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Cited by 297

The DOI matches its Crossref record; 2 of the 2 references it cites were found in a registry or an index.

Activation of Fas by FasL induces apoptosis by a mechanism that cannot be blocked by Bcl-2 or Bcl-xL

Open access
Huang, David C. S., Hahne, Michael, Schroeter, Michael, Frei, Karl, Fontana, Adriano, Villunger, Andreas, Newton, Kim, Tschopp, Juerg, Strasser, Andreas·1999·Proceedings of the National Academy of Sciences

Abstract

Fas activation triggers apoptosis in many cell types. Studies with anti-Fas antibodies have produced conflicting results on Fas signaling, particularly the role of the Bcl-2 family in this process. Comparison between physiological ligand and anti-Fas antibodies revealed that only extensive Fas aggregation, by membrane bound FasL or aggregated soluble FasL consistently triggered apoptosis, whereas antibodies could act as death agonists or antagonists. Studies on Fas signaling in cell lines and primary cells from transgenic mice revealed that FADD/MORT1 and caspase-8 were required for apoptosis. In contrast, Bcl-2 or Bcl-x L did not block FasL-induced apoptosis in lymphocytes or hepatocytes, demonstrating that signaling for cell death induced by Fas and the pathways to apoptosis regulated by the Bcl-2 family are distinct.

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Crossref · 10.1073/pnas.96.26.14871

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Metadata

Authors
Huang, D. C. S., Hahne, M., Schroeter, M., Frei, K., Fontana, A., Villunger, A., Newton, K., Tschopp, J., & Strasser, A.
Venue
Proceedings of the National Academy of Sciences
Published
1999-12-21
Volume
96
Issue
26
Pages
14871-14876
ISSN
  • 0027-8424 (ISSN-L)
  • 1091-6490
OpenAlex
W1996174406
Cited by
297
References
2
FWCI
10.22
Type
journal article
Language
en
Open access
green

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