Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation. - Wikidata - wikimedia - TriplyDB

Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

http://www.wikidata.org/entity/Q30479422

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Small heat shock proteins in smooth muscle Bacterial Toxins as Pathogen Weapons Against Phagocytes Cytoskeleton as an emerging target of anthrax toxins Thymosin β10 expression driven by the human TERT promoter induces ovarian cancer-specific apoptosis through ROS production A Role for the Chaperone Complex BAG3-HSPB8 in Actin Dynamics, Spindle Orientation and Proper Chromosome Segregation during Mitosis HSPB1 facilitates the formation of non-centrosomal microtubules Lung epithelial injury by B. anthracis lethal toxin is caused by MKK-dependent loss of cytoskeletal integrity Bacillus anthracis edema toxin impairs neutrophil actin-based motility Bacillus anthracis' lethal toxin induces broad transcriptional responses in human peripheral monocytes Cell stress promotes the association of phosphorylated HspB1 with F-actin Distension of the uterus induces HspB1 expression in rat uterine smooth muscle Anthrax toxins inhibit neutrophil signaling pathways in brain endothelium and contribute to the pathogenesis of meningitis Sublethal doses of anthrax lethal toxin on the suppression of macrophage phagocytosis.Thiolutin inhibits endothelial cell adhesion by perturbing Hsp27 interactions with components of the actin and intermediate filament cytoskeleton.Anthrax lethal toxin disrupts the endothelial permeability barrier through blocking p38 signaling.Hsp27-actin interaction.Accelerating axonal growth promotes motor recovery after peripheral nerve injury in mice Anthrax lethal and edema toxins fail to directly impair human platelet function.IGF2BP1 promotes cell migration by regulating MK5 and PTEN signaling Development of an in vitro potency assay for anti-anthrax lethal toxin neutralizing antibodies Hepatic artery bridging lessens temporary ischemic injury to bile canaliculi.Norepinephrine increases blood pressure but not survival with anthrax lethal toxin in rats.Bacillus anthracis lethal toxin reduces human alveolar epithelial barrier function.Comprehensive characterization of heat shock protein 27 phosphorylation in human endothelial cells stimulated by the microbial dithiole thiolutin Anthrax edema toxin induces maturation of dendritic cells and enhances chemotaxis towards macrophage inflammatory protein 3beta.Large potentials of small heat shock proteins.Contribution of small heat shock proteins to muscle development and function.Plasma miR-185 is decreased in patients with esophageal squamous cell carcinoma and might suppress tumor migration and invasion by targeting RAGE.Global impact of Salmonella pathogenicity island 2-secreted effectors on the host phosphoproteome.IGF2BP1: a post-transcriptional "driver" of tumor cell migration.Multiple protein kinases determine the phosphorylated state of the small heat shock protein, HSP27, in SH-SY5Y neuroblastoma cells.Small heat shock proteins in cellular adhesion and migration: evidence from Plasmodium genetics Endothelium-targeted overexpression of heat shock protein 27 ameliorates blood-brain barrier disruption after ischemic brain injury.Non-canonical effects of anthrax toxins on haematopoiesis: implications for vaccine development.Mechanical signals activate p38 MAPK pathway-dependent reinforcement of actin via mechanosensitive HspB1.MK5: A novel regulator of cardiac fibroblast function?The Potential Functions of Small Heat Shock Proteins in the Uterine Musculature during Pregnancy.Fine-tuning of actin dynamics by the HSPB8-BAG3 chaperone complex facilitates cytokinesis and contributes to its impact on cell division.Phosphorylation status of heat shock protein 27 influences neurite growth in adult dorsal root ganglion sensory neurons in vitro.β-Arrestin scaffolds and signaling elements essential for the obestatin/GPR39 system that determine the myogenic program in human myoblast cells.

P2860

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P2860

Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

http://www.wikidata.org/entity/Q30479422

description

2007 nî lūn-bûn

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2007 թուականի Ապրիլին հրատարակուած գիտական յօդուած

@hyw

2007 թվականի ապրիլին հրատարակված գիտական հոդված

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2007年の論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年論文

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2007年论文

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name

Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

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Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

@en

type

label

Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

@ast

Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

@en

prefLabel

Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

@ast

Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

@en

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SJ.EMBOJ.7601687

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The EMBO Journal

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Anthrax lethal toxin paralyzes actin-based motility by blocking Hsp27 phosphorylation.

@en

P2093

Bruce G Gibson

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

Ellen A Bishai

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

Frederick S Southwick

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

Gurjit S Sidhu

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

Jacques Landry

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

Russell L During

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Wei Li

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P2860

The genome sequence of Bacillus anthracis Ames and comparison to closely related bacteria

Activation of the CDC42 effector N-WASP by the Shigella flexneri IcsA protein promotes actin nucleation by Arp2/3 complex and bacterial actin-based motility

Role of proteins of the Ena/VASP family in actin-based motility of Listeria monocytogenes

Essential role of the NH2-terminal WD/EPF motif in the phosphorylation-activated protective function of mammalian Hsp27

ERK and p38 MAPK-activated protein kinases: a family of protein kinases with diverse biological functions

Listeria monocytogenes moves rapidly through the host-cell cytoplasm by inducing directional actin assembly

Gain-of-function mutations conferring actin-severing activity to human macrophage cap G.

Chemotactic signaling pathways in neutrophils: from receptor to actin assembly.

Actin cytoskeleton and small heat shock proteins: how do they interact?

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2240-2250

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10.1038/SJ.EMBOJ.7601687

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9

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26

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6381666

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17446863

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phosphorylation

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1864983

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