Relaxed cleavage specificity within the RelE toxin family. - Wikidata - wikimedia - TriplyDB

Relaxed cleavage specificity within the RelE toxin family.

Relaxed cleavage specificity within the RelE toxin family.

http://www.wikidata.org/entity/Q36911558

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Emerging Roles of Toxin-Antitoxin Modules in Bacterial Pathogenesis Structure of the Proteus vulgaris HigB-(HigA)2-HigB Toxin-Antitoxin Complex The HicA toxin from Burkholderia pseudomallei has a role in persister cell formation Wake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancy Regulatory crosstalk between type I and type II toxin-antitoxin systems in the human pathogen Enterococcus faecalis.Bacterial toxin RelE: a highly efficient ribonuclease with exquisite substrate specificity using atypical catalytic residues Toxin-antitoxin systems as multilevel interaction systems.Regulating toxin-antitoxin expression: controlled detonation of intracellular molecular timebombs Initiation of mRNA decay in bacteria.The Mycobacterium tuberculosis relBE toxin:antitoxin genes are stress-responsive modules that regulate growth through translation inhibition.Transition State Charge Stabilization and Acid-Base Catalysis of mRNA Cleavage by the Endoribonuclease RelE.Cell growth inhibition upon deletion of four toxin-antitoxin loci from the megaplasmids of Sinorhizobium meliloti.AtaT blocks translation initiation by N-acetylation of the initiator tRNAfMet.Translation-dependent mRNA cleavage by YhaV in Escherichia coli.Cut in translation: ribosome-dependent mRNA decay.Reassessing the Role of Type II Toxin-Antitoxin Systems in Formation of Escherichia coli Type II Persister Cells.

P2860

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P2860

Relaxed cleavage specificity within the RelE toxin family.

http://www.wikidata.org/entity/Q36911558

description

2013 nî lūn-bûn

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2013年の論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年論文

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2013年论文

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2013年论文

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2013年论文

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name

Relaxed cleavage specificity within the RelE toxin family.

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type

label

Relaxed cleavage specificity within the RelE toxin family.

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prefLabel

Relaxed cleavage specificity within the RelE toxin family.

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Journal of Bacteriology

P1476

Relaxed cleavage specificity within the RelE toxin family.

@en

P2093

Laurence Van Melderen

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

Nathalie Goeders

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Pierre-Luc Drèze

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

P2860

New connections in the prokaryotic toxin-antitoxin network: relationship with the eukaryotic nonsense-mediated RNA decay system

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

Colicin biology

What is the benefit to Escherichia coli of having multiple toxin-antitoxin systems in its genome?

Coupled degradation of a small regulatory RNA and its mRNA targets in Escherichia coli

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

Doc of Prophage P1 Is Inhibited by Its Antitoxin Partner Phd through Fold Complementation

Inhibitory Mechanism of Escherichia coli RelE-RelB Toxin-Antitoxin Module Involves a Helix Displacement Near an mRNA Interferase Active Site

The Crystal Structure of the Intact E. coli RelBE Toxin-Antitoxin Complex Provides the Structural Basis for Conditional Cooperativity

Molecular Structure and Function of the Novel BrnT/BrnA Toxin-Antitoxin System of Brucella abortus

P304

2541-2549

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scholarly article

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10.1128/JB.02266-12

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11

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195

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2013-03-29T00:00:00Z

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23543711

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3676057

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