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Ellen Van Obberghen-Schilling

Researcher at French Institute of Health and Medical Research

Publications -  50
Citations -  2822

Ellen Van Obberghen-Schilling is an academic researcher from French Institute of Health and Medical Research. The author has contributed to research in topics: Signal transduction & Extracellular matrix. The author has an hindex of 27, co-authored 50 publications receiving 2534 citations. Previous affiliations of Ellen Van Obberghen-Schilling include Centre national de la recherche scientifique & University of Nice Sophia Antipolis.

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cDNA cloning and expression of a hamster α‐thrombin receptor coupled to Ca2+ mobilization

TL;DR: To clone a thrombin receptor cDNA, selective amplification of mRNA sequences displaying homology to the transmembrane domains of G‐protein‐coupled receptor genes was performed by polymerase chain reaction.
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Regulation of the Actin Cytoskeleton by Thrombin in Human Endothelial Cells: Role of Rho Proteins in Endothelial Barrier Function

TL;DR: In this article, the authors examined the signal transduction pathways underlying agonist-stimulated reorganization of the actin cytoskeleton in human umbilical vein endothelial cells and found that Rho is involved in the maintenance of endothelial barrier function and Rac participates in cytoskeletal remodeling by thrombin.
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The p42/p44 MAP kinase pathway prevents apoptosis induced by anchorage and serum removal.

TL;DR: The ability of p42/p44 mitogen-activated protein kinase to generate survival signals that counteract cell death induced by loss of matrix contact, cytoskeletal integrity, and extracellular mitogenic factors is highlighted.
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Distinct signals via Rho GTPases and Src drive shape changes by thrombin and sphingosine-1-phosphate in endothelial cells.

TL;DR: The thrombin-induced contractile and immobile phenotype in endothelial cells reflects both robust RhoA activation and Rac inhibition, whereas Src- and Rac-dependent events couple sphingosine-1-phosphate receptors to the actin polymerizing machinery that drives the extension of lamellipodia and cell migration.