for the community: an overview of programmed cell death in bacteria Wake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancy Phenotypic and genomic comparison of Mycobacterium aurum and surrogate model species to Mycobacterium tuberculosis: implications for drug discovery.Small Circular DNAs in Human Pathology.Toxin Kid uncouples DNA replication and cell division to enforce retention of plasmid R1 in Escherichia coli cells.Sequence-specific antimicrobials using efficiently delivered RNA-guided nucleases.Molecular epidemiology of extended-spectrum beta-lactamase-producing Escherichia coli in Tunisia and characterization of their virulence factors and plasmid addiction systems Transcriptional and proteolytic regulation of the toxin-antitoxin locus vapBC10 (ssr2962/slr1767) on the chromosome of Synechocystis sp. PCC 6803.Structure-function analysis of VapB4 antitoxin identifies critical features of a minimal VapC4 toxin-binding module The MazEF Toxin-Antitoxin System Alters the β-Lactam Susceptibility of Staphylococcus aureus One cannot rule them all: Are bacterial toxins-antitoxins druggable?Structural and functional studies of the Mycobacterium tuberculosis VapBC30 toxin-antitoxin system: implications for the design of novel antimicrobial peptides Modeling sRNA-Regulated Plasmid Maintenance.Identification and Characterization of the HicAB Toxin-Antitoxin System in the Opportunistic Pathogen Pseudomonas aeruginosa.Programmed cell death in bacteria and implications for antibiotic therapy.Detection of endogenous MazF enzymatic activity in Staphylococcus aureus Regulating toxin-antitoxin expression: controlled detonation of intracellular molecular timebombs Doc toxin is a kinase that inactivates elongation factor Tu Toxin-antitoxin genes of the Gram-positive pathogen Streptococcus pneumoniae: so few and yet so many.Toxin-antitoxin systems are ubiquitous and versatile modulators of prokaryotic cell fate.Speculative strategies for new antibacterials: all roads should not lead to Rome.mazEF-mediated programmed cell death in bacteria: "what is this?".Post-transcriptional regulation of gene expression in bacterial pathogens by toxin-antitoxin systems.The correlation between the presence of quorum sensing, toxin-antitoxin system genes and MIC values with ability of biofilm formation in clinical isolates of Pseudomonas aeruginosa The vapB-vapC Operon of Acidovorax citrulli Functions as a Bona-fide Toxin-Antitoxin Module Linkage, mobility, and selfishness in the MazF family of bacterial toxins: a snapshot of bacterial evolution Light activation of Staphylococcus aureus toxin YoeBSa1 reveals guanosine-specific endoribonuclease activity Mapping Protein-Protein Interactions of the Resistance-Related Bacterial Zeta Toxin-Epsilon Antitoxin Complex (ε₂ζ₂) with High Affinity Peptide Ligands Using Fluorescence Polarization.A highly efficient molecular cloning platform that utilises a small bacterial toxin gene.Functional details of the Mycobacterium tuberculosis VapBC26 toxin-antitoxin system based on a structural study: insights into unique binding and antibiotic peptides.Resonance assignments of a VapC family toxin from Clostridium thermocellum.ATP and autophosphorylation driven conformational changes of HipA kinase revealed by ion mobility and crosslinking mass spectrometry.

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P2860

Artificial activation of toxin-antitoxin systems as an antibacterial strategy

http://www.wikidata.org/entity/Q37634568

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article científic

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article scientifique

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articolo scientifico

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artigo científico

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bilimsel makale

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scientific article published on 22 March 2012

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vedecký článok

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vetenskaplig artikel

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videnskabelig artikel

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vědecký článek

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name

Artificial activation of toxin-antitoxin systems as an antibacterial strategy

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Artificial activation of toxin-antitoxin systems as an antibacterial strategy.

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type

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Artificial activation of toxin-antitoxin systems as an antibacterial strategy

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Artificial activation of toxin-antitoxin systems as an antibacterial strategy.

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prefLabel

Artificial activation of toxin-antitoxin systems as an antibacterial strategy

@en

Artificial activation of toxin-antitoxin systems as an antibacterial strategy.

@nl

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J.TIM.2012.02.005

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Trends in Microbiology

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Artificial activation of toxin-antitoxin systems as an antibacterial strategy

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Julia J Williams

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Paul J Hergenrother

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P2860

Bacterial programmed cell death and multicellular behavior in bacteria

Crystal structure of the plasmid maintenance system epsilon/zeta: functional mechanism of toxin zeta and inactivation by epsilon 2 zeta 2 complex formation

RelE, a global inhibitor of translation, is activated during nutritional stress

Toxin-antitoxin loci are highly abundant in free-living but lost from host-associated prokaryotes

Mini-F plasmid genes that couple host cell division to plasmid proliferation

An Escherichia coli chromosomal "addiction module" regulated by guanosine [corrected] 3',5'-bispyrophosphate: a model for programmed bacterial cell death

TADB: a web-based resource for Type 2 toxin-antitoxin loci in bacteria and archaea

Unique type of plasmid maintenance function: postsegregational killing of plasmid-free cells

Intrinsically disordered proteins are potential drug targets

The phage abortive infection system, ToxIN, functions as a protein-RNA toxin-antitoxin pair

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291-298

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scholarly article

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10.1016/J.TIM.2012.02.005

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6

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2012-03-22T00:00:00Z

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221974140

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22445361

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3952271

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