The DOI matches its Crossref record; 138 of the 138 references it cites were found in a registry or an index.
Phosphatase‐mediated crosstalk between MAPK signaling pathways in the regulation of cell survival
Abstract
Mitogen-activated protein kinase (MAPK) pathways constitute a large modular network that regulates a variety of physiological processes, such as cell growth, differentiation, and apoptotic cell death. The function of the ERK pathway has been depicted as survival-promoting, in essence by opposing the proapoptotic activity of the stress-activated c-Jun NH(2)-terminal kinase (JNK)/p38 MAPK pathways. However, recently published work suggests that extracellular regulated kinase (ERK) pathway activity is suppressed by JNK/p38 kinases during apoptosis induction. In this review, we will summarize the current knowledge about JNK/p38-mediated mechanisms that negatively regulate the ERK pathway. In particular, we will focus on phosphatases (PP2A, MKPs) as inhibitors of ERK pathway activity in regulating apoptosis. A model proposed in this review places the negative regulation of the ERK pathway in a central position for the cellular decision-making process that determines whether cells will live or die in response to apoptosis-promoting signals. In addition, we will discuss the potential functional relevance of negative regulation of ERK pathway activity, for physiological and pathological conditions (e.g., cellular transformation).
Overview
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
In the citing paper
“The p38 pathway has been reported to interfere with ERK activity during apoptosis (see 88 for review); thus, ERK activity was assayed in these genotypes by measuring phospho-ERK levels.”
From Functional genomic screen and network analysis reveal novel modifiers of tauopathy dissociated from tau phosphorylation (2011) · cites this paper as [88]
Citations
Cites
1 retracted
A Regulatory Role for p38δ MAPK in Keratinocyte Differentiation
Efimova, T., Broome, A., & Eckert, R. L. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302759200 · Cited by 135
RetractedMutations of the BRAF gene in human cancer
Davies, H., Bignell, G. R., Cox, C., Stephens, P., Edkins, S., Clegg, S., Teague, J., Woffendin, H., Garnett, M. J., Bottomley, W., et al. (2002) · Nature · doi:10.1038/nature00766 · Cited by 10,674
Opposing Effects of ERK and JNK-p38 MAP Kinases on Apoptosis
Xia, Z., Dickens, M., Raingeaud, J., Davis, R. J., & Greenberg, M. E. (1995) · Science · doi:10.1126/science.270.5240.1326 · Cited by 5,273
Signal transduction by the JNK group of MAP kinases
Davis, R. J. (2000) · Cell · doi:10.1016/s0092-8674(00)00116-1 · Cited by 4,237
Mitogen-Activated Protein (MAP) Kinase Pathways: Regulation and Physiological Functions*
Pearson, G. W., Robinson, F. L., Gibson, T. B., Xu, B.-E., Karandikar, M. S., Berman, K. S., & Cobb, M. H. (2001) · Endocrine Reviews · doi:10.1210/edrv.22.2.0428 · Cited by 4,111
AP-1 as a regulator of cell life and death
Shaulian, E., & Karin, M. (2002) · Nature Cell Biology · doi:10.1038/ncb0502-e131 · Cited by 2,961 · cited 1×
“The most classical JNK substrate is the transcription factor c-Jun, from which JNK derived its name (2, 5, 33).”
BackgroundProtein kinases and phosphatases: The Yin and Yang of protein phosphorylation and signaling
Hunter, T. R. (1995) · Cell · doi:10.1016/0092-8674(95)90405-0 · Cited by 2,961
Targeting the Raf-MEK-ERK mitogen-activated protein kinase cascade for the treatment of cancer
Roberts, P. J., & Der, C. J. (2007) · Oncogene · doi:10.1038/sj.onc.1210422 · Cited by 2,788
Roux, P. P., & Blenis, J. (2004) · Microbiology and Molecular Biology Reviews · doi:10.1128/mmbr.68.2.320-344.2004 · Cited by 2,540
Raingeaud, J., Gupta, S., Rogers, J. S., Dickens, M., Han, J., Ulevitch, R. J., & Davis, R. J. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.13.7420 · Cited by 2,244
Flagged first, then by citations
Research works printed but not linked: 1
- 10.1042/bj3530417 · DOI
Cited by
Sorted by citations
Items 101–200 of 826
Li, X., Stevens, P. D., Liu, J., Yang, H., Wang, W. T., Wang, C., Zeng, Z., Schmidt, M. D., Yang, M., Lee, E. Y., et al. (2014) · Gastroenterology · doi:10.1053/j.gastro.2014.02.003 · Cited by 89
Rhodiola roseaL. and Alzheimer's Disease: From Farm to Pharmacy
Nabavi, S. F., Braidy, N., Orhan, İ. E., Badiee, A., Daglia, M., & Nabavi, S. M. (2016) · Phytotherapy Research · doi:10.1002/ptr.5569 · Cited by 90
Hung, Y.-F., Chen, C.-Y., Shih, Y.-C., Liu, H.-Y., Huang, C.-M., & Hsueh, Y.-P. (2018) · Journal of Cell Biology · doi:10.1083/jcb.201712113 · Cited by 86
LRRK2 signaling pathways: the key to unlocking neurodegeneration?
Berwick, D. C., & Harvey, K. (2011) · Trends in Cell Biology · doi:10.1016/j.tcb.2011.01.001 · Cited by 86
Jiang, Y., Wang, X., & Hu, D. (2017) · Cell Death and Disease · doi:10.1038/cddis.2017.220 · Cited by 86
Battaglia-Hsu, S.-F., Akchiche, N., Noel, N., Alberto, J., Jeannesson, É., Orozco-Barrios, C. E., Martínez‐Fong, D., Daval, J., & Guéant, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0811794106 · Cited by 86
Almalki, S. G., & Agrawal, D. K. (2017) · Stem Cell Research & Therapy · doi:10.1186/s13287-017-0568-4 · Cited by 86
Oxidative Stress and Pathways of Molecular Hydrogen Effects in Medicine
Slezák, J., Kura, B., LeBaron, T. W., Singal, P. K., Buday, J., & Barančík, M. (2020) · Current Pharmaceutical Design · doi:10.2174/1381612826666200821114016 · Cited by 95
TRAIL combinations: The new ‘trail’ for cancer therapy (Review)
Refaat, A., Abdrabou, A., & Reda, A. M. (2014) · Oncology Letters · doi:10.3892/ol.2014.1922 · Cited by 87
Extracellular Acidification Elicits Spatially and Temporally Distinct Ca2+ Signals
Huang, W., Swietach, P., Vaughan‐Jones, R. D., Ansorge, O., & Glitsch, M. D. (2008) · Current Biology · doi:10.1016/j.cub.2008.04.049 · Cited by 84
Liu, R., Zheng, H., Zhou, Z., Dong, J., & Chen, C. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m808919200 · Cited by 82
Shah, S., King, E. M., Chandrasekhar, A., & Newton, R. C. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.540799 · Cited by 81
García, C., Aranda, J., Arnold, E., Thébault, S. C., Macotela, Y., López‐Casillas, F., Mendoza, V., Quiroz–Mercado, H., Hernández-Montiel, H. L., Lin, S.-H., et al. (2008) · Journal of Clinical Investigation · doi:10.1172/jci34508 · Cited by 81
Subclonal mutations in SETBP1 confer a poor prognosis in juvenile myelomonocytic leukemia
Stieglitz, E., Troup, C. B., Gelston, L. C., Haliburton, J. R., Chow, E. D., Yu, K. B., Akutagawa, J., Taylor-Weiner, A. N., Liu, Y. L., Wang, Y., et al. (2014) · Blood · doi:10.1182/blood-2014-09-601690 · Cited by 79
Feng, W., Su, S., Song, C., Yu, F. D., Zhou, J., Li, J., Jia, R., Xu, P., & Tang, Y. (2022) · Antioxidants · doi:10.3390/antiox11102029 · Cited by 80
Galluzzo, P., Martini, C., Bulzomi, P., Leone, S., Bolli, A., Pallottini, V., & Marino, M. (2009) · Molecular Nutrition & Food Research · doi:10.1002/mnfr.200800239 · Cited by 80
Huang, X., Huang, Y., Ouyang, Z., Cai, J. X., Yan, Y., & Qin, Q. (2011) · Journal of General Virology · doi:10.1099/vir.0.029173-0 · Cited by 78
Ghosh, S., Baltussen, M. G., Ivanov, N. M., Haije, R., Jakštaitė, ., Zhou, T., & Huck, W. T. S. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00681 · Cited by 84
Castro, N., & Lange, C. A. (2010) · Breast Cancer Research · doi:10.1186/bcr2622 · Cited by 77
Bott, A., Erdem, N., Lerrer, S., Hotz‐Wagenblatt, A., Breunig, C., Abnaof, K., Wörner, A., Wilhelm, H., Münstermann, E., Ben‐Baruch, A., et al. (2017) · Oncotarget · doi:10.18632/oncotarget.14915 · Cited by 75
Eskandari, A., & Suntharalingam, K. (2019) · Chemical Science · doi:10.1039/c9sc01275c · Cited by 80
Warr, N., Bogani, D., Siggers, P., Brixey, R., Tateossian, H., Dopplapudi, A., Wells, S. E., Cheeseman, M. T., Xia, Y., D, H. O. M., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0019572 · Cited by 76
Workman, H. C., Sweeney, C. A., & Carraway, K. L. (2009) · Cancer Research · doi:10.1158/0008-5472.can-08-2089 · Cited by 76
Ishii, T., Takanashi, Y., Sugita, K., Miyazawa, M., Yanagihara, R., Yasuda, K., Onouchi, H., Kawabe, N., Nakata, M., Yamamoto, Y., et al. (2016) · Aging Cell · doi:10.1111/acel.12523 · Cited by 78
Tentner, A. R., Lee, M. J., Ostheimer, G. J., Samson, L. D., Lauffenburger, D. A., & Yaffe, M. B. (2012) · Molecular Systems Biology · doi:10.1038/msb.2012.1 · Cited by 74
Non-Genomic Effects of Xenoestrogen Mixtures
Viñas, R., Jeng, Y., & Watson, C. S. (2012) · International Journal of Environmental Research and Public Health · doi:10.3390/ijerph9082694 · Cited by 79
Viñas, R., & Watson, C. S. (2013) · Environmental Health · doi:10.1186/1476-069x-12-26 · Cited by 74
Lu, Y., Li, R., Zhu, J., Wu, Y., Li, D., Dong, L., Li, Y., Wen, X., Yu, F., Zhang, H., et al. (2018) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.13952 · Cited by 74
Aviello, G., Rowland, I. R., Gill, C. I., Acquaviva, A. M., Capasso, F., McCann, M. J., Capasso, R., Izzo, A. A., & Borrelli, F. (2009) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2009.00815.x · Cited by 74
Tian, X. Y., Yung, L. H., Wong, W. T., Liu, J., Leung, F. P., Liu, L., Chen, Y., Kong, S. K., Kwan, K. M., Ng, S., et al. (2011) · Journal of Molecular and Cellular Cardiology · doi:10.1016/j.yjmcc.2011.10.013 · Cited by 74
Steroidogenesis—Adrenal Cell Signal Transduction
Gallo‐Payet, N., & Battista, M. (2014) · Comprehensive physiology · doi:10.1002/cphy.c130050 · Cited by 87
Zamora‐Olivares, D., Kaoud, T. S., Dalby, K. N., & Anslyn, E. V. (2013) · Journal of the American Chemical Society · doi:10.1021/ja407397z · Cited by 73
The role of mitogen‐ and stress‐activated protein kinase pathways in melanoma
Lopez‐Bergami, P. (2011) · Pigment Cell & Melanoma Research · doi:10.1111/j.1755-148x.2011.00908.x · Cited by 75
Dual-Specificity Phosphatase Regulation in Neurons and Glial Cells
Pérez‐Sen, R., Queipo, M. J., Gil‐Redondo, J. C., Ortega, F., Gómez‐Villafuertes, R., Miras‐Portugal, M. T., & Delicado, E. G. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20081999 · Cited by 71
Breckpot, K., & Escors, D. (2009) · Endocrine Metabolic & Immune Disorders - Drug Targets · doi:10.2174/187153009789839156 · Cited by 70
Jung, T. W., Hwang, H., Hong, H. C., Choi, H. Y., Yoo, H. J., Baik, S. H., & Choi, K. M. (2014) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2014.04.012 · Cited by 73
Lo, U., Selvaraj, V., Plane, J. M., Chechneva, O. V., Otsu, K., & Deng, W. (2014) · Scientific Reports · doi:10.1038/srep07405 · Cited by 69
Xu, C., Wang, X., Zhu, Y., Dong, X., Liu, C., Zhang, H., Liu, L., Huang, S., & Chen, L. (2016) · Neuropharmacology · doi:10.1016/j.neuropharm.2016.01.030 · Cited by 69
New Insights into the Process of Placentation and the Role of Oxidative Uterine Microenvironment
Mendes, S., Timóteo-Ferreira, F., Almeida, H., & Silva, E. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/9174521 · Cited by 74
Cadmium is a potent inhibitor of PPM phosphatases and targets the M1 binding site
Pan, C., Liu, H., Gong, Z., Yu, X., Hou, X., Xie, D., Zhu, X.-B., Li, H., Tang, J., Xu, Y., et al. (2013) · Scientific Reports · doi:10.1038/srep02333 · Cited by 68
Targeting MAPK (Ras/ERK) and PI3K/Akt pathways in pituitary tumorigenesis
Çakır, M., & Grossman, A. B. (2009) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728220903170675 · Cited by 69
Wang, Y., Zhou, X., Lei, Y., Chu, Y., Yu, X., Tong, Q., Zhu, T., Yu, H., Fang, S., Li, G., et al. (2022) · Cancer Letters · doi:10.1016/j.canlet.2022.215884 · Cited by 67
Li, C., Xing, G., Dong, M., Li, Z., Li, J., Wang, G., Zou, D.-J., Wang, R., Liu, J., & Niu, Y. (2010) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2010.03.013 · Cited by 66
Duan, Y., Li, J., Jing, X., Ding, X., Yu, Y., & Zhao, Q. (2020) · Cancer Management and Research · doi:10.2147/cmar.s243495 · Cited by 68
Huang, G., Tang, B., TANG, K., Dong, X., Deng, J., Liao, L., Liao, Z., Yang, H., & He, S. (2014) · Oncology Reports · doi:10.3892/or.2014.3099 · Cited by 66
RetractedHofstetter, C. P., Burkhardt, J., Shin, B. J., Gursel, D. B., Mubita, L. L., Gorrepati, R., Brennan, C. W., Holland, E. C., & Boockvar, J. A. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030059 · Cited by 66
Glucocorticoids promote apoptosis of proinflammatory monocytes by inhibiting ERK activity
Achuthan, A. A., Aslam, A. S. M., Nguyen, Q., Lam, P. Y., Fleetwood, A. J., Frye, A. T., Louis, C., Lee, M.-C., Smith, J. E., Cook, A. D., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0332-4 · Cited by 67
Anti-Inflammatory and Neuroprotective Effects of Constituents Isolated fromRhodiola rosea
Lee, Y., Jung, J., Jang, S., Kim, J., Ali, Z., Khan, I. A., & Oh, S. (2013) · Evidence-based Complementary and Alternative Medicine · doi:10.1155/2013/514049 · Cited by 65
Increased extracellular matrix density disrupts E-cadherin/β-catenin complex in gastric cancer cells
Jang, M., Koh, I., Lee, J. E., Lim, J. Y., Cheong, J., & Kim, P. (2018) · Biomaterials Science · doi:10.1039/c8bm00843d · Cited by 67
Fluoxetine-induced apoptosis in hepatocellular carcinoma cells.
Mun, A.-R., Lee, S., Kim, G.-B., Kang, H., Kim, J., & Kim, S. (2013) · PubMed · Cited by 64
Poddar, R., & Paul, S. (2012) · Journal of Neurochemistry · doi:10.1111/jnc.12102 · Cited by 63
Yu, H.-C., Hung, M.-H., Chen, Y.-L., Chu, P.-Y., Wang, C. Y., Chao, T.-T., Liu, C.-Y., Shiau, C.-W., & Chen, K.-F. (2014) · Cell Death and Disease · doi:10.1038/cddis.2014.325 · Cited by 63
Paraneoplastic CDR2 and CDR2L antibodies affect Purkinje cell calcium homeostasis
Schubert, M., Panja, D., Haugen, M., Bramham, C. R., & Vedeler, C. A. (2014) · Acta Neuropathologica · doi:10.1007/s00401-014-1351-6 · Cited by 63
Xiang, Q.-D., Yu, Q., Wang, H., Zhao, M.-M., Liu, S., Nie, S., & Xie, M. (2017) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.7b01763 · Cited by 64
Huang, J., Huang, N., Xu, S., Luo, Y., Li, Y., Jin, H. D., Yu, C., Shi, J., & Jin, F. J. (2020) · The Journal of Nutritional Biochemistry · doi:10.1016/j.jnutbio.2020.108552 · Cited by 66
Dentin Matrix Protein 1 (DMP1) Signals via Cell Surface Integrin
Wu, H., Teng, P.-N., Jayaraman, T., Onishi, S., Li, J., Bannon, L. J., Huang, H., Close, J. M., & Sfeir, C. S. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.194746 · Cited by 63
Wandzioch, E., Pusey, M., Werda, A., Bail, S., Bhaskar, A., Nestor, M., Yang, J., & Rice, L. M. (2014) · Cancer Research · doi:10.1158/0008-5472.can-13-3130 · Cited by 64
Faust, D., Schmitt, C. R., Oesch, F., Oesch‐Bartlomowicz, B., Schreck, I., Weiß, C., & Dietrich, C. (2012) · Cell Communication and Signaling · doi:10.1186/1478-811x-10-6 · Cited by 62
Chang, W., Liu, T., Yang, W.-K., Lee, C.-C., Lin, Y., Chen, T., & Chang, J. (2011) · Cancer Research · doi:10.1158/0008-5472.can-10-1037 · Cited by 61
Nanosecond pulsed electric fields activate MAPK pathways in human cells
Morotomi‐Yano, K., Akiyama, H., & Yano, K. (2011) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2011.09.002 · Cited by 61
Super-low Dose Endotoxin Pre-conditioning Exacerbates Sepsis Mortality
Chen, K., Geng, S., Yuan, R., Diao, N., Upchurch, Z., & Li, L. (2015) · EBioMedicine · doi:10.1016/j.ebiom.2015.03.001 · Cited by 63
Croons, V., Martinet, W., Herman, A. G., Timmermans, J., & Meyer, G. R. Y. D. (2009) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.108.149948 · Cited by 59
Dziegielewska, B., Brautigan, D. L., Larner, J. M., & Dziegielewski, J. (2013) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-13-0485 · Cited by 64
Kück, U., Beier, A., & Teichert, I. (2015) · Fungal Genetics and Biology · doi:10.1016/j.fgb.2015.10.001 · Cited by 61
Regulatory Actions of Estrogen Receptor Signaling in the Cardiovascular System
Ueda, K., Adachi, Y., Liu, P., Fukuma, N., & Takimoto, E. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2019.00909 · Cited by 60
Ueda, K., & Karas, R. H. (2012) · Steroids · doi:10.1016/j.steroids.2012.12.006 · Cited by 62
Viñas, R., Goldblum, R. M., & Watson, C. S. (2013) · Endocrine Disruptors · doi:10.4161/endo.25411 · Cited by 60
Wang, A., Liu, J., Zhuang, X., Yu, S., Zhu, S. Y., Liu, Y., & Chen, X. (2020) · Stem Cells and Development · doi:10.1089/scd.2019.0277 · Cited by 59
Lee, H.-S., Hwang, C. Y., Shin, S., Kwon, K., & Cho, K. (2014) · Science Signaling · doi:10.1126/scisignal.2005260 · Cited by 62
p53 Plays an Important Role in Cell Fate Determination after Exposure to Microcystin-LR
Takumi, S., Komatsu, M., Furukawa, T., Ikeda, R., Sumizawa, T., Akenaga, H., Maeda, Y., Aoyama, K., Arizono, K., Ando, S., et al. (2010) · Environmental Health Perspectives · doi:10.1289/ehp.1001899 · Cited by 58
Huang, C., Zhang, P., Wang, W., Xu, Y., Wang, M., Chen, X., & Dong, X. (2014) · APOPTOSIS · doi:10.1007/s10495-014-0983-2 · Cited by 58
Jonckheere, N., Skrypek, N., Merlin, J., Dessein, A., Dumont, P., Leteurtre, E., Harris, A., Desseyn, J., Susini, C., Frénois, F., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0032232 · Cited by 65
Guo, F., Hildeman, D. A., Tripathi, P., Velu, C. S., Grimes, H. L., & Zheng, Y. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1010249107 · Cited by 56
Porter, F. W., Brown, B., & Palmenberg, A. C. (2010) · Journal of Virology · doi:10.1128/jvi.01484-09 · Cited by 57
Chen, K., Lu, Y., Liu, C., Zhang, L., Fang, Z., & Yu, G. (2018) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2018.07.047 · Cited by 57
Branched-chain ketoacid overload inhibits insulin action in the muscle
Biswas, D., Dao, K. T., Mercer, A., Cowie, A. M., Duffley, L., Hiani, Y. E., Kienesberger, P. C., & Pulinilkunnil, T. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.013121 · Cited by 58
Intestinal Cell Proliferation and Senescence Are Regulated by Receptor Guanylyl Cyclase C and p21
Basu, N., Saha, S., Khan, I., Ramachandra, S. G., & Visweswariah, S. S. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.511311 · Cited by 57
Crosstalk and Competition in Signaling Networks
Rowland, M. A., Fontana, W., & Deeds, E. J. (2012) · Biophysical Journal · doi:10.1016/j.bpj.2012.10.006 · Cited by 57
Zhu, G., Li, Y.-W., Tse, A. K., Hau, D. K.-P., Leung, C., Yu, Z., & Fong, W. F. (2011) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2011.06.008 · Cited by 57
Pro-survival effects of JNK and p38 MAPK pathways in LPS-induced activation of BV-2 cells
Svensson, C., Part, K., Künnis-Beres, K., Kaldmäe, M., Fernaeus, S. Z., & Land, T. (2011) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2011.02.083 · Cited by 56
Beta-Asarone Attenuates Neuronal Apoptosis Induced by Beta Amyloid in Rat Hippocampus
Liu, J., Li, C., Xing, G., Li, Z. H. O. U., Dong, M., Geng, Y.-T., Li, X., Li, J., Wang, G., Zou, D.-J., et al. (2010) · YAKUGAKU ZASSHI · doi:10.1248/yakushi.130.737 · Cited by 57
Chen, H., Jia, W., Li, H., Han, H., Li, D., Zhang, X., Li, J., Yuan, Y., & Wu, C. (2019) · NeuroMolecular Medicine · doi:10.1007/s12017-019-08582-2 · Cited by 57
Oxidative stress response induced by chemotherapy in leukemia treatment (Review)
Zhang, J., Lei, W., Chen, X., Wang, S., & Qian, W. (2018) · Molecular and Clinical Oncology · doi:10.3892/mco.2018.1549 · Cited by 59
Dias, E. M., Matos, P., Pereira, P., Batoréu, M. C. C., Silva, M. J., & Jordan, P. (2010) · Toxicology in Vitro · doi:10.1016/j.tiv.2010.05.018 · Cited by 56
Gobbi, G., Ricci, F., Malinverno, C., Carubbi, C., Pambianco, M., Panfilis, G. D., Vitale, M., & Mirandola, P. (2009) · Laboratory Investigation · doi:10.1038/labinvest.2009.61 · Cited by 56
Chen, M., Wan, L., Zhang, J., Zhang, J., Mendez, L., Clohessy, J. G., Berry, K., Victor, J., Yin, Q., Zhu, Y., et al. (2018) · Nature Communications · doi:10.1038/s41467-017-02272-y · Cited by 61
Liang, Z., Yuan, Z., Guo, J., Wu, J., Yi, J., Deng, J., & Shan, Y. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20030478 · Cited by 56
Xu, T., Wu, X., Chen, Q., Zhu, S., Liu, Y., Pan, D., Chen, X., & Li, D. (2014) · PLoS ONE · doi:10.1371/journal.pone.0102292 · Cited by 55
Regulation of protein phosphatase 2A (PP2A) tumor suppressor function by PME-1
Kaur, A., & Westermarck, J. K. (2016) · Biochemical Society Transactions · doi:10.1042/bst20160161 · Cited by 58
Self-citationKe, Z., Lu, J., Zhu, J., Yang, Z., Jin, Z., & Yuan, L. (2019) · Infection Genetics and Evolution · doi:10.1016/j.meegid.2019.104077 · Cited by 55
Zhu, Z., Li, W., Zhang, X., Wang, C., Gao, L., Yang, F., Cao, W., Li, K., Tian, H. W., Liu, X., et al. (2019) · Journal of Virology · doi:10.1128/jvi.01350-19 · Cited by 56
Loughlin, D. T., & Artlett, C. M. (2011) · PLoS ONE · doi:10.1371/journal.pone.0018676 · Cited by 54
Wei, W., Jiao, Y., Postlethwaite, A. E., Stuart, J. M., Wang, Y., Sun, D., & Gu, W. (2012) · Genes and Immunity · doi:10.1038/gene.2012.54 · Cited by 53
Tripathy, S. K., De, U., Dehury, N., Laha, P., Panda, M. K., Kim, H. S., & Patra, S. (2016) · Dalton Transactions · doi:10.1039/c6dt00929h · Cited by 54
Li, R., Wu, Y., Zou, S., Wang, X., Li, Y., Xu, K., Gong, F., Liu, Y., Wang, J., Liao, Y., et al. (2017) · Neurochemical Research · doi:10.1007/s11064-017-2333-6 · Cited by 54
Park, J. G., Aziz, N., & Cho, J. Y. (2019) · Therapeutic Advances in Medical Oncology · doi:10.1177/1758835919875574 · Cited by 57
Lv, X. C., & Zhou, H. (2012) · Canadian Journal of Physiology and Pharmacology · doi:10.1139/y2012-051 · Cited by 53
ILT3.Fc–CD166 Interaction Induces Inactivation of p70 S6 Kinase and Inhibits Tumor Cell Growth
Xu, Z., Chang, C., Li, M., Zhang, Q., Vasilescu, E. R., D’Agati, V. D., Floratos, A., Vlad, G., & Suciu‐Foca, N. (2017) · The Journal of Immunology · doi:10.4049/jimmunol.1700553 · Cited by 54
Takanche, J. S., Kim, J.-E., Kim, J., Lee, M., Jeon, J., Park, I., & Yi, H. (2018) · Artificial Cells Nanomedicine and Biotechnology · doi:10.1080/21691401.2018.1513940 · Cited by 56
In vitro immunomodulatory effects of human milk oligosaccharides on murine macrophage RAW264.7 cells
Zhang, W., Yan, J., Wu, L., Yu, Y., Ye, R. D., Zhang, Y., & Liang, X. (2018) · Carbohydrate Polymers · doi:10.1016/j.carbpol.2018.11.039 · Cited by 52
Metadata
- Authors
- Junttila, M. R., Li, S., & Westermarck, J.
- Affiliations
- Åbo Akademi University (FI)
- University of Helsinki (FI)
- Venue
- The FASEB Journal
- Publisher
- Wiley
- Published
- 2007-11-26
- Volume
- 22
- Issue
- 4
- Pages
- 954-965
- ISSN
- 0892-6638 (ISSN-L)
- 1530-6860
- OpenAlex
- W2003060606
- Cited by
- 826
- References
- 138
- Citations by year
- 2026: 12 · 2025: 21 · 2024: 24 · 2023: 19 · 2022: 32 · 2021: 48 · 2020: 28 · 2019: 36 · 2018: 42 · 2017: 41 · 2016: 58 · 2015: 49 · 2014: 76 · 2013: 72 · 2012: 74
- FWCI
- 3.08
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- The FASEB Journal (publishedVersion)
- PubMed (publishedVersion)
- 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 › Melanoma and MAPK Pathways
- Keywords
- ERK signaling, phosphatase, protein phosphatase 2A, apoptosis, cell survival
- MeSH terms
- Animals, Cell Survival, Humans, Models, Biological, Phosphoprotein Phosphatases, Mitogen-Activated Protein Kinases, MAP Kinase Signaling System
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