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cAMP- and cGMP-dependent protein kinase phosphorylation sites of the focal adhesion vasodilator-stimulated phosphoprotein (VASP) in vitro and in intact human platelets.
- E. Butt, K. Abel, +4 authors U. Walter
- Biology, Medicine
- The Journal of biological chemistry
- 20 May 1994
Experiments with 32P-labeled platelets provided evidence that VASP is phosphorylated at the same three identified sites also in intact cells and that selective activation of cAK or cGK primarily increased the phosphorylation of both serine 2 and serine 1 but not threonine. Expand
The first comprehensive and quantitative analysis of human platelet protein composition allows the comparative analysis of structural and functional pathways.
The proteome of platelets highly purified from fresh blood donations is examined, using elaborate protocols to ensure negligible contamination by leukocytes, erythrocytes, and plasma, and indicates the feasibility of differential and comprehensive proteome analyses from small blood donations. Expand
The proline‐rich focal adhesion and microfilament protein VASP is a ligand for profilins.
The data support the hypothesis that profilin and VASP act in concert to convey signal transduction to actin filament formation and suggest that both proteins also interact within living cells. Expand
A novel proline‐rich motif present in ActA of Listeria monocytogenes and cytoskeletal proteins is the ligand for the EVH1 domain, a protein module present in the Ena/VASP family
It is demonstrated that ActA–EVH1 binding is a paradigm for a novel class of eukaryotic protein–protein interactions involving a proline‐rich ligand that is clearly different from those described for SH3 and WW/WWP domains. Expand
The EVH2 Domain of the Vasodilator-stimulated Phosphoprotein Mediates Tetramerization, F-actin Binding, and Actin Bundle Formation*
- C. Bachmann, L. Fischer, U. Walter, M. Reinhard
- Medicine, Biology
- The Journal of Biological Chemistry
- 13 August 1999
Analysis of the functional contribution of highly conserved blocks within this region indicated that residues 259–276 of human VASP are essential for the interaction with F-actin, whereas residues 343–380 are required for tetramerization, probably via coiled-coil formation. Expand
The nitric oxide and cGMP signal transduction system: regulation and mechanism of action.
Effects of Angiotensin II Infusion on the Expression and Function of NAD(P)H Oxidase and Components of Nitric Oxide/cGMP Signaling
It is concluded that angiotensin II-induced increases in the activity and the expression of NAD(P)H oxidase are at least in part PKC-dependent and may trigger NOS III uncoupling, leading to impaired NO/cGMP signaling and to endothelial dysfunction in this animal model. Expand
Taming platelets with cyclic nucleotides.
Due to their multiple sites of action and strong inhibitory potencies, cyclic nucleotides and their regulatory pathways are of particular interest for developing new approaches for the treatment of thrombotic and cardiovascular disorders. Expand
A focal adhesion factor directly linking intracellularly motile Listeria monocytogenes and Listeria ivanovii to the actin‐based cytoskeleton of mammalian cells.
Following Listeria infection the host vasodilator‐stimulated phosphoprotein (VASP), a microfilament‐ and focal adhesion‐associated substrate of both the cAMP‐ and cGMP‐dependent protein kinases, accumulates on the surface of intracytoplasmic bacteria prior to the detection of F‐actin ‘clouds’. Expand
Resistance to thienopyridines: Clinical detection of coronary stent thrombosis by monitoring of vasodilator‐stimulated phosphoprotein phosphorylation
- P. Barragan, J. Bouvier, +7 authors M. Eigenthaler
- Catheterization and cardiovascular interventions…
- 1 July 2003
A prospective evaluation of a new vasodilator‐stimulated phosphoprotein (VASP) phosphorylation assay in order to detect patients with high‐risk coronary subacute stent thrombosis despite thienopyridine regimen found it may be useful for the detection of coronary SAT. Expand