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Institution

University of Münster

EducationMünster, Germany
About: University of Münster is a education organization based out in Münster, Germany. It is known for research contribution in the topics: Population & Transplantation. The organization has 35609 authors who have published 69059 publications receiving 2278534 citations. The organization is also known as: University of Munster & University of Muenster.


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Journal ArticleDOI
05 Dec 2014-Science
TL;DR: Results reveal that recruited neutrophils scan for activated platelets, and they suggest that the neutrophil’ bipolarity allows the integration of signals present at both the endothelium and the circulation before inflammation proceeds, which alleviated collateral inflammatory damage to tissues in several injury models in mice.
Abstract: Immune and inflammatory responses require leukocytes to migrate within and through the vasculature, a process that is facilitated by their capacity to switch to a polarized morphology with an asymmetric distribution of receptors. We report that neutrophil polarization within activated venules served to organize a protruding domain that engaged activated platelets present in the bloodstream. The selectin ligand PSGL-1 transduced signals emanating from these interactions, resulting in the redistribution of receptors that drive neutrophil migration. Consequently, neutrophils unable to polarize or to transduce signals through PSGL-1 displayed aberrant crawling, and blockade of this domain protected mice against thromboinflammatory injury. These results reveal that recruited neutrophils scan for activated platelets, and they suggest that the neutrophils' bipolarity allows the integration of signals present at both the endothelium and the circulation before inflammation proceeds.

506 citations

Journal ArticleDOI
TL;DR: In this article, a single-column separation procedure for purification of Hf and Lu by ion exchange using Eichrom® Ln-Spec resin was presented, allowing measurements of Zr/Nb with a precision of better than ±5% (2σ).
Abstract: [1] The application of multiple collector inductively coupled plasma source mass spectrometry (MC-ICPMS) to 176Lu-176Hf and 92Nb-92Zr chronometry has been hampered by complex Zr-Hf purification procedures that involve multiple ion exchange column steps. This study presents a single-column separation procedure for purification of Hf and Lu by ion exchange using Eichrom® Ln-Spec resin. The sample is loaded in pure HCl, and element yields are not dependent on the sample matrix. For 92Nb-92Zr chronometry, a one-column procedure for purification of Zr using Biorad® AG-1-× 8 resin is described. Titanium and Mo are completely removed from the Zr, thus enabling accurate 92Zr measurements. Zirconium and Nb are quantitatively separated from rock samples using Eichrom Ln-Spec resin, allowing measurements of Zr/Nb with a precision of better than ±5% (2σ). The Ln-Spec and anion resin procedures may be combined into a three-column method for separation of Zr-Nb, Hf, Ta, and Lu from rock samples. For the first time, this procedure permits combined isotope dilution measurements of Nb/Ta, Zr/Hf, and Lu/Hf using a mixed 94Zr-176Lu-180Hf-180Ta tracer. Analytical protocols for Zr and Hf isotope measurements using the Micromass Isoprobe, a second generation, single-focusing MC-ICPMS, are reported. Using the Isoprobe at Munster, 2σ external precisions of ±0.5ɛ units for Hf and Zr isotope measurements are achieved using as little as 5 ng (Hf) to 10 ng (Zr) of the element. The 176Hf/177Hf and Lu/Hf for rock reference materials agree well with other published MC-ICPMS and thermal ionization mass spectrometry (TIMS) data.

505 citations

Journal ArticleDOI
TL;DR: The dynamics of angiogenesis is reviewed in the context of key molecules and pathways controlling tip cell selection, sprouting and the formation of new vessels.

505 citations

Journal ArticleDOI
M. G. Aartsen1, K. Abraham2, Markus Ackermann, Jenni Adams3  +313 moreInstitutions (49)
TL;DR: In this paper, an isotropic, unbroken power-law flux with a normalization at 100 TeV neutrino energy of (0.90 -0.27 +0.30) × 10-18 Gev-1 cm-2 s-1 sr-1 and a hard spectral index of γ = 2.13 ± 0.13.
Abstract: The IceCube Collaboration has previously discovered a high-energy astrophysical neutrino flux using neutrino events with interaction vertices contained within the instrumented volume of the IceCube detector. We present a complementary measurement using charged current muon neutrino events where the interaction vertex can be outside this volume. As a consequence of the large muon range the effective area is significantly larger but the field of view is restricted to the Northern Hemisphere. IceCube data from 2009 through 2015 have been analyzed using a likelihood approach based on the reconstructed muon energy and zenith angle. At the highest neutrino energies between 194 TeV and 7.8 PeV a significant astrophysical contribution is observed, excluding a purely atmospheric origin of these events at 5.6s significance. The data are well described by an isotropic, unbroken power-law flux with a normalization at 100 TeV neutrino energy of (0.90 -0.27 +0.30) × 10-18 Gev-1 cm-2 s-1 sr-1and a hard spectral index of γ = 2.13 ± 0.13. The observed spectrum is harder in comparison to previous IceCube analyses with lower energy thresholds which may indicate a break in the astrophysical neutrino spectrum of unknown origin. The highest-energy event observed has a reconstructed muon energy of (4.5 ± 1.2) PeV which implies a probability of less than 0.005% for this event to be of atmospheric origin. Analyzing the arrival directions of all events with reconstructed muon energies above 200 TeV no correlation with known γ-ray sources was found. Using the high statistics of atmospheric neutrinos we report the current best constraints on a prompt atmospheric muon neutrino flux originating from charmed meson decays which is below 1.06 in units of the flux normalization of the model in Enberg et al.

503 citations

Journal ArticleDOI
TL;DR: The activation of a new subfamily of G protein-coupled receptors, termed proteinase-activated receptors (PARs), necessitates a paradigm shift in thinking about hormone action, to include proteinases as key modulators of biological function.
Abstract: Serine proteinases such as thrombin, mast cell tryptase, trypsin, or cathepsin G, for example, are highly active mediators with diverse biological activities. So far, proteinases have been considered to act primarily as degradative enzymes in the extracellular space. However, their biological actions in tissues and cells suggest important roles as a part of the body’s hormonal communication system during inflammation and immune response. These effects can be attributed to the activation of a new subfamily of G protein-coupled receptors, termed proteinase-activated receptors (PARs). Four members of the PAR family have been cloned so far. Thus, certain proteinases act as signaling molecules that specifically regulate cells by activating PARs. After stimulation, PARs couple to various G proteins and activate signal transduction pathways resulting in the rapid transcription of genes that are involved in inflammation. For example, PARs are widely expressed by cells involved in immune responses and inflammation...

503 citations


Authors

Showing all 36075 results

NameH-indexPapersCitations
Hyun-Chul Kim1764076183227
Klaus Müllen1642125140748
Giacomo Bruno1581687124368
Anders M. Dale156823133891
Holger J. Schünemann141810113169
Joachim Heinrich136130976887
Markus Merschmeyer132118884975
Klaus Ley12949557964
Robert W. Mahley12836360774
Robert J. Kurman12739760277
Bart Barlogie12677957803
Thomas Schwarz12370154560
Carlos Caldas12254773840
Klaus Weber12152460346
Andrey L. Rogach11757646820
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Performance
Metrics
No. of papers from the Institution in previous years
YearPapers
2023253
2022831
20213,683
20203,499
20193,236
20182,918