The DOI matches its Crossref record; 94 of the 94 references it cites were found in a registry or an index.
Apoptosome Structure, Assembly, and Procaspase Activation
Open accessAbstract
Apaf-1 like molecules assemble into a ring-like platform known as the apoptosome. This cell death platform then activates procaspases in the intrinsic cell death pathway. In this review, crystal structures of Apaf-1 monomers and CED-4 dimers have been combined with apoptosome structures, to provide insights into the assembly of cell death platforms from humans, nematodes and flies. In humans, caspase recognition domains of procaspase-9 and Apaf-1 interact with each other to form a CARD-CARD disk, which interacts with the platform to create an asymmetric proteolysis machine. The disk tethers multiple pc-9 catalytic domains to the platform to raise their local concentration and this leads to zymogen activation. These advances have now set the stage for further studies of this critical activation process on the apoptosome.
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Metadata
- Authors
- Yuan, S., & Akey, C. W.
- Venue
- Structure
- Publisher
- Elsevier BV
- Published
- 2013-04
- Volume
- 21
- Issue
- 4
- Pages
- 501-515
- ISSN
- 0969-2126 (ISSN-L)
- OpenAlex
- W1984046437
- Cited by
- 281
- References
- 94
- FWCI
- 11.30
- Type
- journal article
- Language
- en
- Open access
- bronze
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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.
