YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB - Wikidata - wikimedia - TriplyDB

YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB

YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB

http://www.wikidata.org/entity/Q34494824

about

The ζ toxin induces a set of protective responses and dormancy Emerging Roles of Toxin-Antitoxin Modules in Bacterial Pathogenesis Comparative genomics of defense systems in archaea and bacteria Beyond the cytoskeleton: mesoscale assemblies and their function in spatial organization Toxin-antitoxin systems: Biology, identification, and application Structural insights into the inhibition mechanism of bacterial toxin LsoA by bacteriophage antitoxin Dmd Die for the community: an overview of programmed cell death in bacteria Bacterial actin and tubulin homologs in cell growth and division Bacterial genome instability A widespread bacteriophage abortive infection system functions through a Type IV toxin-antitoxin mechanism.Crystal structure of the toxin Msmeg_6760, the structural homolog of Mycobacterium tuberculosis Rv2035, a novel type II toxin involved in the hypoxic response.Direct interaction of FtsZ and MreB is required for septum synthesis and cell division in Escherichia coli.VapC from the leptospiral VapBC toxin-antitoxin module displays ribonuclease activity on the initiator tRNA.Characterization of Escherichia coli dinJ-yafQ toxin-antitoxin system using insights from mutagenesis data Toxins vapC and pasB from prokaryotic TA modules remain active in mammalian cancer cells.Toxin-antitoxin systems are important for niche-specific colonization and stress resistance of uropathogenic Escherichia coli Characterization of a Streptococcus mutans intergenic region containing a small toxic peptide and its cis-encoded antisense small RNA antitoxin.Revealing bacterial targets of growth inhibitors encoded by bacteriophage T7.Toxin-antitoxin systems influence biofilm and persister cell formation and the general stress response Bacterial persistence increases as environmental fitness decreases.A novel membrane-bound toxin for cell division, CptA (YgfX), inhibits polymerization of cytoskeleton proteins, FtsZ and MreB, in Escherichia coli.Evidence That Bacteriophage λ Kil Peptide Inhibits Bacterial Cell Division by Disrupting FtsZ Protofilaments and Sequestering Protein Subunits.Toxin YafQ Reduces Escherichia coli Growth at Low Temperatures.Polyvalent Proteins, a Pervasive Theme in the Intergenomic Biological Conflicts of Bacteriophages and Conjugative Elements.Characterization of a mazEF toxin-antitoxin homologue from Staphylococcus equorum.Identification and Characterization of the HicAB Toxin-Antitoxin System in the Opportunistic Pathogen Pseudomonas aeruginosa.Mechanism of endonuclease cleavage by the HigB toxin Bacterial cell wall biogenesis is mediated by SEDS and PBP polymerase families functioning semi-autonomously.Toxin-antitoxin systems as multilevel interaction systems.Regulating toxin-antitoxin expression: controlled detonation of intracellular molecular timebombs RnlB Antitoxin of the Escherichia coli RnlA-RnlB Toxin-Antitoxin Module Requires RNase HI for Inhibition of RnlA Toxin Activity.Interaction of Type IV Toxin/Antitoxin Systems in Cryptic Prophages of Escherichia coli K-12.Toxins-antitoxins: diversity, evolution and function.Regulation of growth and death in Escherichia coli by toxin-antitoxin systems.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.Illumination of growth, division and secretion by metabolic labeling of the bacterial cell surface.Prokaryotic toxin-antitoxin systems: novel regulations of the toxins.Desperate times call for desperate measures: benefits and costs of toxin-antitoxin systems.Bacterial Actins and Their Interactors.

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P2860

YeeV is an Escherichia coli toxin that inhibits cell division by targeting the cytoskeleton proteins, FtsZ and MreB

http://www.wikidata.org/entity/Q34494824

description

2010 nî lūn-bûn

@nan

2010 թուականի Նոյեմբերին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի նոյեմբերին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

@zh-hk

2010年論文

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2010年論文

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2010年论文

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name

YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

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YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

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YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

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type

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YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

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YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

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YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

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YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

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YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

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YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

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P932

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P356

J.1365-2958.2010.07433.X

P1433

Molecular Microbiology

P1476

YeeV is an Escherichia coli to ...... eleton proteins, FtsZ and MreB

@en

P2093

Masayori Inouye

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

Naoki Awano

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

Qian Tan

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

P2860

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

An actin-like gene can determine cell polarity in bacteria

Prokaryotic origin of the actin cytoskeleton

Crystal structure of the MazE/MazF complex: molecular bases of antidote-toxin recognition

The Structural Basis for mRNA Recognition and Cleavage by the Ribosome-Dependent Endonuclease RelE

Tight regulation, modulation, and high-level expression by vectors containing the arabinose PBAD promoter

One-step inactivation of chromosomal genes in Escherichia coli K-12 using PCR products

Genomic libraries and a host strain designed for highly efficient two-hybrid selection in yeast

Control of cell shape in bacteria: helical, actin-like filaments in Bacillus subtilis

Characterization of ChpBK, an mRNA interferase from Escherichia coli.

P304

109-118

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scholarly article

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10.1111/J.1365-2958.2010.07433.X

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P407

P433

1

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P478

79

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2010-11-05T00:00:00Z

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49691652

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21166897

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P921

Escherichia coli

P932

3021753

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