E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates - Test2 - elhamkhani - TriplyDB

E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates

E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates

http://www.wikidata.org/entity/Q34119372

about

Bacteria-host relationship: ubiquitin ligases as weapons of invasion Cell biology of infection by Legionella pneumophila Bacterial Type IV secretion systems: versatile virulence machines The Legionella effector SidC defines a unique family of ubiquitin ligases important for bacterial phagosomal remodeling.The ubiquitin system: a critical regulator of innate immunity and pathogen-host interactions Modulation of the host innate immune and inflammatory response by translocated bacterial proteins Structural basis of substrate recognition by a bacterial deubiquitinase important for dynamics of phagosome ubiquitination Legionella metaeffector exploits host proteasome to temporally regulate cognate effector.The E Block motif is associated with Legionella pneumophila translocated substrates.Metabolism of the vacuolar pathogen Legionella and implications for virulence.Lipidation by the host prenyltransferase machinery facilitates membrane localization of Legionella pneumophila effector proteins.A novel BAT3 sequence generated by alternative RNA splicing of exon 11B displays cell type-specific expression and impacts on subcellular localization.Experimental evolution of Legionella pneumophila in mouse macrophages leads to strains with altered determinants of environmental survival.Massive expansion of Ubiquitination-related gene families within the Chlamydiae.Large-scale identification and translocation of type IV secretion substrates by Coxiella burnetii.Identification of two Legionella pneumophila effectors that manipulate host phospholipids biosynthesis Exploitation of evolutionarily conserved amoeba and mammalian processes by Legionella.The Coxiella burnetii cryptic plasmid is enriched in genes encoding type IV secretion system substrates.Protein kinase LegK2 is a type IV secretion system effector involved in endoplasmic reticulum recruitment and intracellular replication of Legionella pneumophila Exploitation of Host Polyubiquitination Machinery through Molecular Mimicry by Eukaryotic-Like Bacterial F-Box Effectors.Post-translational modifications are key players of the Legionella pneumophila infection strategy Secrets of a successful pathogen: legionella resistance to progression along the autophagic pathway.Alterations of host cell ubiquitination machinery by pathogenic bacteria.Minimization of the Legionella pneumophila genome reveals chromosomal regions involved in host range expansion.The transcriptome of Legionella pneumophila-infected human monocyte-derived macrophages.Endoplasmic Reticulum Tubule Protein Reticulon 4 Associates with the Legionella pneumophila Vacuole and with Translocated Substrate Ceg9.Molecular Characterization of LubX: Functional Divergence of the U-Box Fold by Legionella pneumophila.Orientia tsutsugamushi Strain Ikeda Ankyrin Repeat-Containing Proteins Recruit SCF1 Ubiquitin Ligase Machinery via Poxvirus-Like F-Box Motifs MavN is a Legionella pneumophila vacuole-associated protein required for efficient iron acquisition during intracellular growth.Host Cell-catalyzed S-Palmitoylation Mediates Golgi Targeting of the Legionella Ubiquitin Ligase GobX.Lysine11-Linked Polyubiquitination of the AnkB F-Box Effector of Legionella pneumophila.Implication of the VirD4 coupling protein of the Lvh type 4 secretion system in virulence phenotypes of Legionella pneumophila Iron Limitation Triggers Early Egress by the Intracellular Bacterial Pathogen Legionella pneumophila Chlamydia trachomatis-induced alterations in the host cell proteome are required for intracellular growth.A Legionella effector modulates host cytoskeletal structure by inhibiting actin polymerization Diversity of bacterial manipulation of the host ubiquitin pathways.Control of host cell phosphorylation by legionella pneumophila.Interactions of bacterial proteins with host eukaryotic ubiquitin pathways.Manipulation of host vesicular trafficking and innate immune defence by Legionella Dot/Icm effectors.Post-translational modifications of host proteins by Legionella pneumophila: a sophisticated survival strategy.

P2860

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P2860

E3 ubiquitin ligase activity and targeting of BAT3 by multiple Legionella pneumophila translocated substrates

http://www.wikidata.org/entity/Q34119372

description

2010 nî lūn-bûn

@nan

2010 թուականի Յունիսին հրատարակուած գիտական յօդուած

@hyw

2010 թվականի հունիսին հրատարակված գիտական հոդված

@hy

2010年の論文

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2010年論文

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2010年論文

@zh-hant

2010年論文

@zh-hk

2010年論文

@zh-mo

2010年論文

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2010年论文

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name

E3 ubiquitin ligase activity a ...... ophila translocated substrates

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E3 ubiquitin ligase activity a ...... ophila translocated substrates

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P2860

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Infection and Immunity

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E3 ubiquitin ligase activity a ...... ophila translocated substrates

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Alexander W Ensminger

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

Ralph R Isberg

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P2860

Molecular mimicry by an F-box effector of Legionella pneumophila hijacks a conserved polyubiquitination machinery within macrophages and protozoa

Identification of a family of human F-box proteins

The Genome of the Amoeba Symbiont "Candidatus Amoebophilus asiaticus" Reveals Common Mechanisms for Host Cell Interaction among Amoeba-Associated Bacteria

Evidence in the Legionella pneumophila genome for exploitation of host cell functions and high genome plasticity

Structure of the Cul1-Rbx1-Skp1-F boxSkp2 SCF ubiquitin ligase complex

HLA-B-associated transcript 3 (Bat3)/Scythe is essential for p300-mediated acetylation of p53

Legionella pneumophila inhibits macrophage apoptosis by targeting pro-death members of the Bcl2 protein family

Sequencing technologies - the next generation

A novel ubiquitination factor, E4, is involved in multiubiquitin chain assembly.

Functional interaction of 13 yeast SCF complexes with a set of yeast E2 enzymes in vitro.

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3905-3919

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scholarly article

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10.1128/IAI.00344-10

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9

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78

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2010-06-14T00:00:00Z

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20547746

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2937443

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