CIP2A interacts with TopBP1 and is selectively essential for DNA damage-induced basal-like breast cancer tumorigenesis
Open accessPublished version of a preprint
Abstract
Despite saturated genetic profiling of breast cancers, oncogenic drivers for the clinically challenging basal-like breast cancer (BLBC) subtype are still poorly understood. Here, we demonstrate that CIP2A is selectively essential for DNA damage-induced initiation of mouse BLBC tumors, but not of other cancer types. Mechanistically, CIP2A was discovered genome-widely the closest functional homologue for DNA-damage proteins TopBP1, RHNO, POLQ, NBN and PARP1. CIP2A directly interacts with the ATR-activation domain of TopBP1, and dampens both, chromatin binding of TopBP1 and RAD51, and G2/M checkpoint in DNA-damaged cells. CIP2A also drives BLBC-associated proliferative MYC and E2F1 signaling. Consistently with high DNA-damage response activity BLBCs, and CIP2A’s novel role in checkpoint signaling, CIP2A was found essential for DNA-damaged, and BRCA-mutant BLBC cells. Selective role for CIP2A as BLBC driver was supported by association of high CIP2A expression with poor patient prognosis only in BLBC, but not in other breast cancer types. Therapeutically, small molecule reactivators of PP2A (SMAPs) phenocopy CIP2A-dependent DNA damage response, and inhibit in vivo growth of patient-derived BLBC xenograft. In summary, we discover sub-type selective essential role for CIP2A in BLBC initiation and maintenance that can be explained by its newly discovered association with DNA-damage response, coordinated with regulation of proliferative signaling. The results also identify therapeutic strategy for CIP2A-dependent BLBCs.
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?
CIP2A is widely over-expressed in different human cancer types.
“Of these, CIP2A is widely over-expressed in different human cancer types and drives tumour growth both in xenograft and transgenic mouse models18–24.”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [24]
The human BLBC results (p. 7) report high CIP2A expression in basal-like breast cancer, and the Discussion (p. 10) describes CIP2A overexpression in BLBC. These passages do not establish that CIP2A is widely overexpressed across different human cancer types; the Discussion distinguishes its BLBC findings from earlier assumptions about involvement in multiple solid cancers. (LLM, conf=0.82)
Experimental — accuracy not yet measuredCIP2A drives tumour growth in xenograft and transgenic mouse models.
“Of these, CIP2A is widely over-expressed in different human cancer types and drives tumour growth both in xenograft and transgenic mouse models18–24.”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [24]
The Introduction (p. 2) says CIP2A is essential for initiating basal-like breast tumors in transgenic mouse models, supporting the mouse-model part of the claim. Our copy does not report xenograft tumor growth, and its finding concerns tumor initiation in a specific breast cancer subtype rather than tumor growth generally (Introduction, p. 2; Figure 5, p. 9). (LLM, conf=0.86)
Experimental — accuracy not yet measuredTargeting of the head domain is an efficient strategy to block malignant growth of CIP2A-driven TNBC cells.
“They also identify targeting of the head domain as an efficient strategy to block malignant growth of CIP2A-driven TNBC cells24 (Fig. 3K).”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [24]
The Results section, “Transcriptional CIP2A targeting by SMAPs as potential BLBC therapy” (page unavailable), reports reduced viability in basal-like TNBC cell lines and reduced growth of a basal-like breast cancer xenograft after treatment. It does not identify the CIP2A head domain as the target or show that targeting that domain caused the growth inhibition. (LLM, conf=0.88)
Experimental — accuracy not yet measuredMISIIR-TAg mice with wild-type and homozygous CIP2A deficiency show similar ovarian tumor development.
“we reported recently that there is no difference in OvCa tumorigenesis between MISIIR-TAg X CIP2AWT and MISIIR-TAg X CIP2AHOZ mice (17)(Fig. 2E).”
From Ovarian Cancers with Low CIP2A Tumor Expression Constitute an APR-246–Sensitive Disease Subtype (2022) · cites this paper as [17]
CIP2A is a central DNA damage response protein essential for BRCA-mutated triple-negative breast cancer cells.
“However, recent identification of CIP2A as a central DNA damage response (DDR) protein essential for BRCA-mutated triple-negative breast cancer (TNBC) cells24,26, indicates that CIP2A has broader role in cancer beyond MYC regulation.”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [24]
There is no difference in ovarian cancer tumorigenesis between MISIIR-TAg X CIP2A WT and MISIIR-TAg X CIP2A HOZ mice.
“Consistent with human data that OvCa tumors may develop in CIP2A-independent manner (Table S1), we reported recently that there is no difference in OvCa tumorigenesis between MISIIR-TAg X CIP2A WT and MISIIR-TAg X CIP2A HOZ mice (24)(Fig.2E).”
From Ovarian cancers with low CIP2A tumor expression constitute an APR-246 sensitive disease subtype (2021) · cites this paper as [24]
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
Lehmann, B. D., Bauer, J. A., Chen, X., Sanders, M. E., Chakravarthy, A. B., Shyr, Y., & Pietenpol, J. A. (2011) · Journal of Clinical Investigation · doi:10.1172/jci45014 · Cited by 5,592 · see citing works
Improved vectors and genome-wide libraries for CRISPR screening
Sanjana, N. E., Shalem, O., & Zhang, F. (2014) · Nature Methods · doi:10.1038/nmeth.3047 · Cited by 5,239 · see citing works
Genome-scale CRISPR-Cas9 knockout screening in human cells
Shalem, O., Sanjana, N. E., Hartenian, E., Shi, X., Scott, D. A., Mikkelsen, T. S., Heckl, D., Ebert, B. L., Root, D. E., Doench, J. G., et al. (2014) · Science · doi:10.1126/science.1247005 · Cited by 5,234 · see citing works
CellProfiler: image analysis software for identifying and quantifying cell phenotypes
Carpenter, A. E., Jones, T. R., Lamprecht, M. R., Clarke, C., Kang, I. H., Friman, O., Guertin, D. A., Chang, J. H., Lindquist, R. A., Moffat, J., et al. (2006) · Genome biology · doi:10.1186/gb-2006-7-10-r100 · Cited by 5,077 · see citing works
Next-generation characterization of the Cancer Cell Line Encyclopedia
Ghandi, M., Huang, F. W., Jané-Valbuena, J., Kryukov, G. V., Lo, C. C., McDonald, E. R., Barretina, J., Gelfand, E. T., Bielski, C. M., Li, H., et al. (2019) · Nature · doi:10.1038/s41586-019-1186-3 · Cited by 3,394 · see citing works
Cancer Susceptibility and the Functions of BRCA1 and BRCA2
Venkitaraman, A. R. (2002) · Cell · doi:10.1016/s0092-8674(02)00615-3 · Cited by 1,713 · see citing works
Basal-Like Breast Cancer: A Critical Review
Rakha, E. A., Reis-Filho, J. S., & Ellis, I. O. (2008) · Journal of Clinical Oncology · doi:10.1200/jco.2007.13.1748 · Cited by 1,164 · see citing works
Homologous-recombination-deficient tumours are dependent on Polθ-mediated repair
Ceccaldi, R., Liu, J., Amunugama, R., Hajdú, I., Primack, B., Petalcorin, M. I. R., O’Connor, K. W., Konstantinopoulos, P. A., Elledge, S. J., Boulton, S. J., et al. (2015) · Nature · doi:10.1038/nature14184 · Cited by 914 · see citing works
Molecular alterations in triple-negative breast cancer—the road to new treatment strategies
Denkert, C., Liedtke, C., Tutt, A. N. J., & von Minckwitz, G. (2016) · The Lancet · doi:10.1016/s0140-6736(16)32454-0 · Cited by 875 · see citing works
Gene essentiality and synthetic lethality in haploid human cells
Blomen, V. A., Májek, P., Jae, L. T., Bigenzahn, J. W., Nieuwenhuis, J., Staring, J., Sacco, R., van Diemen, F. R., Olk, N., Stukalov, A., et al. (2015) · Science · doi:10.1126/science.aac7557 · Cited by 857 · see citing works
Checking on DNA damage in S phase
Bartek, J., Lukas, C., & Lukas, J. (2004) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm1493 · Cited by 758 · see citing works
ColonyArea: An ImageJ Plugin to Automatically Quantify Colony Formation in Clonogenic Assays
Guzmán, C., Bagga, M., Kaur, A., Westermarck, J. K., & Abankwa, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0092444 · Cited by 720 · see citing works
Self-citationCIP2A inhibits PP2A in human malignancies
Junttila, M. R., Puustinen, P., Niemelä, M., Ahola, R., Arnold, H., Böttzauw, T., Ala-aho, R., Nielsen, C., Ivaska, J., Taya, Y., et al. (2007) · Cell · doi:10.1016/j.cell.2007.04.044 · Cited by 677 · see citing works
Self-citationA Compendium of Mutational Signatures of Environmental Agents
Kucab, J. E., Zou, X., Morganella, S., Joel, M., Nanda, A. S., Nagy, E., Gomez, C., Degasperi, A., Harris, R., Jackson, S. P., et al. (2019) · Cell · doi:10.1016/j.cell.2019.03.001 · Cited by 660 · see citing works
Derksen, P. W. B., Liu, X., Saridin, F., van der Gulden, H., Zevenhoven, J., Evers, B., van Beijnum, J. R., Griffioen, A. W., Vink, J., Krimpenfort, P., et al. (2006) · Cancer Cell · doi:10.1016/j.ccr.2006.09.013 · Cited by 591 · see citing works
Species- and cell type-specific requirements for cellular transformation
Rangarajan, A., Hong, S. J., Gifford, A., & Weinberg, R. A. (2004) · Cancer Cell · doi:10.1016/j.ccr.2004.07.009 · Cited by 555 · see citing works
γ-H2AX Dephosphorylation by Protein Phosphatase 2A Facilitates DNA Double-Strand Break Repair
Chowdhury, D., Keogh, M., Ishii, H., Peterson, C. L., Buratowski, S., & Lieberman, J. (2005) · Molecular Cell · doi:10.1016/j.molcel.2005.10.003 · Cited by 549 · see citing works
Loss of p53 triggers WNT-dependent systemic inflammation to drive breast cancer metastasis
Wellenstein, M. D., Coffelt, S. B., Duits, D. E. M., van Miltenburg, M. H., Slagter, M., de Rink, I., Henneman, L., Kas, S. M., Prekovic, S., Hau, C.-S., et al. (2019) · Nature · doi:10.1038/s41586-019-1450-6 · Cited by 500 · see citing works
Liu, X., Holstege, H. H., van der Gulden, H. M. L., Treur-Mulder, M., Zevenhoven, J., Velds, A., Kerkhoven, R. M., van Vliet, M. H., Wessels, L. F. A., Peterse, J. L., et al. (2007) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0702969104 · Cited by 474 · see citing works
The consequences of Rad51 overexpression for normal and tumor cells
Klein, H. L. (2008) · DNA repair · doi:10.1016/j.dnarep.2007.12.008 · Cited by 357 · see citing works
Connolly, D. C., Bao, R., Nikitin, A. Y., Stephens, K. C., Poole, T. W., Xiang, H., Harris, S. S., Vanderhyden, B. C., & Hamilton, T. C. (2003) · PubMed · Cited by 311 · see citing works
Self-citationChopra, N., Tovey, H., Pearson, A., Cutts, R., Toms, C., Proszek, P., Hubank, M. J. F., Dowsett, M., Dodson, A. R., Daley, F. M., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-16142-7 · Cited by 261 · see citing works
Cotta‐Ramusino, C., McDonald, E. R., Hurov, K. E., Sowa, M. E., Harper, J. W., & Elledge, S. J. (2011) · Science · doi:10.1126/science.1203430 · Cited by 221 · see citing works
CIP2A Is Associated with Human Breast Cancer Aggressivity
Côme, C., Laine, A., Chanrion, M., Edgren, H., Mattila, E., Liu, X., Jonkers, J., Ivaska, J., Isola, J., Darbon, J.-M., et al. (2009) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-08-3283 · Cited by 221 · see citing works
Self-citationActivation of tumor suppressor protein PP2A inhibits KRAS-driven tumor growth
Sangodkar, J., Perl, A., Tohme, R., Kiselar, J., Kastrinsky, D. B., Zaware, N., Izadmehr, S., Mazhar, S., Wiredja, D. D., O’Connor, C. M., et al. (2017) · Journal of Clinical Investigation · doi:10.1172/jci89548 · Cited by 196 · see citing works
Self-citationTargeting c-MYC by antagonizing PP2A inhibitors in breast cancer
Janghorban, M., Farrell, A. S., Allen-Petersen, B. L., Pelz, C., Daniel, C. J., Oddo, J., Langer, E. M., Christensen, D. J., & Sears, R. C. (2014) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1317630111 · Cited by 186 · see citing works
MYC-Dependent Regulation and Prognostic Role of CIP2A in Gastric Cancer
Khanna, A., Böckelman, C., Hemmes, A., Junttila, M. R., Wiksten, J.-P., Lundin, M., Junnila, S., Murphy, D. J., Evan, G. I., Haglund, C., et al. (2009) · JNCI: Journal of the National Cancer Institute · doi:10.1093/jnci/djp103 · Cited by 185 · see citing works
Self-citationClaspin Operates Downstream of TopBP1 To Direct ATR Signaling towards Chk1 Activation
Liu, S., Bekker‐Jensen, S., Mailand, N., Lukas, C., Bártek, J., & Lukas, J. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00492-06 · Cited by 184 · see citing works
Selective PP2A enhancement through biased heterotrimer stabilization
Leonard, D., Huang, W., Izadmehr, S., O’Connor, C. M., Wiredja, D. D., Wang, Z., Zaware, N., Chen, Y., Schlatzer, D. M., Kiselar, J., et al. (2020) · Cell · doi:10.1016/j.cell.2020.03.038 · Cited by 176 · cited 10× · see citing works
“Similar to other in vivo studies 479 with SMAPs (14,46,47), we did not observe any treatment-related adverse effects in mice.”
InfluentialSelf-citationMechanisms of Genomic Instability in Breast Cancer
Duijf, P. H. G., Nanayakkara, D. M., Nones, K., Srihari, S., Kalimutho, M., & Khanna, K. K. (2019) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2019.04.004 · Cited by 168 · see citing works
A Role for the MRN Complex in ATR Activation via TOPBP1 Recruitment
Duursma, A. M., Driscoll, R., Elias, J. E., & Cimprich, K. A. (2013) · Molecular Cell · doi:10.1016/j.molcel.2013.03.006 · Cited by 153 · see citing works
PP2A inhibition is a druggable MEK inhibitor resistance mechanism in KRAS-mutant lung cancer cells
Kauko, O., O’Connor, C. M., Kulesskiy, E., Sangodkar, J., Aakula, A., Izadmehr, S., Yetukuri, L., Yadav, B., Padzik, A., Laajala, T. D., et al. (2018) · Science Translational Medicine · doi:10.1126/scitranslmed.aaq1093 · Cited by 149 · see citing works
Self-citationFission yeast cut mutations revisited: control of anaphase
Yanagida, M. (1998) · Trends in Cell Biology · doi:10.1016/s0962-8924(98)01236-7 · Cited by 139 · see citing works
MDC1 Interacts with TOPBP1 to Maintain Chromosomal Stability during Mitosis
Leimbacher, P.-A., Jones, S. E., Shorrocks, A.-M. K., Zompit, M. D. M., Day, M. W., Blaauwendraad, J., Bundschuh, D., Bonham, S., Fischer, R., Fink, D. A., et al. (2019) · Molecular Cell · doi:10.1016/j.molcel.2019.02.014 · Cited by 136 · see citing works
Genetic screens in isogenic mammalian cell lines without single cell cloning
DeWeirdt, P. C., Sangree, A. K., Hanna, R. E., Sanson, K. R., Hegde, M., Strand, C., Persky, N. S., & Doench, J. G. (2020) · Nature Communications · doi:10.1038/s41467-020-14620-6 · Cited by 133 · see citing works
Laine, A., Sihto, H., Come, C., Rosenfeldt, M. T., Zwolinska, A., Niemelä, M., Khanna, A., Chan, E. K., Kähäri, V.-M., Kellokumpu-Lehtinen, P.-L., et al. (2013) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0292 · Cited by 130 · see citing works
Self-citationPPAR influences susceptibility to DMBA-induced mammary, ovarian and skin carcinogenesis
Nicol, C. J. B. (2004) · Carcinogenesis · doi:10.1093/carcin/bgh160 · Cited by 120 · see citing works
KDM4 Inhibition Targets Breast Cancer Stem–like Cells
Metzger, E., Stepputtis, S. S., Strietz, J., Preca, B., Urban, S., Willmann, D., Allen, A., Zenk, F. L., Iovino, N., Bronsert, P., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-17-1754 · Cited by 112 · see citing works
Self-citationNon-genomic mechanisms of protein phosphatase 2A (PP2A) regulation in cancer
Kauko, O., & Westermarck, J. (2018) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2018.01.005 · Cited by 111 · see citing works
Self-citationVainonen, J. P., Momeny, M., & Westermarck, J. K. (2021) · Science Translational Medicine · doi:10.1126/scitranslmed.abe2967 · Cited by 105 · see citing works
Self-citationA consensus set of genetic vulnerabilities to ATR inhibition
Hustedt, N., Álvarez-Quilón, A., McEwan, A., Yuan, J. Y., Cho, T., Koob, L., Hart, T., & Durocher, D. (2019) · Open Biology · doi:10.1098/rsob.190156 · Cited by 104 · see citing works
TopBP1 is required at mitosis to reduce transmission of DNA damage to G1 daughter cells
Pedersen, R. T., Kruse, T., Nilsson, J., Oestergaard, V. H., & Lisby, M. (2015) · The Journal of Cell Biology · doi:10.1083/jcb.201502107 · Cited by 102 · see citing works
Oncoprotein CIP2A is stabilized via interaction with tumor suppressor PP2A/B56
Wang, J., Okkeri, J., Pavic, K., Wang, Z., Kauko, O., Halonen, T., Sarek, G., Ojala, P. M., Rao, Z., Xu, W., et al. (2017) · The EMBO Reports · doi:10.15252/embr.201642788 · Cited by 95 · cited 1× · see citing works
“CIP2A western blots from 538 MDA-MB-468 (D) and patient-derived stem cell-like cells (14-72)(E) on treatment with indicated SMAPs for 539 24h.”
MethodSelf-citationMoudrý, P., Watanabe, K., Wolanin, K., Bártková, J., Wassing, I. E., Watanabe, S., Strauss, R., Pedersen, R. T., Oestergaard, V. H., Lisby, M., et al. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201507042 · Cited by 87 · see citing works
Óskarsson, T., Essers, M. A. G., Dubois, N. C., Offner, S. E., Dubey, C., Roger, C., METZGER, D., Chambon, P., Hümmler, E., Beard, P., et al. (2006) · Genes & Development · doi:10.1101/gad.381206 · Cited by 82 · see citing works
TOPBP1 recruits TOP2A to ultra-fine anaphase bridges to aid in their resolution
Broderick, R., Nieminuszczy, J., Blackford, A. N., Winczura, A., & Niedźwiedź, W. (2015) · Nature Communications · doi:10.1038/ncomms7572 · Cited by 80 · see citing works
Niemelä, M., Kauko, O., Sihto, H., Mpindi, J.-P., Nicorici, D., Pernilä, P., Kallioniemi, O.-P., Joensuu, H., Hautaniemi, S., & Westermarck, J. (2012) · Oncogene · doi:10.1038/onc.2011.599 · Cited by 79 · see citing works
Self-citationAbba, M. C., Zhong, Y., Lee, J., Kil, H., Lu, Y., Takata, Y., Simper, M., Gaddis, S., Shen, J., & Aldaz, C. M. (2016) · Oncotarget · doi:10.18632/oncotarget.11733 · Cited by 77 · see citing works
Khanna, A., Okkeri, J., Bilgen, T., Tiirikka, T., Vihinen, M., Visakorpi, T., & Westermarck, J. K. (2011) · PLoS ONE · doi:10.1371/journal.pone.0017979 · Cited by 67 · see citing works
Self-citationBoth DNA topoisomerase II-binding protein 1 and BRCA1 regulate the G2-M cell cycle checkpoint.
Yamane, K., Chen, J., & Kinsella, T. J. (2003) · PubMed · Cited by 66 · see citing works
Kauko, O., Imanishi, S. Y., Kulesskiy, E., Yetukuri, L., Laajala, T. D., Sharma, M., Pavic, K., Aakula, A., Rupp, C., Jumppanen, M., et al. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011265 · Cited by 65 · see citing works
Self-citationEpithelial vimentin plays a functional role in mammary gland development
Virtakoivu, R., Peuhu, E., Mai, A., Wärri, A. M., & Ivaska, J. (2017) · Development · doi:10.1242/dev.154229 · Cited by 64 · see citing works
Self-citationWohlbold, L., Merrick, K. A., De, S., Amat, R., Kim, J. H., Larochelle, S., Allen, J. J., Zhang, C., Shokat, K. M., Petrini, J. H. J., et al. (2012) · PLoS Genetics · doi:10.1371/journal.pgen.1002935 · Cited by 60 · see citing works
Myant, K., Qiao, X., Halonen, T., Come, C., Laine, A., Janghorban, M., Partanen, J. I., Cassidy, J., Ogg, E.-L., Cammareri, P., et al. (2015) · Cell Reports · doi:10.1016/j.celrep.2015.07.003 · Cited by 59 · see citing works
Self-citationGive me a break, but not in mitosis
Giunta, S., & Jackson, S. P. (2011) · Cell Cycle · doi:10.4161/cc.10.8.15334 · Cited by 58 · see citing works
CIP2A promotes proliferation of spermatogonial progenitor cells and spermatogenesis in mice
Ventelä, S., Côme, C., Mäkelä, J.-A., Hobbs, R. M., Mannermaa, L., Kallajoki, M., Chan, E. K., Pandolfi, P. P., Toppari, J., & Westermarck, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0033209 · Cited by 58 · see citing works
Self-citationClinical significance of cancerous inhibitor of protein phosphatase 2A in human cancers
Khanna, A., & Pimanda, J. E. (2016) · International Journal of Cancer · doi:10.1002/ijc.29431 · Cited by 57 · see citing works
Chao, T.-T., Wang, C., Chen, Y., Lai, C., Chang, F.-Y., Tsai, Y.-T., Chao, C.-H. H., Shiau, C., Huang, Y.-C. T., Yu, C., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.2941 · Cited by 50 · see citing works
Protein phosphatase 2A activation as a therapeutic strategy for managing MYC-driven cancers
Farrington, C. C., Yuan, E., Mazhar, S., Izadmehr, S., Hurst, L., Allen-Petersen, B. L., Janghorban, M., Chung, E. M., Wolczanski, G., Galsky, M. D., et al. (2020) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(17)49933-9 · Cited by 47 · see citing works
Self-citationChk1 Targeting Reactivates PP2A Tumor Suppressor Activity in Cancer Cells
Khanna, A., Kauko, O., Böckelman, C., Laine, A., Schreck, I., Partanen, J. I., Szwajda, A., Bormann, S., Bilgen, T., Helenius, M., et al. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-1002 · Cited by 45 · see citing works
Self-citationFunction of TopBP1 in Genome Stability
Sokka, M., Parkkinen, S., Pospiech, H., & Syväoja, J. E. (2010) · Subcellular Biochemistry · doi:10.1007/978-90-481-3471-7_7 · Cited by 38 · see citing works
Protein phosphatase 2A activation as a therapeutic strategy for managing MYC-driven cancers
Farrington, C. C., Yuan, E., Mazhar, S., Izadmehr, S., Hurst, L., Allen-Petersen, B. L., Janghorban, M., Chung, E. M., Wolczanski, G., Galsky, M. D., et al. (2019) · Journal of Biological Chemistry · doi:10.1074/jbc.ra119.011443 · Cited by 38 · see citing works
Self-citationp53 and ATM/ATR Regulate 7,12-Dimethylbenz[a]anthracene-Induced Immunosuppression
Gao, J., Mitchell, L., Lauer, F. T., & Burchiel, S. W. (2007) · Molecular Pharmacology · doi:10.1124/mol.107.039230 · Cited by 36 · see citing works
Novel Biomarkers in the Continuum of Breast Cancer
Stearns, V. (2016) · Advances in experimental medicine and biology · doi:10.1007/978-3-319-22909-6 · Cited by 35 · see citing works
Prodhomme, M. K., Pommier, R. M., Franchet, C., Fauvet, F., Bergoglio, V., Brousset, P., Morel, A., Brunac, A., Devouassoux‐Shisheboran, M., Pétrilli, V., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-2626 · Cited by 33 · see citing works
Merisaari, J., Denisova, O. V., Doroszko, M., Joncour, V. L., Johansson, P., Leenders, W. P. J., Kastrinsky, D. B., Zaware, N., Narla, G., Laakkonen, P. M., et al. (2020) · Brain Communications · doi:10.1093/braincomms/fcaa002 · Cited by 33 · see citing works
Self-citationPiecing Together a Broken Tumor Suppressor Phosphatase for Cancer Therapy
Westermarck, J. K., & Neel, B. G. (2020) · Cell · doi:10.1016/j.cell.2020.04.005 · Cited by 28 · see citing works
Self-citationOgiwara, H. (2006) · Nucleic Acids Research · doi:10.1093/nar/gkl411 · Cited by 27 · see citing works
Zheng, X.-F., Kalev, P., & Chowdhury, D. (2015) · DNA repair · doi:10.1016/j.dnarep.2015.04.014 · Cited by 20 · see citing works
Khanna, A., Thoms, J. A. I., Stringer, B. W., Chung, S. A., Ensbey, K. S., Jue, T. R., Jahan, Z., Subramanian, S., Anande, G., Shen, H. M., et al. (2020) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-19-0934 · Cited by 19 · see citing works
Tian, Y., Chen, H., Qiao, L., Zhang, W., Zheng, J., Zhao, W., Chen, J. J., & Zhang, W. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13693 · Cited by 17 · see citing works
Kim, W. J. (2001) · Nucleic Acids Research · doi:10.1093/nar/29.8.1724 · Cited by 16 · see citing works
A Phenotypic Mouse Model of Basaloid Breast Tumors
Kim, S., Roopra, A., & Alexander, C. M. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030979 · Cited by 14 · see citing works
TOPBP1 takes RADical command in recombinational DNA repair
Liu, Y., & Smolka, M. B. (2016) · The Journal of Cell Biology · doi:10.1083/jcb.201601028 · Cited by 7 · see citing works
Myant, K., Qiao, X., Halonen, T., Côme, C., Laine, A., Partanen, J. I., Ogg, E.-L., Laiterä, T., Janghorban, M., Okkeri, J., et al. (2015) · Molecular Cancer Research · doi:10.1158/1557-3125.myc15-pr03 · Cited by 2 · see citing works
Self-citation
Flagged first, then by citations
2 of the 77 references couldn’t be matched to a known paper.
Cited by
Sorted by citations
Adam, S., Rossi, S. E., Moatti, N., De Marco Zompit, M., Xue, Y., Ng, T. F., Álvarez-Quilón, A., Desjardins, J., Bhaskaran, V., Martino, G., et al. (2021) · Nature Cancer · doi:10.1038/s43018-021-00266-w · Cited by 121 · see citing works
Mitotic clustering of pulverized chromosomes from micronuclei
Lin, Y.-F., Hu, Q., Mazzagatti, A., Valle-Inclán, J. E., Maurais, E. G., Dahiya, R., Guyer, A., Sanders, J. T., Engel, J. L., Nguyen, G., et al. (2023) · Nature · doi:10.1038/s41586-023-05974-0 · Cited by 81 · see citing works
Mitotic tethering enables inheritance of shattered micronuclear chromosomes
Trivedi, P., Steele, C. D., Au, F. K. C., Alexandrov, L. B., & Cleveland, D. W. (2023) · Nature · doi:10.1038/s41586-023-06216-z · Cited by 80 · see citing works
The CIP2A-TOPBP1 complex safeguards chromosomal stability during mitosis
Zompit, M. D. M., Esteban, M. T., Mooser, C., Adam, S., Rossi, S. E., Jeanrenaud, A., Leimbacher, P.-A., Fink, D. A., Shorrocks, A.-M. K., Blackford, A. N., et al. (2022) · Nature Communications · doi:10.1038/s41467-022-31865-5 · Cited by 66 · see citing works
CIP2A induces PKM2 tetramer formation and oxidative phosphorylation in non-small cell lung cancer
Liang, L.-J., Yang, F., Wang, D., Zhang, Y., Yu, H., Wang, Z., Sun, B., Liu, Y., Wang, G., & Zhou, G. (2024) · Cell Discovery · doi:10.1038/s41421-023-00633-0 · Cited by 47 · see citing works
Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A
Pavic, K., Gupta, N., Omella, J. D., Derua, R., Aakula, A., Huhtaniemi, R., Määttä, J. A., Höfflin, N., Okkeri, J., Wang, Z., et al. (2023) · Nature Communications · doi:10.1038/s41467-023-36693-9 · Cited by 36 · see citing works
“The data show that the CIP2A(1-560) residues cross-linked to B56α are located primarily in the N-terminal head domain (K18, K21, E23, E34, K40) with an additional residue at the C-terminus (K490) (Fig.”
BackgroundMethodInfluentialSelf-citationUSP13: Multiple Functions and Target Inhibition
Li, X., Yang, G. H., Zhang, W., Qin, B., Ye, Z., Shi, H., Zhao, X., Chen, Y., Song, B., Mei, Z., et al. (2022) · Frontiers in Cell and Developmental Biology · doi:10.3389/fcell.2022.875124 · Cited by 34 · see citing works
Phosphorylation-dependent assembly of DNA damage response systems and the central roles of TOPBP1
Day, M., Oliver, A. W., & Pearl, L. H. (2021) · DNA repair · doi:10.1016/j.dnarep.2021.103232 · Cited by 32 · see citing works
Emerging insights into serine/threonine-specific phosphoprotein phosphatase function and selectivity
Kokot, T., & Köhn, M. (2022) · Journal of Cell Science · doi:10.1242/jcs.259618 · Cited by 30 · see citing works
Leem, J., Kim, J., & Oh, J. S. (2023) · Nucleic Acids Research · doi:10.1093/nar/gkad213 · Cited by 25 · see citing works
Neale, D. B., Morris, J. C., Verrills, N. M., & Ammit, A. J. (2025) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2025.108834 · Cited by 24 · see citing works
CIP2A coordinates phosphosignaling, mitosis, and the DNA damage response
Nagelli, S. G., & Westermarck, J. K. (2023) · Trends in cancer · doi:10.1016/j.trecan.2023.09.001 · Cited by 22 · see citing works
Self-citationKu70 Binding to YAP Alters PARP1 Ubiquitination to Regulate Genome Stability and Tumorigenesis
Shu, Y., Jin, X., Ji, M., Zhang, Z., Wang, X., Liang, H., Lu, S., Dong, S., Lin, Y., Guo, Y., et al. (2024) · Cancer Research · doi:10.1158/0008-5472.can-23-4034 · Cited by 21 · see citing works
A small-molecule inhibitor of TopBP1 exerts anti-MYC activity and synergy with PARP inhibitors
Lin, F., Liu, K., Garan, L. A. W., Folly-Kossi, H., Song, Y., Lin, S., & Lin, W.-C. (2023) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2307793120 · Cited by 21 · see citing works
Bownes, L. V., Marayati, R., Quinn, C. H., Beierle, A. M., Hutchins, S. C., Julson, J. R., Erwin, M. H., Stewart, J. E., Mroczek‐Musulman, E., Ohlmeyer, M. H. J., et al. (2022) · Cancers · doi:10.3390/cancers14081952 · Cited by 20 · see citing works
Andriani, L., Ling, Y.-X., Yang, S., Zhao, Q., Ma, X.-Y., Huang, M.-Y., Zhang, Y., Zhang, F.-L., Li, D., & Shao, Z. (2024) · Cancer Letters · doi:10.1016/j.canlet.2024.217008 · Cited by 16 · see citing works
Recent insights into the causes and consequences of chromosome mis-segregation
Devillers, R., dos Santos, A., Destombes, Q., Laplante, M., & Elowe, S. (2024) · Oncogene · doi:10.1038/s41388-024-03163-5 · Cited by 15 · see citing works
Chromothripsis: an emerging crossroad from aberrant mitosis to therapeutic opportunities
Ejaz, U., Dou, Z., Yao, P. Y., Wang, Z., Liu, X., & Yao, X. (2024) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjae016 · Cited by 12 · see citing works
Thirty Years of BRCA1: Mechanistic Insights and Their Impact on Mutation Carriers
Moser, S. C., & Jonkers, J. (2025) · Cancer Discovery · doi:10.1158/2159-8290.cd-24-1326 · Cited by 12 · see citing works
Chen, B., Hu, H., & Chen, X. (2023) · Frontiers in Genetics · doi:10.3389/fgene.2023.1110656 · Cited by 11 · see citing works
The Effects of Protein Phosphatase 2A Activation with Novel Tricyclic Sulfonamides on Hepatoblastoma
Bownes, L. V., Julson, J. R., Quinn, C. H., Hutchins, S. C., Erwin, M. H., Markert, H. R., Stewart, J. E., Mroczek‐Musulman, E., Aye, J. M., Yoon, K. J., et al. (2023) · Journal of Pediatric Surgery · doi:10.1016/j.jpedsurg.2023.02.017 · Cited by 9 · see citing works
Emerging roles of the CIP2A–TopBP1 complex in genome integrity
Ummethum, H., Li, J., Lisby, M., & Oestergaard, V. H. (2023) · NAR Cancer · doi:10.1093/narcan/zcad052 · Cited by 7 · see citing works
Arribas, R. L., Viejo, L., Bravo, I., Martinez-Castillo, M., Ramos, E., Romero, A., García‐Frutos, E. M., Janssens, V., Montiel, C., & Rı́os, C. D. L. (2023) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2023.115245 · Cited by 7 · see citing works
Evaluating Novel Protein Phosphatase 2A Activators as Therapeutics for Emphysema
Soto, B., Ahmed, H., Pillai, M., Park, S. S., Ploszaj, M. A., Reece, J., Taluru, H., Bobrow, D., Yu, H. K. Y., Lafortune, P., et al. (2023) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2023-0105oc · Cited by 6 · see citing works
Nivruthi, S., Preetha, D., Saranya, I., & Selvamurugan, N. (2025) · Seminars in Oncology · doi:10.1016/j.seminoncol.2025.152340 · Cited by 5 · see citing works
Ovarian Cancers with Low CIP2A Tumor Expression Constitute an APR-246–Sensitive Disease Subtype
Cvrljevic, A. N., Butt, U., Huhtinen, K., Grönroos, T. J., Böckelman, C., Lassus, H., Butzow, R., Haglund, C., Kaipio, K., Arsiola, T., et al. (2022) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0622 · Cited by 5 · see citing works
Self-citationLee, C., & Oh, J. S. (2024) · Nucleic Acids Research · doi:10.1093/nar/gkae1207 · Cited by 4 · see citing works
The impact of TOPBP1 mutations in human cancers on the DNA damage response
Yan, Z., Ge, X., Wang, J., Xu, F., Li, M., Liu, X., Yu, X., & Wu, C. (2022) · Genome Instability & Disease · doi:10.1007/s42764-022-00072-3 · Cited by 4 · see citing works
UCHL1 Promotes Gastric Cancer Progression by Regulating CIP2A Degradation
Lee, G.-Y., Jeong, I.-H., Kim, B. S., Kim, H., & Lee, P. C.-W. (2025) · Pharmaceuticals · doi:10.3390/ph18101468 · Cited by 3 · see citing works
TTF2 processes sites of incomplete DNA replication during mitosis via sister-chromatid exchanges.
Fujisawa, R., & Labib, K. P. M. (2026) · Science · doi:10.1126/science.aeh2300 · Cited by 2 · see citing works
PP2A activation overcomes leptomeningeal dissemination in group 3 medulloblastoma
Nazam, N., Erwin, M. H., Julson, J. R., Quinn, C. H., Beierle, A. M., Bownes, L. V., Stewart, J. E., Kang, K., Butey, S. P., Mroczek‐Musulman, E., et al. (2024) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2024.107892 · Cited by 3 · see citing works
Wang, Y., Yan, X., Qu, X., Mao, J., Wang, J., Yang, M., & Tao, M. (2022) · Pathology - Research and Practice · doi:10.1016/j.prp.2022.154287 · Cited by 3 · see citing works
Mitotic single-stranded DNA suppression by DDIAS.
Xue, Y., Rashed, F. B., Mao, D. Y. L., Abe, K., Lin, Z.-Y., Krastev, D., Setiaputra, D., Hoeg, L., Bonnet, C., Kumar, A., et al. (2026) · Molecules and Cells · doi:10.1016/j.molcel.2026.07.034 · Cited by 1 · see citing works
DDIAS shields single-stranded DNA in mitosis and promotes vertebrate brain development
Tsukada, K., Lototska, L., 塚田, 絢., Sarusie, M. V., Gönenç, I. I., Sherlaw‐Sturrock, C., Kanade, M., Palek, M., Oliver, A. W., Jones, S. E., et al. (2026) · Cell · doi:10.1016/j.cell.2026.07.041 · Cited by 5 · see citing works
CIP2A promotes bronchiolitis obliterans by activating the NF‑κB pathway
Zhou, X., Zhao, X., Li, Y., & Zhang, B. (2025) · Molecular Medicine Reports · doi:10.3892/mmr.2025.13473 · Cited by 2 · see citing works
Zhao, X., Feng, S., Nitie, X., Muluo, S., & Lei, Y. (2025) · Cancer Biology & Therapy · doi:10.1080/15384047.2025.2545062 · Cited by 2 · see citing works
SL-Miner: a web server for mining evidence and prioritization of cancer-specific synthetic lethality
Liu, X., Hu, J., & Zheng, J. (2024) · Bioinformatics · doi:10.1093/bioinformatics/btae016 · Cited by 1 · see citing works
Zhao, X., Chen, B., Xu, F., Zhang, J., Yao, Z., Wang, R., Zhang, J., Zhou, S., Hou, Y., Xu, S., et al. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2600248123 · Cited by 1 · see citing works
Szudy‐Szczyrek, A., Mlak, R., Mazurek, M., Krajka, T., Chocholska, S., Bitkowska, P., Jutrzenka, M., Szczyrek, M., Homa‐Mlak, I., Krajka, A., et al. (2023) · Cells · doi:10.3390/cells12071029 · Cited by 1 · see citing works
Targeting BRCA-mutated tumors in mitosis
Menolfi, D., & Zha, S. (2021) · Nature Cancer · doi:10.1038/s43018-021-00293-7 · Cited by 1 · see citing works
DDIAS is a single-stranded DNA-binding effector of the TOPBP1-CIP2A complex in mitosisPreprint
Tsukada, K., Lototska, L., Tsukada, A., Gönenç, I. I., Sherlaw-Sturrock, C. A., Kanade, M., Oliver, A. W., Jones, S. E., Jhujh, S. S., Bannister, J., et al. (2026) · bioRxiv · doi:10.1101/2025.09.09.675193 · Cited by 2 · see citing works
Ovarian cancers with low CIP2A tumor expression constitute an APR-246 sensitive disease subtype
Cvrljevic, A. N., Butt, U., Huhtinen, K., Grönroos, T. J., Böckelman, C., Lassus, H., Kaipio, K., Arsiola, T., Laajala, T. D., Connolly, D. C., et al. (2021) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.1101/2021.03.31.437804 · Cited by 5 · see citing works
Self-citationLiang, L.-J., Zhang, Y., Wang, D., Wang, F.-Y., Xie, D.-W., Yu, H. J., Wang, Z., Sun, B., Gao, S., Guo, H. B., et al. (2022) · Research Square · doi:10.21203/rs.3.rs-1232624/v1
Cvrljevic, A. N., Butt, U., Huhtinen, K., Grönroos, T. J., Böckelman, C., Lassus, H. J., Bützow, R. C., Haglund, C. H., Kaipio, K., Arsiola, T., et al. (2023) · doi:10.1158/1535-7163.c.6543912.v1
Self-citationZhao, C., Weng, X., He, W., & Lei, Y. (2025) · Archivum Immunologiae et Therapiae Experimentalis · doi:10.2478/aite-2025-0016
Zeinali, E., Bagheri, V., Rostami, E., Mansouri, A., & Sarab, G. A. (2025) · Human Gene · doi:10.1016/j.humgen.2025.201437 · Cited by 1 · see citing works
Emerging roles of the cancerous inhibitor of protein phosphatase 2A (CIP2A) in ovarian cancer
Filipe, A., Saravi, S., Mustafov, D., Panfilov, S., Banger, S., Mousavikivaj, S., Braoudaki, M., Kailasam, S., Riazalhosseini, Y., Sahai, M. A., et al. (2025) · Scientific Reports · doi:10.1038/s41598-025-05013-0
The Emerging Role of the Cancerous Inhibitor of Protein Phosphatase 2A in Pulmonary Diseases
Hamza, H., Nirmal, D., Pappas, S., Ebubechukwu, U. J., Gill, S., Al-Ajam, A., Ohlmeyer, M. H. J., & Geraghty, P. M. (2025) · Medicina · doi:10.3390/medicina61101740
TOPBP1–PLK1 interaction preserves genome integrity during mitosis
Li, J., Petersen, K. V., Ummethum, H., Bagge, J., Hinsby, E. W., Lisby, M., Nilsson, J., & Oestergaard, V. H. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag462
Bosquet, J. G., Shahi, M., Yadav, S., Kanwar, N., Tapia, A. L., McGree, M. E., Dowdy, S. C., Couch, F. J., Halling, K. C., Weroha, S. J., et al. (2026) · Gynecologic Oncology · doi:10.1016/j.ygyno.2026.05.021
Hayward, S. B., Vaitsiankova, A., Lama-Díaz, T., Chou, J., Taglialatela, A., Huang, J., Wijesekarahanthi, Y., Heyza, J. R., Leuzzi, G., Chen, C., et al. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.06.07.728858 · Cited by 2 · see citing works
Lin, F., Lin, S., Liu, K., Xiao, Y., Garan, L. A. W., Folly-Kossi, H., & Lin, W.-C. (2026) · Science Advances · doi:10.1126/sciadv.aeg1996
Zhu, M., He, J., Li, J., Kang, H., Dong, Y. S., Wang, S., Mou, Y., Zhang, Y., Liu, J., Sun, X., et al. (2026) · Research Square · doi:10.21203/rs.3.rs-9848947/v1
Dynamic chromatin tethering of MDC1 regulates genome stability
Heyza, J. R., Mikhova, M., Phillips, C., Mehmood, S., Perez, G. I., Broadbent, D. G., & Schmidt, J. C. (2026) · Nucleic Acids Research · doi:10.1093/nar/gkag866 · Cited by 3 · see citing works
Dependency Map correlation analysis reveals WDR89 as a genome maintenance factor
Minaker, S. W., Negri, G. L., Morin, G. B., & Stirling, P. C. (2026) · Molecular Biology of the Cell · doi:10.1091/mbc.e26-02-0067
- Authors
- Laine, A., Nagelli, S. G., Farrington, C., Butt, U., Cvrljevic, A. N., Vainonen, J. P., Feringa, F. M., Grönroos, T. J., Gautam, P., Khan, S., Sihto, H., Qiao, X., Pavic, K., Connolly, D. C., Kronqvist, P., Elo, L. L., Maurer, J., Wennerberg, K., Medema, R. H., Joensuu, H., Peuhu, E., de Visser, K., Narla, G., & Westermarck, J.
- Affiliations
- Åbo Akademi University (FI)
- University of Michigan (US)
- The Netherlands Cancer Institute (NL)
- University of Turku (FI)
- University of Helsinki (FI)
- Fox Chase Cancer Center (US)
- Universitätsklinikum Aachen (DE)
- Corresponding author
- Westermarck, Jukka
- ORCID
- Nagelli, Srikar G.
- Farrington, Caroline
- Butt, Umar
- Cvrljevic, Anna N.
- Vainonen, Julia P.
- Feringa, Femke M.
- Grönroos, Tove J.
- Gautam, Prson
- Khan, Sofia
- Sihto, Harri
- Qiao, Xi
- Pavic, Karolina
- Connolly, Denise C.
- Kronqvist, Pauliina
- Elo, Laura L.
- Maurer, Jochen
- Wennerberg, Krister
- Joensuu, Heikki
- Peuhu, Emilia
- Narla, Goutham
- Westermarck, Jukka
- Venue
- Cancer Research
- Publisher
- openRxiv
- Published
- 2020-08-31
- Volume
- 81
- Issue
- 16
- Pages
- 4319-4331
- ISSN
- 0008-5472 (ISSN-L)
- PMC
- PMC8373817
- OpenAlex
- W3169418599
- Cited by
- 54
- References
- 77
- Citations by year
- 2026: 11 · 2025: 11 · 2024: 8 · 2023: 13 · 2022: 8 · 2021: 3
- FWCI
- 2.51
- Type
- journal article
- Language
- en
- Open access
- hybrid
- doi.org
- Licence
- Locations
- Cancer Research (publishedVersion, cc-by-nc-nd)
- bioRxiv (Cold Spring Harbor Laboratory) (acceptedVersion, cc-by-nc-nd)
- PubMed Central (publishedVersion, cc-by-nc-nd)
- PubMed (publishedVersion)
- Työväentutkimus Vuosikirja (submittedVersion, other-oa)
- RWTH Publications (RWTH Aachen) (submittedVersion)
- VU Research Portal (submittedVersion, other-oa)
- Data Archiving and Networked Services (DANS) (submittedVersion, other-oa)
- Funders
- U.S. Department of Defense (W81XWH)
- Case Western Reserve University
- Deutsche Forschungsgemeinschaft (407869199)
- Academy of Finland (296801, 323096, 310561, 314443)
- Suomen Kulttuurirahasto
- Turun Yliopisto (310561)
- Orionin Tutkimussäätiö
- Svenska Kulturfonden
- K. Albin Johanssons Stiftelse
- Turun Yliopistollinen Keskussairaala
- Biocenter Finland
- Oncode Institute
- National Institutes of Health
- Fox Chase Cancer Center (P30CA006927)
- Varsinais-Suomen Rahasto
- National Heart, Lung, and Blood Institute (R01HL144741)
- National Cancer Institute (R01CA181654, R01CA240993, CA240993, CA 006927, CA181654, P30CA006927)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › DNA Repair Mechanisms
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Breast Cancer Treatment Studies
- Health Sciences › Medicine › Oncology › Cancer-related Molecular Pathways
- Keywords
- CIP2A, TopBP1, basal-like breast cancer, triple-negative breast cancer, homologous recombination deficiency, DNA damage response, spindle assembly checkpoint, G2/M checkpoint, BRCA deficiency, MYC signaling, tumor initiation, protein-protein interaction, prognostic factors, therapeutic target
- MeSH terms
- Animals, Autoantigens, Breast Neoplasms, Carrier Proteins, Cell Cycle, DNA Damage, DNA-Binding Proteins, Female, Humans, Immunohistochemistry, Membrane Proteins, Mice, Transgenic, Mitosis, Mutation, Nuclear Proteins, Recombination, Genetic, 9,10-Dimethyl-1,2-benzanthracene, Signal Transduction, Mice, Knockout, Proteome, Cell Line, Tumor, Intracellular Signaling Peptides and Proteins, Cell Proliferation, Mice, Carcinogenesis
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
