PML Is a Direct p53 Target that Modulates p53 Effector Functions
Open accessAbstract
The p53 tumor suppressor promotes cell cycle arrest or apoptosis in response to stress. Previous work suggests that the promyelocytic leukemia gene (PML) can act upstream of p53 to enhance transcription of p53 targets by recruiting p53 to nuclear bodies (NBs). We show that PML is itself a p53 target gene that also acts downstream of p53 to potentiate its antiproliferative effects. Hence, p53 is required for PML induction in response to oncogenes and DNA damaging chemotherapeutics. Furthermore, the PML gene contains p53 binding sites that confer p53 responsiveness to a heterologous reporter and can bind p53 in vitro and in vivo. Finally, cells lacking PML show a reduced propensity to undergo senescence or apoptosis in response to p53 activation, despite the induction of several p53 target genes. These results identify an additional element of PML regulation and establish PML as a mediator of p53 tumor suppressor functions.
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Members of the TRIM protein family, such as PML (TRIM19) and TRIM22, are transcriptionally activated by p53 and have been shown to alter the p53 response.
“Members of the TRIM protein family, such as PML (TRIM19)222 and TRIM22,223 are transcriptionally activated by p53 and have been shown to alter the p53 response.224”
From Census and evaluation of p53 target genes (2017) · cites this paper as [222]
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Cites
WAF1, a potential mediator of p53 tumor suppression
El-Deiry, W. S., Tokino, T., Velculescu, V. E., Levy, D. B., Parsons, R., Trent, J. M., Lin, D., Mercer, W. E., Kinzler, K. W., & Vogelstein, B. (1993) · Cell · doi:10.1016/0092-8674(93)90500-p · Cited by 8,321 · see citing works
Vogelstein, B., Lane, D., & Levine, A. J. (2000) · Nature · doi:10.1038/35042675 · Cited by 6,607 · see citing works
Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
Serrano, M., Lin, A. W., McCurrach, M. E., Beach, D., & Lowe, S. W. (1997) · Cell · doi:10.1016/s0092-8674(00)81902-9 · Cited by 5,178 · cited 5× · see citing works
“…of other Ras ef-larly, p53 / - and PML / -deficient mouse embryo fibro- blasts (MEFs) show defects in a premature senescence fector functions and is sufficient to induce premature senescence (Lin et al., 1998).program induced by oncogenic ras (Pearson et al., 2000; Serrano et al., 1997).”
BackgroundMethodInfluentialSelf-citationp53 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 · see citing works
Self-citationCrystal 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 2,559 · see citing works
PUMA, a Novel Proapoptotic Gene, Is Induced by p53
Nakano, K., & Vousden, K. H. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00214-3 · Cited by 2,315 · see citing works
The c-myc oncogene driven by immunoglobulin enhancers induces lymphoid malignancy in transgenic mice
Adams, J. M., Harris, A. W., Pinkert, C. A., Corcoran, L. M., Alexander, W. S., Cory, S., Palmiter, R. D., & Brinster, R. L. (1985) · Nature · doi:10.1038/318533a0 · Cited by 1,778 · see citing works
Atmospheric carbon dioxide concentrations over the past 60 million years
Pearson, P. N., & Palmer, M. R. (2000) · Nature · doi:10.1038/35021000 · Cited by 1,771 · see citing works
Fridman, J. S., & Lowe, S. W. (2003) · Oncogene · doi:10.1038/sj.onc.1207116 · Cited by 1,401 · see citing works
Self-citationp53- and Drug-Induced Apoptotic Responses Mediated by BH3-Only Proteins Puma and Noxa
Villunger, A., Michalak, E. M., Coultas, L., Müllauer, F., Böck, G., Ausserlechner, M. J., Adams, J. M., & Strasser, A. (2003) · Science · doi:10.1126/science.1090072 · Cited by 1,327 · see citing works
PUMA Induces the Rapid Apoptosis of Colorectal Cancer Cells
Yu, J., Zhang, L., Hwang, P. M., Kinzler, K. W., & Vogelstein, B. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00213-1 · Cited by 1,282 · see citing works
Decision making by p53: life, death and cancer
Oren, M. (2003) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4401183 · Cited by 1,063 · see citing works
Melnick, A. M., & Licht, J. D. (1999) · Blood · doi:10.1182/blood.v93.10.3167.410k44_3167_3215 · Cited by 1,024 · see citing works
Lin, A. W., Barradas, M., Stone, J. C., van Aelst, L., Serrano, M., & Lowe, S. W. (1998) · Genes & Development · doi:10.1101/gad.12.19.3008 · Cited by 945 · see citing works
Self-citationTakaoka, A., Hayakawa, S., Yanai, H., Stoiber, D., Negishi, H., Kikuchi, H., Sasaki, S., Imai, K., Shibue, T., Honda, K., et al. (2003) · Nature · doi:10.1038/nature01850 · Cited by 847 · see citing works
PML regulates p53 acetylation and premature senescence induced by oncogenic Ras
Pearson, M. A., Carbone, R., Sebastiani, C., Cioce, M., Fagioli, M., Saito, S., Higashimoto, Y., Appella, E., Minucci, S., Pandolfi, P. P., et al. (2000) · Nature · doi:10.1038/35018127 · Cited by 838 · see citing works
Self-citationSenescence of human fibroblasts induced by oncogenic Raf
Zhu, J., Woods, D., McMahon, M., & Bishop, J. M. (1998) · Genes & Development · doi:10.1101/gad.12.19.2997 · Cited by 826 · see citing works
Disruption of the ARF-Mdm2-p53 tumor suppressor pathway in Myc-induced lymphomagenesis
Eischen, C. M., Weber, J. D., Roussel, M. F., Sherr, C. J., & Cleveland, J. L. (1999) · Genes & Development · doi:10.1101/gad.13.20.2658 · Cited by 819 · see citing works
p63 and p73 are required for p53-dependent apoptosis in response to DNA damage
Flores, E. R., Tsai, K. Y., Crowley, D. G., Sengupta, S., Yang, A., McKeon, F., & Jacks, T. (2002) · Nature · doi:10.1038/416560a · Cited by 801 · see citing works
A novel macromolecular structure is a target of the promyelocyte-retinoic acid receptor oncoprotein
Dyck, J. A., Maul, G. G., Miller, W. H., Chen, J. D., Kakizuka, A., & Evans, R. M. (1994) · Cell · doi:10.1016/0092-8674(94)90340-9 · Cited by 783 · see citing works
Bett, A. J., Haddara, W. M. R., PREVEC, L., & Graham, F. L. (1994) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.91.19.8802 · Cited by 742 · see citing works
Mediation of c-Myc-Induced Apoptosis by p53
Hermeking, H., & Eick, D. (1994) · Science · doi:10.1126/science.8091232 · Cited by 738 · see citing works
Prives, C. (1998) · Cell · doi:10.1016/s0092-8674(00)81774-2 · Cited by 623 · see citing works
p19ARF links the tumour suppressor p53 to Ras
Palmero, I., Pantoja, C., & Serrano, M. (1998) · Nature · doi:10.1038/25870 · Cited by 617 · see citing works
E1A signaling to p53 involves the p19ARFtumor suppressorPreprint
de Stanchina, E., McCurrach, M. E., Zindy, F., Shieh, S.-Y., Ferbeyre, G., Samuelson, A. V., Prives, C. L., Roussel, M. F., Sherr, C. J., & Lowe, S. W. (1998) · Genes & Development · doi:10.1101/gad.12.15.2434 · Cited by 607 · see citing works
Self-citationThe transcriptional role of PML and the nuclear body
Zhong, S., Salomoni, P., & Pandolfi, P. P. (2000) · Nature Cell Biology · doi:10.1038/35010583 · Cited by 576 · see citing works
Self-citationThe Role of PML in Tumor Suppression
Salomoni, P., & Pandolfi, P. P. (2002) · Cell · doi:10.1016/s0092-8674(02)00626-8 · Cited by 564 · see citing works
Self-citationPml is essential for multiple apoptotic pathways
Wang, Z., Ruggero, D., Ronchetti, S., Zhong, S., Gaboli, M. P., Rivi, R., & Pandolfi, P. P. (1998) · Nature Genetics · doi:10.1038/3073 · Cited by 558 · see citing works
Self-citationPML is induced by oncogenic <i>ras</i> and promotes premature senescence
Ferbeyre, G., de Stanchina, E., Querido, E., Baptiste, N., Prives, C., & Lowe, S. W. (2000) · Genes & Development · doi:10.1101/gad.14.16.2015 · Cited by 536 · see citing works
Self-citationRole of PML in Cell Growth and the Retinoic Acid Pathway
Wang, Z. G., Delva, L., Gaboli, M. P., Rivi, R., Giorgio, M., Cordon‐Cardo, C., Grosveld, F. G., & Pandolfi, P. P. (1998) · Science · doi:10.1126/science.279.5356.1547 · Cited by 516 · see citing works
Self-citationCancer and ageing: rival demons?
Campisi, J. (2003) · Nature Reviews Cancer · doi:10.1038/nrc1073 · Cited by 512 · see citing works
The function of PML in p53-dependent apoptosis
Guo, A., Salomoni, P., Luo, J., Shih, A. H., Zhong, S., Gu, W., & Pandolfi, P. P. (2000) · Nature Cell Biology · doi:10.1038/35036365 · Cited by 466 · see citing works
Self-citationINK4a/ARF mutations accelerate lymphomagenesis and promote chemoresistance by disabling p53
Schmitt, C. A., McCurrach, M. E., de Stanchina, E., Wallace-Brodeur, R. R., & Lowe, S. W. (1999) · Genes & Development · doi:10.1101/gad.13.20.2670 · Cited by 458 · see citing works
Self-citationZhu, J., Koken, M. H. M., Quignon, F., Chelbi‐Alix, M. K., Degos, L., Wang, Z. Y., Chen, Z., & de Thé, H. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3978 · Cited by 426 · see citing works
PML induces a novel caspase-independent death process
Quignon, F., BELS, F. D., Koken, M. H. M., et al. (1998) · Nature Genetics · doi:10.1038/3068 · Cited by 381 · see citing works
Regulation of p53 activity in nuclear bodies by a specific PML isoform
Fogal, V., Gostissa, M., Sandy, P., Zacchi, P., Sternsdorf, T., Jensen, K., Pandolfi, P. P., Will, H., Schneider, C., & Sal, G. D. (2000) · The EMBO Journal · doi:10.1093/emboj/19.22.6185 · Cited by 372 · see citing works
Self-citationMcCurrach, M. E., Connor, T. M. F., Knudson, C. M., Korsmeyer, S. J., & Lowe, S. W. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.6.2345 · Cited by 368 · see citing works
Self-citationHemann, M. T., Fridman, J. S., Zilfou, J. T., Hernando, E., Paddison, P. J., Cordon‐Cardo, C., Hannon, G. J., & Lowe, S. W. (2003) · Nature Genetics · doi:10.1038/ng1091 · Cited by 354 · see citing works
Self-citationDifferential SMN2 expression associated with SMA severity
Gavrilov, D. K., Shi, X., Das, K., Gilliam, T. C., & Wang, C. H. (1998) · Nature Genetics · doi:10.1038/3030 · Cited by 337 · see citing works
Juven‐Gershon, T., Barak, Y., Zauberman, A., George, D. L., & Oren, M. (1993) · PubMed · Cited by 332 · see citing works
Pondering the Promyelocytic Leukemia Protein (PML) Puzzle: Possible Functions for PML Nuclear Bodies
Borden, K. L. B. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.15.5259-5269.2002 · Cited by 314 · see citing works
The p53MH algorithm and its application in detecting p53-responsive genes
Hoh, J., Jin, S. V., Parrado, T., Edington, J., Levine, A. J., & Ott, J. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.132268899 · Cited by 295 · see citing works
Oncogenic <i>ras</i> and p53 Cooperate To Induce Cellular Senescence
Ferbeyre, G., de Stanchina, E., Lin, A. W., Querido, E., McCurrach, M. E., Hannon, G. J., & Lowe, S. W. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.10.3497-3508.2002 · Cited by 290 · see citing works
Self-citationRole and fate of PML nuclear bodies in response to interferon and viral infections
Regad, T., & Chelbi‐Alix, M. K. (2001) · Oncogene · doi:10.1038/sj.onc.1204854 · Cited by 284 · see citing works
Stadler, M., Chelbi‐Alix, M. K., Koken, M. H. M., Venturini, L., Lee, C., Saı̈b, A., Quignon, F., Pelicano, L., Guillemin, M.-C., & Schindler, C. (1995) · PubMed · Cited by 266 · see citing works
DNA viruses and viral proteins that interact with PML nuclear bodies
Everett, R. D. (2001) · Oncogene · doi:10.1038/sj.onc.1204759 · Cited by 247 · see citing works
Attardi, L. D., Lowe, S. W., Brugarolas, J., & Jacks, T. (1996) · The EMBO Journal · doi:10.1002/j.1460-2075.1996.tb00739.x · Cited by 238 · see citing works
Self-citationPML-dependent apoptosis after DNA damage is regulated by the checkpoint kinase hCds1/Chk2
Yang, S., Kuo, C. S., Bisi, J., & Kim, M. K. (2002) · Nature Cell Biology · doi:10.1038/ncb869 · Cited by 238 · see citing works
Deconstructing PML‐induced premature senescence
Bischof, O., Kirsh, O., Pearson, M. A., Itahana, K., Pelicci, P. G., & Dejean, A. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf341 · Cited by 229 · see citing works
Induction of the PML protein by interferons in normal and APL cells.
Chelbi‐Alix, M. K., Pelicano, L., Quignon, F., Koken, M. H. M., Venturini, L., Stadler, M., Pavlovic, J., Degos, L., & de Thé, H. (1995) · PubMed · Cited by 216 · see citing works
Role of Promyelocytic Leukemia (Pml) Protein in Tumor Suppression
Rego, E. M., Wang, Z., Peruzzi, D., He, L.-Z., Cordon‐Cardo, C., & Pandolfi, P. P. (2001) · The Journal of Experimental Medicine · doi:10.1084/jem.193.4.521 · Cited by 159 · see citing works
Self-citationKunz, C., Pebler, S., Otte, J., & von der Ahe, D. (1995) · Nucleic Acids Research · doi:10.1093/nar/23.18.3710 · Cited by 144 · see citing works
The Promyelocytic Leukemia Protein Protects p53 from Mdm2-mediated Inhibition and Degradation
Louria‐Hayon, I., Grossman, T., Sionov, R. V., Alsheich-Bartok, O., Pandolfi, P. P., & Haupt, Y. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m301264200 · Cited by 135 · see citing works
Self-citationThornborrow, E. C., Patel, S., Mastropietro, A. E., Schwartzfarb, E. M., & Manfredi, J. J. (2002) · Oncogene · doi:10.1038/sj.onc.1205069 · Cited by 132 · see citing works
PML interaction with p53 and its role in apoptosis and replicative senescence
Pearson, M. A., & Pelicci, P. G. (2001) · Oncogene · doi:10.1038/sj.onc.1204856 · Cited by 124 · see citing works
Piazza, F., Gurrieri, C., & Pandolfi, P. P. (2001) · Oncogene · doi:10.1038/sj.onc.1204855 · Cited by 105 · see citing works
Self-citationKurki, S., Latonen, L., & Laiho, M. (2003) · Journal of Cell Science · doi:10.1242/jcs.00714 · Cited by 91 · see citing works
Physical and Functional Interactions between PML and MDM2
Wei, X., Yu, Z. K., Ramalingam, A., Grossman, S. R., Jiang, Y., Bloch, D. B., & Maki, C. G. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m212215200 · Cited by 74 · see citing works
Mutations of the PML tumor suppressor gene in acute promyelocytic leukemia
Gurrieri, C. (2003) · Blood · doi:10.1182/blood-2003-07-2200 · Cited by 70 · see citing works
UV-C-induced DNA damage leads to p53-dependent nuclear trafficking of PML
Seker, H., Rubbi, C. P., Linke, S. P., et al. (2003) · Oncogene · doi:10.1038/sj.onc.1206140 · Cited by 52 · see citing works
Oliver, G. (2004) · European Journal of Cancer Care · doi:10.1111/j.1365-2354.2004.00540.x · Cited by 7 · see citing works
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- responsive genes. Proc. Natl. Acad. Sci. USA 99, 8467-8472.
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Transcriptional control of human p53-regulated genes
Riley, T., Sontag, E., Chen, P., & Levine, A. (2008) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2395 · Cited by 1,921 · see citing works
Post-translational modification of p53 in tumorigenesis
Bode, A. M., & Dong, Z. (2004) · Nature Reviews Cancer · doi:10.1038/nrc1455 · Cited by 1,270 · see citing works
Census and evaluation of p53 target genes
Fischer, M. (2017) · Oncogene · doi:10.1038/onc.2016.502 · Cited by 971 · see citing works
p53 Dynamics Control Cell Fate
Purvis, J. E., Karhohs, K. W., Mock, C., Batchelor, E., Loewer, A., & Lahav, G. (2012) · Science · doi:10.1126/science.1218351 · Cited by 770 · see citing works
Zhang, R., Poustovoitov, M. V., Ye, X., Santos, H. A., Chen, W., Daganzo, S. M., Erzberger, J. P., Serebriiskii, I. G., Canutescu, A. A., Dunbrack, R. L., et al. (2005) · Developmental Cell · doi:10.1016/j.devcel.2004.10.019 · Cited by 699 · see citing works
Distinct p53 Transcriptional Programs Dictate Acute DNA-Damage Responses and Tumor Suppression
Brady, C. A., Jiang, D., Mello, S. S., Johnson, T. M., Jarvis, L. A., Kozak, M. M., Broz, D. K., Basak, S., Park, E. J., McLaughlin, M. E., et al. (2011) · Cell · doi:10.1016/j.cell.2011.03.035 · Cited by 533 · see citing works
RAR and RXR modulation in cancer and metabolic disease
Altucci, L., Leibowitz, M. D., Ogilvie, K. M., de Lera, A. R., & Gronemeyer, H. (2007) · Nature Reviews Drug Discovery · doi:10.1038/nrd2397 · Cited by 517 · see citing works
Molecular dissection of formation of senescence-associated heterochromatin foci
Zhang, R., Chen, W., & Adams, P. D. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.02019-06 · Cited by 415 · see citing works
Kosar, M., Bartkova, J., Hubackova, S., Hodny, Z., Lukas, J., & Bartek, J. (2011) · Cell Cycle · doi:10.4161/cc.10.3.14707 · Cited by 283 · see citing works
DNA Damage Signaling and p53-dependent Senescence after Prolonged β-Interferon Stimulation
Moiseeva, O., Mallette, F. A., Mukhopadhyay, U. K., Moores, A., & Ferbeyre, G. (2006) · Molecular Biology of the Cell · doi:10.1091/mbc.e05-09-0858 · Cited by 252 · see citing works
Self-citationCellular Senescence in Postmitotic Cells: Beyond Growth Arrest
Sapieha, P., & Mallette, F. A. (2018) · Trends in Cell Biology · doi:10.1016/j.tcb.2018.03.003 · Cited by 193 · see citing works
Deconstructing p53 transcriptional networks in tumor suppression
Bieging, K. T., & Attardi, L. D. (2012) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.10.006 · Cited by 194 · see citing works
Assessing cell and organ senescence biomarkers
de Jesus, B. B., & Blasco, M. A. (2012) · Circulation Research · doi:10.1161/circresaha.111.247866 · Cited by 187 · see citing works
Regulation of E2Fs and senescence by PML nuclear bodies
Vernier, M., Bourdeau, V., Gaumont-Leclerc, M.-F., Moiseeva, O., Bégin, V., Saad, F., Mes-Masson, A.-M., & Ferbeyre, G. (2011) · Genes & Development · doi:10.1101/gad.1975111 · Cited by 177 · see citing works
Self-citationEischen, C. M. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026096 · Cited by 161 · see citing works
The transcription factor p53: Not a repressor, solely an activator.
Fischer, M., Steiner, L., & Engeland, K. (2014) · Cell Cycle · doi:10.4161/15384101.2014.949083 · Cited by 153 · see citing works
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Niwa-Kawakita, M., Ferhi, O., Soilihi, H., Le Bras, M., Lallemand-Breitenbach, V., & de Thé, H. (2017) · Journal of Experimental Medicine · doi:10.1084/jem.20160301 · Cited by 104 · see citing works
Liu, G., & Chen, X. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.26.4.1398-1413.2006 · Cited by 104 · see citing works
Identification of novel direct transcriptional targets of glucocorticoid receptor
U, M., Shen, L., Oshida, T., Miyauchi, J., Yamada, M., & Miyashita, T. (2004) · Leukemia · doi:10.1038/sj.leu.2403516 · Cited by 97 · see citing works
Yates, K. E., Korbel, G. A., Shtutman, M., Roninson, I. B., & DiMaio, D. (2008) · Aging Cell · doi:10.1111/j.1474-9726.2008.00411.x · Cited by 77 · see citing works
Sarkari, F., Wang, X., Nguyen, T., & Frappier, L. (2011) · PLoS ONE · doi:10.1371/journal.pone.0016598 · Cited by 59 · see citing works
TRIMming p53’s anticancer activity
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Münch, S., Weidtkamp-Peters, S., Klement, K., Grigaravicius, P., Monajembashi, S., Salomoni, P., Pandolfi, P. P., Weißhart, K., & Hemmerich, P. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.01345-13 · Cited by 32 · see citing works
Self-citation
- Authors
- de Stanchina, E., Querido, E., Narita, M., Davuluri, R. V., Pandolfi, P. P., Ferbeyre, G., & Lowe, S. W.
- Affiliations
- Cold Spring Harbor Laboratory (US)
- The Ohio State University (US)
- Memorial Sloan Kettering Cancer Center (US)
- Université de Montréal (CA)
- Corresponding author
- Lowe, Scott W
- ORCID
- Venue
- Molecular Cell
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 13
- Issue
- 4
- Pages
- 523-535
- ISSN
- 1097-2765 (ISSN-L)
- OpenAlex
- W2118656013
- Cited by
- 312
- References
- 61
- Citations by year
- 2026: 6 · 2025: 3 · 2024: 8 · 2023: 4 · 2022: 8 · 2021: 5 · 2020: 12 · 2019: 6 · 2018: 14 · 2017: 10 · 2016: 15 · 2015: 11 · 2014: 22 · 2013: 24 · 2012: 19
- FWCI
- 10.08
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Licence
- www.elsevier.com/tdm/userlicense/1.0/ (tdm)
- www.elsevier.com/legal/tdmrep-license (tdm)
- www.elsevier.com/open-access/userlicense/1.0/ (vor, 3454 d)
- doi.org/10.15223/policy-017 (stm-asf)
- doi.org/10.15223/policy-037 (stm-asf)
- doi.org/10.15223/policy-012 (stm-asf)
- doi.org/10.15223/policy-029 (stm-asf)
- doi.org/10.15223/policy-004 (stm-asf)
- Locations
- Molecular Cell (publishedVersion)
- PubMed (publishedVersion)
- Cold Spring Harbor Laboratory Institutional Repository (Cold Spring Harbor Laboratory) (acceptedVersion)
- Funders
- National Institute on Aging (AG-16379)
- National Cancer Institute (P30CA008748)
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Cell death mechanisms and regulation
- Health Sciences › Medicine › Physiology › Telomeres, Telomerase, and Senescence
- Keywords
- promyelocytic leukemia protein, PML, p53, p53 target genes, p53 binding sites, nuclear bodies, apoptosis, cellular senescence, DNA damage response, transcriptional regulation, tumor suppression
- MeSH terms
- Promyelocytic Leukemia Protein, Animals, Base Sequence, Binding Sites, Cell Line, Cell Survival, Fibroblasts, Humans, Neoplasm Proteins, Nuclear Proteins, Promoter Regions, Genetic, Genes, ras, Retroviridae, Transcription Factors, Signal Transduction, Leukemia, Promyelocytic, Acute, Gene Expression Regulation, Neoplastic, Genes, Tumor Suppressor, Genes, p53, Tumor Suppressor Protein p53, Cellular Senescence, Apoptosis, Genes, Reporter, Mice, Knockout, Tumor Suppressor Proteins, Mice
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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