Mutational processes shape the landscape of TP53 mutations in human cancer
Open accessAbstract
Unlike most tumor suppressor genes, the most common genetic alterations in tumor protein p53 (TP53) are missense mutations 1,2. Mutant p53 protein is often abundantly expressed in cancers and specific allelic variants exhibit dominant-negative or gain-of-function activities in experimental models 3-8. To gain a systematic view of p53 function, we interrogated loss-of-function screens conducted in hundreds of human cancer cell lines and performed TP53 saturation mutagenesis screens in an isogenic pair of TP53 wild-type and null cell lines. We found that loss or dominant-negative inhibition of wild-type p53 function reliably enhanced cellular fitness. By integrating these data with the Catalog of Somatic Mutations in Cancer (COSMIC) mutational signatures database 9,10, we developed a statistical model that describes the TP53 mutational spectrum as a function of the baseline probability of acquiring each mutation and the fitness advantage conferred by attenuation of p53 activity. Collectively, these observations show that widely-acting and tissue-specific mutational processes combine with phenotypic selection to dictate the frequencies of recurrent TP53 mutations.
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
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?
TP53 was primarily mutated at known hotspots R175, R248, R273, and R282, or had nonsense or frameshift mutations.
“TP53 was primarily mutated at known hotspots R175, R248, R273, and R282 (refs. 59–61), or had nonsense or frameshift mutations”
From The origins and genetic interactions of KRAS mutations are allele- and tissue-specific (2021) · cites this paper as [59]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Cites
Integrative Analysis of Complex Cancer Genomics and Clinical Profiles Using the cBioPortal
Gao, J., Aksoy, B. A., Dogrusoz, U., Dresdner, G., Gross, B., Sumer, S. O., Sun, Y., Jacobsen, A., Sinha, R., Larsson, E., et al. (2013) · Science Signaling · doi:10.1126/scisignal.2004088 · Cited by 15,160 · see citing works
Signatures of mutational processes in human cancer
Initiative, A. P. C. G., Alexandrov, L. B., ICGC Breast Cancer Consortium, ICGC MMML-Seq Consortium, PedBrain, I., Nik-Zainal, S., Wedge, D. C., Aparicio, S. A. J. R., Behjati, S., Biankin, A. V., et al. (2013) · Nature · doi:10.1038/nature12477 · Cited by 9,660 · see citing works
Self-citationThe Cancer Cell Line Encyclopedia enables predictive modelling of anticancer drug sensitivity
Barretina, J., Caponigro, G., Stransky, N., Venkatesan, K., Margolin, A. A., Kim, S., Wilson, C. J., Lehár, J., Kryukov, G. V., Sonkin, D., et al. (2012) · Nature · doi:10.1038/nature11003 · Cited by 7,950 · see citing works
Self-citationIn 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
Defining a Cancer Dependency Map
Tsherniak, A., Vazquez, F., Montgomery, P. G., Weir, B. A., Kryukov, G., Cowley, G. S., Gill, S., Harrington, W. F., Pantel, S., Krill-Burger, J. M., et al. (2017) · Cell · doi:10.1016/j.cell.2017.06.010 · Cited by 3,276 · see citing works
Self-citationMomand, J., Zambetti, G. P., Olson, D. C., George, D., & Levine, A. J. (1992) · Cell · doi:10.1016/0092-8674(92)90644-r · Cited by 3,113 · see citing works
p53-dependent apoptosis modulates the cytotoxicity of anticancer agents
Lowe, S. W., Ruley, H. E., Jacks, T., & Housman, D. E. (1993) · Cell · doi:10.1016/0092-8674(93)90719-7 · Cited by 2,911 · see citing works
p53 is required for radiation-induced apoptosis in mouse thymocytes
Lowe, S. W., Schmitt, E. M., Smith, S. W., Osborne, B. A., & Jacks, T. (1993) · Nature · doi:10.1038/362847a0 · Cited by 2,864 · see citing works
Requirement for p53 and p21 to Sustain G <sub>2</sub> Arrest After DNA Damage
Bunz, F., Dutriaux, A., Lengauer, C., Waldman, T., Zhou, S., Brown, J. P., Sedivy, J. M., Kinzler, K. W., & Vogelstein, B. (1998) · Science · doi:10.1126/science.282.5393.1497 · Cited by 2,803 · see citing works
Systematic identification of genomic markers of drug sensitivity in cancer cells
Garnett, M. J., Edelman, E. J., Heidorn, S. J., Greenman, C. D., Dastur, A., Lau, K. W., Greninger, P., Thompson, I. R., Luo, X., Soares, J., et al. (2012) · Nature · doi:10.1038/nature11005 · Cited by 2,456 · see citing works
Easy quantitative assessment of genome editing by sequence trace decomposition
Brinkman, E. K., Chen, T., Amendola, M., & van Steensel, B. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku936 · Cited by 2,390 · see citing works
Thymocyte apoptosis induced by p53-dependent and independent pathways
Clarke, A. R., Purdie, C. A., Harrison, D. J., Morris, R. G., Bird, C. C., Hooper, M. L., & Wyllie, A. H. (1993) · Nature · doi:10.1038/362849a0 · Cited by 2,271 · see citing works
AACR Project GENIE: Powering Precision Medicine through an International Consortium
The AACR Project GENIE Consortium, The AACR Project GENIE Consortium, André, F., Arnedos, M., Baras, A. S., Baselga, J., Bedard, P. L., Berger, M. F., Bierkens, M., Calvo, F., et al. (2017) · Cancer Discovery · doi:10.1158/2159-8290.cd-17-0151 · Cited by 1,964 · see citing works
A role for sunlight in skin-cancer – UV-induced p53 mutations in squamous-cell carcinoma
Brash, D. E., Rudolph, J. A., Simon, J. A., Lin, A., McKenna, G. J., Baden, H. P., Halperin, A. J., & Pontén, J. (1991) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.88.22.10124 · Cited by 1,959 · see citing works
Meyers, R. M., Bryan, J. G., McFarland, J. M., Weir, B. A., Sizemore, A. E., Xu, H., Dharia, N. V., Montgomery, P. G., Cowley, G. S., Pantel, S., et al. (2017) · Nature Genetics · doi:10.1038/ng.3984 · Cited by 1,952 · see citing works
Self-citationZhang, Y., Xiong, Y., & Yarbrough, W. G. (1998) · Cell · doi:10.1016/s0092-8674(00)81401-4 · Cited by 1,626 · see citing works
Petitjean, A., Mathe, E., Kato, S., Ishioka, C., Tavtigian, S. V., Hainaut, P., & Olivier, M. (2007) · Human Mutation · doi:10.1002/humu.20495 · Cited by 1,598 · see citing works
Mutational hot spot in the p53 gene in human hepatocellular carcinomas
Hsu, I., Metcalf, R. A., Sun, T., Welsh, J. A., Wang, N. J., & Harris, C. C. (1991) · Nature · doi:10.1038/350427a0 · Cited by 1,533 · see citing works
Selective G to T mutations of p53 gene in hepatocellular carcinoma from southern Africa
Paillerets, B. B., Kew, M. C., Wands, J. R., & Öztürk, M. (1991) · Nature · doi:10.1038/350429a0 · Cited by 1,433 · 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
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
Sequential cancer mutations in cultured human intestinal stem cells
Drost, J., van Jaarsveld, R. H., Ponsioen, B., Zimberlin, C., van Boxtel, R., Buijs, A., Sachs, N., Overmeer, R. M., Offerhaus, G. J., Begthel, H., et al. (2015) · Nature · doi:10.1038/nature14415 · Cited by 1,067 · see citing works
Disruption of p53 in human cancer cells alters the responses to therapeutic agents.
Bunz, F., Hwang, P. M., Torrance, C., Waldman, T., Zhang, Y., Dillehay, L., Williams, J., Lengauer, C., Kinzler, K. W., & Vogelstein, B. (1999) · Journal of Clinical Investigation · doi:10.1172/jci6863 · Cited by 1,044 · see citing works
Mdm2 Is a RING Finger-dependent Ubiquitin Protein Ligase for Itself and p53
Fang, S., Jensen, J. P., Ludwig, R. L., Vousden, K. H., & Weissman, A. M. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.12.8945 · Cited by 1,044 · see citing works
Clock-like mutational processes in human somatic cells
Alexandrov, L. B., Jones, P. H., Wedge, D. C., Sale, J. E., Campbell, P. J., Nik‐Zainal, S., & Stratton, M. R. (2015) · Nature Genetics · doi:10.1038/ng.3441 · Cited by 1,038 · see citing works
Kato, S., Han, S., Liu, W., Otsuka, K., Shibata, H., Kanamaru, R., & Ishioka, C. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1431692100 · Cited by 877 · see citing works
Disruption of the ARF-Mdm2-p53 tumor suppressor pathway in Myc-induced lymphomagenesis
Eischen, C. M., Weber, J. D., Roussel, M. F., Sherr, C. J., & Cleveland, J. L. (1999) · Genes & Development · doi:10.1101/gad.13.20.2658 · Cited by 819 · see citing works
Harnessing Connectivity in a Large-Scale Small-Molecule Sensitivity Dataset
Seashore-Ludlow, B., Rees, M. G., Cheah, J. H., Cokol, M., Price, E. V., Coletti, M. E., Jones, V., Bodycombe, N. E., Soule, C. K., Gould, J., et al. (2015) · Cancer Discovery · doi:10.1158/2159-8290.cd-15-0235 · Cited by 813 · 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
5-Methylcytosine as an Endogenous Mutagen in the Human LDL Receptor and p53 Genes
Rideout, W. M., Coetzee, G. A., Olumi, A. F., & Jones, P. A. (1990) · Science · doi:10.1126/science.1697983 · Cited by 640 · see citing works
Milner, J., & Medcalf, E. (1991) · Cell · doi:10.1016/0092-8674(91)90384-b · Cited by 612 · see citing works
Aguilar, F., Hussain, S. P., & Cerutti, P. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.18.8586 · Cited by 490 · see citing works
Rapid ATM-dependent phosphorylation of MDM2 precedes p53 accumulation in response to DNA damage
Khosravi, R., Maya, R., Gottlieb, T., Oren, M., Shiloh, Y., & Shkedy, D. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.26.14973 · Cited by 461 · see citing works
Cowley, G., Weir, B., Vazquez, F., Tamayo, P., Scott, J. A., Rusin, S., East-Seletsky, A., Ali, L., Gerath, W. F. J., Pantel, S., et al. (2014) · Scientific Data · doi:10.1038/sdata.2014.35 · Cited by 398 · see citing works
Self-citationMathé, E. A. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkj518 · Cited by 340 · see citing works
The p53 protein is an unusually shaped tetramer that binds directly to DNA.
Friedman, P. N., Chen, X., Bargonetti, J., & Prives, C. L. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.8.3319 · Cited by 264 · see citing works
Puisieux, A., Lim, S.-K., Groopman, J. D., & Öztürk, M. (1991) · PubMed · Cited by 260 · see citing works
Somatic TP53 Mutations in the Era of Genome SequencingPreprint
Hainaut, P. L., & Pfeifer, G. P. (2016) · Cold Spring Harbor Perspectives in Medicine · doi:10.1101/cshperspect.a026179 · Cited by 247 · see citing works
A Noncommercial Dual Luciferase Enzyme Assay System for Reporter Gene Analysis
Dyer, B. W., Ferrer, F. A., Klinedinst, D. K., & Rodríguez, R. (2000) · Analytical Biochemistry · doi:10.1006/abio.2000.4605 · Cited by 238 · see citing works
Harvey, M., Vogel, H. S., Morris, D. K., Bradley, A., Bernstein, A., & Donehower, L. A. (1995) · Nature Genetics · doi:10.1038/ng0395-305 · Cited by 228 · see citing works
Prospective functional classification of all possible missense variants in PPARG
UK Monogenic Diabetes Consortium, Majithia, A. R., Myocardial Infarction Genetics Consortium, UK Congenital Lipodystrophy Consortium, Tsuda, B., Agostini, M., Gnanapradeepan, K., Rice, R., Peloso, G., Patel, K. A., et al. (2016) · Nature Genetics · doi:10.1038/ng.3700 · Cited by 227 · see citing works
Self-citationOncogenic ras activates the ARF-p53 pathway to suppress epithelial cell transformation
Lin, A. W., & Lowe, S. W. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.091100298 · Cited by 213 · see citing works
Targeted point mutations of p53 lead to dominant-negative inhibition of wild-type p53 function
de Vries, A., Flores, E. R., Miranda, B., Hsieh, H.-M., van Oostrom, C. T. M., Sage, J., & Jacks, T. (2002) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.052713099 · Cited by 207 · see citing works
Comprehensive mutational scanning of a kinase in vivo reveals substrate-dependent fitness landscapes
Melnikov, A., Rogov, P., Wang, L., Gnirke, A., & Mikkelsen, T. S. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku511 · Cited by 177 · see citing works
p53 Domains: Structure, Oligomerization, and Transformation
Wang, P., Reed, M. J., Wang, Y., Mayr, G. A., Stenger, J. E., Anderson, M. E., Schwedes, J. F., & Tegtmeyer, P. (1994) · Molecular and Cellular Biology · doi:10.1128/mcb.14.8.5182-5191.1994 · Cited by 161 · see citing works
Phenotypic Characterization of a Comprehensive Set of MAPK1/ERK2 Missense Mutants
Brenan, L., Andreev, A., Cohen, O., Pantel, S., Kamburov, A., Cacchiarelli, D., Persky, N. S., Zhu, C., Bagul, M., Goetz, E. M., et al. (2016) · Cell Reports · doi:10.1016/j.celrep.2016.09.061 · Cited by 159 · see citing works
Self-citationTornaletti, S., Rozek, D., & Pfeifer, G. P. (1993) · PubMed · Cited by 151 · see citing works
Mutations in the p53 tumor suppressor gene in human cutaneous squamous cell carcinomas
Pierceall, W. E., Mukhopadhyay, T. K., Goldberg, L. H., & Ananthaswamy, H. N. (1991) · Molecular Carcinogenesis · doi:10.1002/mc.2940040606 · Cited by 123 · see citing works
p53 Promotes Cell Survival due to the Reversibility of Its Cell-Cycle Checkpoints
Lukin, D. J., Carvajal, L. A., Liu, W.-J., Resnick‐Silverman, L., & Manfredi, J. J. (2014) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-14-0177 · Cited by 86 · see citing works
A distinct p53 target gene set predicts for response to the selective p53–HDM2 inhibitor NVP-CGM097
Jeay, S., Gaulis, S., Ferretti, S., Bitter, H., Ito, M., Valat, T., Murakami, M., Ruetz, S., Guthy, D. A., Rynn, C., et al. (2015) · eLife · doi:10.7554/elife.06498 · Cited by 85 · see citing works
Bennett, R. P., Cox, C. A., & Hoeffler, J. P. (1998) · BioTechniques · doi:10.2144/98243pf01 · Cited by 29 · 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
Disease variant prediction with deep generative models of evolutionary data
Frazer, J., Notin, P., Dias, M., Gomez, A., Min, J. K., Brock, K., Gal, Y., & Marks, D. S. (2021) · Nature · doi:10.1038/s41586-021-04043-8 · Cited by 791 · see citing works
Bernard, E., Nannya, Y., Hasserjian, R. P., Devlin, S. M., Tuechler, H., Medina-Martinez, J. S., Yoshizato, T., Shiozawa, Y., Saiki, R., Malcovati, L., et al. (2020) · Nature Medicine · doi:10.1038/s41591-020-1008-z · Cited by 648 · see citing works
Sequence modeling and design from molecular to genome scale with Evo
Nguyen, E., Poli, M., Durrant, M. G., Kang, B., Katrekar, D., Li, D. B., Bartie, L. J., Thomas, A. W., King, S. H., Brixi, G., et al. (2024) · Science · doi:10.1126/science.ado9336 · Cited by 580 · see citing works
WRN helicase is a synthetic lethal target in microsatellite unstable cancers
Chan, E. M., Shibue, T., McFarland, J. M., Gaeta, B., Ghandi, M., Dumont, N., Gonzalez, A., McPartlan, J. S., Li, T., Zhang, Y., et al. (2019) · Nature · doi:10.1038/s41586-019-1102-x · Cited by 458 · see citing works
Self-citationTakeda, D. Y., Spisák, S., Seo, J.-H., Bell, C., O’Connor, E., Korthauer, K., Ribli, D., Csabai, I., Solymosi, N., Szállási, Z., et al. (2018) · Cell · doi:10.1016/j.cell.2018.05.037 · Cited by 317 · see citing works
Self-citationCas9 activates the p53 pathway and selects for p53-inactivating mutations
Enache, O. M., Rendo, V., Abdusamad, M., Lam, D., Davison, D., Pal, S., Currimjee, N., Hess, J., Pantel, S., Nag, A., et al. (2020) · Nature Genetics · doi:10.1038/s41588-020-0623-4 · Cited by 285 · see citing works
Self-citationThe origins and genetic interactions of KRAS mutations are allele- and tissue-specific
Cook, J. H., Melloni, G. E. M., Gulhan, D. C., Park, P. J., & Haigis, K. M. (2021) · Nature Communications · doi:10.1038/s41467-021-22125-z · Cited by 208 · see citing works
Selective USP7 inhibition elicits cancer cell killing through a p53-dependent mechanism.
Schauer, N. J., Liu, X., Magin, R. S., Doherty, L. M., Chan, W. C., Ficarro, S. B., Hu, W., Roberts, R. M., Iacob, R. E., Stolte, B., et al. (2020) · Scientific Reports · doi:10.1038/s41598-020-62076-x · Cited by 125 · see citing works
Self-citationSuiter, C. C., Moriyama, T., Matreyek, K. A., Yang, W., Scaletti, E. R., Nishii, R., Yang, W., Hoshitsuki, K., Singh, M., Trehan, A., et al. (2020) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1915680117 · Cited by 121 · see citing works
Predicting the pathogenicity of missense variants using features derived from AlphaFold2
Schmidt, A., Röner, S., Mai, K., Klinkhammer, H., Kircher, M., & Ludwig, K. U. (2023) · Bioinformatics · doi:10.1093/bioinformatics/btad280 · Cited by 79 · see citing works
Badonyi, M., & Marsh, J. A. (2025) · Nature Communications · doi:10.1038/s41467-025-63234-3 · Cited by 19 · see citing works
“Weidenti fi edsixMAVEsin which at least two of the aforementioned molecular disease mechanisms, or functional consequences in the case of HyC variants, have been con fi dently detected in the same gene: TP53 30 , HRAS 27 , MC4R 28 , HMBS 29 , TP53 30 , PTPN11 31 , and MTHFR 32 .”
InfluentialAre <i>TP53</i> mutations all alike?
Wong, T. N., & Link, D. C. (2024) · Hematology · doi:10.1182/hematology.2024000556 · Cited by 11 · see citing works
- Authors
- Giacomelli, A. O., Yang, X., Lintner, R. E., McFarland, J. M., Duby, M., Kim, J., Howard, T. P., Takeda, D. Y., Ly, S. H., Kim, E., Gannon, H. S., Hurhula, B., Sharpe, T., Goodale, A., Fritchman, B., Steelman, S., Vazquez, F., Tsherniak, A., Aguirre, A. J., Doench, J. G., Piccioni, F., Roberts, C. W. M., Meyerson, M., Getz, G., Johannessen, C. M., Root, D. E., & Hahn, W. C.
- Affiliations
- Broad Institute (US)
- St. Jude Children's Research Hospital (US)
- Corresponding author
- Hahn, William C.
- ORCID
- Giacomelli, Andrew O.
- Yang, Xiaoping
- Lintner, Robert E.
- McFarland, James M.
- Duby, Marc
- Kim, Jaegil
- Howard, Thomas P.
- Takeda, David Y.
- Kim, Eejung
- Gannon, Hugh S.
- Goodale, Amy
- Vazquez, Francisca
- Tsherniak, Aviad
- Aguirre, Andrew J.
- Doench, John G.
- Piccioni, Federica
- Roberts, Charles W. M.
- Meyerson, Matthew
- Getz, Gad
- Johannessen, Cory M.
- Root, David E.
- Hahn, William C.
- Venue
- Nature Genetics
- Published
- 2018-09-17
- Volume
- 50
- Issue
- 10
- Pages
- 1381-1387
- ISSN
- 1061-4036 (ISSN-L)
- 1546-1718
- PMC
- PMC6168352
- OpenAlex
- W2891731267
- Cited by
- 556
- References
- 52
- Citations by year
- 2026: 63 · 2025: 88 · 2024: 100 · 2023: 75 · 2022: 60 · 2021: 76 · 2020: 53 · 2019: 37 · 2018: 2
- FWCI
- 15.64
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Licence
- www.springer.com/tdm (tdm)
- Locations
- Nature Genetics (publishedVersion)
- PubMed (publishedVersion)
- Europe PMC (PubMed Central) (acceptedVersion)
- PubMed Central (acceptedVersion)
- Funders
- Massachusetts General Hospital
- Broad Institute
- Nature
- National Institutes of Health (UL1TR001102)
- National Cancer Institute (U01CA176058, U01CA199253, K08CA218420)
- National Institute of General Medical Sciences (T32GM007753, T32GM007226)
- National Center for Advancing Translational Sciences
- Topics
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Cancer Genomics and Diagnostics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Chromatin Remodeling and Cancer
- Keywords
- TP53 mutation, mutational signatures, mutational processes, loss-of-function screen, saturation mutagenesis, dominant-negative p53, tumor suppressor, somatic mutations, cell fitness, phenotypic selection, COSMIC, cancer cell lines
- MeSH terms
- A549 Cells, Alleles, Cells, Cultured, DNA Mutational Analysis, Humans, Mutation, Neoplasms, Tumor Suppressor Protein p53, Mutagenesis, Sequence Analysis, DNA, Databases, Genetic, High-Throughput Nucleotide Sequencing, CRISPR-Cas Systems
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
