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Identification of specific PP2A complexes involved in human cell transformation
Open accessAbstract
The SV40 small t antigen (ST) interacts with the serine-threonine protein phosphatase 2A (PP2A). To investigate the role of this interaction in transformation, we suppressed the expression of the PP2A B56gamma subunit in human embryonic kidney (HEK) epithelial cells expressing SV40 large T antigen, hTERT, and H-RAS. Suppression of PP2A B56gamma expression inhibited PP2A-specific phosphatase activity similar to that achieved by ST and conferred the ability to grow in an anchorage-independent fashion and to form tumors. Overexpression of PP2A B56gamma3 in tumorigenic HEK cells expressing ST or human lung cancer cell lines partially reversed the tumorigenicity of these cells. These observations identify specific PP2A complexes involved in human cell transformation.
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“Among the PP2A complexes, PP2A trimers with B56 subunits are predominantly human tumour suppressors4–7.”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [7]
In the citing paper
“However, fully consistent with the requirement of PP2A-B56 inhibition for anchorage-independent growth6,7, CIP2A K21A targeted clones were almost completely incompetent to grow as spheres on soft agar (Fig. 3F, G).”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [7]
In the citing paper
“The protein phosphatase 2A (PP2A) heterotrimer PP2A-B56α is a human tumour suppressor.”
From Structural mechanism for inhibition of PP2A-B56α and oncogenicity by CIP2A (2023) · cites this paper as [7]
In the citing paper
“Consistently, ectopic expression of B56γ in lung, breast and prostate cancer cell lines reduced cell proliferation and colony formation in soft agar, suggesting a potential tumor suppressor role of B56γ in multiple cell types (Chen et al., 2004).”
From PP2A holoenzymes, substrate specificity driving cellular functions and deregulation in cancer (2019) · cites this paper as Chen et al., 2004
In the citing paper
“This notion corroborates with the previous notion on the role of B′ subunits as tumor suppressors [45–49].”
From PP2A-B′ holoenzyme substrate recognition, regulation and role in cytokinesis (2017) · cites this paper as [49]
Citations
Cites
Polakis, P. (2000) · Genes & Development · doi:10.1101/gad.14.15.1837 · Cited by 3,183
THE STRUCTURE AND REGULATION OF PROTEIN PHOSPHATASES
Cohen, P. (1989) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.58.070189.002321 · Cited by 2,543
Creation of human tumour cells with defined genetic elements
Hahn, W. C., Counter, C. M., Lundberg, A. S., Beijersbergen, R. L., Brooks, M. W., & Weinberg, R. A. (1999) · Nature · doi:10.1038/22780 · Cited by 2,345
Self-citationBialojan, C., & Takai, A. (1988) · Biochemical Journal · doi:10.1042/bj2560283 · Cited by 1,689
Lentivirus-delivered stable gene silencing by RNAi in primary cells.
Stewart, S. A., Dykxhoorn, D. M., Palliser, D., Mizuno, H., Yu, E. Y., An, D., Sabatini, D., Chen, I. S. Y., Hahn, W., Sharp, P., et al. (2003) · RNA: A publication of the RNA Society · doi:10.1261/rna.2192803 · Cited by 1,619
Self-citationRegulation of protein kinase cascades by protein phosphatase 2A
Millward, T. A., Zołnierowicz, S., & Hemmings, B. A. (1999) · Trends in Biochemical Sciences · doi:10.1016/s0968-0004(99)01375-4 · Cited by 793
Telomerase maintains telomere structure in normal human cells
Kenichi, M., Yu, E. Y., Shilagardi, K., Ben‐Porath, I., Currier, J. L., Metz, G. B., Brooks, M. W., Kaneko, S., Seishi, M., DeCaprio, J. A., et al. (2006) · Kanazawa University Repository for Academic Resources (DSpace) (Kanazawa University) · Cited by 738
Self-citationEnumeration of the Simian Virus 40 Early Region Elements Necessary for Human Cell Transformation
Hahn, W. C., Dessain, S. K., Brooks, M. W., King, J. E., Elenbaas, B., Sabatini, D. M., DeCaprio, J. A., & Weinberg, R. A. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.7.2111-2123.2002 · Cited by 626
Self-citationOkadaic acid: an additional non-phorbol-12-tetradecanoate-13-acetate-type tumor promoter.
Suganuma, M., Fujiki, H., Suguri, H., YOSHIZAWA, S., Hirota, M., Nakayasu, M., Ojika, M., Wakamatsu, K., Yamada, K., & Sugimura, T. (1988) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.85.6.1768 · Cited by 597
Pallas, D. C., Shahrik, L. K., Martin, B. L., Jaspers, S. R., Miller, T. B., Brautigan, D. L., & Roberts, T. M. (1990) · Cell · doi:10.1016/0092-8674(90)90726-u · Cited by 573
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Items 101–200 of 325
Sontag, J. M., & Sontag, E. (2006) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-006-6300-7 · Cited by 61
PP2A-Mediated Anticancer Therapy
Chen, W., Wang, Z., Jiang, C., & Ding, Y. (2013) · Gastroenterology Research and Practice · doi:10.1155/2013/675429 · Cited by 59
Self-citationLi, H., Rodrik-Outmezguine, V. S., Pielak, R. M., Knirr, S., Yang, Z., & Foster, D. A. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m504192200 · Cited by 58
EZH2-mediated PP2A inactivation confers resistance to HER2-targeted breast cancer therapy
Bao, Y., Oguz, G., Lee, W. C., Lee, P. L., Ghosh, K., Li, J., Wang, P., Lobie, P. E., Ehmsen, S., Ditzel, H. J., et al. (2020) · Nature Communications · doi:10.1038/s41467-020-19704-x · Cited by 58
Chen, S., Chen, L., Ye, L., Jiang, Y., Li, Q., Zhang, H., Zhang, R., Li, H., Yu, D., Zhang, R., et al. (2021) · Journal of Hazardous Materials · doi:10.1016/j.jhazmat.2021.127624 · Cited by 54
Self-citationMoreno, C. S., Ramachandran, S., Ashby, D. G., Laycock, N., Plattner, C. A., Chen, W., Hahn, W. C., & Pallas, D. C. (2004) · Cancer Research · doi:10.1158/0008-5472.can-04-1150 · Cited by 56
Self-citationSTRIPAK directs PP2A activity toward MAP4K4 to promote oncogenic transformation of human cells
Kim, J. W., Berrios, C. J., Kim, M., Schade, A. E., Adelmant, G., Yeerna, H., Damato, E., Iniguez, A. B., Swanson, S. K., Florens, L. A., et al. (2020) · eLife · doi:10.7554/elife.53003 · Cited by 54
Self-citationOncogenic transformation and experimental models of human cancer
Anna, C. S. (2007) · Frontiers in bioscience · doi:10.2741/2661 · Cited by 56
Qin, J., Chen, H.-G., Yan, Q., Deng, M., Liu, J., Doerge, S., Ma, W., Dong, Z., & Li, D. W.-C. (2008) · Cancer Research · doi:10.1158/0008-5472.can-08-0839 · Cited by 55
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Enjoji, S., Yabe, R., Tsuji, S., Yoshimura, K., Kawasaki, H., Sakurai, M., Sakai, Y., Takenouchi, H., Yoshino, S., Hazama, S., et al. (2018) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-17-0393 · Cited by 49
Mei, J., Tian, H., Huang, H.-S., Hsu, C., Liou, Y., Wu, N., Zhang, W., & Chu, T. (2021) · Cell Proliferation · doi:10.1111/cpr.13029 · Cited by 50
Schaffhausen, B. S., & Roberts, T. M. (2008) · Virology · doi:10.1016/j.virol.2008.09.042 · Cited by 53
Loss of protein phosphatase 2A regulatory subunit B56δ promotes spontaneous tumorigenesis in vivo
Lambrecht, C., Libbrecht, L., Sagaert, X., Pauwels, P., Hoorne, Y., Crowther, J., Louis, J. V., Sents, W., Sablina, A., & Janssens, V (2018) · Oncogene · doi:10.1038/onc.2017.350 · Cited by 50
Shouse, G., Nobumori, Y., & Liu, X. (2010) · Oncogene · doi:10.1038/onc.2010.161 · Cited by 49
Hung, M.-H., Chen, Y.-L., Chu, P.-Y., Shih, C.-T., Yu, H.-C., Tai, W.-T., Shiau, C.-W., & Chen, K.-F. (2016) · Oncogene · doi:10.1038/onc.2016.21 · Cited by 48
Sun, B., Chen, M., Hawks, C. L., Pereira‐Smith, O. M., & Hornsby, P. J. (2005) · Neoplasia · doi:10.1593/neo.05172 · Cited by 48
Modeling the role of p53 pulses in DNA damage- induced cell death decision
Sun, T., Chen, C., Wu, Y., Zhang, S., Cui, J., & Shen, P. (2009) · BMC Bioinformatics · doi:10.1186/1471-2105-10-190 · Cited by 48
Inactivation of PP2A by a recurrent mutation drives resistance to MEK inhibitors
O’Connor, C. M., Leonard, D., Wiredja, D., Avelar, R. A., Wang, Z., Schlatzer, D., Bryson, B., Tokala, E., Taylor, S. E., Upadhyay, A., et al. (2020) · Oncogene · doi:10.1038/s41388-019-1012-2 · Cited by 48
Riz, I., & Hawley, R. G. (2005) · Oncogene · doi:10.1038/sj.onc.1208727 · Cited by 51
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Sablina, A. A., & Hahn, W. C. (2007) · Cell Adhesion & Migration · doi:10.4161/cam.1.3.4986 · Cited by 47
Self-citationMicrocystin-LR in Primary Liver Cancers: An Overview
Gu, S., Jiang, M., & Zhang, B. (2022) · Toxins · doi:10.3390/toxins14100715 · Cited by 46
Genetically engineered mouse models and human osteosarcoma
Ng, A. J., Mutsaers, A. J., Baker, E. K., & Walkley, C. R. (2012) · Clinical Sarcoma Research · doi:10.1186/2045-3329-2-19 · Cited by 45
Palma, R. M. D., Parnham, S. R., Li, Y., Oaks, J. J., Peterson, Y. K., Szulc, Z. M., Roth, B. M., Xing, Y., & Öğretmen, B. (2019) · The FASEB Journal · doi:10.1096/fj.201802264r · Cited by 44
PPP2R5C couples hepatic glucose and lipid homeostasis
Cheng, Y.-S., Seibert, O., Klöting, N., Dietrich, A., Straßburger, K., Fernández-Veledo, S., Vendrell, J. J., Zorzano, A., Blüher, M., Herzig, S., et al. (2015) · PLoS Genetics · doi:10.1371/journal.pgen.1005561 · Cited by 43
α4 is highly expressed in carcinogen-transformed human cells and primary human cancers
Chen, L.-P., Lai, Y.-D., Li, D.-C., Zhu, X.-N., Yang, P., Li, W., Zhu, W., Zhao, J., Li, X.-D., Xiao, Y.-M., et al. (2011) · Oncogene · doi:10.1038/onc.2011.20 · Cited by 43
Self-citationThe APC/C Inhibitor XErp1/Emi2 Is Essential for Xenopus Early Embryonic Divisions
Tischer, T., Hörmanseder, E., & Mayer, T. U. (2012) · Science · doi:10.1126/science.1228394 · Cited by 47
Dunn, E. F., & Connor, J. H. (2010) · Journal of Virology · doi:10.1128/jvi.01671-10 · Cited by 45
Mechanisms of the HRSL3 tumor suppressor function in ovarian carcinoma cells
Nazarenko, I. A., Schäfer, R., & Sers, C. (2007) · Journal of Cell Science · doi:10.1242/jcs.000018 · Cited by 43
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Sents, W., Meeusen, B., Kalev, P., Radaelli, E., Sagaert, X., Miermans, E., Haesen, D., Lambrecht, C., Dewerchin, M., Carmeliet, P., et al. (2017) · Cancer Research · doi:10.1158/0008-5472.can-16-2911 · Cited by 42
Lee, T.-Y., Lai, T.-Y., Lin, S.-C., Wu, C.-W., Ni, I.-F., Yang, Y.-S., Hung, L., Law, B. K., & Chiang, C.-W. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.094953 · Cited by 41
Leclerc, D., Lévesque, N., Cao, Y., Deng, L.-Y., Wu, Q. H., Powell, J., Sapienza, C., & Rozen, R. R. (2013) · Cancer Prevention Research · doi:10.1158/1940-6207.capr-13-0198 · Cited by 41
Goswami, S., Mani, R., Nunes, J. J., Chiang, C., Zapolnik, K., Hu, E. Y., Frissora, F. W., Mo, X., Walker, L. A., Yan, P. S., et al. (2021) · Blood · doi:10.1182/blood.2020010344 · Cited by 41
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Mustelin, T. (2007) · Humana Press eBooks · doi:10.1385/1-59745-267-x:9 · Cited by 43
Keen, J. C., Zhou, Q. Y., Park, B. H., Pettit, C., Mack, K. M., Blair, B., BRENNER, K. R., & Davidson, N. E. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m505317200 · Cited by 40
Esplin, E. D., Ramos, P., Martinez, B., Tomlinson, G. E., Mumby, M. C., & Evans, G. A. (2005) · Genes Chromosomes and Cancer · doi:10.1002/gcc.20284 · Cited by 40
Breuer, R., Becker, M. S., Brechmann, M., Mock, T., Arnold, R., & Krammer, P. H. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.533547 · Cited by 40
Pandey, P., Seshacharyulu, P., Das, S., Rachagani, S., Ponnusamy, M. P., Yan, Y., Johansson, S. L., Datta, K., Lin, M. F., & Batra, S. K. (2013) · British Journal of Cancer · doi:10.1038/bjc.2013.160 · Cited by 39
The impact of phosphatases on proliferative and survival signaling in cancer
Narla, G., Sangodkar, J., & Ryder, C. B. (2018) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-018-2826-8 · Cited by 39
Nader, C. P., Cidem, A., Verrills, N. M., & Ammit, A. J. (2019) · Respiratory Research · doi:10.1186/s12931-019-1192-x · Cited by 41
Development of human cell models for assessing the carcinogenic potential of chemicals
Pang, Y., Li, W., Ma, R., Ji, W., Wang, Q., Li, D., Xiao, Y., Wei, Q., Lai, Y., Yang, P., et al. (2008) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2008.08.009 · Cited by 39
Self-citationResistance to targeted treatment of gastroenteropancreatic neuroendocrine tumors
Beyens, M., Vandamme, T., Peeters, M., Camp, G. V., & de Beeck, K. O. (2018) · Endocrine Related Cancer · doi:10.1530/erc-18-0420 · Cited by 38
Role of β-Catenin Activation Levels and Fluctuations in Controlling Cell Fate
Pedone, E., & Marucci, L. (2019) · Genes · doi:10.3390/genes10020176 · Cited by 39
Oncogenic transformation of human cells: shortcomings of rodent model systems
Akagi, T. (2004) · Trends in Molecular Medicine · doi:10.1016/j.molmed.2004.09.001 · Cited by 38
Liang, J. L., Tan, L., Zhang, Y., Guo, Z., & Xu, L. (2011) · Journal of Zhejiang University SCIENCE B · doi:10.1631/jzus.b1100121 · Cited by 37
Yabe, R., Miura, A., Usui, T., Mudrak, I., Ogris, E., Ohama, T., & Sato, K. (2015) · PLoS ONE · doi:10.1371/journal.pone.0145226 · Cited by 37
Kim, M.-O., Choe, M. H., Yoon, Y. N., Ahn, J., Yoo, M., Jung, K., An, S., Hwang, S., Oh, J. S., & Kim, J. (2017) · Biochemical Pharmacology · doi:10.1016/j.bcp.2017.08.009 · Cited by 39
MicroRNA-652 induces NED in LNCaP and EMT in PC3 prostate cancer cells
Nam, R. K., Benatar, T., Amemiya, Y., Wallis, C. J. D., Romero, J. M., Tsagaris, M., Sherman, C., Sugar, L., & Seth, A. K. (2018) · Oncotarget · doi:10.18632/oncotarget.24937 · Cited by 38
Walter, G., & Ruediger, R. (2012) · Cell Cycle · doi:10.4161/cc.11.3.19057 · Cited by 38
Role for PP2A in ARF signaling to p53
Moule, M. G., Collins, C. H., McCormick, F. P., & Fried, M. (2004) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0405533101 · Cited by 37
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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
“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.”
BackgroundMethodInfluentialKe, W., Zhou, Y., Lai, Y., Long, S., Fang, L., & Xiao, S. (2021) · Redox Biology · doi:10.1016/j.redox.2021.102207 · Cited by 36
Biased holoenzyme assembly of protein phosphatase 2A (PP2A): From cancer to small molecules
Haanen, T. J., O’Connor, C. M., & Narla, G. (2022) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2022.102656 · Cited by 38
Elshazly, A. M., & Gewirtz, D. A. (2022) · Cancer Drug Resistance · doi:10.20517/cdr.2022.09 · Cited by 35
Heterogeneous nuclear ribonucleoprotein A2 is a SET-binding protein and a PP2A inhibitor
Vera, J., Jaumot, M., Estanyol, J. M., Brun, S., Agell, N., & Bachs, O. (2005) · Oncogene · doi:10.1038/sj.onc.1209050 · Cited by 36
Bai, X., Zhang, Q., Ye, L., Hu, Q., Fu, Q., Zhi, X., Su, W., Su, R.-G., Ma, T., Chen, W., et al. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0800 · Cited by 36
Self-citationGaribal, J., Hollville, É., Bell, A. I., Kelly, G. L., Renouf, B., Kawaguchi, Y., Rickinson, A. B., & Wiels, J. (2007) · Journal of Virology · doi:10.1128/jvi.02435-06 · Cited by 36
He, C., Qiu, Y., Han, P., Chen, Y., Zhang, L., Yuan, Q., Zhang, T., Cheng, T., Yuan, L., Huang, C., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0787-3 · Cited by 35
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The protein phosphatase 2A B56γ regulatory subunit is required for heart development
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Epigenetic mechanisms affect mutant p53 transgene expression in WAP-mutp53 transgenic mice
Krepulat, F., Löhler, J., Heinlein, C., Hermannstädter, A., Tolstonog, G. V., & Deppert, W. (2005) · Oncogene · doi:10.1038/sj.onc.1208557 · Cited by 34
DNA tumor viruses — the spies who lyse us
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Wang, H., Liu, J., Lin, S., Wang, B., Xing, M., Guo, Z., & Xu, L. (2014) · Chemosphere · doi:10.1016/j.chemosphere.2014.03.130 · Cited by 33
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Tao, G., Toivola, D. M., Zhou, Q., Strnad, P., Xu, B., Michie, S. A., & Omary, M. B. (2006) · Journal of Cell Science · doi:10.1242/jcs.02861 · Cited by 33
Robles, O., & McDonald, F. E. (2009) · Organic Letters · doi:10.1021/ol902365n · Cited by 33
Wainszelbaum, M. J., Liu, J., Chen, K., Srikanth, P., Samovski, D., Su, X., & Stahl, P. D. (2012) · PLoS ONE · doi:10.1371/journal.pone.0031225 · Cited by 32
Tang, X., & Wang, Y. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0607856103 · Cited by 31
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Dynia, D. W., Steinmetz, A. G., & Kocinsky, H. S. (2009) · American Journal of Physiology-Renal Physiology · doi:10.1152/ajprenal.00182.2009 · Cited by 32
Messner, D. J., Romeo, C., Boynton, A. L., & Rossie, S. S. (2006) · Journal of Cellular Biochemistry · doi:10.1002/jcb.20919 · Cited by 32
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Chen, L., Guo, P., Li, W., Fang, F., Zhu, W., Fan, J., Wang, F., Gao, Y., Zhao, Q., Wang, Q., et al. (2020) · Hepatology · doi:10.1002/hep.31457 · Cited by 31
Self-citationÁlvarez‐Fernández, M., Halim, V. A., Aprelia, M., Mohammed, S., & Medema, R. H. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.253724 · Cited by 30
Mainwaring, L. A., & Kenney, A. M. (2011) · Oncogene · doi:10.1038/onc.2010.564 · Cited by 31
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de Curtis, I. (2010) · Experimental Cell Research · doi:10.1016/j.yexcr.2010.09.014 · Cited by 29
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Peris, I., Romero-Murillo, S., Vicente, C., Narla, G., & Odero, M. D. (2023) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2023.188953 · Cited by 30
Andrabi, S., Hwang, J. H., Choe, J. K., Roberts, T. M., & Schaffhausen, B. S. (2011) · Journal of Virology · doi:10.1128/jvi.05034-11 · Cited by 27
Zhu, X., Li, D., Zhang, Z., Zhu, W., Li, W., Zhao, J., Xing, X., He, Z., Wang, S., Wang, F., et al. (2016) · Molecular Carcinogenesis · doi:10.1002/mc.22605 · Cited by 27
Self-citationKotadia, S., Kao, L.-R., Comerford, S. A., Jones, R. T., Hammer, R. E., & Megraw, T. L. (2008) · Oncogene · doi:10.1038/onc.2008.254 · Cited by 27
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Lee, W., Kim, D., Lee, M., & Choi, K. (2006) · PROTEOMICS · doi:10.1002/pmic.200600480 · Cited by 27
Chen, L., Guo, P., Zhang, H., Li, W., Gao, C., Huang, Z., Fan, J., Zhang, Y., Li, X., Liu, X., et al. (2018) · Journal of Biological Chemistry · doi:10.1074/jbc.ra118.006319 · Cited by 25
Self-citationKurimchak, A., & Graña, X. (2012) · Genes & Cancer · doi:10.1177/1947601912473479 · Cited by 29
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Schaick, J. C. A.-V., Kim, S., DiFabio, C., Lee, M., Broman, K. W., & Reilly, K. M. (2012) · Neuro-Oncology · doi:10.1093/neuonc/nor206 · Cited by 26
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Sim, A. T. R., Ludowyke, R. I., & Verrills, N. M. (2006) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2006.04.011 · Cited by 25
Li, X., Nan, A., Xiao, Y., Chen, Y., & Lai, Y. (2015) · Toxicology · doi:10.1016/j.tox.2015.03.007 · Cited by 26
Jannasch, K., Dullin, C., Heinlein, C., Krepulat, F., Wegwitz, F., Deppert, W., & Alves, F. (2009) · International Journal of Cancer · doi:10.1002/ijc.24332 · Cited by 24
Gilan, O., Diesch, J., Amalia, M., Jastrzebski, K., Chüeh, A. C., Verrills, N. M., Pearson, R. B., Mariadason, J. M., Tulchinsky, E. M., Hannan, R. D., et al. (2014) · Oncogene · doi:10.1038/onc.2014.26 · Cited by 24
Avelar, R. A., Armstrong, A. J., Carvette, G., Gupta, R., Puleo, N., Colina, J. A., Joseph, P. L., Sobeck, A. M., O’Connor, C. M., Raines, B., et al. (2023) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-21-0880 · Cited by 25
Magnúsdóttir, A., Stenmark, P., Flodin, S., Nyman, T., Hammarström, M., Ehn, M., H., M. A. B., Berglund, H., & Nordlund, P. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.c600100200 · Cited by 24
Wang, L., Guo, X., Zhou, W., Ding, Y., Shi, J., Wu, X., Liu, Y., Xu, Y., Yang, H., & Geng, D. (2018) · Acta Biomaterialia · doi:10.1016/j.actbio.2018.04.013 · Cited by 21
Mahale, A. M., Khan, Z., Igarashi, M., Nanjangud, G. J., Qiao, R., Yao, S., Lee, S. W., & Aaronson, S. A. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-3021 · Cited by 21
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Nasa, I., & Kettenbach, A. N. (2020) · Biochemical Society Transactions · doi:10.1042/bst20200177 · Cited by 22
Fleisig, H. B., & Wong, J. M. Y. (2011) · Oncogene · doi:10.1038/onc.2011.292 · Cited by 21
Metadata
- Authors
- Chen, W., Possemato, R., Campbell, K. T., Plattner, C. A., Pallas, D. C., & Hahn, W. C.
- Affiliations
- Brigham and Women's Hospital (US)
- Emory University (US)
- Corresponding author
- Hahn, William C
- Venue
- Cancer Cell
- Publisher
- Elsevier BV
- Published
- 2004-02
- Volume
- 5
- Issue
- 2
- Pages
- 127-136
- ISSN
- 1535-6108 (ISSN-L)
- OpenAlex
- W1971212979
- Cited by
- 325
- References
- 56
- Citations by year
- 2026: 1 · 2025: 6 · 2024: 2 · 2023: 14 · 2022: 10 · 2021: 12 · 2020: 14 · 2019: 16 · 2018: 13 · 2017: 9 · 2016: 8 · 2015: 13 · 2014: 15 · 2013: 14 · 2012: 19
- FWCI
- 9.95
- Type
- journal article
- Language
- en
- Update notices
- erratum (2024-06-10)
- Open access
- bronze
- doi.org
- Licence
- Locations
- Cancer Cell (publishedVersion)
- PubMed (publishedVersion)
- Funders
- National Cancer Institute (R01 CA57327, P01 CA 50661, K01CA94223, K01CA094223, P01CA050661, R01CA057327)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Signaling Pathways in Disease
- Keywords
- protein phosphatase 2A, small T antigen, SV40 large T antigen, cell transformation, anchorage-independent growth, tumorigenicity, H-Ras, hTERT, lung cancer
- MeSH terms
- Animals, Antigens, Viral, Tumor, Cell Transformation, Neoplastic, Cells, Cultured, Cloning, Molecular, DNA-Binding Proteins, Enzyme Activation, Epithelial Cells, Humans, Phosphoprotein Phosphatases, Phosphorylation, Protein Binding, Genes, ras, Signal Transduction, Telomerase, Protein Subunits, Protein Phosphatase 2
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