S
Stefan W. Schneider
Researcher at University of Hamburg
Publications - 136
Citations - 7312
Stefan W. Schneider is an academic researcher from University of Hamburg. The author has contributed to research in topics: Von Willebrand factor & Endothelial stem cell. The author has an hindex of 38, co-authored 136 publications receiving 6342 citations. Previous affiliations of Stefan W. Schneider include Heidelberg University & Yale University.
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Journal ArticleDOI
Nanomedicine--challenge and perspectives.
Kristina Riehemann,Stefan W. Schneider,Thomas A. Luger,Biana Godin,Mauro Ferrari,Harald Fuchs +5 more
TL;DR: This Review gives an overview of selected recent developments and applications of nanomedicine.
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Shear-induced unfolding triggers adhesion of von Willebrand factor fibers.
Stefan W. Schneider,Stefan Nuschele,Achim Wixforth,Christian Gorzelanny,Alfredo Alexander-Katz,Roland R. Netz,Matthias F. Schneider +6 more
TL;DR: The results presented here help unravel how an increase in hydrodynamic shear stress activates VWF's adhesion potential, leading to the counterintuitive phenomena of enhanced adsorption rate under strong shear conditions.
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Neuronal Control of Skin Function: The Skin as a Neuroimmunoendocrine Organ
TL;DR: Together, a close multidirectional interaction between neuromediators, high-affinity receptors, and regulatory proteases is critically involved to maintain tissue integrity and regulate inflammatory responses in the skin.
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Surface dynamics in living acinar cells imaged by atomic force microscopy: identification of plasma membrane structures involved in exocytosis.
TL;DR: The atomic force microscope has enabled us to observe plasma membrane dynamics of the exocytic process in living cells in real time and suggest depressions to be the fusion pores identified earlier in mast cells by freeze-fracture electron microscopy and by electrophysiological measurements.
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Molecular weights of individual proteins correlate with molecular volumes measured by atomic force microscopy.
TL;DR: It is concluded that single (native and denatured) proteins can be imaged by AFM in three dimensions and identified by their specific molecular volumes.