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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 (show PRKG1 Proteins)/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 (show FBLIM1 Proteins), beta-catenin (show CTNNB1 Proteins) and uPA (show PRAP1 Proteins) 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 (show ZYX Proteins) and TES (show TES Proteins) are tension-dependent members of focal adherens junctions independent of the alpha-catenin (show CTNNA1 Proteins)-vinculin (show VCL Proteins) 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 l (show HIF1A Proteins)ung adenocarcinoma cell permeability by repressing vasodilator-stimulated phosphoprotein (VASP) expression through the activation of hypoxia inducible factor 1 alpha subunit (HIF-1alpha).
VASP selectively mediate activated T-cell trafficking by promoting the diapedesis step of transendothelial migration in a alpha4 integrin-dependent manner.
We identified a phosphorylation-dependent mechanism that regulates selective recruitment of these effectors to Lamellipodin: Abl (show ABL1 Proteins)-mediated Lamellipodin phosphorylation promotes its association with both Scar/WAVE and Ena/VASP, whereas Src (show SRC Proteins)-dependent phosphorylation enhances binding to Scar/WAVE but not to Ena/VASP
Thus, unlike host proteins characterized in Shigella pathogenesis that promote bacterial spread, VASP and EVL function to limit it.
Data show that the hypoxia inducible factor 1 alpha subunit (HIF-1alpha (show HIF1A Proteins)) protein level in lung tissues increased significantly at four hours and eight hours, whereas the vasodilator-stimulated phosphoprotein (VASP) protein level decreased significantly.
Collectively, our studies highlighted that the CuB-induced actin aggregation and cofilin (show CFL1 Proteins)-actin rod formation was mediated via the Ga13/RhoA (show RHOA Proteins)/PKA/VASP pathway.
Ena/VASP regulates mDia2 (show DIAPH3 Proteins)-initiated filopodial morphology, dynamics, and function.
cancer cells reaching liver sinusoids induced up-regulation of VASP
Low VASP activation was associated with high fat diet (HFD). Effects of HFD on aortic inflammation and insulin (show INS Proteins) resistance were recapitulated by VASP knockout, implying a role for VASP to constrain inflammatory signaling and maintain insulin (show INS Proteins) sensitivity.
Mena/VASP and alphaII-Spectrin complexes regulate cytoplasmic actin networks in cardiomyocytes and protect from conduction abnormalities and dilated cardiomyopathy.
CDC42 activation inhibits this activity and promotes IRSp53-dependent recruitment and clustering of VASP to drive actin assembly.
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