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IAP proteins: blocking the road to death's door
Abstract
The 'inhibitor of apoptosis' (IAP) gene family, which was discovered less than a decade ago, encodes a group of structurally related proteins that, in addition to their ability to suppress apoptotic cell death, are involved in an increasing number of seemingly unrelated cellular functions. Here, we review the functional and structural properties of this fascinating group of proteins, and of several recently identified IAP-binding factors that regulate IAP function.
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“Cytosolic SMAC precipitates apoptosis by associating with members of the inhibitor of apoptosis (IAP) protein family, including X-linked inhibitor of apoptosis (XIAP) [162, 163, 181].”
From Molecular mechanisms of cell death: recommendations of the nomenclature committee on cell death 2018. (2018) · cites this paper as [181]
Citations
Cites
Apoptosis: A Basic Biological Phenomenon with Wideranging Implications in Tissue Kinetics
Kerr, J. F. R., Wyllie, A. H., & Currie, A. R. (1972) · British Journal of Cancer · doi:10.1038/bjc.1972.33 · Cited by 15,673
Apoptosis in the Pathogenesis and Treatment of Disease
Thompson, C. B. (1995) · Science · doi:10.1126/science.7878464 · Cited by 6,524
NF-κB AND REL PROTEINS: Evolutionarily Conserved Mediators of Immune Responses
Ghosh, S., May, M. J., & Kopp, E. B. (1998) · Annual Review of Immunology · doi:10.1146/annurev.immunol.16.1.225 · Cited by 5,182
Cleavage of BID by Caspase 8 Mediates the Mitochondrial Damage in the Fas Pathway of Apoptosis
Li, H., Zhu, H., Xu, C.-J., & Yuan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81590-1 · Cited by 4,445
Identification and characterization of a spinal muscular atrophy-determining gene
Lefebvre, S., Bürglen, L., Reboullet, S., Clermont, O., Burlet, P., Viollet, L., Bénichou, B., Cruaud, C., Millasseau, P., Zeviani, M., et al. (1995) · Cell · doi:10.1016/0092-8674(95)90460-3 · Cited by 3,995
Du, C., Fang, M., Li, Y., Li, L., & Wang, X. (2000) · Cell · doi:10.1016/s0092-8674(00)00008-8 · Cited by 3,513
A novel anti-apoptosis gene, survivin, expressed in cancer and lymphoma
Ambrosini, G., Adida, C., & Altieri, D. C. (1997) · Nature Medicine · doi:10.1038/nm0897-917 · Cited by 3,174
Zou, H., Henzel, W. J., Liu, X., Lutschg, A., & Wang, X. (1997) · Cell · doi:10.1016/s0092-8674(00)80501-2 · Cited by 3,145
Wang, C.-Y., Mayo, M., Korneluk, R., Goeddel, D., & Baldwin, A. (1998) · Science · doi:10.1126/science.281.5383.1680 · Cited by 2,950
Programmed Cell Death in Animal Development
Jacobson, M. D., Weil, M., & RAFF, M. C. (1997) · Cell · doi:10.1016/s0092-8674(00)81873-5 · Cited by 2,685
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Danial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
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Pakos‐Zebrucka, K., Koryga, I., Mnich, K., Ljujic, M., Samali, A., & Gorman, A. M. (2016) · The EMBO Reports · doi:10.15252/embr.201642195 · Cited by 2,659
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Riedl, S. J., & Shi, Y. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1496 · Cited by 1,933
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Mehlen, P., & Puisieux, A. (2006) · Nature reviews. Cancer · doi:10.1038/nrc1886 · Cited by 1,919
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Longley, D., & Johnston, P. (2005) · The Journal of Pathology · doi:10.1002/path.1706 · Cited by 1,726
Pistritto, G., Trisciuoglio, D., Ceci, C., Garufi, A., & D’Orazi, G. (2016) · Aging · doi:10.18632/aging.100934 · Cited by 1,710
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Varfolomeev, E., Blankenship, J. W., Wayson, S. M., Fedorova, A. V., Kayagaki, N., Garg, P., Zobel, K., Dynek, J. N., Elliott, L. O., Wallweber, H. J. A., et al. (2007) · Cell · doi:10.1016/j.cell.2007.10.030 · Cited by 1,218
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Bertrand, M. J. M., Milutinovic, S., Dickson, K. M., Ho, W. C., Boudreault, A., Durkin, J. P., Gillard, J. W., Jaquith, J. B., Morris, S. J., & Barker, P. A. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.05.014 · Cited by 1,134
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Saelens, X., Festjens, N., Walle, L. V., van Gurp, M., Loo, G., & Vandenabeele, P. (2004) · Oncogene · doi:10.1038/sj.onc.1207523 · Cited by 1,021
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Ola, M. S., Nawaz, M. I., & Ahsan, H. (2011) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-010-0709-x · Cited by 933
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Fuentes‐Prior, P., & Salvesen, G. S. (2004) · Biochemical Journal · doi:10.1042/bj20041142 · Cited by 907
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Eckelman, B. P., Salvesen, G. S., & Scott, F. L. (2006) · The EMBO Reports · doi:10.1038/sj.embor.7400795 · Cited by 813
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Mita, A. C., Mita, M. M., Nawrocki, S. T., & Giles, F. J. (2008) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-0746 · Cited by 760
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Tschopp, J., Martinon, F., & Burns, K. (2003) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1019 · Cited by 739
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Shiozaki, E. N., Chai, J., Rigotti, D. J., Riedl, S. J., Li, P., Srinivasula, S. M., Alnemri, E. S., Fairman, R., & Shi, Y. (2003) · Molecular Cell · doi:10.1016/s1097-2765(03)00054-6 · Cited by 731
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Schickel, R., Boyerinas, B. M., Sm, P., & Peter, M. E. (2008) · Oncogene · doi:10.1038/onc.2008.274 · Cited by 721
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Ghavami, S., Hashemi, M. M., Ande, S. R., Yeganeh, B., Xiao, W., Eshraghi, M., Bus, C., Kadkhoda, K., Wiecheć, E., Halayko, A. J., et al. (2009) · Journal of Medical Genetics · doi:10.1136/jmg.2009.066944 · Cited by 721
Molecular targets in cerebral ischemia for developing novel therapeutics
Mehta, S. L., Manhas, N., & Raghubir, R. (2007) · Brain Research Reviews · doi:10.1016/j.brainresrev.2006.11.003 · Cited by 716
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Rigaud, S., Fondanèche, M., Lambert, N., Pasquier, B., Mateo, V., Soulas-Sprauel, P., Galicier, L., Deist, F. L., Rieux‐Laucat, F., Revy, P., et al. (2006) · Nature · doi:10.1038/nature05257 · Cited by 703
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Apoptosis and Necrosis in the Liver: A Tale of Two Deaths?
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Lawen, A. (2003) · BioEssays · doi:10.1002/bies.10329 · Cited by 493
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Sharma, S. V., & Settleman, J. E. (2007) · Genes & Development · doi:10.1101/gad.1609907 · Cited by 451
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Chemosensitization and Radiosensitization of Tumors by Plant Polyphenols
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Cai, Q., Sun, H., Peng, Y., Lü, J., Nikolovska‐Coleska, Z., McEachern, D., Liu, L., Qiu, S., Yang, C., Miller, R. S., et al. (2011) · Journal of Medicinal Chemistry · doi:10.1021/jm101505d · Cited by 274
Metadata
- Authors
- Salvesen, G. S., & Duckett, C. S.
- Affiliations
- Sanford Burnham Prebys Medical Discovery Institute (US)
- University of Michigan (US)
- Corresponding author
- Duckett, Colin S.
- Venue
- Nature Reviews Molecular Cell Biology
- Published
- 2002-06
- Volume
- 3
- Issue
- 6
- Pages
- 401-410
- ISSN
- 1471-0072 (ISSN-L)
- 1471-0080
- OpenAlex
- W1492587973
- Semantic Scholar
- 37eaa4d6440b014eff358aeee58f3772e77e8934
- Cited by
- 1,756
- References
- 157
- Citations by year
- 2026: 12 · 2025: 8 · 2024: 20 · 2023: 25 · 2022: 26 · 2021: 32 · 2020: 46 · 2019: 48 · 2018: 42 · 2017: 43 · 2016: 43 · 2015: 59 · 2014: 63 · 2013: 90 · 2012: 81
- FWCI
- 9.92
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Molecular Cell Biology (publishedVersion)
- PubMed (publishedVersion)
- 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
- inhibitor of apoptosis proteins, apoptosis, cell death regulation, protein structure
- MeSH terms
- Animals, Binding Sites, Gene Expression Regulation, Humans, Proteins, Cysteine Proteinase Inhibitors, Apoptosis, Insect Proteins, Inhibitor of Apoptosis Proteins
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
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