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Doc toxin is a kinase that inactivates elongation factor Tu

Doc toxin is a kinase that inactivates elongation factor Tu

http://www.wikidata.org/entity/Q37635836

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Emerging Roles of Toxin-Antitoxin Modules in Bacterial Pathogenesis Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems The Caenorhabditis elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and Histones Structure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic Bacteria Crystal Structure of the Escherichia coli Fic Toxin-Like Protein in Complex with Its Cognate Antitoxin Functional validation of putative toxin-antitoxin genes from the Gram-positive pathogen Streptococcus pneumoniae: phd-doc is the fourth bona-fide operon Unfolded protein response-regulated Drosophila Fic (dFic) protein reversibly AMPylates BiP chaperone during endoplasmic reticulum homeostasis.Crystal structure of the human, FIC-domain containing protein HYPE and implications for its functions.Structure-function analysis of VapB4 antitoxin identifies critical features of a minimal VapC4 toxin-binding module Teaching Fido new ModiFICation tricks In silico identification of AMPylating enzymes and study of their divergent evolution.High-throughput identification of proteins with AMPylation using self-assembled human protein (NAPPA) microarrays.Molecular basis of ribosome recognition and mRNA hydrolysis by the E. coli YafQ toxin.Mechanism of endonuclease cleavage by the HigB toxin Structural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems.Structure and function of Fic proteins.Elfamycins: inhibitors of elongation factor-Tu.Toxin-antitoxin systems in bacterial growth arrest and persistence.HypE-specific nanobodies as tools to modulate HypE-mediated target AMPylation.rAMPing Up Stress Signaling: Protein AMPylation in Metazoans.Zinc regulates a switch between primary and alternative S18 ribosomal proteins in Mycobacterium tuberculosis.A novel link between Fic (filamentation induced by cAMP)-mediated adenylylation/AMPylation and the unfolded protein response Fic Proteins of Campylobacter fetus subsp. venerealis Form a Network of Functional Toxin-Antitoxin Systems.Homologous VapC Toxins Inhibit Translation and Cell Growth by Sequence-Specific Cleavage of tRNAfMet.The genome sequence of Escherichia coli tailed phage D6 and the diversity of Enterobacteriales circular plasmid prophages.Identification of Fic-1 as an enzyme that inhibits bacterial DNA replication by AMPylating GyrB, promoting filament formation.Toxin-Antitoxin Systems in Bacteria and Archaea

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Doc toxin is a kinase that inactivates elongation factor Tu

http://www.wikidata.org/entity/Q37635836

description

article científic

@ca

article scientifique

@fr

articolo scientifico

@it

artigo científico

@pt

bilimsel makale

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scientific article published on 21 January 2014

@en

vedecký článok

@sk

vetenskaplig artikel

@sv

videnskabelig artikel

@da

vědecký článek

@cs

name

Doc toxin is a kinase that inactivates elongation factor Tu

@en

Doc toxin is a kinase that inactivates elongation factor Tu.

@nl

type

label

Doc toxin is a kinase that inactivates elongation factor Tu

@en

Doc toxin is a kinase that inactivates elongation factor Tu.

@nl

prefLabel

Doc toxin is a kinase that inactivates elongation factor Tu

@en

Doc toxin is a kinase that inactivates elongation factor Tu.

@nl

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JBC.M113.544429

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Journal of Biological Chemistry

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Doc toxin is a kinase that inactivates elongation factor Tu

@en

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Christine M Dunham

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

Francesca P Rothenbacher

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Jonathan W Cruz

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Nancy A Woychik

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

Tatsuya Maehigashi

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

William S Lane

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

P2860

Adenylylation control by intra- or intermolecular active-site obstruction in Fic proteins

The fic domain: regulation of cell signaling by adenylylation

AMPylation of Rho GTPases by Vibrio VopS disrupts effector binding and downstream signaling

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

Genome of bacteriophage P1

Kinetic proofreading: a new mechanism for reducing errors in biosynthetic processes requiring high specificity

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

The RosettaDock server for local protein-protein docking

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

Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity

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7788-7798

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scholarly article

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10.1074/JBC.M113.544429

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2014-01-21T00:00:00Z

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