Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA - Wikidata - awgldk - TriplyDB

Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA

Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA

http://www.wikidata.org/entity/Q27660007

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Regulation of small GTPases by GEFs, GAPs, and GDIs Phosphoinositides: tiny lipids with giant impact on cell regulation High-affinity binding of phosphatidylinositol 4-phosphate by Legionella pneumophila DrrA VipD of Legionella pneumophila Targets Activated Rab5 and Rab22 to Interfere with Endosomal Trafficking in Macrophages Structural analyses of Legionella LepB reveal a new GAP fold that catalytically mimics eukaryotic RasGAP Structural Insights into a Unique Legionella pneumophila Effector LidA Recognizing Both GDP and GTP Bound Rab1 in Their Active State The crystal structure of LidA, a translocated substrate of the Legionella pneumophila type IV secretion system Structural Basis for PI(4)P-Specific Membrane Recruitment of the Legionella pneumophila Effector DrrA/SidM Guanine nucleotide exchange factors (GEFs) have a critical but not exclusive role in organelle localization of Rab GTPases.The Mon1-Ccz1 GEF activates the Rab7 GTPase Ypt7 via a longin-fold-Rab interface and association with PI3P-positive membranes.Modulation of Rab GTPase function by a protein phosphocholine transferase Structure of the Legionella Virulence Factor, SidC Reveals a Unique PI(4)P-Specific Binding Domain Essential for Its Targeting to the Bacterial Phagosome A novel probe for phosphatidylinositol 4-phosphate reveals multiple pools beyond the Golgi.The machinery at endoplasmic reticulum-plasma membrane contact sites contributes to spatial regulation of multiple Legionella effector proteins.Aminoacyl-tRNA-charged eukaryotic elongation factor 1A is the bona fide substrate for Legionella pneumophila effector glucosyltransferases The E Block motif is associated with Legionella pneumophila translocated substrates.Comprehensive analysis of the HEPN superfamily: identification of novel roles in intra-genomic conflicts, defense, pathogenesis and RNA processing.Subversion of membrane transport pathways by vacuolar pathogens Structure-Function Analyses of the Interactions between Rab11 and Rab14 Small GTPases with Their Shared Effector Rab Coupling Protein (RCP)AMPylation is critical for Rab1 localization to vacuoles containing Legionella pneumophila.Manipulation of host membrane machinery by bacterial pathogens Recent insights into Pasteurella multocida toxin and other G-protein-modulating bacterial toxins.Hijacking of Membrane Contact Sites by Intracellular Bacterial Pathogens.Manipulation of host vesicular trafficking and innate immune defence by Legionella Dot/Icm effectors.A trapper keeper for TRAPP, its structures and functions.A Rab-centric perspective of bacterial pathogen-occupied vacuoles.Formation of a pathogen vacuole according to Legionella pneumophila: how to kill one bird with many stones.Invited review: Small GTPases and their GAPs.Quantifying lipid changes in various membrane compartments using lipid binding protein domains.Rab GTPases and their interacting protein partners: Structural insights into Rab functional diversity.Taking control: Hijacking of Rab GTPases by intracellular bacterial pathogens.The Legionella pneumophila effector DrrA is sufficient to stimulate SNARE-dependent membrane fusion.Discovery of Rab1 binding sites using an ensemble of clustering methods.Rab GTPases and tethering in the yeast endocytic pathway.Characterization of enzymes from Legionella pneumophila involved in reversible adenylylation of Rab1 protein.The versatile Legionella effector protein DrrA.GOP-1 promotes apoptotic cell degradation by activating the small GTPase Rab2 in C. elegans.The Legionella pneumophila effector Ceg4 is a phosphotyrosine phosphatase that attenuates activation of eukaryotic MAPK pathways.Dynamics of phosphoinositide conversion in clathrin-mediated endocytic traffic.A guanine nucleotide exchange factor (GEF) limits Rab GTPase-driven membrane fusion.

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Structural mechanism of host Rab1 activation by the bifunctional Legionella type IV effector SidM/DrrA

http://www.wikidata.org/entity/Q27660007

description

2010 nî lūn-bûn

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2010 թուականի Մարտին հրատարակուած գիտական յօդուած

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2010 թվականի մարտին հրատարակված գիտական հոդված

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2010年の論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年論文

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2010年论文

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Structural mechanism of host R ...... lla type IV effector SidM/DrrA

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Feng Shao

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Liping Liu

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Liyan Hu

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Qing Yao

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Yan Zhou

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Yongqun Zhu

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P2860

Structural basis for Rab GTPase activation by VPS9 domain exchange factors

Nucleotide exchange via local protein unfolding--structure of Rab8 in complex with MSS4.

Structural insights into the dual nucleotide exchange and GDI displacement activity of SidM/DrrA

Identification of a GDI displacement factor that releases endosomal Rab GTPases from Rab-GDI

Structure of Rab GDP-dissociation inhibitor in complex with prenylated YPT1 GTPase

A Catalytic Coiled Coil: Structural Insights into the Activation of the Rab GTPase Sec4p by Sec2p

Crystal structure of the Sec4p{middle dot}Sec2p complex in the nucleotide exchanging intermediate state

The Structural Basis for Activation of the Rab Ypt1p by the TRAPP Membrane-Tethering Complexes

Rab proteins as membrane organizers

Saccharomyces cerevisiae Pra1p/Yip3p interacts with Yip1p and Rab proteins.

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20176951

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