De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
about
Recycling Endosomes and Viral InfectionElucidating Host-Pathogen Interactions Based on Post-Translational Modifications Using Proteomics ApproachesSubversion of Cell-Autonomous Immunity and Cell Migration by Legionella pneumophila EffectorsMass 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 pneumophilaActivation 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 analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAPStructural 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 SidDAgainst the tide: the role of bacterial adhesion in host colonizationLegionella pneumophila regulates the small GTPase Rab1 activity by reversible phosphorylcholinationStructural basis of substrate recognition by a bacterial deubiquitinase important for dynamics of phagosome ubiquitinationStructure of the Legionella Virulence Factor, SidC Reveals a Unique PI(4)P-Specific Binding Domain Essential for Its Targeting to the Bacterial PhagosomeRab1 in cell signaling, cancer and other diseasesThe 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 biosynthesisInhibiting 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 SidJComparative and functional genomics of legionella identified eukaryotic like proteins as key players in host-pathogen interactions.Subversion 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.Host-pathogen interaction profiling using self-assembling human protein arraysLegionella pneumophila LidA affects nucleotide binding and activity of the host GTPase Rab1Yersinia pestis Requires Host Rab1b for Survival in Macrophages.Posttranslational modifications of Rab GTPases help their insertion into membranes.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.Implication of proteins containing tetratricopeptide repeats in conditional virulence phenotypes of Legionella pneumophila.The taming of a Rab GTPase by Legionella pneumophila.
P2860
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P2860
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
description
2011 թուականի Յուլիսին հրատարակուած գիտական յօդուած
@hyw
2011 թվականի հուլիսին հրատարակված գիտական հոդված
@hy
article publié dans la revue scientifique Science
@fr
artículu científicu espublizáu en 2011
@ast
im Juli 2011 veröffentlichter wissenschaftlicher Artikel
@de
scientific journal article
@en
vedecký článok (publikovaný 2011/07/22)
@sk
vědecký článek publikovaný v roce 2011
@cs
wetenschappelijk artikel (gepubliceerd op 2011/07/22)
@nl
наукова стаття, опублікована в липні 2011
@uk
name
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@ast
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@en
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@nl
type
label
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@ast
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@en
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@nl
prefLabel
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@ast
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@en
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@nl
P2093
P2860
P356
P1433
P1476
De-AMPylation of the small GTPase Rab1 by the pathogen Legionella pneumophila
@en
P2093
Alfred Yergey
Andrew H. Gaspar
M. Ramona Neunuebel
Matthias P. Machner
Peter S. Backlund
P2860
P304
P356
10.1126/SCIENCE.1207193
P407
P577
2011-07-22T00:00:00Z