Cross talk between paxillin and Rac is critical for mediation of barrier-protective effects by oxidized phospholipids.
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- Type
- article
- Published
- 2008-10-01
- Cited by
- 37
- References
- 57
- OpenAlex
- https://openalex.org/W18676874
- Semantic Scholar
- https://api.semanticscholar.org/CorpusID:37270497
Keywords
Variety (cybernetics), Criminology, Political science, Geography, Sociology
References
- Paxillin and focal adhesion signalling
- Oxidized Phospholipids Negatively Regulate Dendritic Cell Maturation Induced by TLRs and CD401
- Differential regulation of pulmonary endothelial monolayer integrity by varying degrees of cyclic stretch.
- Characterization of Tyrosine Phosphorylation of Paxillin in Vitro by Focal Adhesion Kinase (*)
- GEF-H1 is involved in agonist-induced human pulmonary endothelial barrier dysfunction.
- Oxidized lipids: The two faces of vascular inflammation
- PKCdelta regulates endothelial basal barrier function through modulation of RhoA GTPase activity.
- Structurally similar oxidized phospholipids differentially regulate endothelial binding of monocytes and neutrophils.
- Reactive oxygen species in mechanotransduction.
- Modulatory role of focal adhesion kinase in regulating human pulmonary arterial endothelial barrier function
- Paxillin: a focal adhesion-associated adaptor protein
- Tiam1 and βPIX mediate Rac‐dependent endothelial barrier protective response to oxidized phospholipids
- Adhesion assembly, disassembly and turnover in migrating cells – over and over and over again
- Polar head groups are important for barrier-protective effects of oxidized phospholipids on pulmonary endothelium.
- Influence of tidal volume on pulmonary NO release, tissue lipid peroxidation and surfactant phospholipids.
- Microtubule disassembly induces cytoskeletal remodeling and lung vascular barrier dysfunction: Role of Rho‐dependent mechanisms
- Focal adhesion kinase: in command and control of cell motility
- FAK–Src signalling through paxillin, ERK and MLCK regulates adhesion disassembly
- Nitrated lipids: a class of cell-signaling molecules.
- Inhibition of LPS- and CpG DNA-induced TNF-α response by oxidized phospholipids
Cited by
- Barrier Enhancing Signals in Pulmonary Edema
- Rac1 inactivation by lethal toxin from Clostridium sordellii modifies focal adhesions upstream of actin depolymerization
- Oxidized phospholipids protect against lung injury and endothelial barrier dysfunction caused by heat-inactivated Staphylococcus aureus.
- Afadin controls p120-catenin – ZO-1 interactions leading to endothelial barrier enhancement by oxidized phospholipids
- c-Abl mediated tyrosine phosphorylation of paxillin regulates LPS-induced endothelial dysfunction and lung injury.
- Activation of aortic endothelial cells by oxidized phospholipids: a phosphoproteomic analysis
- Endothelial barrier disruption and recovery is controlled by substrate stiffness
- Oxidized phosphatidylcholine formation and action in oligodendrocytes
- cAMP with other signaling cues converges on Rac1 to stabilize the endothelial barrier— a signaling pathway compromised in inflammation
- PAK1 AS A THERAPEUTIC TARGET
- Oxidized phospholipids in control of inflammation and endothelial barrier
- Association between adherens junctions and tight junctions via Rap1 promotes barrier protective effects of oxidized phospholipids.
- Atrial natriuretic peptide attenuates LPS-induced lung vascular leak: role of PAK1.
- Impaired integrin‐mediated adhesion contributes to reduced barrier properties in VASP‐deficient microvascular endothelium
- Sphingosine-1-phosphate modulation of basal permeability and acute inflammatory responses in rat venular microvessels.
- Rho/Ras-GTPase-dependent and -independent activity of clostridial glucosylating toxins.
- Identification of paxilin domains interacting with β-catenin
- Role of Rac 1 and cAMP in endothelial barrier stabilization and thrombin‐induced barrier breakdown
- Effective Treatment of Edema and Endothelial Barrier Dysfunction With Imatinib
- Blood Brothers: Hemodynamics and Cell–Matrix Interactions in Endothelial Function
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