Structure/Function analysis of p55 tumor necrosis factor receptor and fas-associated death domain. Effect on necrosis in L929sA cells.

@article{Boone2000StructureFunctionAO,
  title={Structure/Function analysis of p55 tumor necrosis factor receptor and fas-associated death domain. Effect on necrosis in L929sA cells.},
  author={Elke Boone and Tom Vanden Berghe and Geert van Loo and Gert De Wilde and N De Wael and Dominique Vercammen and Walter Fiers and Guy Haegeman and Peter Vandenabeele},
  journal={The Journal of biological chemistry},
  year={2000},
  volume={275 48},
  pages={37596-603}
}
Tumor necrosis factor (TNF) induces a typical apoptotic cell death program in various cell lines by interacting with the p55 tumor necrosis factor receptor (TNF-R55). In contrast, triggering of the fibrosarcoma cell line L929sA gives rise to characteristic cellular changes resulting in necrosis. The intracellular domain of TNF-R55 can be subdivided into two parts: a membrane-proximal domain (amino acids 202-325) and a C-terminal death domain (DD) (amino acids 326-413), which has been shown to… CONTINUE READING

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