The DOI matches its Crossref record; 23 of the 23 references it cites were found in a registry or an index.
Apoptosis‐inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis
Abstract
Apoptosis‐inducing factor (AIF) is encoded by one single gene located on the X chromosome. AIF is ubiquitously expressed, both in normal tissues and in a variety of cancer cell lines. The AIF precursor is synthesized in the cytosol and is imported into mitochondria. The mature AIF protein, a flavoprotein (prosthetic group: flavine adenine dinucleotide) with significant homology to plant ascorbate reductases and bacterial NADH oxidases, is normally confined to the mitochondrial intermembrane space. In a variety of different apoptosis‐inducing conditions, AIF translocates through the outer mitochondrial membrane to the cytosol and to the nucleus. Ectopic (extra‐mitochondrial) AIF induces nuclear chromatin condensation, as well as large scale (∼50 kb) DNA fragmentation. Thus, similar to cytochrome c, AIF is a phylogenetically old, bifunctional protein with an electron acceptor/donor (oxidoreductase) function and a second apoptogenic function. In contrast to cytochrome c, however, AIF acts in a caspase‐independent fashion. The molecular mechanisms via which AIF induces apoptosis are discussed.
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Cites
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Induction of Apoptotic Program in Cell-Free Extracts: Requirement for dATP and Cytochrome c
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Molecular characterization of mitochondrial apoptosis-inducing factor
Susin, S. A., Lorenzo, H. K., Zamzami, N., Marzo, I., Snow, B. E., Brothers, G. M., Mangion, J., Jacotot, E., Costantini, P., Loeffler, M., et al. (1999) · Nature · doi:10.1038/17135 · Cited by 4,060
Self-citationA caspase-activated DNase that degrades DNA during apoptosis, and its inhibitor ICAD
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Mitochondrial control of cell death
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Self-citationBiochemical Pathways of Caspase Activation During Apoptosis
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Mitochondrial control of nuclear apoptosis.
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Self-citationBcl-2 inhibits the mitochondrial release of an apoptogenic protease.
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Cited by
Parthanatos, a messenger of death
David, K. K. (2009) · Frontiers in Bioscience · doi:10.2741/3297 · Cited by 450
“This ubiquitously-expressed mitochondrial protein was isolated for its ability to induce nuclear fragmentation, and was shown to translocate from the mitochondria to the nucleus to induce chromatin condensation and DNA fragmentation (47).”
BackgroundMechanisms of AIF-Mediated Apoptotic DNA Degradation in Caenorhabditis elegans
Wang, X., Yang, C., Chai, J., Shi, Y., & Xue, D. (2002) · Science · doi:10.1126/science.1076194 · Cited by 393
Nitric oxide inhibition of mitochondrial respiration and its role in cell death
Brown, G. C., & Borutaite, V. (2002) · Free Radical Biology and Medicine · doi:10.1016/s0891-5849(02)01112-7 · Cited by 377
Mitochondrial death effectors: Relevance to sarcopenia and disuse muscle atrophy
Marzetti, E., Hwang, J. C. Y., Lees, H. A., Wohlgemuth, S. E., Dupont-Versteegden, E. E., Carter, C. S., Bernabei, R., & Leeuwenburgh, C. (2010) · Biochimica et Biophysica Acta (BBA) - General Subjects · doi:10.1016/j.bbagen.2009.05.007 · Cited by 174
Marzetti, E., Lawler, J. M., Hiona, A., Manini, T., Seo, A. Y., & Leeuwenburgh, C. (2008) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2007.05.028 · Cited by 113
Metadata
- Authors
- Daugas, E., Nochy, D., Ravagnan, L., Loeffler, M., Susin, S. A., Zamzami, N., & Kroemer, G.
- Venue
- FEBS Letters
- Publisher
- Wiley
- Published
- 2000-07-03
- Volume
- 476
- Issue
- 3
- Pages
- 118-123
- ISSN
- 0014-5793 (ISSN-L)
- 1873-3468
- OpenAlex
- W2086144679
- Cited by
- 466
- References
- 23
- FWCI
- 13.29
- Type
- journal article
- Language
- en
- Open access
- closed
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- Daugas, E., Nochy, D., Ravagnan, L., Loeffler, M., Susin, S. A., Zamzami, N., & Kroemer, G. (2000). Apoptosis‐inducing factor (AIF): a ubiquitous mitochondrial oxidoreductase involved in apoptosis. FEBS Letters. https://doi.org/10.1016/s0014-5793(00)01731-2
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