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- W31468489 abstract "Signaling through TNF receptors is probably paradigmatic of that which occurs through many of its homologs. The action of TNF is pleotropic in that it can initiate both apoptotic and proliferative pathways. The mechanisms of signal integration that commit the cell to one or the other fate have yet to be fully elucidated. Receptor-proximal events in both cases appear to be mediated through protein-interaction domains in receptors and cytosolic adaptor proteins. Crystallographic analysis of the TNF-Rl receptor and its complex with TNF-β suggests that ligands and their receptors assemble into complexes with two- and three-fold symmetry and that higher order lattice-like structures could be generated though the operation of this symmetry. TRAF proteins are homotrimeric, as are their complexes with TNF-R2 peptides and with TRADD, suggesting that the symmetry of extracellular components is recapitulated in the intracellular signaling complexes formed upon receptor ligation. On the other hand, death domains have not been found to assemble into homotypic complexes with three-fold symmetry. The organization of TNF signaling complexes is likely to be key to the mechanism of signal transduction and propagation. Thus, elucidation of the structures of TNF signaling complexes, however transient, will represent a significant achievement in our understanding of TNF signaling mechanisms." @default.
- W31468489 created "2016-06-24" @default.
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- W31468489 date "2003-01-01" @default.
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- W31468489 title "Structure and Function of Tumor Necrosis Factor at the Cell Surface" @default.
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- W31468489 doi "https://doi.org/10.1016/b978-012124546-7/50408-3" @default.
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