The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu - Test2 - elhamkhani - TriplyDB

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

http://www.wikidata.org/entity/Q42050878

about

Emerging Roles of Toxin-Antitoxin Modules in Bacterial Pathogenesis Keeping the Wolves at Bay: Antitoxins of Prokaryotic Type II Toxin-Antitoxin Systems Type II toxin: antitoxin systems. More than small selfish entities?Toxin-Antitoxin systems: their role in persistence, biofilm formation, and pathogenicity The Caenorhabditis elegans Protein FIC-1 Is an AMPylase That Covalently Modifies Heat-Shock 70 Family Proteins, Translation Elongation Factors and Histones Structural and biophysical characterization of Staphylococcus aureus SaMazF shows conservation of functional dynamics An intrinsically disordered entropic switch determines allostery in Phd-Doc regulation 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 Wake me when it's over - Bacterial toxin-antitoxin proteins and induced dormancy A bacterial toxin inhibits DNA replication elongation through a direct interaction with the β sliding clamp.The bacterial translation stress response.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 novPTMenzy: a database for enzymes involved in novel post-translational modifications.In silico identification of AMPylating enzymes and study of their divergent evolution.One cannot rule them all: Are bacterial toxins-antitoxins druggable?Global Profiling of Huntingtin-associated protein E (HYPE)-Mediated AMPylation through a Chemical Proteomic Approach.Molecular basis of ribosome recognition and mRNA hydrolysis by the E. coli YafQ toxin.Defining the mRNA recognition signature of a bacterial toxin protein.A Salmonella Toxin Promotes Persister Formation through Acetylation of tRNA Mechanism of endonuclease cleavage by the HigB toxin Structural Determinants for Antitoxin Identity and Insulation of Cross Talk between Homologous Toxin-Antitoxin Systems.Toxin-antitoxin systems as multilevel interaction systems.Doc toxin is a kinase that inactivates elongation factor Tu Evolutionary Dynamics of Pathoadaptation Revealed by Three Independent Acquisitions of the VirB/D4 Type IV Secretion System in Bartonella Post-transcriptional regulation of gene expression in bacterial pathogens by toxin-antitoxin systems.Structure and function of Fic proteins.Elfamycins: inhibitors of elongation factor-Tu.Toxin-antitoxin systems in bacterial growth arrest and persistence.Desperate times call for desperate measures: benefits and costs of toxin-antitoxin systems.HypE-specific nanobodies as tools to modulate HypE-mediated target AMPylation.rAMPing Up Stress Signaling: Protein AMPylation in Metazoans.Legionella and Coxiella effectors: strength in diversity and activity.Toxin-antitoxin systems and their role in disseminating and maintaining antimicrobial resistance.Type II Toxin-Antitoxin Distribution and Adaptive Aspects on Xanthomonas Genomes: Focus on Xanthomonas citri A Novel Fic (Filamentation Induced by cAMP) Protein from Clostridium difficile Reveals an Inhibitory Motif-independent Adenylylation/AMPylation Mechanism.

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P2860

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

http://www.wikidata.org/entity/Q42050878

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

@zh-hant

2013年論文

@zh-hk

2013年論文

@zh-mo

2013年論文

@zh-tw

2013年论文

@wuu

2013年论文

@zh

2013年论文

@zh-cn

name

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

@en

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

@nl

type

label

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

@en

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

@nl

prefLabel

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

@en

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

@nl

P1433

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P433

Q42050878-2530D8E0-D494-4C7E-A761-B7E4AE5995D3

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Q42050878-2FB14C85-84EB-40F7-9FE1-62CBC75798ED

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P932

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P356

P1433

Nature Chemical Biology

P1476

The Fic protein Doc uses an inverted substrate to phosphorylate and inactivate EF-Tu

@en

P2093

Daniel Castro-Roa

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

Nico A J van Nuland

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

Remy Loris

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

Steven De Gieter

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

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

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

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

Evolution of Enzymatic Activities in the Enolase Superfamily: Stereochemically Distinct Mechanisms in Two Families of cis , cis -Muconate Lactonizing Enzymes † ‡

Allostery and intrinsic disorder mediate transcription regulation by conditional cooperativity

Structural basis of Fic-mediated adenylylation

Structure of the Legionella effector AnkX reveals the mechanism of phosphocholine transfer by the FIC domain

Crystal structure of the ternary complex of Phe-tRNAPhe, EF-Tu, and a GTP analog

Crystal structure of intact elongation factor EF-Tu from Escherichia coli in GDP conformation at 2.05 A resolution

P2888

P304

811-817

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P31

scholarly article

P356

10.1038/NCHEMBIO.1364

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P433

12

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P478

9

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P50

Abel Garcia-Pino

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2013-10-20T00:00:00Z

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P5875

258060358

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P698

24141193

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P921

phosphorylation

P932

3836179

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