The DOI matches its Crossref record; 30 of the 30 references it cites were found in a registry or an index.
Caspase-9, Bcl-XL, and Apaf-1 Form a Ternary Complex
Open accessAbstract
Genetic analysis of apoptosis in the nematode Caenorhabditis elegans has revealed the cell death machine to be composed of three core interacting components. CED-4 (equivalent to mammalian Apaf-1) is a nucleotide binding molecule that complexes with the zymogen form of the death protease CED-3, leading to its autoactivation and cell death. CED-9 blocks death by complexing with CED-4 and attenuating its ability to promote CED-3 activation. An equivalent ternary complex was found to be present in mammalian cells involving Apaf-1, the mammalian death protease caspase-9, and Bcl-XL, an anti-apoptotic member of the Bcl-2 family. Consistent with a central role for caspase-9, a dominant negative form effectively inhibited cell death initiated by a wide variety of inducers.
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Cited by
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Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis
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Metadata
- Authors
- Pan, G., O'Rourke, K., & Dixit, V. M.
- Venue
- Journal of Biological Chemistry
- Publisher
- Elsevier BV
- Published
- 1998-03
- Volume
- 273
- Issue
- 10
- Pages
- 5841-5845
- ISSN
- 0021-9258 (ISSN-L)
- OpenAlex
- W2043651078
- Cited by
- 521
- References
- 30
- FWCI
- 33.20
- Type
- journal article
- Language
- en
- Open access
- hybrid
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- Pan, G., O'Rourke, K., & Dixit, V. M. (1998). Caspase-9, Bcl-XL, and Apaf-1 Form a Ternary Complex. Journal of Biological Chemistry. https://doi.org/10.1074/jbc.273.10.5841
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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.
Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.
