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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.
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“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]
Citations
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
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
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 5,218
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
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
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
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
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
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 2,456
Self-citationVousden, K. H., & Lane, D. P. (2007) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm2147 · Cited by 2,351
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
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
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 2,097
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
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
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
Linzer, D. I. H., & Levine, A. J. (1979) · Cell · doi:10.1016/0092-8674(79)90293-9 · Cited by 1,814
Muller, P. A. J., & Vousden, K. H. (2013) · Nature Cell Biology · doi:10.1038/ncb2641 · Cited by 1,647
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 1,454
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
Mutant p53: one name, many proteinsPreprint
Freed-Pastor, W. A., & Prives, C. L. (2012) · Genes & Development · doi:10.1101/gad.190678.112 · Cited by 1,290
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
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
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
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
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
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 1,037
Rivlin, N., Brosh, R., Oren, M., & Rotter, V. (2011) · Genes & Cancer · doi:10.1177/1947601911408889 · Cited by 1,033
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
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
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
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
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
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 815
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
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
Michalovitz, D., Halevy, O., & Oren, M. (1990) · Cell · doi:10.1016/0092-8674(90)90113-s · Cited by 769
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 760
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 742
Self-citationCooperation 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 734
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
DeLeo, 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
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 720
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 687
Vaseva, A. V., & Moll, U. M. (2008) · Biochimica et Biophysica Acta (BBA) - Bioenergetics · doi:10.1016/j.bbabio.2008.10.005 · Cited by 634
Milner, J., & Medcalf, E. (1991) · Cell · doi:10.1016/0092-8674(91)90384-b · Cited by 612
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 611
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 607
The expanding universe of p53 targets
Menendez, D., Inga, A., & Resnick, M. A. (2009) · Nature Reviews Cancer · doi:10.1038/nrc2730 · Cited by 568
The Differential Effects of Mutant p53 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
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 543
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
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
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
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
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 478
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 477
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
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
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 456
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
Structure–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 442
Blandino, G., Levine, A. J., & Oren, M. (1999) · Oncogene · doi:10.1038/sj.onc.1202314 · Cited by 439
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 439
Self-citationTumour-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
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 408
Self-citationLehmann, 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
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 398
Lavigueur, 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
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 377
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 370
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 363
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 359
Kress, M., May, E., Cassingena, R., & May, P. (1979) · Journal of Virology · doi:10.1128/jvi.31.2.472-483.1979 · Cited by 359
Zhou, G., Liu, Z., & Myers, J. N. (2016) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25592 · Cited by 355
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
Shaulian, E., Zauberman, A., Ginsberg, D., & Oren, M. (1992) · Molecular and Cellular Biology · doi:10.1128/mcb.12.12.5581 · Cited by 343
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 341
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
Li, D., Marchenko, N. D., & Moll, U. M. (2011) · Cell Death & Differentiation · doi:10.1038/cdd.2011.71 · Cited by 336
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 321
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
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
Yin, Y., Stephen, C. W., Luciani, M. G., & Fåhræus, R. (2002) · Nature Cell Biology · doi:10.1038/ncb801 · Cited by 305
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 301
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 299
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
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 293
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 290
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 286
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
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
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
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
Wolf, D., Harris, N., & Rotter, V. (1984) · Cell · doi:10.1016/0092-8674(84)90532-4 · Cited by 247
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
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 246
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
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 227
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 226
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
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
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
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
Bossi, G., Lapi, E., Strano, S., Rinaldo, C., Blandino, G., & Sacchi, A. (2005) · Oncogene · doi:10.1038/sj.onc.1209026 · Cited by 202
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
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 190
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 181
Screening thep53 status of human cell lines using a yeast functional assay
Jia, L., Osada, M., Ishioka, C., Gamo, M., Ikawa, S., Suzuki, T., Shimodaira, H., Niitani, T., Kudo, T., Akiyama, M., et al. (1997) · Molecular Carcinogenesis · doi:10.1002/(sici)1098-2744(199708)19:4 · Cited by 178
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 162
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
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
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 157
Salim, K. Y., Vareki, S. M., Danter, W. R., San‐Marina, S., & Koropatnick, J. D. (2016) · Oncotarget · doi:10.18632/oncotarget.9133 · Cited by 155
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
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 152
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
Vikhanskaya, F., Lee, M. K., Mazzoletti, M., Broggini, M., & Sabapathy, K. (2007) · Nucleic Acids Research · doi:10.1093/nar/gkm099 · Cited by 145
Self-citationDirect 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 145
Wang, 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
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
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 138
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 137
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 137
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
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 120
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
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
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 108
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 105
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 104
Self-citationAggarwal, 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
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
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 100
Xu, 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 98
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
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
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
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
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
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
North, S., Pluquet, O., Maurici, D., Ghissassi, F. E., & Hainaut, P. L. (2002) · Molecular Carcinogenesis · doi:10.1002/mc.10038 · Cited by 75
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
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
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
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
Tal, P., Eizenberger, S., Cohen, E., Goldfinger, N., Pietrokovski, S., Oren, M., & Rotter, V. (2016) · Oncotarget · doi:10.18632/oncotarget.7857 · Cited by 73
Kucab, J. E., Phillips, D. H., & Arlt, V. M. (2010) · FEBS Journal · doi:10.1111/j.1742-464x.2010.07676.x · Cited by 70
Ohki, R., Kawase, T., Ohta, T., Ichikawa, H., & Taya, Y. (2006) · Cancer Science · doi:10.1111/j.1349-7006.2006.00375.x · Cited by 64
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
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 62
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
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
Sun, Y., Dong, Z., Nakamura, K., & Colburn, N. H. (1993) · The FASEB Journal · doi:10.1096/fasebj.7.10.8344492 · Cited by 54
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
Kucab, J. E., Phillips, D. H., & Arlt, V. M. (2010) · FEBS Journal · doi:10.1111/j.1742-4658.2010.07676.x · Cited by 50
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
The Contrived Mutant p53 Oncogene – Beyond Loss of Functions
Sabapathy, K. (2015) · Frontiers in Oncology · doi:10.3389/fonc.2015.00276 · Cited by 45
Self-citationPrognostic 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
Assessing 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
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
Merino, D. M., & Malkin, D. M. (2014) · Sub-cellular biochemistry/Subcellular biochemistry · doi:10.1007/978-94-017-9211-0_1 · Cited by 39
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
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
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
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
Lee, M. K., & Sabapathy, K. (2008) · Journal of Cell Science · doi:10.1242/jcs.022822 · Cited by 31
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 31
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 30
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
Galea, C. A., Bowman, P., & Kriwacki, R. W. (2005) · Protein Science · doi:10.1110/ps.051622005 · Cited by 27
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
Role of tumor suppressor genes in transplacental lung carcinogenesis
Rollins, L. A., Leone‐Kabler, S., O’Sullivan, M. G., & Miller, M. S. (1998) · Molecular Carcinogenesis · doi:10.1002/(sici)1098-2744(199803)21:3 · Cited by 23
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
The application of gene therapy in China.
Peng, Z., Qing, Y., & Li, B. (2008) · PubMed · Cited by 19
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
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
Bromley, D., Bauer, M. R., Fersht, A. R., & Daggett, V. (2016) · Protein Engineering Design and Selection · doi:10.1093/protein/gzw035 · Cited by 16
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
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
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
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
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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
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 895
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 771
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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
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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
Metadata
- 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
- 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
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › 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
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