Legionella pneumophila SidD is a deAMPylase that modifies Rab1
about
Subversion of Cell-Autonomous Immunity and Cell Migration by Legionella pneumophila EffectorsRegulation of small GTPases by GEFs, GAPs, and GDIsMass spectrometry-based proteomic approaches to study pathogenic bacteria-host interactionsChemical reporters for exploring ADP-ribosylation and AMPylation at the host-pathogen interfaceBacterial pathogens commandeer Rab GTPases to establish intracellular nichesCell biology of infection by Legionella pneumophilaBacterial Type IV secretion systems: versatile virulence machinesActivation of Ran GTPase by a Legionella effector promotes microtubule polymerization, pathogen vacuole motility and infectionProtein LidA from Legionella is a Rab GTPase supereffectorVipD of Legionella pneumophila Targets Activated Rab5 and Rab22 to Interfere with Endosomal Trafficking in MacrophagesMechanism of Rab1b deactivation by the Legionella pneumophila GAP LepBStructural Insights into a Unique Legionella pneumophila Effector LidA Recognizing Both GDP and GTP Bound Rab1 in Their Active StateStructural Basis for Rab1 De-AMPylation by the Legionella pneumophila Effector SidDThe Legionella pneumophila GTPase Activating Protein LepB Accelerates Rab1 Deactivation by a Non-canonical Hydrolytic MechanismLegionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholinationStructure of the Legionella Virulence Factor, SidC Reveals a Unique PI(4)P-Specific Binding Domain Essential for Its Targeting to the Bacterial PhagosomeInnate immunity kinase TAK1 phosphorylates Rab1 on a hotspot for posttranslational modifications by host and pathogenCoxiella burnetii type IV secretion-dependent recruitment of macrophage autophagosomes.The machinery at endoplasmic reticulum-plasma membrane contact sites contributes to spatial regulation of multiple Legionella effector proteins.Identification of novel Coxiella burnetii Icm/Dot effectors and genetic analysis of their involvement in modulating a mitogen-activated protein kinase pathway.Copper-catalyzed azide-alkyne cycloaddition (click chemistry)-based detection of global pathogen-host AMPylation on self-assembled human protein microarrays.Identification of two Legionella pneumophila effectors that manipulate host phospholipids biosynthesisExploitation of evolutionarily conserved amoeba and mammalian processes by Legionella.Unfolded protein response-regulated Drosophila Fic (dFic) protein reversibly AMPylates BiP chaperone during endoplasmic reticulum homeostasis.Inhibiting AMPylation: a novel screen to identify the first small molecule inhibitors of protein AMPylation.Post-translational modifications are key players of the Legionella pneumophila infection strategySpatiotemporal regulation of a Legionella pneumophila T4SS substrate by the metaeffector SidJLpg0393 of Legionella pneumophila is a guanine-nucleotide exchange factor for Rab5, Rab21 and Rab22.Comparative and functional genomics of legionella identified eukaryotic like proteins as key players in host-pathogen interactions.The Legionella Kinase LegK2 Targets the ARP2/3 Complex To Inhibit Actin Nucleation on Phagosomes and Allow Bacterial Evasion of the Late Endocytic PathwaySubversion of membrane transport pathways by vacuolar pathogensA chemical reporter for protein AMPylation.Toxicity and SidJ-Mediated Suppression of Toxicity Require Distinct Regions in the SidE Family of Legionella pneumophila EffectorsCatch and release: Rab1 exploitation by Legionella pneumophila.High-throughput identification of proteins with AMPylation using self-assembled human protein (NAPPA) microarrays.Legionella pneumophila LidA affects nucleotide binding and activity of the host GTPase Rab1Yersinia pestis Requires Host Rab1b for Survival in Macrophages.Endoplasmic Reticulum Tubule Protein Reticulon 4 Associates with the Legionella pneumophila Vacuole and with Translocated Substrate Ceg9.Dot/Icm Effector Translocation by Legionella longbeachae Creates a Replicative Vacuole Similar to That of Legionella pneumophila despite Translocation of Distinct Effector Repertoires.The taming of a Rab GTPase by Legionella pneumophila.
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Legionella pneumophila SidD is a deAMPylase that modifies Rab1
description
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Nature
@fr
artículu científicu espublizáu en 2011
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scientific journal article
@en
vedecký článok (publikovaný 2011/07/06)
@sk
vědecký článek publikovaný v roce 2011
@cs
wetenschappelijk artikel (gepubliceerd op 2011/07/06)
@nl
наукова стаття, опублікована в липні 2011
@uk
مقالة علمية (نشرت في 6-7-2011)
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name
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@ast
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@en
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@nl
type
label
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@ast
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@en
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@nl
prefLabel
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@ast
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@en
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@nl
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P1433
P1476
Legionella pneumophila SidD is a deAMPylase that modifies Rab1
@en
P2093
Yunhao Tan
Zhao-Qing Luo
P2860
P2888
P304
P356
10.1038/NATURE10307
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P577
2011-07-06T00:00:00Z
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P6179
1008388576