U
Ulrich Walter
Researcher at Technische Universität München
Publications - 166
Citations - 4686
Ulrich Walter is an academic researcher from Technische Universität München. The author has contributed to research in topics: Platelet activation & Platelet. The author has an hindex of 36, co-authored 164 publications receiving 4279 citations. Previous affiliations of Ulrich Walter include IBM & Argonne National Laboratory.
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Journal ArticleDOI
Flow Cytometry Analysis of Intracellular VASP Phosphorylation for the Assessment of Activating and Inhibitory Signal Transduction Pathways in Human Platelets Definition and Detection of Ticlopidine/Clopidogrel Effects
TL;DR: A novel flow cytometry-based method using aosphorylation-specific antibody was developed for fast and easy quantification of the phosphorylation state of a specific intracellular platelet protein.
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Stoichiometric and reversible phosphorylation of a 46-kDa protein in human platelets in response to cGMP- and cAMP-elevating vasodilators.
TL;DR: The hypothesis that VASP phosphorylation is an important component of the intracellular mechanism of action of these vasodilator-stimulated phosphoprotein in human platelets is supported.
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Concentration and regulation of cyclic nucleotides, cyclic-nucleotide-dependent protein kinases and one of their major substrates in human platelets Estimating the rate of CAMP-regulated and cGMP-regulated protein phosphorylation in intact cells
TL;DR: The results suggest for human platelets that relatively small increase in cAMP levels are required for activation of most of PKA, whereas even several-fold increases in platelet cGMP levels are capable of stimulating only a small fraction of total PKG.
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Calcium-dependent membrane association sensitizes soluble guanylyl cyclase to nitric oxide.
Ulrike Zabel,Christoph Kleinschnitz,Phil Oh,Pavel I Nedvetsky,Albert Smolenski,Helmut Müller,Petra Kronich,Peter Kugler,Ulrich Walter,Jan E. Schnitzer,Harald H.H.W. Schmidt +10 more
TL;DR: The data suggest that the entire NO signalling pathway is more spatially confined than previously assumed and that sGC dynamically translocates to the plasma membrane, where it is sensitized to NO.
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Functional analysis of cGMP-dependent protein kinases I and II as mediators of NO/cGMP effects.
Albert Smolenski,A. Mick Burkhardt,Martin Eigenthaler,Elke Butt,Stepan Gambaryan,Suzanne M. Lohmann,Ulrich Walter +6 more
TL;DR: The analysis of vasodilator-stimulated phosphoprotein (VASP) phosphorylation by polyclonal antibodies and newly developed monoclonal antibodies allows the quantitative measurement of cGK activity in intact cells.