E
Edith Magnenat
Researcher at Merck Serono
Publications - 13
Citations - 1511
Edith Magnenat is an academic researcher from Merck Serono. The author has contributed to research in topics: Peptide sequence & Enzyme. The author has an hindex of 11, co-authored 13 publications receiving 1480 citations.
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Journal ArticleDOI
The Platelet Collagen Receptor Glycoprotein VI Is a Member of the Immunoglobulin Superfamily Closely Related to FcαR and the Natural Killer Receptors
TL;DR: The ability of the cloned GPVI cDNA to code for a functional platelet collagen receptor was demonstrated in the megakaryocytic cell line Dami, and it inhibited collagen-induced platelet aggregation.
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Bcl-2 Undergoes Phosphorylation by c-Jun N-terminal Kinase/Stress-activated Protein Kinases in the Presence of the Constitutively Active GTP-binding Protein Rac1
Kinsey Maundrell,Bruno Antonsson,Edith Magnenat,Montserrat Camps,Marco Muda,Christian Chabert,Corine Gillieron,Ursula Boschert,Elizabeth Vial-Knecht,Jean-Claude Martinou,Steve Arkinstall +10 more
TL;DR: This is the first report of Bcl-2 phosphorylation by the JNK/SAPK class of MAP kinases and could indicate a key modification allowing control of B cl-2 function by cell surface receptors, Rho family GTPases, and/or cellular stresses.
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Phosphorylation of bid by casein kinases I and II regulates its cleavage by caspase 8.
Solange Desagher,Astrid Osen-Sand,Sylvie Montessuit,Edith Magnenat,Francis Vilbois,Alena Hochmann,Laurent Journot,Bruno Antonsson,Jean-Claude Martinou +8 more
TL;DR: Data indicate that phosphorylation of Bid represents a new mechanism whereby cells control apoptosis, and a mutant of Bid that cannot be phosphorylated was found to be more toxic than wild-type Bid.
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Aggretin, a Heterodimeric C-type Lectin from Calloselasma rhodostoma (Malayan Pit Viper), Stimulates Platelets by Binding to α2β1 Integrin and Glycoprotein Ib, Activating Syk and Phospholipase Cγ2, but Does Not Involve the Glycoprotein VI/Fc Receptor γ Chain Collagen Receptor
Alexei Navdaev,Jeannine M. Clemetson,János Polgár,Beate E. Kehrel,Martin Glauner,Edith Magnenat,Timothy N. C. Wells,Kenneth J. Clemetson +7 more
TL;DR: It is shown that binding to glycoprotein (GP) Ib is also required to activate platelet membrane glycoproteins, and supports an independent, GPIb- and integrin-based pathway for activation of p72SYK not involving the Fcγ receptor.
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Asp-49 is not an absolute prerequisite for the enzymic activity of low-M(r) phospholipases A2: purification, characterization and computer modelling of an enzymically active Ser-49 phospholipase A2, ecarpholin S, from the venom of Echis carinatus sochureki (saw-scaled viper).
TL;DR: Experimental evidence is provided that Asp-49 is not an absolute prerequisite for the enzymic activity of PLA2s, and that proteins with amino acid(s) other than Asp at position 49 can exhibit significant phospholipase activity.