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Ena/VASP function in retinal axons is required for terminal arborization but not pathway navigation.
VASP role in the actin filament elongation
Our results reveal a dual role of VASP in endothelial permeability. In addition to its well-documented function in barrier integrity, we show that S-nitrosylation of VASP contributes to the onset of endothelial permeability.
findings have uncovered a PKG/VASP signaling pathway in Vascular Smooth Muscle Cells as a key molecular mechanism underlying T3-induced vascular relaxation.
This study provides the first evidence of VASP manipulation by an intravacuolar bacterial pathogen
VASP silencing downregulated Migfilin, beta-catenin and uPA and impaired spheroid invasion.
VASP phosphorylation assay could be useful in studies aimed at investigating relations between clopidogrel active metabolite bioavailability and clinical events.
VASP, zyxin and TES are tension-dependent members of focal adherens junctions independent of the alpha-catenin-vinculin module.
Data show that the phosphorylation status of vasodilator-stimulated phosphoprotein (VASP) at serine S322 can be predictive for breast cancer progression to an aggressive phenotype.
The authors propose that Lpd delivers Ena/VASP proteins to growing barbed ends and increases their actin polymerase activity by tethering them to actin filaments.
Data show that tumor necrosis factor-alpha (TNF-alpha) increased A549 lung adenocarcinoma cell permeability by repressing vasodilator-stimulated phosphoprotein (VASP) expression through the activation of hypoxia inducible factor 1 alpha subunit (HIF-1alpha).
The authors demonstrate that vasodilator-stimulated phosphoprotein (VASP), which is critical for regulation of actin assembly, cell adhesion and motility, is a direct substrate of Yersinia pestis YpkA kinase activity.
Ena/VASP's ability to bind F-actin and profilin-complexed G-actin are important for its effect, whereas Ena/VASP tetramerization is not necessary.
In clinical practice,LCR and CYP2C19 gene polymorphism should be assessed in NCIS patients receiving clopidogrel treatment.
VASP phosphorylation at Ser(157) mediates its localization at the membrane, but that VASP Ser(157) phosphorylation and membrane localization are not sufficient to activate its actin catalytic activity
PKA regulates VASP phosphorylation in Ras-transformed cells in a non-cell-autonomous manner.
Serine phosphorylation of vasodilator-stimulated phosphoprotein (VASP) regulates colon cancer cell survival and apoptosis.
VASP reconstitution of actin-based motility depends on the recruitment of F-actin seeds from the solution produced by cofilin
low serum concentration of vaspin is a risk factor for the progression of T2DM
palladin functions as a dynamic scaffolding protein that promotes the assembly of dorsal stress fibers by recruiting VASP to these structures.
Overexpression of VASP in endothelial cells blocked inflammation and insulin resistance induced by palmitate.
Vasodilator-stimulated phosphoprotein (VASP) is a member of the Ena-VASP protein family. Ena-VASP family members contain an EHV1 N-terminal domain that binds proteins containing E/DFPPPPXD/E motifs and targets Ena-VASP proteins to focal adhesions. In the mid-region of the protein, family members have a proline-rich domain that binds SH3 and WW domain-containing proteins. Their C-terminal EVH2 domain mediates tetramerization and binds both G and F actin. VASP is associated with filamentous actin formation and likely plays a widespread role in cell adhesion and motility. VASP may also be involved in the intracellular signaling pathways that regulate integrin-extracellular matrix interactions. VASP is regulated by the cyclic nucleotide-dependent kinases PKA and PKG.
, Vasodilator-stimulated phosphoprotein