The DOI matches its Crossref record; 93 of the 93 references it cites were found in a registry or an index.
Bcl-2 family proteins and mitochondria
Open accessAbstract
The Bcl-2 family of proteins plays a pivotal role in regulating cell life and death. Many of these proteins reside in the outer mitochondrial membrane, oriented towards the cytosol. Cytoprotective Bcl-2 family proteins such as Bcl-2 and Bcl-XL prevent mitochondrial permeability transition pore opening and release of apoptogenic proteins from mitochondria under many circumstances that would otherwise result in either apoptosis or necrosis. In contrast, some pro-apoptotic members of this family such as Bax can induce these destructive changes in mitochondria in both mammalian cells and when expressed exogenously in yeast. The mechanisms by which Bcl-2 family proteins control cell life and death remain elusive, but may include both the ability to form ion channels or pores in membranes and physical interactions with a variety of proteins implicated in apoptosis regulation.
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Cites
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Bcl-2 heterodimerizes in vivo with a conserved homolog, Bax, that accelerates programed cell death
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Prevention of Apoptosis by Bcl-2: Release of Cytochrome c from Mitochondria Blocked
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The Release of Cytochrome c from Mitochondria: A Primary Site for Bcl-2 Regulation of Apoptosis
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Bcl-2 is an inner mitochondrial membrane protein that blocks programmed cell death
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bcl-x, a bcl-2-related gene that functions as a dominant regulator of apoptotic cell death
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Self-citationCaspases: Intracellular Signaling by Proteolysis
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Cited by
Mitochondrial Transport of Cations: Channels, Exchangers, and Permeability Transition
Bernardi, P. (1999) · Physiological Reviews · doi:10.1152/physrev.1999.79.4.1127 · Cited by 1,535
Apoptosis and Molecular Targeting Therapy in Cancer
Hassan, M., Watari, H., AbuAlmaaty, A., Ohba, Y., & Sakuragi, N. (2014) · BioMed Research International · doi:10.1155/2014/150845 · Cited by 1,121
RetractedMitochondrial dysfunction and oxidative stress in aging and cancer
Kudryavtseva, A. V., Krasnov, G. S., Dmitriev, A. A., Alekseev, B. Y., Kardymon, O. L., Sadritdinova, A. F., Fedorova, M. S., Pokrovsky, A. V., Melnikova, N. V., Kaprin, A. D., et al. (2016) · Oncotarget · doi:10.18632/oncotarget.9821 · Cited by 543
Apoptosis as a Novel Target for Cancer Chemoprevention
Sun, S.-Y., Hail, N., & Lotan, R. (2004) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/djh123 · Cited by 502
Programmed Cell Death in Cerebral Ischemia
Graham, S. H., & Chen, J. (2001) · Journal of Cerebral Blood Flow & Metabolism · doi:10.1097/00004647-200102000-00001 · Cited by 472
Metadata
- Authors
- Reed, J., Jurgensmeier, J., & Matsuyama, S.
- Venue
- Biochimica et Biophysica Acta (BBA) - Bioenergetics
- Publisher
- Elsevier BV
- Published
- 1998-08
- Volume
- 1366
- Issue
- 1-2
- Pages
- 127-137
- ISSN
- 0005-2728 (ISSN-L)
- OpenAlex
- W1988355439
- Cited by
- 379
- References
- 93
- FWCI
- 10.36
- Type
- journal article
- Language
- en
- Open access
- bronze
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- Reed, J., Jurgensmeier, J., & Matsuyama, S. (1998). Bcl-2 family proteins and mitochondria. Biochimica et Biophysica Acta (BBA) - Bioenergetics. https://doi.org/10.1016/s0005-2728(98)00108-x
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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.
