The DOI matches its Crossref record; 5 of the 5 references it cites were found in a registry or an index.
p53 Has a Direct Apoptogenic Role at the Mitochondria
Open accessOverview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
Cites
p53 is required for radiation-induced apoptosis in mouse thymocytes
Lowe, S. W., Schmitt, E. M., Smith, S. W., Osborne, B. A., & Jacks, T. (1993) · Nature · doi:10.1038/362847a0 · Cited by 2,864
Crystal Structure of a p53 Tumor Suppressor-DNA Complex: Understanding Tumorigenic Mutations
Cho, Y., Gorina, S., Jeffrey, P. D., & Pavletich, N. P. (1994) · Science · doi:10.1126/science.8023157 · Cited by 2,551 · cited 1×
“Lp53(1–305), Lp53(1–220), and Lp53(80–393) were able to bind to drophobic core of the sandwich (Cho et al., 1994).”
BackgroundNoxa, a BH3-Only Member of the Bcl-2 Family and Candidate Mediator of p53-Induced Apoptosis
Oda, E., Ohki, R., Murasawa, H., Nemoto, J., Shibue, T., Yamashita, T., Tokino, T., Taniguchi, T., & Tanaka, †. N. (2000) · Science · doi:10.1126/science.288.5468.1053 · Cited by 2,112
Mechanisms of p53-dependent apoptosis
Schuler, M., & Green, D. R. (2001) · Biochemical Society Transactions · doi:10.1042/bst0290684 · Cited by 641 · cited 2×
“Here, cytosolic p53 can induce mitochondrial cytochrome c we provide evidence that p53 translocation to the mirelease (Schuler and Green, 2001).”
BackgroundA polymorphic microsatellite that mediates induction of PIG3 by p53
Contente, A., Dittmer, A., Koch, M. C., Roth, J., & Dobbelstein, M. (2002) · Nature Genetics · doi:10.1038/ng836 · Cited by 274
Cited by
Galluzzi, L., Vitale, I., Aaronson, S. A., Abrams, J. M., Adam, D., Agostinis, P., Alnemri, E. S., Altucci, L., Amelio, I., Andrews, D. W., et al. (2018) · Cell Death & Differentiation · doi:10.1038/s41418-017-0012-4 · Cited by 6,680
Self-citationDanial, N. N., & Korsmeyer, S. J. (2004) · Cell · doi:10.1016/s0092-8674(04)00046-7 · Cited by 4,651
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
Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy
Fulda, S., & Debatin, K.-M. (2006) · Oncogene · doi:10.1038/sj.onc.1209608 · Cited by 2,312
Direct Activation of Bax by p53 Mediates Mitochondrial Membrane Permeabilization and Apoptosis
Chipuk, J. E., Kuwana, T., Bouchier-Hayes, L., Droin, N. M., Newmeyer, D. D., Schuler, M., & Green, D. R. (2004) · Science · doi:10.1126/science.1092734 · Cited by 2,108
The first 30 years of p53: growing ever more complex.
Levine, A. J., & Oren, M. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2723 · Cited by 1,967
Mitochondria: More Than Just a Powerhouse
McBride, H. M., Neuspiel, M., & Wasiak, S. (2006) · Current Biology · doi:10.1016/j.cub.2006.06.054 · Cited by 1,985
Kruse, J.-P., & Gu, W. (2009) · Cell · doi:10.1016/j.cell.2009.04.050 · Cited by 1,610
Baar, M. P., Brandt, R. M. C., Putavet, D. A., Klein, J. D. D., Derks, K. W. J., Bourgeois, B. R. M., Stryeck, S., Rijksen, Y., van Willigenburg, H., Feijtel, D. A., et al. (2017) · Cell · doi:10.1016/j.cell.2017.02.031 · Cited by 1,454
Fridman, J. S., & Lowe, S. W. (2003) · Oncogene · doi:10.1038/sj.onc.1207116 · Cited by 1,401
Regulating the p53 pathway: in vitro hypotheses, in vivo veritas
Toledo, F., & Wahl, G. M. (2006) · Nature reviews. Cancer · doi:10.1038/nrc2012 · Cited by 1,286
The Cell–Cycle Arrest and Apoptotic Functions of p53 in Tumor Initiation and Progression
Chen, J. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026104 · Cited by 1,222
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270
Calpain-mediated cleavage of Atg5 switches autophagy to apoptosis
Yousefi, S., Perozzo, R., Schmid, I., Ziemiecki, A., Schaffner, T., Scapozza, L., Brunner, T., & Simon, H.-U. (2006) · Nature Cell Biology · doi:10.1038/ncb1482 · Cited by 1,158
Regulation of autophagy by cytoplasmic p53
Tasdemir, E., Maiuri, M. C., Galluzzi, L., Vitale, I., Djavaheri-Mergny, M., D'Amelio, M., Criollo, A., Morselli, E., Zhu, C., Harper, F., et al. (2008) · Nature Cell Biology · doi:10.1038/ncb1730 · Cited by 1,132
Self-citationHaupt, S., Berger, M., Goldberg, Z., & Haupt, Y. (2003) · Journal of Cell Science · doi:10.1242/jcs.00739 · Cited by 1,136
Cytoplasmic functions of the tumour suppressor p53
Green, D. R., & Kroemer, G. (2009) · Nature · doi:10.1038/nature07986 · Cited by 1,106
Targeting p53 pathways: mechanisms, structures, and advances in therapy
Wang, H., Guo, M., Wei, H., & Chen, Y. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01347-1 · Cited by 1,016
p53 ubiquitination: Mdm2 and beyond
Brooks, C. L., & Gu, W. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.01.020 · Cited by 924
Butow, R. A., & Avadhani, N. G. (2004) · Molecular Cell · doi:10.1016/s1097-2765(04)00179-0 · Cited by 882
Hierarchical regulation of mitochondrion-dependent apoptosis by BCL-2 subfamilies
Kim, H., Rafiuddin-Shah, M., Tu, H.-C., Jeffers, J. R., Zambetti, G. P., Hsieh, J. J.-D., & Cheng, E. H.-Y. (2006) · Nature Cell Biology · doi:10.1038/ncb1499 · Cited by 874
Systems biology of cisplatin resistance: past, present and future
Galluzzi, L., Vitale, I., Michels, J., Brenner, C., Szabadkai, G., Harel-Bellan, A., Castedo, M., & Kroemer, G. (2014) · Cell Death & Disease · doi:10.1038/cddis.2013.428 · Cited by 782
Life in the balance: how BH3-only proteins induce apoptosis
Willis, S. N., & Adams, J. M. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.10.001 · Cited by 743
p53 Opens the Mitochondrial Permeability Transition Pore to Trigger Necrosis
Vaseva, A. V., Marchenko, N. D., Ji, K., Tsirka, S. E., Holzmann, S., & Moll, U. M. (2012) · Cell · doi:10.1016/j.cell.2012.05.014 · Cited by 740
Self-citationMartin, L. J., Pan, Y., Price, A. C., Sterling, W., Copeland, N. G., Jenkins, N. A., Price, D. L., & Lee, M. K. (2006) · The Journal of Neuroscience · doi:10.1523/jneurosci.4308-05.2006 · Cited by 684
Role of p53 in Cell Death and Human Cancers
Ozaki, T., & Nakagawara, A. (2011) · Cancers · doi:10.3390/cancers3010994 · Cited by 650
The mitochondrial pathways of apoptosis
Estaquier, J., Vallette, F., Vayssiere, J.-L., & Mignotte, B. (2012) · Advances in experimental medicine and biology · doi:10.1007/978-94-007-2869-1_7 · Cited by 637
Mitochondrial outer membrane permeabilization during apoptosis: the innocent bystander scenario
Chipuk, J. E., Bouchier-Hayes, L., & Green, D. R. (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401963 · Cited by 631
The Mitochondrial Proteome and Human Disease
Calvo, S. E., & Mootha, V. K. (2010) · Annual Review of Genomics and Human Genetics · doi:10.1146/annurev-genom-082509-141720 · Cited by 590
Cisplatin nephrotoxicity: new insights and therapeutic implications
Tang, C., Livingston, M. J., Safirstein, R., & Dong, Z. (2023) · Nature Reviews Nephrology · doi:10.1038/s41581-022-00631-7 · Cited by 548
Coping with stress: multiple ways to activate p53
Horn, H. F., & Vousden, K. H. (2007) · Oncogene · doi:10.1038/sj.onc.1210263 · Cited by 522
Mutant p53 in cancer: from molecular mechanism to therapeutic modulation
Chen, X., Zhang, T., Su, W., Dou, Z., Zhao, D., Jin, X., Lei, H., Wang, J., Xie, X., Cheng, B., et al. (2022) · Cell Death & Disease · doi:10.1038/s41419-022-05408-1 · Cited by 494
Transcription-independent pro-apoptotic functions of p53
Moll, U. M., Wolff, S., Speidel, D., & Deppert, W. (2005) · Current Opinion in Cell Biology · doi:10.1016/j.ceb.2005.09.007 · Cited by 468
Self-citationRegulating tumor suppressor genes: post-translational modifications
Chen, L., Liu, S., & Tao, Y. (2020) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-020-0196-9 · Cited by 449
A complex barcode underlies the heterogeneous response of p53 to stress
Murray-Zmijewski, F., Slee, E. A., & Lu, X. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2451 · Cited by 420
Mitochondrial Dysfunction Contributes to Oncogene-Induced Senescence
Moiseeva, O., Bourdeau, V., Roux, A., Deschênes-Simard, X., & Ferbeyre, G. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01868-08 · Cited by 408
p73 Induces apoptosis via PUMA transactivation and Bax mitochondrial translocation
Melino, G., Bernassola, F., Ranalli, M., Yee, K., Zong, W. X., Corazzari, M., Knight, R. A., Green, D. R., Thompson, C., & Vousden, K. H. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m307469200 · Cited by 368
The flavonoid procyanidin C1 has senotherapeutic activity and increases lifespan in mice
Xu, Q., Fu, Q., Li, Z., Liu, H., Wang, Y., Lin, X., He, R., Zhang, X., Ju, Z., Campisi, J., et al. (2021) · Nature Metabolism · doi:10.1038/s42255-021-00491-8 · Cited by 341
The Mdm2–p53 relationship evolves: Mdm2 swings both ways as an oncogene and a tumor suppressor
Manfredi, J. J. (2010) · Genes & Development · doi:10.1101/gad.1941710 · Cited by 344
The multiple levels of regulation by p53 ubiquitination
Lee, J. T., & Gu, W. (2010) · Cell Death & Differentiation · doi:10.1038/cdd.2009.77 · Cited by 289
Monoubiquitylation promotes mitochondrial p53 translocation
Marchenko, N. D., Wolff, S., Erster, S., Becker, K., & Moll, U. M. (2007) · The EMBO Journal · doi:10.1038/sj.emboj.7601560 · Cited by 286
Self-citationIntracellular Aβ42 activates p53 promoter: a pathway to neurodegeneration in Alzheimer's disease
Ohyagi, Y., Asahara, H., Chui, D.-H., Tsuruta, Y., Sakae, N., Miyoshi, K., Yamada, T., Kikuchi, H., Taniwaki, T., Murai, H., et al. (2005) · The FASEB Journal · doi:10.1096/fj.04-2637fje · Cited by 281
The Role of p53 in Metabolic Regulation
Puzio-Kuter, A. M. (2011) · Genes & Cancer · doi:10.1177/1947601911409738 · Cited by 273
Inhibition of pluripotent stem cell-derived teratoma formation by small molecules
Lee, M.-O., Moon, S. H., Jeong, H.-C., Yi, J.-Y., Lee, T.-H., Shim, S. H., Rhee, Y.-H., Lee, S.-H., Oh, S.-J., Lee, M.-Y., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1303669110 · Cited by 246
Zhao, Y., Chaiswing, L., Velez, J. M., Batinic-Haberle, I., Colburn, N. H., Oberley, T. D., & St. Clair, D. K. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-3835 · Cited by 245
Organelle-specific initiation of cell death
Galluzzi, L., Bravo-San Pedro, J. M., & Kroemer, G. (2014) · Nature Cell Biology · doi:10.1038/ncb3005 · Cited by 239
SIRT3 deregulation is linked to mitochondrial dysfunction in Alzheimer's disease
Lee, J., Kim, Y., Liu, T., Hwang, Y. J., Hyeon, S. J., Im, H., Lee, K., Alvarez, V. E., McKee, A. C., Um, S., et al. (2018) · Aging Cell · doi:10.1111/acel.12679 · Cited by 213
Regulation of AIF expression by p53
Stambolsky, P., Weisz, L., Shats, I., Klein, Y., Goldfinger, N., Oren, M., & Rotter, V (2006) · Cell Death & Differentiation · doi:10.1038/sj.cdd.4401965 · Cited by 194
Levels of HdmX expression dictate the sensitivity of normal and transformed cells to Nutlin-3
Patton, J. T., Mayo, L. D., Singhi, A. D., Gudkov, A. V., Stark, G. R., & Jackson, M. W. (2006) · Cancer Research · doi:10.1158/0008-5472.can-05-3832 · Cited by 189
Brooks, C. L., & Gu, W. (2011) · FEBS Letters · doi:10.1016/j.febslet.2011.05.022 · Cited by 186
Eischen, C. M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026096 · Cited by 161
Another fork in the road—life or death decisions by the tumour suppressor p53
Carvajal, L. A., & Manfredi, J. J. (2013) · The EMBO Reports · doi:10.1038/embor.2013.25 · Cited by 149
Calcium signaling alterations, oxidative stress, and autophagy in aging
Ureshino, R. P., Rocha, K. K., Lopes, G. S., Bincoletto, C., & Smaili, S. S. (2014) · Antioxidants & Redox Signaling · doi:10.1089/ars.2013.5777 · Cited by 143
Filipović, D., Todorović, N., Bernardi, R. E., & Gass, P. (2017) · Brain Structure and Function · doi:10.1007/s00429-016-1218-9 · Cited by 138
The matrix protein CCN1 (CYR61) induces apoptosis in fibroblasts
Todorovicç, V., Chen, C.-C., Hay, N., & Lau, L. F. (2005) · The Journal of Cell Biology · doi:10.1083/jcb.200504015 · Cited by 132
Acquisition of p53 mutations in response to the non-genotoxic p53 activator Nutlin-3
Aziz, M. H., Shen, H., & Maki, C. G. (2011) · Oncogene · doi:10.1038/onc.2011.185 · Cited by 131
Nanocosmetics and Nanomedicines
(2011) · doi:10.1007/978-3-642-19792-5 · Cited by 116
Spurgers, K. B., Gold, D. L., Coombes, K. R., Bohnenstiehl, N. L., Mullins, B., Meyn, R. E., Logothetis, C. J., & McDonnell, T. J. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m513901200 · Cited by 114
DDB2 decides cell fate following DNA damage
Stoyanova, T., Roy, N., Kopanja, D., Bagchi, S., & Raychaudhuri, P. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0812254106 · Cited by 108
Daxx Cooperates with the Axin/HIPK2/p53 Complex to Induce Cell Death
Li, Q., Wang, X., Wu, X., Rui, Y., Liu, W., Wang, J., Wang, X., Liou, Y.-C., Ye, Z., & Lin, S.-C. (2007) · Cancer Research · doi:10.1158/0008-5472.can-06-1671 · Cited by 105
ets-2 Promotes the Activation of a Mitochondrial Death Pathway in Down's Syndrome Neurons
Helguera, P., Pelsman, A., Pigino, G., Wolvetang, E., Head, E., & Busciglio, J. (2005) · The Journal of Neuroscience · doi:10.1523/jneurosci.5107-04.2005 · Cited by 88
Watching the watcher: Regulation of p53 by mitochondria
Holley, A. K., & St Clair, D. K. (2009) · Future Oncology · doi:10.2217/14796694.5.1.117 · Cited by 75
YPEL3, a p53-Regulated Gene that Induces Cellular Senescence
Kelley, K. D., Miller, K. R., Todd, A., Kelley, A. R., Tuttle, R., & Berberich, S. J. (2010) · Cancer Research · doi:10.1158/0008-5472.can-09-3219 · Cited by 73
Wäster, P. K., & Öllinger, K. M. (2009) · Journal of Investigative Dermatology · doi:10.1038/jid.2008.421 · Cited by 72
Role of mitochondrial-mediated signaling pathways in Alzheimer disease and hypoxia
Carvalho, C., Correia, S. C., Santos, R. X., Cardoso, S., Moreira, P. I., Clark, T. A., Zhu, X., Smith, M. A., & Perry, G. (2009) · Journal of Bioenergetics and Biomembranes · doi:10.1007/s10863-009-9247-1 · Cited by 72
Panjarian, S., Kozhaya, L., Arayssi, S., Yehia, M., Bielawski, J., Bielawska, A., Usta, J., Hannun, Y. A., Obeid, L. M., & Dbaibo, G. S. (2008) · Prostaglandins & Other Lipid Mediators · doi:10.1016/j.prostaglandins.2008.02.004 · Cited by 69
Rochette, P. J., & Brash, D. E. (2008) · Mechanisms of Ageing and Development · doi:10.1016/j.mad.2007.12.007 · Cited by 68
Mitochondrial health, the epigenome and healthspan
Aon, M. A., Cortassa, S., Juhaszova, M., & Sollott, S. J. (2016) · Clinical Science · doi:10.1042/cs20160002 · Cited by 66
A role of HAUSP in tumor suppression in a human colon carcinoma xenograft model.
Becker, K., Marchenko, N., Palacios, G., & Moll, U. M. (2008) · Cell Cycle · doi:10.4161/cc.7.9.5756 · Cited by 63
Self-citationSevini, F., Giuliani, C., Vianello, D., Giampieri, E., Santoro, A., Biondi, F., Garagnani, P., Passarino, G., Luiselli, D., Capri, M., et al. (2014) · Experimental Gerontology · doi:10.1016/j.exger.2014.03.022 · Cited by 46
p53 directly regulates the glycosidase FUCA1 to promote chemotherapy-induced cell death
Baudot, A. D., Crighton, D., O'Prey, J., Somers, J., Sierra Gonzalez, P., & Ryan, K. M. (2016) · Cell Cycle · doi:10.1080/15384101.2016.1191714 · Cited by 31
Phosphorylation of Daxx by ATM contributes to DNA damage-induced p53 activation.
Tang, J., Agrawal, T., Cheng, Q., Qu, L., Brewer, M. D., Chen, J., & Yang, X. (2013) · PLoS ONE · doi:10.1371/journal.pone.0055813 · Cited by 28
Wu, Y., Xing, D., Liu, L., & Gao, B. (2008) · Cancer Letters · doi:10.1016/j.canlet.2008.06.006 · Cited by 24
The mitochondrion as a primary site of action of regulatory agents involved in neuroimmunomodulation
PSARRA, A. M. G., SOLAKIDI, S., & SEKERIS, C. E. (2006) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1366.019 · Cited by 22
(2013) · Digital Commons - East Tennessee State University (East Tennessee State University) · Cited by 3
Metadata
- Authors
- Mihara, M., Erster, S., Zaika, A., Petrenko, O., Chittenden, T., Pancoska, P., & Moll, U. M.
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2003-03
- Volume
- 11
- Issue
- 3
- Pages
- 577-590
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2160345685
- Cited by
- 1,777
- References
- 5
- FWCI
- 43.54
- Type
- journal article
- Language
- en
- Open access
- bronze
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 ›
Are you an author, or do you see a problem with this page? Request a review
Data sources
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.
