Publications by authors named "Sylvie Hertig"
Ligands of the tumor necrosis factor superfamily (TNFSF) (4-1BBL, APRIL, BAFF, CD27L, CD30L, CD40L, EDA1, EDA2, FasL, GITRL, LIGHT, lymphotoxin alpha, lymphotoxin alphabeta, OX40L, RANKL, TL1A, TNF, TWEAK, and TRAIL) bind members of the TNF receptor superfamily (TNFRSF). A comprehensive survey of ligand-receptor interactions was performed using a flow cytometry-based assay. All ligands engaged between one and five receptors, whereas most receptors only bound one to three ligands.
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- The study investigates how different forms of Fas ligand (FasL) induce apoptosis (programmed cell death), with membrane-bound FasL triggering the process while the soluble form does not unless cross-linked.
- Researchers engineered hexameric FasL proteins that showed increased cytotoxicity and successfully induced apoptosis by forming a signaling complex.
- The research uncovered three critical steps in Fas-mediated apoptosis—receptor binding, activation, and recruitment of signaling molecules—highlighting that FasL's oligomerization is essential for effective signaling.
Tumor necrosis factor (TNF) ligand and receptor superfamily members play critical roles in diverse developmental and pathological settings. In search for novel TNF superfamily members, we identified a murine chromosomal locus that contains three new TNF receptor-related genes. Sequence alignments suggest that the ligand binding regions of these murine TNF receptor homologues, mTNFRH1, -2 and -3, are most homologous to those of the tumor necrosis factor-related apoptosis-inducing ligand (TRAIL) receptors.
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