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Activation and Association of Stat3 with Src in v-Src-Transformed Cell Lines
Open accessAbstract
STAT proteins are a group of latent cytoplasmic transcription factors which function as signal transducers and activators of transcription. Stat1 and -2 were originally identified to function in interferon signaling, and Stat1 was also found to be activated by epidermal growth factor (EGF) and other cytokines. New members of the STAT gene family are identified. Among them, Stat3 has 52.5% amino acid sequence homology with Stat1 and is activated by platelet-derived growth factor (PDGF), colony-stimulating factor 1 (CSF-1), EGF, interleukin-6, and other cytokines. Treatment of cells with EGF activates Stat1 and Stat3, which become phosphorylated on tyrosine residues to form homo - or heterodimers and translocate into the nucleus, binding to the sis-inducible element (SIE) in the c-fos promoter. Somatic cell genetic analyses demonstrated that Jaks, a family of nontransmembrane protein tyrosine kinases, are required for the activation of Stat1 and Stat2 in interferon-treated cells. However, little is known about the activation of Stat3 by growth factors. Here we report that in all v-Src-transformed cell lines examined, Stat3 is constitutively activated to bind to DNA and the phosphorylation of tyrosine on Stat3 is enhanced by the induction of v-Src expression. We also report that Src is shown to be associated with Stat3 in vivo, as well as in vitro, and phosphorylates Stat3 in vitro. Stat3 is also activated by CSF-1, possibly through CSF-1 receptor-c Src association in NIH 3T3 cells overexpressing CSF-1 receptors. Together, the data suggest that Src is involved in activation of Stat3 in growth factor signal transduction.
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“A number of transformed cell lines as well as samples from human cancers are reported to contain constitutively activated STAT3.”
From STAT3 Contributes to the Mitogenic Response of Hepatocytes during Liver Regeneration (2002) · cites this paper as [21]
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Cites
Dignam, J. D., Lebovitz, R. M., & Roeder, R. G. (1983) · Nucleic Acids Research · doi:10.1093/nar/11.5.1475 · Cited by 11,262
Darnell, J. E., Kerr, L. M., & Stark, G. R. (1994) · Science · doi:10.1126/science.8197455 · Cited by 6,080
The Protein Kinase Family: Conserved Features and Deduced Phylogeny of the Catalytic Domains
Hanks, S. K., Quinn, A. M., & Hunter, T. R. (1988) · Science · doi:10.1126/science.3291115 · Cited by 5,040
Dérijard, B., Hibi, M., Wu, I.-H., Barrett, T., Su, B., Deng, T., Karin, M., & Davis, R. J. (1994) · Cell · doi:10.1016/0092-8674(94)90380-8 · Cited by 3,188
Oncogenes and signal transduction
Cantley, L. C., Auger, K. R., Carpenter, C. F., Duckworth, B. C., Graziani, A., Kapeller, R., & Soltoff, S. P. (1991) · Cell · doi:10.1016/0092-8674(91)90639-g · Cited by 2,697
The stress-activated protein kinase subfamily of c-Jun kinases
Kyriakis, J. M., Banerjee, P. T., Nikolakaki, E., Dai, T., Rubie, E. A., Ahmad, M. F., Avruch, J., & Woodgett, J. R. (1994) · Nature · doi:10.1038/369156a0 · Cited by 2,601
Zhong, Z., Wen, Z., & Darnell, J. E. (1994) · Science · doi:10.1126/science.8140422 · Cited by 2,070
Wen, Z., Zhong, Z., & Darnell, J. E. (1995) · Cell · doi:10.1016/0092-8674(95)90311-9 · Cited by 1,974
Guan, K., & Dixon, J. (1991) · Analytical Biochemistry · doi:10.1016/0003-2697(91)90534-z · Cited by 1,735
Boyle, W. J., van der Geer, P., & Hunter, T. R. (1991) · Methods in enzymology on CD-ROM/Methods in enzymology · doi:10.1016/0076-6879(91)01013-r · Cited by 1,421
Flagged first, then by citations
Research works printed but not linked: 4
- 10.1128/MCB.13.3.1464 · DOI
- Muthuswamy S. K., 1995, Oncogene, 11, 1801
- ven der Geer P., 1991, Mol. Cell. Biol., 11, 4698
- Vignais, M. L., H. B. Sadowski, and M. Z. Gilman. 1995. Activation of STAT proteins by growth factors, A1-368, p. 64. In Abstracts Supplement 19A of the Journal of Cellular Biochemistry 24th Annual Keystone Symposia.
Cited by
Sorted by citations
Items 101–200 of 359
Deo, D. D., Axelrad, T. W., Robert, E. G., Marcheselli, V., Bazan, N. G., & Hunt, J. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m110955200 · Cited by 117
Yeh, M., Gharavi, N. M., Choi, J., Hsieh, X., Reed, E., Mouillesseaux, K. P., Cole, A. L., Reddy, S. T., & Berliner, J. A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312198200 · Cited by 116
Cyclin D1 Represses STAT3 Activation through a Cdk4-independent Mechanism
Bienvenu, F., Gascan, H., & Coqueret, O. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m100795200 · Cited by 115
Saharinen, P., Ekman, N., Sarvas, K., Parker, P. J., Alitalo, K. K., & Silvennoinen, O. (1997) · Blood · doi:10.1182/blood.v90.11.4341 · Cited by 115
Li, Q., Zhang, D., Chen, X., He, L., Li, T., Xu, X., & Li, M. (2015) · Scientific Reports · doi:10.1038/srep16082 · Cited by 114
Kazansky, A. V., Kabotyanski, E. B., Wyszomierski, S. L., Mancini, M. A., & Rosen, J. M. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.32.22484 · Cited by 112
Stimulation of Myelin Basic Protein Gene Transcription by Fyn Tyrosine Kinase for Myelination
Umemori, H., Kadowaki, Y., Hirosawa, K., Yoshida, Y., Hironaka, K., Okano, H., & Yamamoto, T. S. (1999) · Journal of Neuroscience · doi:10.1523/jneurosci.19-04-01393.1999 · Cited by 112
Wang, Y.-Z., Wharton, W., Garcia, R., Kraker, A. J., Jove, R., & Pledger, W. J. (2000) · Oncogene · doi:10.1038/sj.onc.1203548 · Cited by 113
A Novel Sequence in the Coiled-coil Domain of Stat3 Essential for Its Nuclear Translocation
Ma, J., Zhang, T., Novotny-Diermayr, V., Tan, A. L. C., & Cao, X. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304196200 · Cited by 110
Self-citationKhoury, J. D., Medeiros, L. J., Rassidakis, G. Z., Yared, M. A., Tsioli, P., Leventaki, V., Schmitt-Graeff, A. H., Herling, M., Amin, H. M., & Lai, R. L. (2003) · PubMed · Cited by 110
Stat3-Mediated Transformation of NIH-3T3 Cells by the Constitutively Active Q205L Gα o Protein
Ram, P. T., Horvath, C. M., & Iyengar, R. (2000) · Science · doi:10.1126/science.287.5450.142 · Cited by 109
Src Family Kinases: Potential Targets for the Treatment of Human Cancer and Leukemia
Warmuth, M., Damoiseaux, R. D., Liu, Y., Fabbro, D., & Gray, N. S. (2003) · Current Pharmaceutical Design · doi:10.2174/1381612033454126 · Cited by 111
Pin1 is required for the Ser727 phosphorylation-dependent Stat3 activity
Lufei, C., Koh, T. H., Uchida, T., & Cao, X. (2007) · Oncogene · doi:10.1038/sj.onc.1210567 · Cited by 106
Self-citationWard, A. C., Hermans, M. H. A., Smith, L., van Aesch, Y. M., Schelen, A. M., Antonissen, C., & Touw, I. P. (1999) · Blood · doi:10.1182/blood.v93.1.113 · Cited by 105
Yang, Z., Guo, L., Liu, D., Sun, L., Chen, H., Deng, Q., Liu, Y., Yu, M., Yuan-fang Ma, A., Guo, N., et al. (2014) · Oncotarget · doi:10.18632/oncotarget.3241 · Cited by 101
Benitah, S. A., Valerón, P. F., Rincon, S. V. D., Fernández‐Pérez, L., Perona, R., & Lacal, J. C. (2001) · Molecular Biology of the Cell · doi:10.1091/mbc.12.10.3282 · Cited by 103
MEN2A-RET-induced cellular transformation by activation of STAT3
Schuringa, J. J., Wojtachnio, K., Hagens, W. I., Vellenga, E., Buys, C. H. C. M., Hofstra, R. M. W., & Kruijer, W. (2001) · Oncogene · doi:10.1038/sj.onc.1204715 · Cited by 104
ErbB-2 Activates Stat3α in a Src- and JAK2-dependent Manner
Ren, Z. J., & Schaefer, T. S. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m112438200 · Cited by 102
PTEN is a negative regulator of STAT3 activation in human papillomavirus-infected cells
Sun, S., & Steinberg, B. M. (2002) · Journal of General Virology · doi:10.1099/0022-1317-83-7-1651 · Cited by 101
The role of STATs in proliferation, differentiation, and apoptosis
Mui, A. (1999) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050394 · Cited by 101
Chaturvedi, P., Sharma, S., & Reddy, E. P. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.6.3295 · Cited by 104
The Role of Inflammation in Pancreatic Cancer
Hausmann, S., Kong, B., Michalski, C. W., Erkan, M., & Frieß, H. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-3-0348-0837-8_6 · Cited by 101
Regulation of Stat3 Activation by MEK Kinase 1
Lim, C. P., & Cao, X. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007592200 · Cited by 99
Self-citationActivation of STAT transcription factors by herpesvirus Saimiri Tip-484 requires p56lck
Lund, T. C., Garcia, R., Medveczky, M. M., Jove, R., & Medveczky, P. G. (1997) · Journal of Virology · doi:10.1128/jvi.71.9.6677-6682.1997 · Cited by 96
Okutani, Y., Kitanaka, A., Tanaka, T., Kamano, H., Ohnishi, H., Kubota, Y., Ishida, T., & Takahara, J. (2001) · Oncogene · doi:10.1038/sj.onc.1204807 · Cited by 95
Nucleocytoplasmic shuttling of persistently activated STAT3
Herrmann, A., Vogt, M., Mönnigmann, M., Clahsen, T., Sommer, U., Haan, S., Poli, V., Heinrich, P. C., & Müller-Newen, G. (2007) · Journal of Cell Science · doi:10.1242/jcs.03482 · Cited by 94
Constitutively Active Gα16 Stimulates STAT3 via a c-Src/JAK- and ERK-dependent Mechanism
Lo, R. K. H., Cheung, H. O.-L., & Wong, Y. H. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m307299200 · Cited by 93
CD45: direct and indirect government of immune regulation
Huntington, N. D., & Tarlinton, D. M. (2004) · Immunology Letters · doi:10.1016/j.imlet.2004.05.011 · Cited by 93
Zong, C. S., Zeng, L., Jiang, Y., Sadowski, H. B., & Wang, L. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.43.28065 · Cited by 91
Rawlings, J. S., Rennebeck, G., Harrison, S. M. W., Xi, R., & Harrison, D. A. (2004) · BMC Cell Biology · doi:10.1186/1471-2121-5-38 · Cited by 90
Insulin-Like Growth Factor I Receptor Signaling in Transformation by src Oncogenes
Valentinis, B., Morrione, A., Taylor, S. J., & Baserga, R. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.7.3744 · Cited by 88
Zheng, R., Friedman, A. D., & Small, D. (2002) · Blood · doi:10.1182/blood-2002-03-0936 · Cited by 86
Lu, Y., Zhang, K., Li, C., Yao, Y., Tao, D., Liu, Y., Zhang, S., & Ma, Y. (2012) · PLoS ONE · doi:10.1371/journal.pone.0030999 · Cited by 87
Focal Adhesion Kinase Activates Stat1 in Integrin-mediated Cell Migration and Adhesion
Xie, B., Zhao, J., Kitagawa, M., Durbin, J. E., Madri, J. A., Guan, J., & Fu, X.-Y. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009063200 · Cited by 87
Regulation of Angiotensin II-induced Phosphorylation of STAT3 in Vascular Smooth Muscle Cells
Liang, H., Venema, V. J., Wang, X., Ju, H., Venema, R. C., & Marrero, M. B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.28.19846 · Cited by 86
Hovsepian, E., Penas, F., Siffo, S., Mirkin, G. A., & Goren, N. (2013) · PLoS ONE · doi:10.1371/journal.pone.0079445 · Cited by 89
Read, R. D., Bach, E. A., & Cagan, R. L. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.15.6676-6689.2004 · Cited by 87
Subramaniam, P. S., Torres, B. A., & Johnson, H. M. (2001) · Cytokine · doi:10.1006/cyto.2001.0905 · Cited by 90
CD24 controls Src/STAT3 activity in human tumors
Bretz, N. P., Salnikov, A. V., Perne, C., Keller, S., Wang, X., Mierke, C. T., Fogel, M., Erbe-Hoffmann, N., Schlange, T., Moldenhauer, G., et al. (2012) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-012-1055-9 · Cited by 84
Briscoe, J., Kohlhuber, F., & Müller, M. M. (1996) · Trends in Cell Biology · doi:10.1016/0962-8924(96)10028-3 · Cited by 82
Chiarugi, P., Cirri, P., Marra, F., Raugei, G., Fiaschi, T., Camici, G., Manao, G., Romanelli, R. G., & Ramponi, G. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.6776 · Cited by 83
The molecular pathogenesis of acute myeloid leukemia
Steffen, B., Müller‐Tidow, C., Schwäble, J., Berdel, W. E., & Serve, H. L. (2005) · Critical Reviews in Oncology/Hematology · doi:10.1016/j.critrevonc.2004.10.012 · Cited by 85
Venema, R. C., Venema, V. J., Eaton, D. C., & Marrero, M. B. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.46.30795 · Cited by 81
Deb, A., Zamanian‐Daryoush, M., Xu, Z., Kadereit, S., & Williams, B. R. G. (2001) · The EMBO Journal · doi:10.1093/emboj/20.10.2487 · Cited by 81
Hung, W., & Elliott, B. E. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m010715200 · Cited by 81
Targeting Signal Transduction Pathways in Colorectal Cancer—More Than Skin Deep
Cohen, S. J., Cohen, R. B., & Meropol, N. J. (2005) · Journal of Clinical Oncology · doi:10.1200/jco.2005.02.194 · Cited by 84
Functional implication of the interaction between EGF receptor and C-SRC
Leu, T. (2003) · Frontiers in bioscience · doi:10.2741/980 · Cited by 81
c‐Src drives intestinal regeneration and transformation
Cordero, J. B., Ridgway, R. A., Valeri, N., Nixon, C., Frame, M. C., Muller, W. J., Vidal, M., & Sansom, O. J. (2014) · The EMBO Journal · doi:10.1002/embj.201387454 · Cited by 77
Roles of the JAK-STAT system in signal transduction via cytokine receptors
Watanabe, S., & Arai, K. (1996) · Current Opinion in Genetics & Development · doi:10.1016/s0959-437x(96)80088-8 · Cited by 76
Mankan, A. K., & Greten, F. R. (2011) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2011.601739 · Cited by 77
Gupta, S. C., Phromnoi, K., & Aggarwal, B. B. (2012) · Biochemical Pharmacology · doi:10.1016/j.bcp.2012.12.018 · Cited by 74
Basu, A., Meyer, K., Lai, K., Saito, K., Bisceglie, A. M. D., Grosso, L. E., Ray, R. B., & Ray, R. (2006) · Virology · doi:10.1016/j.virol.2006.02.023 · Cited by 74
Activation of STAT3 by the c-Fes Protein-tyrosine Kinase
Nelson, K. L., Rogers, J. A., Bowman, T. L., Jove, R., & Smithgall, T. E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.12.7072 · Cited by 74
Lee, C., Moon, S., Jeong, J.-H., Lee, S., Lee, M., Yoo, S.-M., Lee, H. S., Kang, H. C., Lee, J. Y., Lee, W. S., et al. (2018) · Cell Death and Disease · doi:10.1038/s41419-018-0433-0 · Cited by 73
Patel, K., Kollory, A., Takashima, A., Sarkar, S., Faller, D. V., & Ghosh, S. K. (2014) · Cancer Letters · doi:10.1016/j.canlet.2014.01.020 · Cited by 76
The Cleaved Cytoplasmic Tail of Polycystin-1 Regulates Src-Dependent STAT3 Activation
Talbot, J. J., Song, X., Wang, X., Rinschen, M. M., Doerr, N., LaRivière, W. B., Schermer, B., Pei, Y., Torres, V. E., & Weimbs, T. (2014) · Journal of the American Society of Nephrology · doi:10.1681/asn.2013091026 · Cited by 72
Kim, R. H., & Sodek, J. (1999) · PubMed · Cited by 72
Mechanisms of STAT Protein Activation by Oncogenic KIT Mutants in Neoplastic Mast Cells
Chaix, A., Lopez, S., Voisset, E., Gros, L., Dubreuil, P. C., & Sepulveda, P. D. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.182642 · Cited by 76
Yang, X., Qiao, D.-H., Meyer, K., & Friedl, A. (2009) · Cancer Research · doi:10.1158/0008-5472.can-07-6385 · Cited by 66
Fox, E. M., Bernaciak, T. M., Wen, J., Weaver, A. M., Shupnik, M. A., & Silva, C. M. (2008) · Molecular Endocrinology · doi:10.1210/me.2007-0419 · Cited by 68
Yan, X., Li, P., Zhan, Y., Qi, M., Liu, J., An, Z., Yang, W., Xiao, H., Wu, H., Qi, Y., et al. (2018) · Biochemical Pharmacology · doi:10.1016/j.bcp.2018.01.031 · Cited by 65
Norkina, O., Dolganiuc, A., Shapiro, T., Kodys, K., Mandrekar, P., & Szabó, G. (2007) · Journal of Leukocyte Biology · doi:10.1189/jlb.0207099 · Cited by 67
SD-1029 Inhibits Signal Transducer and Activator of Transcription 3 Nuclear Translocation
Duan, Z., Bradner, J. E., Greenberg, E. F., Levine, R. L., Foster, R., Mahoney, J., & Seiden, M. V. (2006) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-1330 · Cited by 67
c-Src Activates both STAT1 and STAT3 in PDGF-Stimulated NIH3T3 Cells
Cirri, P., Chiarugi, P., Marra, F., Raugei, G., Camici, G., Manao, G., & Ramponi, G. (1997) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.1997.7493 · Cited by 67
Sachsenmaier, C., Sadowski, H. B., & Cooper, J. A. (1999) · Oncogene · doi:10.1038/sj.onc.1202694 · Cited by 66
Hwang, J. H., Kim, D. W., Suh, J. M., Kim, H., Song, J. H., Hwang, E. S., Park, K. C., Chung, H. K., Kim, J., Lee, T., et al. (2003) · Molecular Endocrinology · doi:10.1210/me.2002-0401 · Cited by 64
A Distinct Function of STAT Proteins in Erythropoietin Signal Transduction
Kirito, K., Uchida, M., Yamada, M. F., Miura, Y., & Komatsu, N. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.26.16507 · Cited by 67
Danial, N. N., Losman, J. A., Lu, T., Yip, N. H., Krishnan, K., Krolewski, J. J., Goff, S. P., Wang, J. Y. J., & Rothman, P. B. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.11.6795 · Cited by 63
Marcotte, R., Zhou, L., Kim, H. L., Roskelly, C. D., & Muller, W. J. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01731-08 · Cited by 62
Wang, Y., Ripperger, J. A., Fey, G. H., Samols, D. R., Kordula, T., Wetzler, M., Etten, R. A. V., & Baumann, H. (1999) · Hepatology · doi:10.1002/hep.510300318 · Cited by 62
Interleukin-7 (IL-7) and IL-7 receptor (IL-7R) signalling complex in human solid tumours.
Al-Rawi, M. A. A., Mansel, R. E., & Jiang, W. G. (2003) · PubMed · doi:10.14670/hh-18.911 · Cited by 61
Griffiths, G. J., Koh, M. Y., Brunton, V. G., Cawthorne, C., Reeves, N. A., Greaves, M., Tilby, M. J., Pearson, D. G., Ottley, C. J., Workman, P., et al. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m408550200 · Cited by 60
TEL/PDGFβR fusion protein activates STAT1 and STAT5
Wilbanks, A. M., Mahajan, S., Frank, D. A., Druker, B. J., Gilliland, D. G., & Carroll, M. P. (2000) · Experimental Hematology · doi:10.1016/s0301-472x(00)00138-7 · Cited by 62
Alteration of SHP-1/p-STAT3 Signaling: A Potential Target for Anticancer Therapy
Huang, T., Su, J.-C., Liu, C., Shiau, C., & Chen, K. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18061234 · Cited by 60
Activated Stat Related Transcription Factors in Acute Leukemia
Gouilleux‐Gruart, V., Debierre-Grockiego, F., Gouilleux, F., Capiod, J., Claisse, J., Delobel, J., & Prin, L. (1997) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428199709058334 · Cited by 59
Novotny‐Diermayr, V., Zhang, T., Gu, L., & Cao, X. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m206727200 · Cited by 57
Self-citationEngagement of the B-cell antigen receptor activates STAT through Lyn in a Jak-independent pathway
Wang, L., Kurosaki, T., & Corey, S. J. (2006) · Oncogene · doi:10.1038/sj.onc.1210092 · Cited by 57
Takahashi, T., Fukuda, K., Pan, J., Kodama, H., Sano, M., Makino, S., Katō, T., Manabe, T., & Ogawa, S. (1999) · Circulation Research · doi:10.1161/01.res.85.10.884 · Cited by 56
Grb2 regulates Stat3 activation negatively in epidermal growth factor signalling
Zhang, T., Ma, J., & Cao, X. (2003) · Biochemical Journal · doi:10.1042/bj20030668 · Cited by 56
Self-citationFerrand, A., Bertrand, C., Portolan, G., Cui, G., Carlson, J. E., Pradayrol, L., Fourmy, D., Dufresne, M., Wang, T. C., & Seva, C. (2005) · Cancer Research · doi:10.1158/0008-5472.can-04-0978 · Cited by 56
Short Hairpin RNA-Mediated Fibronectin Knockdown Delays Tumor Growth in a Mouse Glioma Model
Sengupta, S., Nandi, S., Hindi, E. S., Wainwright, D. A., Han, Y., & Lesniak, M. S. (2010) · Neoplasia · doi:10.1593/neo.10662 · Cited by 59
Lee, H. K., Seo, I. A., Suh, D. J., Hong, J., Yoo, Y. H., & Park, H. T. (2008) · Journal of Neurochemistry · doi:10.1111/j.1471-4159.2008.05826.x · Cited by 55
Choudhury, G. G., Ghosh‐Choudhury, N., & Abboud, H. E. (1998) · Journal of Clinical Investigation · doi:10.1172/jci1044 · Cited by 55
Signal transduction pathways and resistance to targeted therapies in glioma
Tomiyama, A., & Ichimura, K. (2019) · Seminars in Cancer Biology · doi:10.1016/j.semcancer.2019.01.004 · Cited by 54
Sellers, L. A., Feniuk, W., Humphrey, P. P. A., & Lauder, H. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.23.16423 · Cited by 53
Poh, A. R., & Ernst, M. (2023) · Oncogene · doi:10.1038/s41388-023-02701-x · Cited by 54
Paukku, K., Valgeirsdóttir, S., Saharinen, P., Bergman, M., Heldin, C., & Silvennoinen, O. (2000) · PubMed Central · Cited by 53
Lund, T. C., Prator, P. C., Medveczky, M. M., & Medveczky, P. G. (1999) · Journal of Virology · doi:10.1128/jvi.73.2.1689-1694.1999 · Cited by 51
Truncated STAT proteins are prevalent at relapse of acute myeloid leukemia
Xia, Z., Sait, S. N. J., Baer, M. R., Barcos, M. P., Donohue, K. A., Lawrence, D. D., Ford, L. A., Block, A. M. W., Baumann, H., & Wetzler, M. (2001) · Leukemia Research · doi:10.1016/s0145-2126(00)00158-2 · Cited by 51
The Src Inhibitor AZD0530 Blocks Invasion and May Act as a Radiosensitizer in Lung Cancer Cells
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Ramana, C. V., Kumar, A., & Enelow, R. I. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.074 · Cited by 50
Hepatitis C virus NS5A mediated STAT3 activation requires co-operation of Jak1 kinase
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Kohlmaier, A., Fassnacht, C., Jin, Y., Reuter, H., Begum, J., Dutta, D., & Edgar, B. A. (2014) · Oncogene · doi:10.1038/onc.2014.163 · Cited by 52
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O’Shea, J. J., Notarangelo, L. D., Johnston, J. A., & Candotti, F. (1997) · Journal of Clinical Immunology · doi:10.1023/a:1027388508570 · Cited by 50
STAT3 activation accompanies keratinocyte differentiation.
Hauser, P. J., Agrawal, D., Hackney, J. A., & Pledger, W. J. (1998) · PubMed · Cited by 48
Cross-regulation of JAK and Src kinases
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Metadata
- Authors
- Cao, X., Tay, A., Guy, G. R., & Tan, Y. H.
- Affiliations
- National University of Singapore (SG)
- ORCID
- Tan, Y. H.
- Venue
- Molecular and Cellular Biology
- Publisher
- Informa UK Limited
- Published
- 1996-04-01
- Volume
- 16
- Issue
- 4
- Pages
- 1595-1603
- ISSN
- 0270-7306 (ISSN-L)
- 1098-5549
- PMC
- PMC231145
- OpenAlex
- W2135055828
- Cited by
- 359
- References
- 48
- Citations by year
- 2026: 1 · 2025: 2 · 2024: 2 · 2023: 4 · 2021: 6 · 2020: 4 · 2019: 2 · 2018: 4 · 2017: 5 · 2016: 7 · 2015: 8 · 2014: 13 · 2013: 7 · 2012: 14
- FWCI
- 13.79
- Type
- journal article
- Language
- en
- Open access
- green
- europepmc.org
- Locations
- Molecular and Cellular Biology (publishedVersion)
- Europe PMC (PubMed Central) (publishedVersion)
- PubMed Central (publishedVersion)
- PubMed (publishedVersion)
- National University of Singapore (submittedVersion)
- Funders
- National Science Board
- Topics
- Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Kinase Regulation and GTPase Signaling
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
- Keywords
- STAT3, Src kinase, v-Src, tyrosine phosphorylation, STAT3 activation, protein-protein interaction, CSF-1 receptor, colony-stimulating factor 1, growth factor signaling, JAK kinases, interferon signaling, STAT1, STAT2, transcription factor dimerization, 3T3 fibroblasts
- MeSH terms
- Animals, Cell Line, Transformed, DNA-Binding Proteins, Enzyme Activation, Epidermal Growth Factor, Phosphorylation, Platelet-Derived Growth Factor, Trans-Activators, Gene Expression, Macrophage Colony-Stimulating Factor, Receptors, Colony-Stimulating Factor, Genes, src, 3T3 Cells, src-Family Kinases, STAT3 Transcription Factor, Mice
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