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The Bcl2 family: regulators of the cellular life-or-death switch
Abstract
Tissue homeostasis is regulated by apoptosis, the cell-suicide programme that is executed by proteases called caspases. The Bcl2 family of intracellular proteins is the central regulator of caspase activation, and its opposing factions of anti- and pro-apoptotic members arbitrate the life-or-death decision. Apoptosis is often impaired in cancer and can limit conventional therapy. A better understanding of how the Bcl2 family controls caspase activation should result in new, more effective therapeutic approaches.
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“This family consists of anti-apoptotic and pro-apoptotic proteins that act synergistically as apoptotic switches, ultimately determining the cell’s fate.358–360”
From Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials (2023) · cites this paper as [359]
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Flagged first, then by citations
2 of the 155 references couldn’t be matched to a known paper.
Research works printed but not linked: 2
- Cory, S., Vaux, D. L., Strasser, A., Harris, A. W. & Adams, J. M. Insights from Bcl2 and Myc: malignancy involves abrogation of apoptosis as well as sustained proliferation. Cancer Res. 59, S1685–S1692 (1999).
- Lassus, P., Opitz-Araya, X. & Lazebnik, Y. Caspase-2 is required for stress-induced apoptosis and acts prior to mitochondrial permeabilization. Science (in the press).In certain cell lines, stress stimuli are shown to activate caspase-2 upstream of mitochondrial disruption. Together with other recent findings by Marsden et al . (see text), this work argues strongly that Bcl2 function extends beyond guarding mitochondrial integrity and is likely to involve direct regulation of the activation of several initiator caspases.
Cited by
Sorted by citations
Apoptosis: A Review of Programmed Cell Death
Elmore, S. (2007) · Toxicologic Pathology · doi:10.1080/01926230701320337 · Cited by 13,853
Mitochondrial membrane permeabilization in cell death
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miR-15 and miR-16 induce apoptosis by targeting BCL2
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Regulation of cell death: the calcium–apoptosis link
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Anticancer activities of histone deacetylase inhibitors
Bolden, J. E., Peart, M. J., & Johnstone, R. W. (2006) · Nature Reviews Drug Discovery · doi:10.1038/nrd2133 · Cited by 2,919
Metadata
- Authors
- Cory, S., & Adams, J. M.
- Affiliations
- The Royal Melbourne Hospital (AU)
- Venue
- Nature Reviews Cancer
- Published
- 2002-09-01
- Volume
- 2
- Issue
- 9
- Pages
- 647-656
- ISSN
- 1474-175X (ISSN-L)
- 1474-1768
- OpenAlex
- W2087877138
- Cited by
- 4,032
- References
- 155
- Citations by year
- 2026: 118 · 2025: 111 · 2024: 115 · 2023: 115 · 2022: 132 · 2021: 143 · 2020: 133 · 2019: 155 · 2018: 171 · 2017: 174 · 2016: 189 · 2015: 165 · 2014: 194 · 2013: 214 · 2012: 188
- FWCI
- 12.89
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Nature reviews. Cancer (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Leukemia and Lymphoma Society
- National Institutes of Health
- National Health and Medical Research Council
- National Medical Research Council
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Ubiquitin and proteasome pathways
- Keywords
- Bcl-2 family proteins, apoptosis, caspase activation, anti-apoptotic proteins, pro-apoptotic proteins, life-or-death decisions, cancer therapy, tissue homeostasis
- MeSH terms
- Animals, Humans, Models, Molecular, Neoplasms, Protein Conformation, Apoptosis, Proto-Oncogene Proteins c-bcl-2, Caspases
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