Therapeutic targeting of p53: all mutants are equal, but some mutants are more equal than others
Abstract
TP53, which encodes the tumour-suppressor protein p53, is the most frequently mutated gene across all cancer types. The presence of mutant p53 predisposes to cancer development, promotes the survival of cancer cells, and is associated with ineffective therapeutic responses and unfavourable prognoses. Despite these effects, no drug that abrogates the oncogenic functions of mutant p53 has yet been approved for the treatment of cancer. Current investigational therapeutic strategies are mostly aimed at restoring the wild-type activity of mutant p53, based on the assumption that all p53 mutants are functionally equal. Our increasing knowledge of mutant forms of p53, however, supports the antithetical hypothesis that not all p53 mutants have equivalent cellular effects; hence, a judicious approach to therapeutic targeting of mutant p53 is required. In this Review, we propose a categorization of the major classes of p53 mutants based on their functionality in tumour suppression and response to therapy. The emerging picture is that the mutations across TP53 form a 'rainbow of mutants', with varying degrees of functionality and different pathobiological consequences, necessitating the use of diverse therapeutic strategies to selectively target specific classes of mutation. The utility of this knowledge of TP53 mutations in developing selective therapeutic options, and in facilitating clinical decision-making is discussed.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
Activation of p53 in some cases may have the opposite effect.
“indicating that activation of p53 in some cases may have the opposite effect, which was consistent with results from other studies [94–96].”
From Targeting p53–MDM2 interaction by small-molecule inhibitors: learning from MDM2 inhibitors in clinical trials (2022) · cites this paper as [95]
Cites
PD-1 and PD-L1 Immune Checkpoint Blockade to Treat Breast Cancer
Hartkopf, A. D., Taran, F., Wallwiener, M., Walter, C. B., Krämer, B., Grischke, E., & Brucker, S. Y. (2016) · Breast Care · doi:10.1159/000453569 · Cited by 30,989 · see citing works
p53 Mutations in Human Cancers
Hollstein, M., Sidransky, D., Vogelstein, B., & Harris, C. C. (1991) · Science · doi:10.1126/science.1905840 · Cited by 8,018 · 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 · see citing works
In Vivo Activation of the p53 Pathway by Small-Molecule Antagonists of MDM2
Vassilev, L. T., Vu, B. T., Graves, B., Carvajal, D., Podlaski, F., Filipovic, Z., Kong, N., Kammlott, U., Lukacs, C., Klein, C., et al. (2004) · Science · doi:10.1126/science.1092472 · Cited by 4,661 · see citing works
Mice deficient for p53 are developmentally normal but susceptible to spontaneous tumours
Donehower, L. A., Harvey, M., Slagle, B. L., McArthur, M. J., Montgomery, C. A., Butel, J. S., & Bradley, A. (1992) · Nature · doi:10.1038/356215a0 · Cited by 4,649 · see citing works
Germ Line p53 Mutations in a Familial Syndrome of Breast Cancer, Sarcomas, and Other Neoplasms
Malkin, D., Li, F. P., Strong, L. C., Fraumeni, J. F., Nelson, C. E., Kim, D. H., Kassel, J., Gryka, M. A., Bischoff, F. Z., Tainsky, M. A., et al. (1990) · Science · doi:10.1126/science.1978757 · Cited by 3,765 · see citing works
Discovery and saturation analysis of cancer genes across 21 tumour types
Lawrence, M. S., Stojanov, P., Mermel, C. H., Robinson, J. T., Garraway, L. A., Golub, T. R., Meyerson, M., Gabriel, S. B., Lander, E. S., & Getz, G. (2014) · Nature · doi:10.1038/nature12912 · Cited by 3,096 · see citing works
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 2,559 · see citing works
T antigen is bound to a host protein in SY40-transformed cells
Lane, D. P., & Crawford, L. V. (1979) · Nature · doi:10.1038/278261a0 · Cited by 2,443 · see citing works
Self-citationVousden, K. H., & Lane, D. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2147 · Cited by 2,275 · see citing works
Self-citationStructure of the MDM2 Oncoprotein Bound to the p53 Tumor Suppressor Transactivation Domain
Kussie, P. H., Gorina, S., Marechal, V., Elenbaas, B., Moreau, J., Levine, A. J., & Pavletich, N. P. (1996) · Science · doi:10.1126/science.274.5289.948 · Cited by 2,206 · see citing works
TP53 mutations in human cancers: origins, consequences, and clinical use.
Olivier, M., Hollstein, M., & Hainaut, P. (2010) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001008 · Cited by 2,199 · see citing works
Chromosome 17 Deletions and p53 Gene Mutations in Colorectal Carcinomas
Baker, S. J., Fearon, E. R., Nigro, J. M., Hamilton, S. R., Preisinger, A. C., Jessup, J. M., vanTuinen, P., Ledbetter, D. H., Barker, D. F., Nakamura, Y., et al. (1989) · Science · doi:10.1126/science.2649981 · Cited by 2,067 · see citing works
Tumor spectrum analysis in p53-mutant mice
Jacks, T., Remington, L., Williams, B. O., Schmitt, E. M., Halachmi, S., Bronson, R. T., & Weinberg, R. A. (1994) · Current Biology · doi:10.1016/s0960-9822(00)00002-6 · Cited by 2,051 · see citing works
The p53 proto-oncogene can act as a suppressor of transformation
Finlay, C. A., Hinds, P. W., & Levine, A. J. (1989) · Cell · doi:10.1016/0092-8674(89)90045-7 · Cited by 1,987 · see citing works
The clonal and mutational evolution spectrum of primary triple-negative breast cancers
Shah, S. P., Roth, A., Goya, R., Oloumi, A., Ha, G., Zhao, Y., Turashvili, G., Ding, J., Tse, K., Haffari, G., et al. (2012) · Nature · doi:10.1038/nature10933 · Cited by 1,967 · see citing works
Linzer, D. I. H., & Levine, A. J. (1979) · Cell · doi:10.1016/0092-8674(79)90293-9 · Cited by 1,814 · see citing works
Muller, P. A. J., & Vousden, K. H. (2013) · Nature Cell Biology · doi:10.1038/ncb2641 · Cited by 1,647 · see citing works
Unravelling mechanisms of p53-mediated tumour suppression
Bieging-Rolett, K. T., Mello, S. S., & Attardi, L. D. (2014) · Nature reviews. Cancer · doi:10.1038/nrc3711 · Cited by 1,389 · see citing works
Mutant p53 gain of function in two mouse models of Li-Fraumeni syndrome
Olive, K. P., Tuveson, D. A., Ruhe, Z. C., Yin, B., Willis, N. A., Bronson, R. T., Crowley, D., & Jacks, T. (2004) · Cell · doi:10.1016/j.cell.2004.11.004 · Cited by 1,308 · see citing works
Mutant p53: one name, many proteinsPreprint
Freed-Pastor, W. A., & Prives, C. L. (2012) · Genes & Development · doi:10.1101/gad.190678.112 · Cited by 1,246 · see citing works
Germ-line transmission of a mutated p53 gene in a cancer-prone family with Li–Fraumeni syndrome
Srivastava, S. K., Zou, Z., Pirollo, K. F., Blattner, W. A., & Chang, E. H. (1990) · Nature · doi:10.1038/348747a0 · Cited by 1,210 · see citing works
P53 in survival, death and metabolic health: a lifeguard with a licence to kill.
Kruiswijk, F., Labuschagne, C. F., & Vousden, K. H. (2015) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm4007 · Cited by 1,080 · see citing works
Gain of function of a p53 hot spot mutation in a mouse model of Li-Fraumeni syndrome
Lang, G. A., Iwakuma, T., Suh, Y.-A., Liu, G., Rao, V. A., Parant, J. M., Valentin-Vega, Y. A., Terzian, T., Caldwell, L. C., Strong, L. C., et al. (2004) · Cell · doi:10.1016/j.cell.2004.11.006 · Cited by 1,069 · see citing works
Restoration of the tumor suppressor function to mutant p53 by a low-molecular-weight compound
Bykov, V. J. N., Issaeva, N., Shilov, A., Hultcrantz, M., Pugacheva, E., Chumakov, P., Bergman, J., Wiman, K. G., & Selivanova, G. (2002) · Nature Medicine · doi:10.1038/nm0302-282 · Cited by 1,067 · see citing works
Baker, S. J., Preisinger, A. C., Jessup, J. M., Paraskeva, C., Markowitz, S. D., Willson, J. K. V., Hamilton, S. R., & Vogelstein, B. (1990) · PubMed · Cited by 1,065 · see citing works
Rivlin, N., Brosh, R., Oren, M., & Rotter, V. (2011) · Genes & Cancer · doi:10.1177/1947601911408889 · Cited by 1,033 · see citing works
Role of Tyrosine Kinase Inhibitors in Cancer Therapy
Arora, A., & Scholar, E. M. (2005) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.105.084145 · Cited by 1,013 · see citing works
Heise, C. C., Sampson-Johannes, A., Williams, A., McCormick, F. P., Hoff, D. D. V., & Kirn, D. H. (1997) · Nature Medicine · doi:10.1038/nm0697-639 · Cited by 941 · see citing works
Oncogenic Forms of p53 Inhibit p53-Regulated Gene Expression
Kern, S. E., Pietenpol, J., Thiagalingam, S., Seymour, A., Kinzler, K. W., & Vogelstein, B. (1992) · Science · doi:10.1126/science.1589764 · Cited by 940 · see citing works
Gain of function mutations in p53
Dittmer, D., Pati, S., Zambetti, G., Chu, S., Teresky, A. K., Moore, M., Finlay, C., & Levine, A. J. (1993) · Nature Genetics · doi:10.1038/ng0593-42 · Cited by 894 · see citing works
TP53 mutations in human cancers: Functional selection and impact on cancer prognosis and outcomes
Petitjean, A., Achatz, M. I. W., Borresen-Dale, A. L., Hainaut, P., & Olivier, M. (2007) · Oncogene · doi:10.1038/sj.onc.1210302 · Cited by 884 · see citing works
Mutant p53 disrupts mammary tissue architecture via the mevalonate pathway
Freed-Pastor, W. A., Mizuno, H., Zhao, X., Langerød, A., Moon, S.-H., Rodriguez-Barrueco, R., Barsotti, A., Chicas, A., Li, W., Polotskaia, A., et al. (2012) · Cell · doi:10.1016/j.cell.2011.12.017 · Cited by 865 · see citing works
Pharmacological Rescue of Mutant p53 Conformation and Function
Foster, B. A., Coffey, H. A., Morin, M. J., & Rastinejad, F. (1999) · Science · doi:10.1126/science.286.5449.2507 · Cited by 802 · see citing works
Mutant p53 drives invasion by promoting integrin recycling
Muller, P. A. J., Caswell, P. T., Doyle, B., Iwanicki, M. P., Tan, E. H., Karim, S., Lukashchuk, N., Gillespie, D. A., Ludwig, R. L., Gosselin, P., et al. (2009) · Cell · doi:10.1016/j.cell.2009.11.026 · Cited by 796 · see citing works
Driver mutations in TP53 are ubiquitous in high grade serous carcinoma of the ovary
Ahmed, A. A., Etemadmoghadam, D., Temple, J., Lynch, A. G., Riad, M., Sharma, R. N., Stewart, C. J. R., Fereday, S., Caldas, C., DeFazio, A., et al. (2010) · The Journal of Pathology · doi:10.1002/path.2696 · Cited by 786 · see citing works
Michalovitz, D., Halevy, O., & Oren, M. (1990) · Cell · doi:10.1016/0092-8674(90)90113-s · Cited by 769 · see citing works
Small molecule RITA binds to p53, blocks p53–HDM-2 interaction and activates p53 function in tumors
Issaeva, N., Bozko, P. M., Enge, M., Protopopova, M., Verhoef, L. G. G. C., Masucci, M. G., Pramanik, A., & Selivanova, G. (2004) · Nature Medicine · doi:10.1038/nm1146 · Cited by 749 · see citing works
Cooperation between gene encoding p53 tumour antigen and ras in cellular transformation
Parada, L. F., Land, H., Weinberg, R. A., Wolf, D., & Rotter, V. (1984) · Nature · doi:10.1038/312649a0 · Cited by 731 · see citing works
Bouaoun, L., Sonkin, D., Ardin, M., Hollstein, M., Byrnes, G., Zavadil, J., & Olivier, M. (2016) · Human Mutation · doi:10.1002/humu.23035 · Cited by 730 · see citing works
Drugging the p53 pathway: understanding the route to clinical efficacy
Khoo, K. H., Verma, C. S., & Lane, D. P. (2014) · Nature Reviews Drug Discovery · doi:10.1038/nrd4236 · Cited by 723 · see citing works
Self-citationDeLeo, A. B., Jay, G. D., Appella, E., DuBois, G. C., Law, L. W., & Old, L. J. (1979) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.76.5.2420 · Cited by 721 · see citing works
Participation of p53 cellular tumour antigen in transformation of normal embryonic cells
Eliyahu, D., Raz, A., Gruß, P., Givol, D., & Oren, M. (1984) · Nature · doi:10.1038/312646a0 · Cited by 706 · see citing works
Wild-type p53 can inhibit oncogene-mediated focus formation.
Eliyahu, D., Michalovitz, D., Eliyahu, S., Pinhasi-Kimhi, O., & Oren, M. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.22.8763 · Cited by 681 · see citing works
Vaseva, A. V., & Moll, U. M. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.10.005 · Cited by 618 · see citing works
Milner, J., & Medcalf, E. (1991) · Cell · doi:10.1016/0092-8674(91)90384-b · Cited by 612 · see citing works
tp53 mutant zebrafish develop malignant peripheral nerve sheath tumors
Berghmans, S., Murphey, R. D., Wienholds, E., Neuberg, D. S., Kutok, J. L., Fletcher, C. D. �., Morris, J. P., Liu, T. X., Schulte‐Merker, S., Kanki, J. P., et al. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0406252102 · Cited by 599 · see citing works
Tumor Suppressive Functions of p53Preprint
Zilfou, J. T., & Lowe, S. W. (2009) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a001883 · Cited by 572 · see citing works
The expanding universe of p53 targets
Menendez, D., Inga, A., & Resnick, M. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2730 · Cited by 568 · see citing works
The Differential Effects of Mutant <i>p53</i> Alleles on Advanced Murine Lung Cancer
Jackson, E. L., Olive, K. P., Tuveson, D. A., Bronson, R., Crowley, D., Brown, M., & Jacks, T. (2005) · Cancer Research · doi:10.1158/0008-5472.can-05-2193 · Cited by 553 · see citing works
Ribeiro, R. C., Sandrini, F., Figueiredo, B., Zambetti, G. P., Michalkiewicz, E., Lafferty, A. R., DeLacerda, L., Rabin, M., Cadwell, C., Sampaio, G., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.161479898 · Cited by 541 · see citing works
Cellular immortalization by a cDNA clone encoding the transformation-associated phosphoprotein p53
Jenkins, J. R., Rudge, K., & Currie, G. A. (1984) · Nature · doi:10.1038/312651a0 · Cited by 538 · see citing works
Cancer Screening Recommendations for Individuals with Li-Fraumeni Syndrome
Kratz, C. P., Achatz, M. I., Brugières, L., Frebourg, T., Garber, J. E., Greer, M.-L. C., Hansford, J. R., Janeway, K. A., Kohlmann, W. K., McGee, R., et al. (2017) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-17-0408 · Cited by 534 · 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
Gain-of-function p53 mutants co-opt chromatin pathways to drive cancer growth
Zhu, J., Sammons, M. A., Donahue, G., Dou, Z., Vedadi, M., Getlik, M., Barsyte-Lovejoy, D., Al-awar, R., Katona, B. W., Shilatifard, A., et al. (2015) · Nature · doi:10.1038/nature15251 · Cited by 493 · see citing works
Identification of a novel p53 functional domain that is necessary for efficient growth suppression
Walker, K. K., & Levine, A. J. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15335 · Cited by 472 · see citing works
Cooks, T., Pateras, I. S., Tarcic, O., Solomon, H., Schetter, A. J., Wilder, S., Lozano, G., Pikarsky, E., Forshew, T., Rozenfeld, N., et al. (2013) · Cancer Cell · doi:10.1016/j.ccr.2013.03.022 · Cited by 471 · see citing works
Mutant p53 Drives Pancreatic Cancer Metastasis through Cell-Autonomous PDGF Receptor β Signaling
Weissmueller, S., Manchado, E., Saborowski, M., Morris, J. P., Wagenblast, E., Davis, C. A., Moon, S.-H., Pfister, N. T., Tschaharganeh, D. F., Kitzing, T., et al. (2014) · Cell · doi:10.1016/j.cell.2014.01.066 · Cited by 466 · see citing works
Targeting the ERBB family in cancer: couples therapy
Tebbutt, N. C., Pedersen, M. W., & Johns, T. G. (2013) · Nature reviews. Cancer · doi:10.1038/nrc3559 · Cited by 464 · see citing works
UCN-01: a potent abrogator of G2 checkpoint function in cancer cells with disrupted p53
Wang, Q., Fan, S., Eastman, A., Worland, P. J., Sausville, E. A., & O'Connor, P. M. (1996) · JNCI Journal of the National Cancer Institute · doi:10.1093/jnci/88.14.956 · Cited by 453 · see citing works
p53 gain-of-function cancer mutants induce genetic instability by inactivating ATM
Song, H., Hollstein, M., & Xu, Y. (2007) · Nature Cell Biology · doi:10.1038/ncb1571 · Cited by 442 · see citing works
Blandino, G., Levine, A. J., & Oren, M. (1999) · Oncogene · doi:10.1038/sj.onc.1202314 · Cited by 439 · see citing works
Tumour-associated mutant p53 drives the Warburg effect
Zhang, C., Liu, J., Liang, Y., Wu, R., Zhao, Y., Hong, X., Lin, M., Yu, H., Liu, L., Levine, A. J., et al. (2013) · Nature Communications · doi:10.1038/ncomms3935 · Cited by 434 · see citing works
Small peptides activate the latent sequence-specific DNA binding function of p53
Hupp, T. R., Sparks, A., & Lane, D. P. (1995) · Cell · doi:10.1016/0092-8674(95)90165-5 · Cited by 433 · see citing works
Self-citationStructure–function–rescue: the diverse nature of common p53 cancer mutants
Joerger, A. C., & Fersht, A. R. (2007) · Oncogene · doi:10.1038/sj.onc.1210291 · Cited by 430 · see citing works
Lehmann, S., Bykov, V. J. N., Ali, D., Andrén, O., Cherif, H., Tidefelt, U., Uggla, B., Yachnin, J., Juliusson, G., Moshfegh, A., et al. (2012) · Journal of Clinical Oncology · doi:10.1200/jco.2011.40.7783 · Cited by 406 · see citing works
The role of mutant p53 in human cancer
Goh, A. M., Coffill, C. R., & Lane, D. P. (2010) · The Journal of Pathology · doi:10.1002/path.2784 · Cited by 398 · see citing works
Self-citationLavigueur, A., Maltby, V., Mock, D., Rossant, J., Pawson, T. J., & Bernstein, A. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3982 · Cited by 393 · see citing works
Targeted rescue of a destabilized mutant of p53 by an in silico screened drug
Boeckler, F. M., Joerger, A. C., Jaggi, G., Rutherford, T. J., Veprintsev, D. B., & Fersht, A. R. (2008) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0805326105 · Cited by 389 · see citing works
The first five years of single-cell cancer genomics and beyondPreprint
Navin, N. E. (2015) · Genome Research · doi:10.1101/gr.191098.115 · Cited by 368 · see citing works
p53-deficient mice are extremely susceptible to radiation-induced tumorigenesis
Kemp, C. J., Wheldon, T. E., & Balmain, A. (1994) · Nature Genetics · doi:10.1038/ng0994-66 · Cited by 366 · see citing works
Kress, M., May, E., Cassingena, R., & May, P. (1979) · Journal of Virology · doi:10.1128/jvi.31.2.472-483.1979 · Cited by 359 · see citing works
The inherent instability of mutant p53 is alleviated by Mdm2 or p16 INK4a lossPreprint
Terzian, T., Suh, Y., Iwakuma, T., Post, S. M., Neumann, M., Lang, G. A., Pelt, C. S. V., & Lozano, G. (2008) · Genes & Development · doi:10.1101/gad.1662908 · Cited by 356 · see citing works
Improving survival by exploiting tumour dependence on stabilized mutant p53 for treatment
Alexandrova, E. M., Yallowitz, A. R., Li, D., Xu, S., Schulz‐Heddergott, R., Proia, D. A., Lozano, G., Dobbelstein, M., & Moll, U. M. (2015) · Nature · doi:10.1038/nature14430 · Cited by 354 · see citing works
Results of the Phase I trial of RG7112, a small-molecule MDM2 antagonist in leukemia
Andreeff, M., Kelly, K. R., Yee, K., Assouline, S., Strair, R., Popplewell, L., Bowen, D., Martinelli, G., Drummond, M. W., Vyas, P., et al. (2016) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-15-0481 · Cited by 352 · see citing works
Zhou, G., Liu, Z., & Myers, J. N. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25592 · Cited by 344 · see citing works
Selivanova, G., Iotsova, V., Okan, İ., Fritsche, M., Ström, M., Groner, B., Grafström, R. C., & Wiman, K. G. (1997) · Nature Medicine · doi:10.1038/nm0697-632 · Cited by 343 · see citing works
Shaulian, E., Zauberman, A., Ginsberg, D., & Oren, M. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5581 · Cited by 341 · see citing works
A Designed Inhibitor of p53 Aggregation Rescues p53 Tumor Suppression in Ovarian Carcinomas
Soragni, A., Janzen, D. M., Johnson, L. M., Lindgren, A. G., Thai-Quynh Nguyen, A., Tiourin, E., Soriaga, A. B., Lu, J., Jiang, L., Faull, K. F., et al. (2016) · Cancer Cell · doi:10.1016/j.ccell.2015.12.002 · Cited by 341 · see citing works
Li, D., Marchenko, N. D., & Moll, U. M. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.71 · Cited by 336 · see citing works
Rearrangements of the cellular p53 gene in erythroleukaemic cells transformed by Friend virus
Mowat, M. R. A., Cheng, A., Kimura, N., Bernstein, A., & Benchimol, S. (1985) · Nature · doi:10.1038/314633a0 · Cited by 320 · see citing works
Allele-Specific p53 Mutant Reactivation
Yu, X., Vázquez, A., Levine, A. J., & Carpizo, D. R. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.03.042 · Cited by 320 · see citing works
Clinical Overview of MDM2/X-Targeted Therapies
Burgess, A., Chia, K. M., Haupt, S., Thomas, D., Haupt, Y., & Lim, E. (2016) · Frontiers in Oncology · doi:10.3389/fonc.2016.00007 · Cited by 315 · see citing works
Yin, Y., Stephen, C. W., Luciani, M. G., & Fåhræus, R. (2002) · Nature Cell Biology · doi:10.1038/ncb801 · Cited by 305 · see citing works
A novel mechanism of tumorigenesis involving pH-dependent destabilization of a mutant p53 tetramer
DiGiammarino, E. L., Lee, A. S., Cadwell, C., Zhang, W., Bothner, B. B., Ribeiro, R. C., Zambetti, G. P., & Kriwacki, R. W. (2001) · Nature Structural Biology · doi:10.1038/nsb730 · Cited by 293 · see citing works
Valente, L. J., Gray, D. H. D., Michalak, E. M., Hofbauer, J. P., Egle, A., Scott, C. L., Janic, A., & Strasser, A. (2013) · Cell Reports · doi:10.1016/j.celrep.2013.04.012 · Cited by 292 · see citing works
The rebel angel: mutant p53 as the driving oncogene in breast cancer
Walerych, D., Napoli, M., Collavin, L., & Sal, G. D. (2012) · Carcinogenesis · doi:10.1093/carcin/bgs232 · Cited by 287 · see citing works
Next-generation sequencing to guide cancer therapy
Gagan, J., & Allen, E. M. V. (2015) · Genome Medicine · doi:10.1186/s13073-015-0203-x · Cited by 284 · see citing works
A Pin1/Mutant p53 Axis Promotes Aggressiveness in Breast Cancer
Girardini, J. E., Napoli, M., Piazza, S., Rustighi, A., Marotta, C., Radaelli, E., Capaci, V., Jordan, L. B., Quinlan, P., Thompson, A., et al. (2011) · Cancer Cell · doi:10.1016/j.ccr.2011.06.004 · Cited by 283 · see citing works
Li-Fraumeni syndrome: cancer risk assessment and clinical management
McBride, K. A., Ballinger, M. L., Killick, E., Kirk, J., Tattersall, M. H. N., Eeles, R. A., Thomas, D. M., & Mitchell, G. (2014) · Nature Reviews Clinical Oncology · doi:10.1038/nrclinonc.2014.41 · Cited by 279 · see citing works
Two hot spot mutant p53 mouse models display differential gain of function in tumorigenesis
Hanel, W. G., Marchenko, N. D., Xu, S., Yu, S., Weng, W., & Moll, U. M. (2013) · Cell Death and Differentiation · doi:10.1038/cdd.2013.17 · Cited by 278 · see citing works
Wei, S., Kozono, S., Kats, L., Nechama, M., Li, W., Guarnerio, J., Luo, M., You, M.-H., Yao, Y., Kondo, A., et al. (2015) · Nature Medicine · doi:10.1038/nm.3839 · Cited by 272 · see citing works
Courtois-Cox, S., Verhaegh, G. W. C. T., North, S., Luciani, M. G., Lassus, P., Hibner, U., Oren, M., & Hainaut, P. L. (2002) · Oncogene · doi:10.1038/sj.onc.1205874 · Cited by 264 · see citing works
TP53 and gastric carcinoma: A review
Fenoglio‐Preiser, C. M., Wang, J., Stemmermann, G. N., & Noffsinger, A. E. (2003) · Human Mutation · doi:10.1002/humu.10180 · Cited by 252 · see citing works
Reactivation of Mutant p53 and Induction of Apoptosis in Human Tumor Cells by Maleimide Analogs
Bykov, V. J. N., Issaeva, N., Zache, N., Shilov, A., Hultcrantz, M., Bergman, J., Selivanova, G., & Wiman, K. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m501664200 · Cited by 247 · see citing works
Wolf, D., Harris, N., & Rotter, V. (1984) · Cell · doi:10.1016/0092-8674(84)90532-4 · Cited by 245 · see citing works
Walerych, D., Lisek, K., Sommaggio, R., Piazza, S., Ciani, Y., Dalla, E., Rajkowska, K., Gaweda-Walerych, K., Ingallina, E., Tonelli, C., et al. (2016) · Nature Cell Biology · doi:10.1038/ncb3380 · Cited by 239 · see citing works
Small molecule induced reactivation of mutant p53 in cancer cells
Liu, X., Wilcken, R., Joerger, A. C., Chuckowree, I., Amin, J., Spencer, J., & Fersht, A. R. (2013) · Nucleic Acids Research · doi:10.1093/nar/gkt305 · Cited by 235 · see citing works
Ma, C. X., Cai, S., Li, S., Ryan, C. E., Guo, Z., Schaiff, W. T., Li, L., Hoog, J., Goiffon, R., Prat, A., et al. (2012) · Journal of Clinical Investigation · doi:10.1172/jci58765 · Cited by 224 · see citing works
Computational identification of a transiently open L1/S3 pocket for reactivation of mutant p53
Wassman, C. D., Baronio, R., Demir, Ö., Wallentine, B. D., Chen, C.-K., Hall, L., Salehi, F., Lin, D., Chung, B. P., Hatfield, G. W., et al. (2013) · Nature Communications · doi:10.1038/ncomms2361 · Cited by 223 · see citing works
Achatz, M. I., Olivier, M., Calvez‐Kelm, F. L., Martel‐Planche, G., Lopes, A., Rossi, B. M., Ashton‐Prolla, P., Giugliani, R., Palmero, E. I., Vargas, F. R., et al. (2006) · Cancer Letters · doi:10.1016/j.canlet.2005.12.039 · Cited by 218 · see citing works
Martinez, L. A., Naguibneva, I., Lehrmann, H., Vervisch, A., Tchénio, T., Lozano, G., & Harel-Bellan, A. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.222406899 · Cited by 210 · see citing works
Radiosensitization of p53 mutant cells by PD0166285, a novel G(2) checkpoint abrogator.
Wang, Y., Li, J., Booher, R. N., Kraker, A. J., Lawrence, T. S., Leopold, W. R., & Sun, Y. (2001) · PubMed · Cited by 210 · see citing works
Four domains of p300 each bind tightly to a sequence spanning both transactivation subdomains of p53
Teufel, D. P., Freund, S. M. V., Bycroft, M., & Fersht, A. R. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702010104 · Cited by 207 · see citing works
Bossi, G., Lapi, E., Strano, S., Rinaldo, C., Blandino, G., & Sacchi, A. (2005) · Oncogene · doi:10.1038/sj.onc.1209026 · Cited by 202 · see citing works
The execution of the transcriptional axis mutant p53, E2F1 and ID4 promotes tumor neo-angiogenesis
Fontemaggi, G., Dell’Orso, S., Trisciuoglio, D., Shay, T., Melucci, E., Fazi, F., Terrenato, I., Mottolese, M., Muti, P. C., Domany, E., et al. (2009) · Nature Structural & Molecular Biology · doi:10.1038/nsmb.1669 · Cited by 195 · see citing works
Activation of the cryptic DNA binding function of mutant forms of p53
Hupp, T. R., Meek, D. W., Midgley, C., & Lane, D. P. (1993) · Nucleic Acids Research · doi:10.1093/nar/21.14.3167 · Cited by 189 · see citing works
Self-citationMutant p53 reactivation by small molecules makes its way to the clinic
Bykov, V. J. N., & Wiman, K. G. (2014) · FEBS Letters · doi:10.1016/j.febslet.2014.04.017 · Cited by 180 · see citing works
Modulation of cellular and viral promoters by mutant human p53 proteins found in tumor cells
Deb, S., Jackson, C. T., Subler, M. A., & Martin, D. W. (1992) · Journal of Virology · doi:10.1128/jvi.66.10.6164-6170.1992 · Cited by 160 · see citing works
How Many Mutant p53 Molecules Are Needed To Inactivate a Tetramer?
Chan, W. M., Siu, W. Y., Lau, A. W. S., & Poon, R. Y. C. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.8.3536-3551.2004 · Cited by 159 · see citing works
Direct regulation of the centrosome duplication cycle by the p53-p21Waf1/Cip1 pathway
Tarapore, P., Horn, H. F., Tokuyama, Y., & Fukasawa, K. (2001) · Oncogene · doi:10.1038/sj.onc.1204424 · Cited by 158 · see citing works
Brachmann, R. K., Yu, K., Eby, Y. J., Pavletich, N. P., & Boeke, J. D. (1998) · The EMBO Journal · doi:10.1093/emboj/17.7.1847 · Cited by 156 · see citing works
Sarig, R., Rivlin, N., Brosh, R., Bornstein, C., Kamer, I., Ezra, O., Molchadsky, A., Goldfinger, N., Brenner, O. J., & Rotter, V. (2010) · The Journal of Experimental Medicine · doi:10.1084/jem.20100797 · Cited by 155 · see citing works
Phase I Dendritic Cell p53 Peptide Vaccine for Head and Neck Cancer
Schuler, P. J., Harasymczuk, M., Visús, C., DeLeo, A. B., Trivedi, S., Lei, Y. L., Argiris, A. E., Gooding, W. E., Butterfield, L. H., Whiteside, T. L., et al. (2014) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-13-2617 · Cited by 152 · see citing works
Candau, R., Scolnick, D. M., Darpino, P., Ying, C. Y., Halazonetis, T. D., & Berger, S. L. (1997) · Oncogene · doi:10.1038/sj.onc.1201244 · Cited by 152 · see citing works
Salim, K. Y., Vareki, S. M., Danter, W. R., San‐Marina, S., & Koropatnick, J. D. (2016) · Oncotarget · doi:10.18632/oncotarget.9133 · Cited by 152 · see citing works
Tumor-Derived p53 Mutants Induce NF-κB2 Gene Expression
Scian, M. J., Stagliano, K. E., Anderson, M. A. E., Hassan, S., Bowman, M., Miles, M. F., Deb, S. P., & Deb, S. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.22.10097-10110.2005 · Cited by 149 · see citing works
Vikhanskaya, F., Lee, M. K., Mazzoletti, M., Broggini, M., & Sabapathy, K. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm099 · Cited by 145 · see citing works
Self-citationWang, W., Takimoto, R., Rastinejad, F., & El‐Deiry, W. S. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.6.2171-2181.2003 · Cited by 144 · see citing works
Dearth, L. R., Hua, Q., Wang, T., Baroni, T. E., Zeng, J., Chen, S. W., Yi, S. Y., & Brachmann, R. K. (2006) · Carcinogenesis · doi:10.1093/carcin/bgl132 · Cited by 139 · see citing works
Tan, B. S., Tiong, K. H., Choo, H. L., Chung, F. F., Hii, L., Tan, S. H., Yap, I. K., Pani, S., Khor, N. T., Wong, S. F., et al. (2015) · Cell Death and Disease · doi:10.1038/cddis.2015.191 · Cited by 136 · see citing works
Targeting p53 for enhanced radio- and chemo-sensitivity
Lü, C., & El‐Deiry, W. S. (2009) · APOPTOSIS · doi:10.1007/s10495-009-0330-1 · Cited by 134 · see citing works
Wang, Y., Suh, Y., Fuller, M. Y., Jackson, J. G., Xiong, S., Terzian, T., Quintás‐Cardama, A., Bankson, J. A., El‐Naggar, A. K., & Lozano, G. (2011) · Journal of Clinical Investigation · doi:10.1172/jci44504 · Cited by 132 · see citing works
Roles of the functional loss of p53 and other genes in astrocytoma tumorigenesis and progression
Nozaki, M., Tada, M., Kobayashi, H., Zhang, C. L., Sawamura, Y., Abe, H., Ishii, N., & Meir, E. G. V. (1999) · Neuro-Oncology · doi:10.1093/neuonc/1.2.124 · Cited by 126 · see citing works
Mutant p53 targeting by the low molecular weight compound STIMA‐1
Zache, N., Lambert, J. M. R., Rökaeus, N., Shen, J., Hainaut, P. L., Bergman, J., Wiman, K. G., & Bykov, V. J. N. (2008) · Molecular Oncology · doi:10.1016/j.molonc.2008.02.004 · Cited by 116 · see citing works
Shaulian, E., Zauberman, A., Ginsberg, D., et al. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5581-5592.1992 · Cited by 113 · see citing works
Lavigueur, A., Maltby, V., Mock, D., et al. (1989) · Molecular and Cellular Biology · doi:10.1128/mcb.9.9.3982-3991.1989 · Cited by 113 · see citing works
Regulation of the level of the oncoprotein p53 in non-transformed and transformed cells.
Reihsaus, E., Kohler, M., Kraiss, S., Oren, M., & Montenarh, M. (1990) · PubMed · Cited by 109 · see citing works
Weinmann, L., Wischhusen, J., Demma, M. J., Naumann, U., Roth, P., Dasmahapatra, B., & Weller, M. (2008) · Cell Death and Differentiation · doi:10.1038/sj.cdd.4402301 · Cited by 107 · see citing works
Demma, M. J., Maxwell, E., Ramos, R., Liang, L., Li, C., Hesk, D., Rossman, R. R., Mallams, A. K., Doll, R. J., Liu, M., et al. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.083469 · Cited by 107 · see citing works
Aggarwal, M., Saxena, R., Sinclair, E., Fu, Y., Jacobs, A., Dyba, M., Wang, X., Cruz, I., Berry, D., Kallakury, B., et al. (2016) · Cell Death & Differentiation · doi:10.1038/cdd.2016.48 · Cited by 101 · see citing works
Lomax, M. E., Barnes, D. M., Hupp, T. R., Picksley, S. M., & Camplejohn, R. (1998) · Oncogene · doi:10.1038/sj.onc.1201974 · Cited by 100 · see citing works
Clinical Relevance of Gain-Of-Function Mutations of p53 in High-Grade Serous Ovarian Carcinoma
Kang, H. J., Chun, S., Kim, K.-R., Sohn, I., & Sung, C. O. (2013) · PLoS ONE · doi:10.1371/journal.pone.0072609 · Cited by 98 · see citing works
Design of a molecular support for cryo-EM structure determination
Martin, T. G., Bharat, T. A. M., Joerger, A. C., Bai, X., Praetorius, F., Fersht, A. R., Dietz, H., & Scheres, S. H. W. (2016) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1612720113 · Cited by 98 · see citing works
Cell-type, Dose, and Mutation-type Specificity Dictate Mutant p53 Functions In Vivo
Lee, M. K., Teoh, W. W., Phang, B. H., Tong, W., Wang, Z. Q., & Sabapathy, K. (2012) · Cancer Cell · doi:10.1016/j.ccr.2012.10.022 · Cited by 97 · see citing works
Self-citationXu, J., Wang, J., Hu, Y., Qian, J., Xu, B., Chen, H., Zou, W., & Fang, J.-Y. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.75 · Cited by 96 · see citing works
Rovinski, B., Munroe, D. G., Peacock, J. W., Mowat, M. R. A., Bernstein, A., & Benchimol, S. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.2.847 · Cited by 96 · see citing works
Blanden, A. R., Yu, X., Wolfe, A. J., Gilleran, J., Augeri, D. J., O’Dell, R. S., Olson, E. C., Kimball, S. D., Emge, T. J., Movileanu, L., et al. (2015) · Molecular Pharmacology · doi:10.1124/mol.114.097550 · Cited by 86 · see citing works
Hiraki, M., Hwang, S.-Y., Cao, S., Ramadhar, T. R., Byun, S., Yoon, K. W., Lee, J. H., Chu, K., Gurkar, A. U., Kolev, V., et al. (2015) · Chemistry & Biology · doi:10.1016/j.chembiol.2015.07.016 · Cited by 81 · see citing works
Shi, L. M., Myers, T. G., Fan, Y., O'Connor, P. M., Paull, K. D., Friend, S. H., & Weinstein, J. N. (1998) · Molecular Pharmacology · doi:10.1124/mol.53.2.241 · Cited by 78 · see citing works
The evolution of thymic lymphomas in p53 knockout micePreprint
Dudgeon, C., Chan, C. H., Kang, W., Sun, Y., Emerson, R., Robins, H. S., & Levine, A. J. (2014) · Genes & Development · doi:10.1101/gad.252148.114 · Cited by 77 · see citing works
North, S., Pluquet, O., Maurici, D., Ghissassi, F. E., & Hainaut, P. L. (2002) · Molecular Carcinogenesis · doi:10.1002/mc.10038 · Cited by 75 · see citing works
Vikhanskaya, F., Siddique, M. M., Lee, M. K., Broggini, M., & Sabapathy, K. (2005) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-04-1547 · Cited by 75 · see citing works
Self-citationMutant p53 drives multinucleation and invasion through a process that is suppressed by ANKRD11
Noll, J. E., Jeffery, J., Al‐Ejeh, F., Kumar, R., Khanna, K. K., Callen, D. F., & Neilsen, P. M. (2011) · Oncogene · doi:10.1038/onc.2011.456 · Cited by 75 · see citing works
Tal, P., Eizenberger, S., Cohen, E., Goldfinger, N., Pietrokovski, S., Oren, M., & Rotter, V. (2016) · Oncotarget · doi:10.18632/oncotarget.7857 · Cited by 74 · see citing works
Energy requirement for degradation of tumor-associated protein p53.
Gronostajski, R. M., Goldberg, A. L., & Pardee, A. B. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.3.442 · Cited by 73 · see citing works
p53 Oligomerization Is Essential for Its C-terminal Lysine Acetylation
Itahana, Y., Ke, H., & Zhang, Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m805696200 · Cited by 73 · see citing works
Kucab, J. E., Phillips, D. H., & Arlt, V. M. (2010) · FEBS Journal · doi:10.1111/j.1742-464x.2010.07676.x · Cited by 70 · see citing works
Does p53 status influence tumor response to anticancer therapies?
Pirollo, K. F., Bouker, K. B., & Chang, E. H. (2000) · Anti-Cancer Drugs · doi:10.1097/00001813-200007000-00002 · Cited by 64 · see citing works
Ohki, R., Kawase, T., Ohta, T., Ichikawa, H., & Taya, Y. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00375.x · Cited by 60 · see citing works
Heinlein, C., Krepulat, F., Löhler, J., Speidel, D., Deppert, W., & Tolstonog, G. V. (2007) · International Journal of Cancer · doi:10.1002/ijc.23317 · Cited by 59 · see citing works
Promyelocytic Leukemia Protein is Required for Gain of Function by Mutant p53
Haupt, S., Agostino, S. D., Mizrahi, I., Alsheich-Bartok, O., Voorhoeve, M., Damalas, A., Blandino, G., & Haupt, Y. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-4010 · Cited by 59 · see citing works
Induction of gene amplification as a gain-of-function phenotype of mutant p53 proteins.
El-Hizawi, S., Lagowski, J. P., Kulesz-Martin, M. F., & Albor, A. (2002) · PubMed · Cited by 56 · see citing works
Sun, Y., Dong, Z., Nakamura, K., & Colburn, N. H. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.10.8344492 · Cited by 54 · see citing works
Roles of the functional loss of p53 and other genes in astrocytoma tumorigenesis and progression
Nozaki, M., Tada, M., Kobayashi, H., Zhang, C.-L., Sawamura, Y., Abe, H., Ishii, N., & Meir, E. G. V. (1999) · Neuro-Oncology · doi:10.1215/s1522851798000179 · Cited by 53 · see citing works
Kucab, J. E., Phillips, D. H., & Arlt, V. M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07676.x · Cited by 50 · see citing works
The N-Terminally Truncated p53 Isoform △40p53 Influences Prognosis in Mucinous Ovarian Cancer
Hofstetter, G., Berger, A., Berger, R., Zorić, A., Braicu, E. I., Reimer, D., Fiegl, H., Marth, C., Zeimet, A. G., Ulmer, H., et al. (2012) · International Journal of Gynecological Cancer · doi:10.1097/igc.0b013e31823ca031 · Cited by 46 · see citing works
Prognostic implications of circulating anti-p53 antibodies in lung cancer - a review
Kumar, S., Mohan, A., & Guleria, R. (2009) · European Journal of Cancer Care · doi:10.1111/j.1365-2354.2008.01019.x · Cited by 41 · see citing works
The Contrived Mutant p53 Oncogene – Beyond Loss of Functions
Sabapathy, K. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00276 · Cited by 41 · see citing works
Self-citationAssessing the Efficacy of Mdm2/Mdm4-Inhibiting Stapled Peptides Using Cellular Thermal Shift Assays
Tan, B. X., Brown, C. J., Ferrer, F. J., Yuen, T. Y., Quah, S. T., Chan, B. H., Jansson, A. E., Teo, H., Nordlund, P., & Lane, D. P. (2015) · Scientific Reports · doi:10.1038/srep12116 · Cited by 40 · see citing works
Self-citationSimple identification of dominant p53 mutants by a yeast functional assay
Inga, A. (1997) · Carcinogenesis · doi:10.1093/carcin/18.10.2019 · Cited by 40 · see citing works
Merino, D. M., & Malkin, D. M. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9211-0_1 · Cited by 39 · see citing works
Energy Requirement for Degradation of Tumor-Associated Protein p53
Gronostajski, R. M., Goldberg, A. L., & Pardee, A. B. (1984) · Molecular and Cellular Biology · doi:10.1128/mcb.4.3.442-448.1984 · Cited by 39 · see citing works
Phang, B. H., Othman, R., Bougeard, G., Chia, R. H., Frébourg, T., Tang, C. L., Cheah, P. Y., & Sabapathy, K. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1510043112 · Cited by 37 · see citing works
Self-citationZhou, X., Wang, X. W., Xu, L., Hagiwara, K., Nagashima, M., Wolkowicz, R., Zurer, I., Rotter, V., & Harris, C. C. (1999) · PubMed · Cited by 37 · see citing works
Integrity of the 1,25-dihydroxyvitamin D3 receptor in bone, lung, and other cancers
Miller, C. W., Roberta Morosetti, A., Campbell, M. J., Mendoza, S., & Koeffler, H. P. (1997) · Molecular Carcinogenesis · doi:10.1002/(sici)1098-2744(199708)19:4 · Cited by 33 · see citing works
Awaiting a New Era of Cancer Immunotherapy
Hong, C. W., & Zeng, Q. (2012) · Cancer Research · doi:10.1158/0008-5472.can-12-0063 · Cited by 32 · see citing works
Lee, M. K., & Sabapathy, K. (2008) · Journal of Cell Science · doi:10.1242/jcs.022822 · Cited by 31 · see citing works
Self-citationAllele-specific silencing of mutant p53 attenuates dominant-negative and gain-of-function activities
Iyer, S. V., Parrales, A., Begani, P., Narkar, A., Adhikari, A. S., Martinez, L. A., & Iwakuma, T. (2015) · Oncotarget · doi:10.18632/oncotarget.6634 · Cited by 30 · see citing works
Rovinski, B., Munroe, D. G., Peacock, J., et al. (1987) · Molecular and Cellular Biology · doi:10.1128/mcb.7.2.847-853.1987 · Cited by 30 · see citing works
Insights into Wild-Type and Mutant p53 Functions Provided by Genetically Engineered Mice
Donehower, L. A. (2014) · Human Mutation · doi:10.1002/humu.22507 · Cited by 29 · see citing works
Galea, C. A., Bowman, P., & Kriwacki, R. W. (2005) · Protein Science · doi:10.1110/ps.051622005 · Cited by 27 · see citing works
Bristow, R. G., Peacock, J. W., Jang, A., Kim, J., Hill, R. P., & Benchimol, S. (2003) · Oncogene · doi:10.1038/sj.onc.1206405 · Cited by 23 · see citing works
Plummer, S. J., Santibanez‐Koref, M., Kurosaki, T., Liao, S., Noble, B., Fain, P. R., Anton‐Culver, H., & Casey, G. (1994) · PubMed · Cited by 20 · see citing works
The application of gene therapy in China.
Peng, Z., Qing, Y., & Li, B. (2008) · PubMed · Cited by 19 · see citing works
Hansen, S. A., Hart, M. L., Busi, S. B., Parker, T. W., Goerndt, A., Jones, K. B., Amos-Landgraf, J. M., & Bryda, E. C. (2016) · Disease Models & Mechanisms · doi:10.1242/dmm.025767 · Cited by 19 · see citing works
Forslund, A., Kressner, U., Lönnroth, C., Andersson, M., Lindmark, G. E., & Lundholm, K. (2002) · International Journal of Oncology · doi:10.3892/ijo.21.2.409 · Cited by 16 · see citing works
p53 as an Effector or Inhibitor of Therapy ResponsePreprint
Ablain, J., Poirot, B., Esnault, C., Lehmann‐Che, J., & de Thé, H. (2015) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026260 · Cited by 15 · see citing works
Bromley, D., Bauer, M. R., Fersht, A. R., & Daggett, V. (2016) · Protein Engineering Design and Selection · doi:10.1093/protein/gzw035 · Cited by 14 · see citing works
Prevalence of Allelic Loss at TP53 in Endometrial Carcinomas
Semczuk, A., Schneider‐Stock, R., & Szewczuk, W. (2010) · Oncology · doi:10.1159/000314353 · Cited by 12 · see citing works
TP53 Mutational Analysis Enhances the Prognostic Accuracy of IHC4 and PAM50 Assays
Lin, C., Chen, I.-C., Huang, C., Hu, F., Kuo, W., Kuo, K., Wang, C., Wu, P., Chang, D., Wang, M., et al. (2015) · Scientific Reports · doi:10.1038/srep17879 · Cited by 12 · see citing works
PRIMA-1MET induces nucleolar translocation of Epstein-Barr virus-encoded EBNA-5 protein
Stuber, G., Flaberg, E., Petrányi, G., Ötvös, R. H.-G., Rökaeus, N., Kashuba, E., Wiman, K. G., Klein, G., & Székely, L. (2009) · Molecular Cancer · doi:10.1186/1476-4598-8-23 · Cited by 8 · see citing works
p53-independentWAF1 induction by ACNU in human glioblastoma cells
Aoki, H., Ohnishi, K., Wang, X., Takahashi, A., Ohnishi, T., Nakamura, M., & Sakaki, T. (1998) · Molecular Carcinogenesis · doi:10.1002/(sici)1098-2744(199803)21:3 · Cited by 7 · see citing works
Flagged first, then by citations
Cited by
Sorted by citations
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 · see citing works
Regulated cell death (RCD) in cancer: key pathways and targeted therapies
Peng, F., Liao, M., Qin, R., Zhu, S., Peng, C. Y., Fu, L., Chen, Y., & Han, B. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01110-y · Cited by 850 · see citing works
Drugging p53 in cancer: one protein, many targets
Hassin, O., & Oren, M. (2022) · Nature Reviews Drug Discovery · doi:10.1038/s41573-022-00571-8 · Cited by 736 · see citing works
Circular RNA Vaccines against SARS-CoV-2 and Emerging Variants
Qu, L., Yi, Z., Shen, Y., Lin, L., Chen, F., Xu, Y., Wu, Z., Tang, H., Zhang, X., Tian, F., et al. (2021) · doi:10.1101/2021.03.16.435594 · Cited by 636 · see citing works
Somatic mutations precede acute myeloid leukemia years before diagnosis
Desai, P., Mencia-Trinchant, N., Savenkov, O., Simon, M. S., Cheang, G., Lee, S., Samuel, M., Ritchie, E. K., Guzman, M. L., Ballman, K. V., et al. (2018) · Nature Medicine · doi:10.1038/s41591-018-0081-z · Cited by 619 · see citing works
Targeting mutant p53 for cancer therapy: direct and indirect strategies
Hu, J., Cao, J., Topatana, W., Juengpanich, S., Li, S., Zhang, B., Shen, J., Cai, L., Cai, X., & Chen, M. (2021) · Journal of Hematology & Oncology · doi:10.1186/s13045-021-01169-0 · Cited by 557 · see citing works
Regulating 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 · see citing works
Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials
Xie, X., Yu, T., Li, X., Zhang, N., Foster, L. J., Peng, C., Huang, W., & He, G. (2023) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-023-01589-z · Cited by 396 · see citing works
MDM2 inhibition: an important step forward in cancer therapy
Konopleva, M. Y., Martinelli, G., Daver, N. G., Papayannidis, C., Wei, A. H., Higgins, B., Ott, M., Mascarenhas, J. O., & Andreeff, M. (2020) · Leukemia · doi:10.1038/s41375-020-0949-z · Cited by 376 · see citing works
The gut microbiome switches mutant p53 from tumour-suppressive to oncogenic
Kadosh, E., Snir-Alkalay, I., Venkatachalam, A., May, S., Lasry, A., Elyada, E., Zinger, A., Shaham, M., Vaalani, G., Mernberger, M., et al. (2020) · Nature · doi:10.1038/s41586-020-2541-0 · Cited by 378 · see citing works
Targeting p53 for the treatment of cancer
Duffy, M. J., Synnott, N. C., O’Grady, S., & Crown, J. P. (2020) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2020.07.005 · Cited by 351 · see citing works
Deubiquitinase-targeting chimeras for targeted protein stabilization
Henning, N. J., Boike, L., Spradlin, J. N., Ward, C. C., Liu, G., Zhang, E., Belcher, B. P., Brittain, S. M., Hesse, M. J., Dovala, D., et al. (2022) · Nature Chemical Biology · doi:10.1038/s41589-022-00971-2 · Cited by 344 · see citing works
The approved gene therapy drugs worldwide: from 1998 to 2019
Ma, C., Wang, Z.-L., Xu, T., He, Z., & Wei, Y.-Q. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107502 · Cited by 331 · see citing works
The Role of p53 Signaling in Colorectal Cancer
Liebl, M. C., & Hofmann, T. G. (2021) · Cancers · doi:10.3390/cancers13092125 · Cited by 332 · see citing works
The First Approved Gene Therapy Product for Cancer Ad- p53 (Gendicine): 12 Years in the Clinic
Zhang, W., Li, L., Li, D., Liu, J., Li, X., Li, W., Xu, X., Zhang, M. J., Chandler, L. A., Lin, H., et al. (2018) · Human Gene Therapy · doi:10.1089/hum.2017.218 · Cited by 320 · see citing works
The complexity of p53-mediated metabolic regulation in tumor suppression
Liu, Y., & Gu, W. J. (2021) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2021.03.010 · Cited by 260 · see citing works
Mutant p53 in cancer therapy—the barrier or the path
Zhou, X. Y., Hao, Q., & Lu, H. (2018) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjy072 · Cited by 244 · see citing works
Zhu, H., Gao, H., Ji, Y., Zhou, Q., Du, Z., Tian, L., Jiang, Y., Yao, K., & Zhou, Z. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01314-3 · Cited by 223 · see citing works
Control of metabolism by p53 – Cancer and beyond
Labuschagne, C. F., Zani, F., & Vousden, K. H. (2018) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2018.06.001 · Cited by 219 · see citing works
Liu, H., Liu, Y., Yang, F., Zhang, L., Zhang, F., Hu, X., Shao, Z., & Li, D. (2020) · Nucleic Acids Research · doi:10.1093/nar/gkaa130 · Cited by 205 · see citing works
Specific TP53 subtype as biomarker for immune checkpoint inhibitors in lung adenocarcinoma
Sun, H., Liu, S. M., Zhou, J., Xu, J., Zhang, H.-K., Yan, H., Huan, J., Dai, P., Xu, C., Su, J., et al. (2020) · EBioMedicine · doi:10.1016/j.ebiom.2020.102990 · Cited by 205 · see citing works
Translating p53-based therapies for cancer into the clinic
Peuget, S., Zhou, X., & Selivanova, G. (2024) · Nature reviews. Cancer · doi:10.1038/s41568-023-00658-3 · Cited by 198 · see citing works
Towards the overcoming of anticancer drug resistance mediated by p53 mutations
Cao, X., Hou, J., An, Q., Assaraf, Y. G., & Wang, X. (2019) · Drug Resistance Updates · doi:10.1016/j.drup.2019.100671 · Cited by 176 · see citing works
Immunomodulation by anticancer cell cycle inhibitors
Petroni, G., Formenti, S. C., Chen-Kiang, S., & Galluzzi, L. (2020) · Nature Reviews Immunology · doi:10.1038/s41577-020-0300-y · Cited by 163 · see citing works
The many faces of p53: something for everyone
Levine, A. J. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz026 · Cited by 163 · see citing works
Daver, N. G., Maiti, A., Kadia, T. M., Vyas, P., Majeti, R., Wei, A. H., Garcia‐Manero, G., Craddock, C., Sallman, D. A., & Kantarjian, H. M. (2022) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0332 · Cited by 173 · see citing works
Lo, W. M., Parkhurst, M. R., Robbins, P. F., Tran, E., Lu, Y., Jia, L., Gartner, J. J., Pasetto, A., Deniger, D. C., Malekzadeh, P., et al. (2019) · Cancer Immunology Research · doi:10.1158/2326-6066.cir-18-0686 · Cited by 156 · see citing works
Current developments of targeting the p53 signaling pathway for cancer treatment
Huang, J. L. (2020) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2020.107720 · Cited by 155 · see citing works
p53 and metabolism: from mechanism to therapeutics
Simabuco, F. M., Morale, M. G., Pavan, I. C. B., Morelli, A. P., Silva, F. R., & Tamura, R. E. (2018) · Oncotarget · doi:10.18632/oncotarget.25267 · Cited by 152 · see citing works
Polyamines: their significance for maintaining health and contributing to diseases
Xuan, M., Gu, X., Li, J., Huang, D., Chen, X., & He, Y. (2023) · Cell Communication and Signaling · doi:10.1186/s12964-023-01373-0 · Cited by 159 · see citing works
How mutations shape p53 interactions with the genome to promote tumorigenesis and drug resistance
Stiewe, T., & Haran, T. E. (2018) · Drug Resistance Updates · doi:10.1016/j.drup.2018.05.001 · Cited by 139 · see citing works
Understanding p53 functions through p53 antibodies
Sabapathy, K., & Lane, D. P. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz010 · Cited by 139 · see citing works
Self-citationKolb, D., Kolishetti, N., Surnar, B., Sarkar, S., Guin, S., Shah, A. S., & Dhar, S. (2020) · ACS Nano · doi:10.1021/acsnano.9b10037 · Cited by 137 · see citing works
Montalban-Bravo, G., Kanagal-Shamanna, R., Benton, C. B., Class, C. A., Chien, K. S., Sasaki, K., Naqvi, K., Alvarado, Y., Kadia, T. M., Ravandi, F., et al. (2020) · Blood Advances · doi:10.1182/bloodadvances.2019001101 · Cited by 133 · see citing works
p53 as a hub in cellular redox regulation and therapeutic target in cancer
Eriksson, S. E., Ceder, S., Bykov, V. J. N., & Wiman, K. G. (2019) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjz005 · Cited by 123 · see citing works
Emerging Roles of p53 Family Members in Glucose Metabolism
Itahana, Y., & Itahana, K. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19030776 · Cited by 120 · see citing works
Shi, L., Tian, H., Wang, P., Li, L., Zhang, Z., Zhang, J., & Zhao, Y. X. (2020) · Cellular and Molecular Immunology · doi:10.1038/s41423-019-0346-6 · Cited by 115 · see citing works
Best, S. A., Ding, S., Kersbergen, A., Dong, X., Song, J.-Y., Xie, Y., Reljic, B., Li, K., Vince, J. E., Rathi, V., et al. (2019) · Nature Communications · doi:10.1038/s41467-019-12164-y · Cited by 108 · see citing works
Boullosa, L. F., Loenhout, J. V., Flieswasser, T., Waele, J. D., Hermans, C., Lambrechts, H. A. J., Cuypers, B., Laukens, K., Bartholomeus, E., Siozopoulou, V., et al. (2021) · Redox Biology · doi:10.1016/j.redox.2021.101949 · Cited by 111 · see citing works
Acute Myeloid Leukemia: The Good, the Bad, and the Ugly
Kuykendall, A. T., Duployez, N., Boissel, N., Lancet, J. E., & Welch, J. S. (2018) · American Society of Clinical Oncology Educational Book · doi:10.1200/edbk_199519 · Cited by 111 · see citing works
Hassin, O., Nataraj, N. B., Shreberk‐Shaked, M., Aylon, Y., Yaeger, R. D., Fontemaggi, G., Mukherjee, S., Maddalena, M., Seligman, A., Iancu, O., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-30481-7 · Cited by 110 · see citing works
Current status and new treatment approaches in TP53 mutated AML
Hunter, A. M., & Sallman, D. A. (2019) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2019.05.004 · Cited by 102 · see citing works
Jin, S., Yang, X., Li, J., Yang, W., Ma, H., & Zhang, Z. (2019) · Molecular Cancer · doi:10.1186/s12943-019-0993-3 · Cited by 109 · see citing works
Yan, S., Yan, J., Liu, D., Li, X., Kang, Q., You, W., Zhang, J., Wang, L., Tian, Z., Lu, W., et al. (2021) · Theranostics · doi:10.7150/thno.59020 · Cited by 107 · see citing works
Gain-of-Function (GOF) Mutant p53 as Actionable Therapeutic Target
Schulz‐Heddergott, R., & Moll, U. M. (2018) · Cancers · doi:10.3390/cancers10060188 · Cited by 105 · see citing works
Uddin, M. B., Roy, K. R., Hosain, S. B., Khiste, S., Hill, R. A., Jois, S. D. S., Zhao, Y., Tackett, A. J., & Liu, Y. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.12.014 · Cited by 104 · see citing works
Strategies for targeting undruggable targets
Zhang, G., Zhang, J., Gao, Y., Li, Y., & Li, Y. (2021) · Expert Opinion on Drug Discovery · doi:10.1080/17460441.2021.1969359 · Cited by 102 · see citing works
The Interplay Between Tumor Suppressor p53 and Hypoxia Signaling Pathways in Cancer
Zhang, C., Liu, J., Wang, J., Zhang, T., Xu, D., Hu, W., & Feng, Z. (2021) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2021.648808 · Cited by 97 · see citing works
Cell fate regulation governed by p53: Friends or reversible foes in cancer therapy
Song, B., Yang, P., & Zhang, S. (2024) · 癌症:英文版 · doi:10.1002/cac2.12520 · Cited by 97 · see citing works
Huang, Y., Liu, N., Liu, J., Liu, Y., Zhang, C., Long, S., Luo, G., Zhang, L., & Zhang, Y. (2019) · Cell Cycle · doi:10.1080/15384101.2019.1688951 · Cited by 94 · see citing works
Heterogeneity of TP53 Mutations and P53 Protein Residual Function in Cancer: Does It Matter?
Monti, P., Menichini, P., Speciale, A., Cutrona, G., Fais, F., Taìana, E., Neri, A., Bomben, R., Gentile, M., Gattei, V., et al. (2020) · Frontiers in Oncology · doi:10.3389/fonc.2020.593383 · Cited by 92 · see citing works
Ding, Z., Pan, Y., Shang, T., Jiang, T., Lin, Y., Yang, C., Pang, S., Cui, X., Wang, Y., Feng, X., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-41852-z · Cited by 92 · see citing works
Sicari, D., Fantuz, M., Bellazzo, A., Valentino, E., Apollonio, M., Pontisso, I., Cristino, F. D., Ferro, M. D., Bicciato, S., Sal, G. D., et al. (2019) · Oncogene · doi:10.1038/s41388-019-0878-3 · Cited by 91 · see citing works
Drugging “undruggable” genes for cancer treatment: Are we making progress?
Duffy, M. J., & Crown, J. P. (2020) · International Journal of Cancer · doi:10.1002/ijc.33197 · Cited by 85 · see citing works
Canale, M., Andrikou, K., Priano, I., Cravero, P., Pasini, L., Urbini, M., Delmonte, A., Crinò, L., Bronte, G., & Ulivi, P. (2022) · Cancers · doi:10.3390/cancers14051143 · Cited by 93 · see citing works
Deep CRISPR mutagenesis characterizes the functional diversity of TP53 mutations
Funk, J. S., Klimovich, M., Drangenstein, D., Pielhoop, O., Hunold, P., Borowek, A., Noeparast, M., Pavlakis, E., Neumann, M. M., Balourdas, D.-I., et al. (2025) · Nature Genetics · doi:10.1038/s41588-024-02039-4 · Cited by 92 · see citing works
Targeting Therapies for the p53 Protein in Cancer Treatments
Levine, A. J. (2019) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-030518-055455 · Cited by 84 · see citing works
The Emerging Landscape of p53 Isoforms in Physiology, Cancer and Degenerative Diseases
Anbarasan, T., & Bourdon, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20246257 · Cited by 81 · see citing works
Pharmacological reactivation of p53 in the era of precision anticancer medicine
Tuval, A., Strandgren, C., Heldin, A., Palomar-Siles, M., & Wiman, K. G. (2023) · Nature Reviews Clinical Oncology · doi:10.1038/s41571-023-00842-2 · Cited by 84 · see citing works
Structural basis for oligoclonal T cell recognition of a shared p53 cancer neoantigen
Wu, D., Gallagher, D. T., Gowthaman, R., Pierce, B. G., & Mariuzza, R. A. (2020) · Nature Communications · doi:10.1038/s41467-020-16755-y · Cited by 77 · see citing works
The Role of p53 in Progression of Cutaneous Squamous Cell Carcinoma
Piipponen, M., Riihilä, P., Nissinen, L. M., & Kähäri, V. (2021) · Cancers · doi:10.3390/cancers13184507 · Cited by 79 · see citing works
Functions of p53 in pluripotent stem cells
Fu, X., Wu, S., Li, B., Xu, Y., & Liu, J. (2019) · Protein & Cell · doi:10.1007/s13238-019-00665-x · Cited by 78 · see citing works
Cancer Stemness: p53 at the Wheel
Ghatak, D., Ghosh, D. D., & Roychoudhury, S. (2021) · Frontiers in Oncology · doi:10.3389/fonc.2020.604124 · Cited by 75 · see citing works
The Mettl3 epitranscriptomic writer amplifies p53 stress responses
Raj, N., Wang, M., Seoane, J. A., Zhao, R. L., Kaiser, A. M., Moonie, N. A., Demeter, J., Boutelle, A. M., Kerr, C. H., Mulligan, A. S., et al. (2022) · Molecular Cell · doi:10.1016/j.molcel.2022.04.010 · Cited by 74 · see citing works
The ubiquitin ligase TRIM21 regulates mutant p53 accumulation and gain of function in cancer
Liu, J., Zhang, C., Xu, D., Zhang, T., Chang, C., Wang, J., Liu, J., Zhang, L., Haffty, B. G., Zong, W., et al. (2023) · Journal of Clinical Investigation · doi:10.1172/jci164354 · Cited by 74 · see citing works
Advanced Strategies for Therapeutic Targeting of Wild-Type and Mutant p53 in Cancer
Zhang, S., Carlsen, L., Borrero, L. J. H., Seyhan, A. A., Tian, X., & El‐Deiry, W. S. (2022) · Biomolecules · doi:10.3390/biom12040548 · Cited by 71 · see citing works
Turning chiral peptides into a racemic supraparticle to induce the self-degradation of MDM2
Yang, W., Liu, W., Li, X., Yan, J., & He, W. (2022) · Journal of Advanced Research · doi:10.1016/j.jare.2022.05.009 · Cited by 70 · see citing works
Computer-Aided Drug Discovery for Undruggable Targets
Sun, Q., Wang, H., Xie, J., Wang, L., Mu, J., Li, J., Ren, Y., & Lai, L. (2025) · Chemical Reviews · doi:10.1021/acs.chemrev.4c00969 · Cited by 69 · see citing works
Stockhammer, P., Grant, M. J., Wurtz, A., Foggetti, G., Expósito, F., Gu, J., Zhao, H., Choi, J., Chung, S. T., Li, F., et al. (2023) · Journal of Thoracic Oncology · doi:10.1016/j.jtho.2023.10.001 · Cited by 67 · see citing works
Patterns of mutations in TP53 mutated AML
Welch, J. S. (2018) · Best Practice & Research Clinical Haematology · doi:10.1016/j.beha.2018.09.010 · Cited by 67 · see citing works
Role of Dietary Antioxidants in p53‐Mediated Cancer Chemoprevention and Tumor Suppression
Merlin, J. P. J., Rupasinghe, H. P. V., Dellaire, G., & Murphy, K. (2021) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2021/9924328 · Cited by 68 · see citing works
Hároníková, L., Bonczek, O., Zatloukalová, P., Kokas, F. Z., Kucerikova, M., Coates, P. J., Fåhræus, R., & Vojtěšek, B. (2021) · Cellular & Molecular Biology Letters · doi:10.1186/s11658-021-00293-6 · Cited by 71 · see citing works
p53’s Extended Reach: The Mutant p53 Secretome
Pavlakis, E., & Stiewe, T. (2020) · Biomolecules · doi:10.3390/biom10020307 · Cited by 65 · see citing works
Ceramide Signaling and p53 Pathways
Jeffries, K. A., & Krupenko, N. I. (2018) · Advances in cancer research · doi:10.1016/bs.acr.2018.04.011 · Cited by 64 · see citing works
Triangular Relationship between p53, Autophagy, and Chemotherapy Resistance
Xu, J., Patel, N. H., & Gewirtz, D. A. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21238991 · Cited by 64 · see citing works
Structural and Drug Targeting Insights on Mutant p53
Gomes, A. S., Ramos, H., Inga, A., Sousa, E., & Saraiva, L. (2021) · Cancers · doi:10.3390/cancers13133344 · Cited by 63 · see citing works
A Balancing Act: p53 Activity from Tumor Suppression to Pathology and Therapeutic Implications
Wang, M., & Attardi, L. D. (2021) · Annual Review of Pathology Mechanisms of Disease · doi:10.1146/annurev-pathol-042320-025840 · Cited by 60 · see citing works
p53 partial loss-of-function mutations sensitize to chemotherapy
Klimovich, B., Merle, N., Neumann, M. M., Elmshäuser, S., Nist, A., Mernberger, M., Kazdal, D. N., Stenzinger, A., Timofeev, O. N., & Stiewe, T. (2021) · Oncogene · doi:10.1038/s41388-021-02141-5 · Cited by 61 · see citing works
Targeting mutant p53: a key player in breast cancer pathogenesis and beyond
Qayoom, H., Haq, B. U., Sofi, S., Jan, N., Jan, A., & Mir, M. A. (2024) · Cell Communication and Signaling · doi:10.1186/s12964-024-01863-9 · Cited by 66 · see citing works
Therapeutic effects of statins against lung adenocarcinoma via p53 mutant-mediated apoptosis
Chou, C.-W., Lin, C., Hsiao, T.-H., Lo, C.-C., Hsieh, C.-Y., Huang, C.-C., & Sher, Y. (2019) · Scientific Reports · doi:10.1038/s41598-019-56532-6 · Cited by 60 · see citing works
Structural diversity of p63 and p73 isoforms
Osterburg, C., & Dötsch, V. (2022) · Cell Death and Differentiation · doi:10.1038/s41418-022-00975-4 · Cited by 63 · see citing works
Deben, C., Deschoolmeester, V., Waele, J. D., Jacobs, J., den Bossche, J. V., Wouters, A., Peeters, M., Rolfo, C. D., Smits, E., Lardon, F., et al. (2018) · Cancers · doi:10.3390/cancers10040126 · Cited by 59 · see citing works
Song, H., Wu, J., Tang, Y., Dai, Y., Xiang, X., Li, Y., Wu, L., Wu, J., Liang, Y., Xing, Y., et al. (2023) · Science Translational Medicine · doi:10.1126/scitranslmed.abn9155 · Cited by 56 · see citing works
Li, S., Wang, A., Wu, Y., He, S., Wen, S., Zhao, M., Zhu, Y., Hu, X., Luo, Y., & Wang, G. (2023) · Immunological Reviews · doi:10.1111/imr.13274 · Cited by 57 · see citing works
Wild type- and mutant p53 proteins in mitochondrial dysfunction: emerging insights in cancer disease
Blandino, G., Valenti, F., Sacconi, A., & Agostino, S. D. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.05.011 · Cited by 59 · see citing works
Mutant p53 in cell-cell interactionsPreprint
Pilley, S. E., Rodríguez, T. A., & Vousden, K. H. (2021) · Genes & Development · doi:10.1101/gad.347542.120 · Cited by 54 · see citing works
ERK pathway agonism for cancer therapy: evidence, insights, and a target discovery framework
Timofeev, O. N., Giron, P., Lawo, S., Pichler, M., & Noeparast, A. (2024) · npj Precision Oncology · doi:10.1038/s41698-024-00554-5 · Cited by 59 · see citing works
T Cell Recognition of Tumor Neoantigens and Insights Into T Cell Immunotherapy
Sim, M. J. W., & Sun, P. D. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.833017 · Cited by 52 · see citing works
p53/MicroRNA-34 axis in cancer and beyond
Pan, W. D., Chai, B., Langping, L., Lü, Z., & Ma, Z. (2023) · Heliyon · doi:10.1016/j.heliyon.2023.e15155 · Cited by 52 · see citing works
Monoclonal Antibodies against Specific p53 Hotspot Mutants as Potential Tools for Precision Medicine
Hwang, L., Phang, B. H., Liew, O. W., Iqbal, J., Koh, X. H., Koh, X. Y., Othman, R., Xue, Y., Richards, M., Lane, D. P., et al. (2018) · Cell Reports · doi:10.1016/j.celrep.2017.11.112 · Cited by 52 · see citing works
Self-citationp53 Gain-of-Function Mutation Induces Metastasis via BRD4-Dependent CSF-1 Expression
Efe, G., Dunbar, K. J., Sugiura, K., Cunningham, K. M., Carcamo, S., Karaiskos, S., Tang, Q., Cruz‐Acuña, R., Resnick‐Silverman, L., Peura, J., et al. (2023) · Cancer Discovery · doi:10.1158/2159-8290.cd-23-0601 · Cited by 52 · see citing works
Cancer therapeutic targeting using mutant–p53-specific siRNAs
Ubby, I., Krueger, C., Rosato, R., Qian, W., Chang, J., & Sabapathy, K. (2019) · Oncogene · doi:10.1038/s41388-018-0652-y · Cited by 50 · see citing works
Self-citationThe role and mechanism of NAT10‐mediated ac4C modification in tumor development and progression
Gu, Z., Zou, L., Pan, X., Yu, Y., Liu, Y., Zhang, Z., Liu, J., Mao, S., Zhang, J., Guo, C., et al. (2024) · MedComm · doi:10.1002/mco2.70026 · Cited by 52 · see citing works
TP53 in Acute Myeloid Leukemia: Molecular Aspects and Patterns of Mutation
George, B., Kantarjian, H. M., Baran, N., Krocker, J. D., & Rios, A. A. (2021) · International Journal of Molecular Sciences · doi:10.3390/ijms221910782 · Cited by 50 · see citing works
The Tumor Microenvironment: Signal Transduction
Zhang, X., Ma, H., Gao, Y., Liang, Y., Du, Y., Hao, S., & Ni, T. (2024) · Biomolecules · doi:10.3390/biom14040438 · Cited by 55 · see citing works
Singh, S. P., Bhaskar, R., Ghosh, S., Yarlagadda, B., Singh, D. K. K., Verma, P., Sengupta, S., Mladenov, M. I., Hadzi‐Petrushev, N., Stojchevski, R., et al. (2025) · Cancers · doi:10.3390/cancers17071082 · Cited by 55 · see citing works
Lu, J., Ding, Y., Chen, Y., Jiang, J., Chen, Y., Huang, Y., Wu, M., Li, C., Kong, M., Zhao, W., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-24170-0 · Cited by 47 · see citing works
Bomben, R., Rossi, F. M., Vit, F., Bittolo, T., D’Agaro, T., Zucchetto, A., Tissino, E., Pozzo, F., Vendramini, E., Degan, M., et al. (2021) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-21-0701 · Cited by 48 · see citing works
Targeting Mutant p53 for Cancer Treatment: Moving Closer to Clinical Use?
Duffy, M. J., Tang, M., Rajaram, S., O’Grady, S., & Crown, J. P. (2022) · Cancers · doi:10.3390/cancers14184499 · Cited by 48 · see citing works
Chen, A. P., Kummar, S., Moore, N., Rubinstein, L., Zhao, Y., Williams, P. M., Palmisano, A., Sims, D., Coyne, G. O., Rosenberger, C. L., et al. (2021) · JCO Precision Oncology · doi:10.1200/po.20.00372 · Cited by 47 · see citing works
- Authors
- Sabapathy, K., & Lane, D. P.
- Affiliations
- National University of Singapore (SG)
- Agency for Science, Technology and Research (SG)
- Corresponding author
- Sabapathy, Kanaga
- Lane, David P.
- Venue
- Nature Reviews Clinical Oncology
- Published
- 2017-09-26
- Volume
- 15
- Issue
- 1
- Pages
- 13-30
- ISSN
- 1759-4774 (ISSN-L)
- 1759-4782
- OpenAlex
- W2759444489
- Cited by
- 517
- References
- 178
- Citations by year
- 2026: 40 · 2025: 67 · 2024: 74 · 2023: 89 · 2022: 57 · 2021: 64 · 2020: 53 · 2019: 41 · 2018: 26 · 2017: 3 · 2013: 1
- FWCI
- 3.53
- Type
- journal article
- Language
- en
- Open access
- closed
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Reviews Clinical Oncology (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Research Foundation Singapore
- National Medical Research Council
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › PI3K/AKT/mTOR signaling in cancer
- Health Sciences › Medicine › Pathology and Forensic Medicine › Cancer Mechanisms and Therapy
- Keywords
- TP53 mutation, mutant p53, p53-targeted therapy, tumour suppressor, cancer therapy resistance, prognostic factors
- MeSH terms
- Humans, Mutation, Neoplasms, Genes, p53
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