The DOI matches its Crossref record; 15 of the 15 references it cites were found in a registry or an index.
Mitochondria in Apoptosis: Bcl-2 Family Members and Mitochondrial Dynamics
Open accessAbstract
Mitochondria participate in apoptosis through a range of mechanisms that vary between vertebrates and invertebrates. In vertebrates, they release intermembrane space proteins, such as cytochrome c, to promote caspase activation in the cytosol. This process is the result of the loss of integrity of the outer mitochondrial membrane caused by proapoptotic members of the Bcl-2 family. This event is always accompanied by a fissioning of the organelle. Fission of mitochondria has also been reported to participate in apoptosis in Drosophila and Caenorhabditis elegans. However, in these organisms, mitochondrial membrane permeabilization does not occur and the mechanism by which mitochondrial dynamics participates in cell death remains elusive.
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Citations
Cites
Mitochondrial membrane permeabilization in cell death
Kroemer, G., Galluzzi, L., & Brenner, C. (2007) · Physiological Reviews · doi:10.1152/physrev.00013.2006 · Cited by 3,598
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Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
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“Other triggers, including BH3-only proteins, prostaglandins (Lalier et al., 2011), p53 (Chipuk et al., 2004), pH variations (Khaled et al., 1999), or posttranslational modifications (Kutuk and Letai, 2008), all could also be responsible for sending Bax to the OMM.”
BackgroundMitochondrial fusion and fission in cell life and death
Westermann, B. (2010) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3013 · Cited by 2,002 · cited 1×
“The core components of the fusion and fission machineries have been identified as the dynamin-related proteins Drp1, mitofusins (Mfn) 1 and 2, and Opa1 (Box 1) (reviewed in Westermann, 2010).”
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Self-citationThe biosynthesis and functional role of cardiolipin
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The Machines that Divide and Fuse Mitochondria
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Cited by
Activation of apoptosis signalling pathways by reactive oxygen species
Redza-Dutordoir, M., & Averill-Bates, D. A. (2016) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2016.09.012 · Cited by 3,731
Mitochondria: In Sickness and in Health
Nunnari, J., & Suomalainen, A. (2012) · Cell · doi:10.1016/j.cell.2012.02.035 · Cited by 3,479
Control of apoptosis by the BCL-2 protein family: implications for physiology and therapy
Czabotar, P. E., Lessene, G., Strasser, A., & Adams, J. M. (2014) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm3722 · Cited by 3,219
Programmed Cell Death in Animal Development and Disease
Fuchs, Y., & Steller, H. (2011) · Cell · doi:10.1016/j.cell.2011.10.033 · Cited by 1,915
Vyas, S., Zaganjor, E., & Haigis, M. C. (2016) · Cell · doi:10.1016/j.cell.2016.07.002 · Cited by 1,735
Metadata
- Authors
- Martinou, J.-C., & Youle, R. J.
- Venue
- Developmental Cell
- Publisher
- Elsevier BV
- Published
- 2011-07
- Volume
- 21
- Issue
- 1
- Pages
- 92-101
- ISSN
- 1534-5807 (ISSN-L)
- OpenAlex
- W1980100638
- Cited by
- 1,368
- References
- 15
- FWCI
- 40.79
- Type
- journal article
- Language
- en
- Open access
- bronze
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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