Doc toxin is a kinase that inactivates elongation factor Tu
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Emerging Roles of Toxin-Antitoxin Modules in Bacterial PathogenesisKeeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin SystemsThe Caenorhabditis elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and HistonesStructure, Biology, and Therapeutic Application of Toxin-Antitoxin Systems in Pathogenic BacteriaCrystal Structure of the Escherichia coli Fic Toxin-Like Protein in Complex with Its Cognate AntitoxinFunctional validation of putative toxin-antitoxin genes from the Gram-positive pathogen Streptococcus pneumoniae: phd-doc is the fourth bona-fide operonUnfolded 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 moduleTeaching Fido new ModiFICation tricksIn 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 toxinStructural 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 responseFic 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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P2860
Doc toxin is a kinase that inactivates elongation factor Tu
description
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 21 January 2014
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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
Doc toxin is a kinase that inactivates elongation factor Tu
@en
Doc toxin is a kinase that inactivates elongation factor Tu.
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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
P2093
P2860
P356
P1476
Doc toxin is a kinase that inactivates elongation factor Tu
@en
P2093
Christine M Dunham
Francesca P Rothenbacher
Jonathan W Cruz
Nancy A Woychik
Tatsuya Maehigashi
William S Lane
P2860
P304
P356
10.1074/JBC.M113.544429
P407
P577
2014-01-21T00:00:00Z