Cited by 1,201Cytokine Signaling Pathways and InteractionsProtein Tyrosine PhosphatasesNF-κB Signaling Pathways

The DOI matches its Crossref record; 66 of the 66 references it cites were found in a registry or an index.

The role of STATs in transcriptional control and their impact on cellular function

Bromberg, Jacqueline, Darnell, James E·2000·Oncogene

DOI 10.1038/sj.onc.1203476

Open this paper in CoChat — free account

Abstract

The STAT proteins (Signal Transducers and Activators of Transcription), were identified in the last decade as transcription factors which were critical in mediating virtually all cytokine driven signaling. These proteins are latent in the cytoplasm and become activated through tyrosine phosphorylation which typically occurs through cytokine receptor associated kinases (JAKs) or growth factor receptor tyrosine kinases. Recently a number of non-receptor tyrosine kinases (for example src and abl) have been found to cause STAT phosphorylation. Phosphorylated STATs form homo- or hetero-dimers, enter the nucleus and working coordinately with other transcriptional co-activators or transcription factors lead to increased transcriptional initiation. In normal cells and in animals, ligand dependent activation of the STATs is a transient process, lasting for several minutes to several hours. In contrast, in many cancerous cell lines and tumors, where growth factor dysregulation is frequently at the heart of cellular transformation, the STAT proteins (in particular Stats 1, 3 and 5) are persistently tyrosine phosphorylated or activated. The importance of STAT activation to growth control in experiments using anti-sense molecules or dominant negative STAT protein encoding constructs performed in cell lines or studies in animals lacking specific STATs strongly indicate that STATs play an important role in controlling cell cycle progression and apoptosis. Stat1 plays an important role in growth arrest, in promoting apoptosis and is implicated as a tumor suppressor; while Stats 3 and 5 are involved in promoting cell cycle progression and cellular transformation and preventing apoptosis. Many questions remain including: (1) a better understanding of how the STAT proteins through association with other factors increase transcription initiation; (2) a more complete definition of the sets of genes which are activated by different STATs and (3) how these sets of activated genes differ as a function of cell type. Finally, in the context of many cancers, where STATs are frequently persistently activated, an understanding of the mechanisms leading to their constitutive activation and defining the potential importance of persistent STAT activation in human tumorigenesis remains. Oncogene (2000).

Integrity signals

Registry

Crossref · 10.1038/sj.onc.1203476

Cites

66 of 66 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins
Darnell, J. E., Kerr, L. M., & Stark, G. R. (1994) · Science · doi:10.1126/science.8197455 · Cited by 6,080
STATs and Gene Regulation
Darnell, J. E. (1997) · Science · doi:10.1126/science.277.5332.1630 · Cited by 3,979
HOW CELLS RESPOND TO INTERFERONS
Stark, G. R., Kerr, I. M., Williams, B. R. G., Silverman, R. H., & Schreiber, R. D. (1998) · Annual Review of Biochemistry · doi:10.1146/annurev.biochem.67.1.227 · Cited by 3,932
Virus interference. I. the interferon
Isaacs, A., & Lindenmann, J. (1957) · Proceedings of the Royal Society of London. Series B - Biological Sciences · doi:10.1098/rspb.1957.0048 · Cited by 3,451
Stat3 as an Oncogene
Bromberg, J. F., Wrzeszczynska, M. H., Devgan, G., Zhao, Y., Pestell, R. G., Albanese, C., & Darnell, J. E. (1999) · Cell · doi:10.1016/s0092-8674(00)81959-5 · Cited by 2,790
Self-citation
Maximal activation of transcription by statl and stat3 requires both tyrosine and serine phosphorylation
Wen, Z., Zhong, Z., & Darnell, J. E. (1995) · Cell · doi:10.1016/0092-8674(95)90311-9 · Cited by 1,974
Targeted Disruption of the Stat1 Gene in Mice Reveals Unexpected Physiologic Specificity in the JAK–STAT Signaling Pathway
Meraz, M. A., White, J. M., Sheehan, K. C. F., Bach, E. A., Rodig, S. J., Dighe, A. S., Kaplan, D. H., Riley, J. K., Greenlund, A. C., Campbell, D., et al. (1996) · Cell · doi:10.1016/s0092-8674(00)81288-x · Cited by 1,656
Targeted Disruption of the Mouse Stat1 Gene Results in Compromised Innate Immunity to Viral Disease
Durbin, J. E., Hackenmiller, R., Simon, M. C., & Levy, D. E. (1996) · Cell · doi:10.1016/s0092-8674(00)81289-1 · Cited by 1,539
A Matter of Life and Cell Death
Evan, G. I., & Littlewood, T. D. (1998) · Science · doi:10.1126/science.281.5381.1317 · Cited by 1,528
Demonstration of an interferon γ-dependent tumor surveillance system in immunocompetent mice
Kaplan, D. H., Shankaran, V., Dighe, A. S., Stockert, E., Aguet, M., Old, L. J., & Schreiber, R. D. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.13.7556 · Cited by 1,465

Flagged first, then by citations

Show all 66 references

Sorted by citations

Items 201–300 of 1,000

OPB-31121, a novel small molecular inhibitor, disrupts the JAK2/STAT3 pathway and exhibits an antitumor activity in gastric cancer cells
Kim, M., Nam, H.-J., Kim, H., Han, S., Im, S., Kim, T., Oh, D., & Bang, Y. (2013) · Cancer Letters · doi:10.1016/j.canlet.2013.02.010 · Cited by 117
Epigenetic modification of SOCS-1 differentially regulates STAT3 activation in response to interleukin-6 receptor and epidermal growth factor receptor signaling through JAK and/or MEK in head and neck squamous cell carcinomas
Lee, T., Yeh, J., Waes, C. V., & Chen, Z. (2006) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-05-0069 · Cited by 115
The roles of signal transducer and activator of transcription factor 3 in tumor angiogenesis
Gao, P., Niu, N., Wei, T., Tozawa, H., Chen, X., Zhang, W., Zhang, J., Wada, Y., Kapron, C. M., & Liu, J. (2017) · Oncotarget · doi:10.18632/oncotarget.19932 · Cited by 116
Constitutive activation of Stat5b contributes to carcinogenesis in vivo.
Xi, S., Zhang, Q. H., Gooding, W. E., Smithgall, T. E., & Grandis, J. R. (2003) · PubMed · Cited by 114
Uterine Deletion of Gp130 or Stat3 Shows Implantation Failure with Increased Estrogenic Responses
Sun, X., Bartos, A., Whitsett, J. A., & Dey, S. K. (2013) · Molecular Endocrinology · doi:10.1210/me.2013-1086 · Cited by 114
The role of Kaposi's sarcoma-associated herpesvirus/human herpesvirus-8 regulator of transcription activation (RTA) in control of gene expression
West, J. T., & Wood, C. A. (2003) · Oncogene · doi:10.1038/sj.onc.1206555 · Cited by 113
CYP3A4 Mediates Growth of Estrogen Receptor-positive Breast Cancer Cells in Part by Inducing Nuclear Translocation of Phospho-Stat3 through Biosynthesis of (±)-14,15-Epoxyeicosatrienoic Acid (EET)
Mitra, R., Guo, Z., Milani, M., Mesaros, C., Rodriguez, M., Nguyen, J., Luo, X., Clarke, D. J., Lamba, J. K., Schuetz, E. G., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.198515 · Cited by 113
The role of STAT3 in glioblastoma progression through dual influences on tumor cells and the immune microenvironment
Chang, N., Ahn, S. H., Kong, D., Lee, H. W., & Nam, D. (2017) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2017.01.004 · Cited by 117
Time course profiling of the retinal transcriptome after optic nerve transection and optic nerve crush.
Agudo‐Barriuso, M., Pérez-Marín, M. C., Lönngren, U., Sobrado, P., Conesa, A., Cánovas, I., Salinas‐Navarro, M., Miralles-Imperial, J., Hallböök, F., & Vidal‐Sanz, M. (2008) · PubMed Central · Cited by 112
Characterization of STAT3 activation and expression in canine and human osteosarcoma
Fossey, S. L., Liao, A. T., McCleese, J., Bear, M. D., Lin, J., Li, P., Kisseberth, W. C., & London, C. A. (2009) · BMC Cancer · doi:10.1186/1471-2407-9-81 · Cited by 112
Activation of Stat‐3 as one of the early events in tobacco chewing‐mediated oral carcinogenesis
Nagpal, J. K., Mishra, R., & Das, B. R. (2002) · Cancer · doi:10.1002/cncr.10499 · Cited by 113
STAT3 mRNA and protein expression in colorectal cancer: effects on STAT3-inducible targets linked to cell survival and proliferation
Laßmann, S., Schuster, I., Walch, A. K., Göbel, H., Jütting, U., Makowiec, F., Hopt, U. T., & Werner, M. (2007) · Journal of Clinical Pathology · doi:10.1136/jcp.2005.035113 · Cited by 114
Role of the JAK-STAT pathway in PDGF-stimulated proliferation of human airway smooth muscle cells
Simon, A. R., Takahashi, S., Severgnini, M., Fanburg, B. L., & Cochran, B. (2002) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00315.2001 · Cited by 115
Small-molecule inhibitors targeting the DNA-binding domain of STAT3 suppress tumor growth, metastasis and STAT3 target gene expression in vivo
Huang, W., Dong, Z., Chen, Y., Wang, F., Wang, C. J., Peng, H., He, Y., Hangoc, G., Pollok, K. E., Sandusky, G. E., et al. (2015) · Oncogene · doi:10.1038/onc.2015.215 · Cited by 110
Modulation of Signal Transducers and Activators of Transcription 1 and 3 Signaling in Melanoma by High-Dose IFNα2b
Wang, W., Edington, H. D. J., Rao, U. N. M., Jukic, D. M., Land, S. R., Ferrone, S., & Kirkwood, J. M. (2007) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-06-1387 · Cited by 109
Loss of Stat5a delays mammary cancer progression in a mouse model
Ren, S. V., Cai, H. R., Li, M., & Furth, P. A. (2002) · Oncogene · doi:10.1038/sj.onc.1205484 · Cited by 109
Cisplatin-induced CCL5 secretion from CAFs promotes cisplatin-resistance in ovarian cancer via regulation of the STAT3 and PI3K/Akt signaling pathways
Zhou, B., Sun, C., Li, N., Shan, W., Lü, H., Guo, L., Guo, E., Xia, M., WENG, D., Li, M., et al. (2016) · International Journal of Oncology · doi:10.3892/ijo.2016.3442 · Cited by 108
Phase I study of OPB ‐51602, an oral inhibitor of signal transducer and activator of transcription 3, in patients with relapsed/refractory hematological malignancies
Ogura, M., Uchida, T., Terui, Y., Hayakawa, F., Kobayashi, Y., Taniwaki, M., Takamatsu, Y., Naoe, T., Tobinai, K., Munakata, W., et al. (2015) · Cancer Science · doi:10.1111/cas.12683 · Cited by 110
Nonclassical Biological Activities of Quinolone Derivatives
Daneshtalab, M., & Ahmed, A. A. (2011) · Journal of Pharmacy & Pharmaceutical Sciences · doi:10.18433/j3302n · Cited by 109
Ascochlorin, an isoprenoid antibiotic inhibits growth and invasion of hepatocellular carcinoma by targeting STAT3 signaling cascade through the induction of PIAS3
Dai, X., Ahn, K. S., Kim, C., Siveen, K. S., Ong, T. H., Shanmugam, M. K., Li, F., Shi, J., Kumar, A. P., Wang, L. Z., et al. (2015) · Molecular Oncology · doi:10.1016/j.molonc.2014.12.008 · Cited by 107
Alternate interferon signaling pathways
Kalvakolanu, D. V. (2003) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(03)00070-6 · Cited by 109
Growth factor receptors and related signalling pathways as targets for novel treatment strategies of hepatocellular cancer
Höpfner, M., Schuppan, D., & Scherübl, H. (2008) · World Journal of Gastroenterology · doi:10.3748/wjg.14.1 · Cited by 106
Stat3 Activation in Acute Lung Injury
Gao, H., Guo, R., Speyer, C. L., Reuben, J. S., Neff, T. A., Hoesel, L. M., Riedemann, N. C., McClintock, S. D., Sarma, J. V., van Rooijen, N., et al. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.12.7703 · Cited by 107
XPO1 (CRM1) Inhibition Represses STAT3 Activation to Drive a Survivin-Dependent Oncogenic Switch in Triple-Negative Breast Cancer
Cheng, Y., Holloway, M. P., Nguyen, K., McCauley, D., Landesman, Y., Kauffman, M. G., Shacham, S., & Altura, R. A. (2014) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-13-0416 · Cited by 105
Targeting STAT3 in cancer and autoimmune diseases
Gharibi, T., Babaloo, Z., Hosseini, A., Abdollahpour‐Alitappeh, M., Hashemi, V., Marofi, F., Nejati‐Koshki, K., & Baradaran, B. (2020) · European Journal of Pharmacology · doi:10.1016/j.ejphar.2020.173107 · Cited by 105
Stat3 Binds to mtDNA and Regulates Mitochondrial Gene Expression in Keratinocytes
Macias, E., Rao, D., Carbajal, S., Kiguchi, K., & DiGiovanni, J. (2014) · Journal of Investigative Dermatology · doi:10.1038/jid.2014.68 · Cited by 105
Local activation of STAT‐1 and STAT‐3 in the inflamed synovium during zymosan‐induced arthritis: Exacerbation of joint inflammation in STAT‐1 gene–knockout mice
de Hooge, A. S. K., van de Loo, F. A. J., Koenders, M. I., Bennink, M. B., Arntz, O. J., Kolbe, T., & van den Berg, W. B. (2004) · Arthritis & Rheumatism · doi:10.1002/art.20302 · Cited by 103
The JAK/STAT pathway in rheumatoid arthritis: Pathogenic or protective?
Ivashkiv, L. B., & Hu, X. (2003) · Arthritis & Rheumatism · doi:10.1002/art.11095 · Cited by 103
Role of Transcription Factors in Peripheral Nerve Regeneration
Patodia, S., & Raivich, G. (2012) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2012.00008 · Cited by 107
Temporal profiling of methamphetamine‐induced changes in gene expression in the mouse brain: Evidence from cDNA array
Cadet, J. L., Jayanthi, S., McCoy, M. T., Vawter, M. P., & Ladenheim, B. (2001) · Synapse · doi:10.1002/syn.1058 · Cited by 103
Berberine suppresses tumorigenicity and growth of nasopharyngeal carcinoma cells by inhibiting STAT3 activation induced by tumor associated fibroblasts
Tsang, C. M., Cheung, Y. C., Lui, V. W. Y., Yip, Y. L., Zhang, G., Lin, V. W., Cheung, K. C.-P., Feng, Y., & Tsao, S. W. (2013) · BMC Cancer · doi:10.1186/1471-2407-13-619 · Cited by 102
Cellular and molecular mechanisms of liver regeneration: Proliferation, growth, death and protection of hepatocytes
Ozaki, M. (2019) · Seminars in Cell and Developmental Biology · doi:10.1016/j.semcdb.2019.10.007 · Cited by 103
Structure-Based Design of Conformationally Constrained, Cell-Permeable STAT3 Inhibitors
Chen, J., Bai, L., Bernard, D., Nikolovska‐Coleska, Z., Gomez, C., Zhang, J., Han, Y., & Wang, S. (2010) · ACS Medicinal Chemistry Letters · doi:10.1021/ml100010j · Cited by 101
Transcriptional Pausing Caused by NELF Plays a Dual Role in Regulating Immediate-Early Expression of the junB Gene
Aida, M., Chen, Y., Nakajima, K., Yamaguchi, Y., Wada, T., & Handa, H. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02366-05 · Cited by 105
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
miR-337-3p and Its Targets STAT3 and RAP1A Modulate Taxane Sensitivity in Non-Small Cell Lung Cancers
Du, L., Subauste, M. C., DeSevo, C. G., Zhao, Z., Baker, M., Borkowski, R. J., Schageman, J. J., Greer, R. M., Yang, C., Suraokar, M. B., et al. (2012) · PLoS ONE · doi:10.1371/journal.pone.0039167 · Cited by 100
Signal transducer and activator of transcription 3 (STAT3) regulates adipocyte differentiation via peroxisome‐proliferator‐activated receptor γ (PPARγ)
Wang, D., Zhou, Y., Lei, W., Zhang, K., Shi, J., Hu, Y., Shu, G., & Song, J. (2010) · Biology of the Cell · doi:10.1042/bc20090070 · Cited by 100
STAT3 Inhibition Enhances the Therapeutic Efficacy of Immunogenic Chemotherapy by Stimulating Type 1 Interferon Production by Cancer Cells
Yang, H., Yamazaki, T., Pietrocola, F., Zhou, H., Zitvogel, L., Ma, Y., & Kroemer, G. (2015) · Cancer Research · doi:10.1158/0008-5472.can-15-1122 · Cited by 98
Constitutive activation of STAT3 and STAT5 is present in the majority of nasopharyngeal carcinoma and correlates with better prognosis
Hsiao, J. R., Jin, Y., Tsai, S., Shiau, A.-L., Wu, C., & Su, W. (2003) · British Journal of Cancer · doi:10.1038/sj.bjc.6601003 · Cited by 98
Convallatoxin promotes apoptosis and inhibits proliferation and angiogenesis through crosstalk between JAK2/STAT3 (T705) and mTOR/STAT3 (S727) signaling pathways in colorectal cancer
Zhang, Z. H., Li, M. Y., Wang, Z., Zuo, H. X., Wang, J. Y., Xing, Y., Jin, C. H., Xu, G., Piao, L. X., Piao, H., et al. (2020) · Phytomedicine · doi:10.1016/j.phymed.2020.153172 · Cited by 100
HIV-1 Nef activates STAT1 in human monocytes/macrophages through the release of soluble factors
Federico, M., Percario, Z. A., Olivetta, E., Fiorucci, G., Muratori, C., Micheli, A., Romeo, G., & Affabris, E. (2001) · Blood · doi:10.1182/blood.v98.9.2752 · Cited by 99
Role of Dysregulated Cytokine Signaling and Bacterial Triggers in the Pathogenesis of Cutaneous T-Cell Lymphoma
Fanok, M. H., Sun, A. L., Fogli, L. K., Narendran, V., Eckstein, M., Kannan, K. S., Dolgalev, I., Lazaris, C., Heguy, A., Laird, M. E., et al. (2017) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2017.10.028 · Cited by 96
Voluntary exercise protects hippocampal neurons from trimethyltin injury: Possible role of interleukin-6 to modulate tumor necrosis factor receptor-mediated neurotoxicity
Funk, J. A., Gohlke, J. M., Kraft, A. D., McPherson, C. A., Collins, J. B., & Harry, G. J. (2011) · Brain Behavior and Immunity · doi:10.1016/j.bbi.2011.03.012 · Cited by 95
Overview of the STAT‑3 signaling pathway in cancer and the development of specific inhibitors (Review)
Gu, Y., Mohammad, I., & Liu, Z. (2020) · Oncology Letters · doi:10.3892/ol.2020.11394 · Cited by 103
The role of Janus kinases in haemopoiesis and haematological malignancy
Khwaja, A. (2006) · British Journal of Haematology · doi:10.1111/j.1365-2141.2006.06206.x · Cited by 101
Increased expression of interleukin-6 predicts poor response to chemoradiotherapy and unfavorable prognosis in oral squamous cell carcinoma
Jinno, T., Kawano, S., Maruse, Y., Matsubara, R., Goto, Y., Sakamoto, T., Hashiguchi, Y., Kaneko, N., Tanaka, H., Kitamura, R., et al. (2015) · Oncology Reports · doi:10.3892/or.2015.3838 · Cited by 94
Analysis of Signal Transducer and Activator of Transcription 3 (Stat 3) Pathway in Multiple Myeloma
Quintanilla-Martinez, L., Kremer, M., Specht, K., Calzada-Wack, J., Nathrath, M., Schaich, R., Höfler, H., & Fend, F. (2003) · The American Journal of Pathology · doi:10.1016/s0002-9440(10)64278-2 · Cited by 93
Enhanced IL-6/IL-6R Signaling Promotes Growth and Malignant Properties in EBV-Infected Premalignant and Cancerous Nasopharyngeal Epithelial Cells
Zhang, G., Tsang, C. M., Deng, W., Yip, Y. L., Lui, V. W. Y., Wong, S. C. C., Cheung, A. L. M., Hau, P. M., Zeng, M., Lung, M. L., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0062284 · Cited by 93
Stat3 as a Potential Target for Cancer Immunotherapy
Kortylewski, M., & Yu, H. (2007) · Journal of Immunotherapy · doi:10.1097/01.cji.0000211327.76266.65 · Cited by 94
Fragment-based drug design and identification of HJC0123 , a novel orally bioavailable STAT3 inhibitor for cancer therapy
Chen, H., Yang, Z., Ding, C., Chu, L., Zhang, Y., Terry, K., Liu, H., Shen, Q., & Zhou, J. (2013) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2013.01.023 · Cited by 94
LLL-3 inhibits STAT3 activity, suppresses glioblastoma cell growth and prolongs survival in a mouse glioblastoma model
Fuh, B., Sobo, M., Cen, L., Josiah, D. T., Hutzen, B. J., Cisek, K. K., Bhasin, D. K., Regan, N., Lin, L., Chan, C., et al. (2009) · British Journal of Cancer · doi:10.1038/sj.bjc.6604793 · Cited by 93
miR-182-5p Induced by STAT3 Activation Promotes Glioma Tumorigenesis
Xue, J., Zhou, A., Wu, Y., Morris, S., Lin, K., Amin, S. B., Verhaak, R. G. W., Fuller, G. N., Xie, K., Heimberger, A. B., et al. (2016) · Cancer Research · doi:10.1158/0008-5472.can-15-3073 · Cited by 92
Interleukin-6 Induces Myogenic Differentiation via JAK2-STAT3 Signaling in Mouse C2C12 Myoblast Cell Line and Primary Human Myoblasts
Steyn, P. J., Dzobo, K., Smith, R., & Myburgh, K. H. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215273 · Cited by 95
Role of tumor necrosis factor receptor 1 (p55) in hepatocyte proliferation during acetaminophen-induced toxicity in mice
Chiu, H.-J., Gardner, C. R., Dambach, D. M., Durham, S. K., Brittingham, J. A., Laskin, J. D., & Laskin, D. L. (2003) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2003.07.003 · Cited by 94
Interferon-γ-induced Epithelial ICAM-1 Expression and Monocyte Adhesion
Chang, Y., Holtzman, M. J., & Chen, C. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m109924200 · Cited by 92
Mesenchymal cell survival in airway and interstitial pulmonary fibrosis
Bonner, J. C. (2010) · Fibrogenesis & Tissue Repair · doi:10.1186/1755-1536-3-15 · Cited by 93
Zinc transporters and signaling in physiology and pathogenesis
Hojyo, S., & Fukada, T. (2016) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2016.06.020 · Cited by 94
MiR-93-5p inhibits the EMT of breast cancer cells via targeting MKL-1 and STAT3
Xiang, Y., Liao, X., Yu, C., Yao, A., Qin, H., Li, J., Hu, P., Li, H., Guo, W., Gu, C., et al. (2017) · Experimental Cell Research · doi:10.1016/j.yexcr.2017.05.007 · Cited by 91
Effects of IL-6 and AG490 on regulation of Stat3 signaling pathway and invasion of human pancreatic cancer cells in vitro
Huang, C., Yang, G., Jiang, T., Huang, K., Cao, J., & Qiu, Z. (2010) · Journal of Experimental & Clinical Cancer Research · doi:10.1186/1756-9966-29-51 · Cited by 94
STAT3, but not ERKs, mediates the IL-6–induced proliferation of renal cancer cells, ACHN and 769P
Horiguchi, A., Oya, M., Marumo, K., & Murai, M. (2002) · Kidney International · doi:10.1046/j.1523-1755.2002.00206.x · Cited by 91
Interactions of STAT5b-RARα, a novel acute promyelocytic leukemia fusion protein, with retinoic acid receptor and STAT3 signaling pathways
Dong, S., & Tweardy, D. J. (2002) · Blood · doi:10.1182/blood.v99.8.2637 · Cited by 91
Targeting Stat3 with G-Quartet Oligodeoxynucleotides in Human Cancer Cells
Jing, N., Li, Y., Xu, X., Sha, W., Li, P., Feng, L., & Tweardy, D. J. (2003) · DNA and Cell Biology · doi:10.1089/104454903770946665 · Cited by 92
Involvement of heat-shock protein 90 in the interleukin-6-mediated signaling pathway through STAT3
Sato, N., Yamamoto, T., Sekine, Y., Yumioka, T., Junicho, A., Fuse, H., & Matsuda, T. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(02)02941-8 · Cited by 95
STAT3 in Skeletal Muscle Function and Disorders
Guadagnin, E., Mázala, D. A. G., & Chen, Y. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082265 · Cited by 93
Cross‐talk between signal transducer and activator of transcription 3 and estrogen receptor signaling
Yamamoto, T., Matsuda, T., Junicho, A., Kishi, H., Saatcioglu, F., & Atsushi, M. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)02296-1 · Cited by 91
Dictyostelium Finds New Roles to Model
Williams, J. G. (2010) · Genetics · doi:10.1534/genetics.110.119297 · Cited by 95
Molecular signaling regulating anchorage-independent growth of cancer cells.
Wang, L. (2004) · PubMed · Cited by 92
Increased Expression and Secretion of Interleukin-6 in Patients with Barrett’s Esophagus
Dvořáková, K., Payne, C. M., Ramsey, L., Holubec, H., Sampliner, R. E., Rieg, J. A. D., Dvořák, B., Bernstein, H., Bernstein, C., Prasad, A. R., et al. (2004) · Clinical Cancer Research · doi:10.1158/1078-0432.ccr-0437-03 · Cited by 91
Inhibition of Granulocyte-Macrophage Colony-Stimulating Factor Signaling and Microglial Proliferation by Anti-CD45RO: Role of Hck Tyrosine Kinase and Phosphatidylinositol 3-Kinase/Akt
Suh, H.-S., Kim, M.-O., & Lee, S. C. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.5.2712 · Cited by 90
Independent and Cooperative Activation of Chromosomal c-fos Promoter by STAT3
Yang, E., Lerner, L. R., Besser, D., & Darnell, J. E., Jr. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m213073200 · Cited by 88
Transcriptional regulation of erythropoiesis
Perry, C., & Soreq, H. (2002) · European Journal of Biochemistry · doi:10.1046/j.1432-1033.2002.02999.x · Cited by 87
The peroxisome proliferator-activated receptor (PPAR) β/δ agonist GW501516 inhibits IL-6-induced signal transducer and activator of transcription 3 (STAT3) activation and insulin resistance in human liver cells
Serrano-Marco, L., Barroso, E., Kochairi, I. E., Palomer, X., Michalik, L., Wahli, W., & Vázquez‐Carrera, M. (2011) · Diabetologia · doi:10.1007/s00125-011-2401-4 · Cited by 87
Tyrosine Phosphorylation-Independent Nuclear Translocation of a Dictyostelium STAT in Response to DIF Signaling
Fukuzawa, M., Araki, T., Adrian, I., & Williams, J. G. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00222-2 · Cited by 86
STAT5 and Oct-1 Form a Stable Complex That Modulates Cyclin D1 Expression
Magné, S., Caron, S., Charon, M., Rouyez, M.-C., & Dusanter‐Fourt, I. (2003) · Molecular and Cellular Biology · doi:10.1128/mcb.23.24.8934-8945.2003 · Cited by 90
Immune Activation of Type I IFNs by Listeria monocytogenes Occurs Independently of TLR4, TLR2, and Receptor Interacting Protein 2 but Involves TANK-Binding Kinase 1
O’Connell, R. M., Vaidya, S. A., Perry, A. K., Saha, S. K., Dempsey, P. W., & Cheng, G. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.174.3.1602 · Cited by 86
Pterostilbene Suppresses both Cancer Cells and Cancer Stem-Like Cells in Cervical Cancer with Superior Bioavailability to Resveratrol
Shin, H. J., Han, J. M., Choi, Y. S., & Jung, H. J. (2020) · Molecules · doi:10.3390/molecules25010228 · Cited by 85
Induced somatic inactivation of STAT3 in mice triggers the development of a fulminant form of enterocolitis
Alonzi, T. (2004) · Cytokine · doi:10.1016/j.cyto.2003.12.002 · Cited by 85
Gene expression analysis of rheumatoid arthritis synovial lining regions by cDNA microarray combined with laser microdissection: up-regulation of inflammation-associated STAT1, IRF1, CXCL9, CXCL10, and CCL5
Yoshida, S., Arakawa, F., Higuchi, F., Ishibashi, Y., Goto, M., Sugita, Y., Nomura, Y., Niino, D., Shimizu, K., Aoki, R., et al. (2012) · Scandinavian Journal of Rheumatology · doi:10.3109/03009742.2011.623137 · Cited by 86
STAT Signaling in Glioma Cells
Swiatek-Machado, K., & Kaminska, B. (2020) · Advances in experimental medicine and biology · doi:10.1007/978-3-030-30651-9_10 · Cited by 86
Expression levels of the putative zinc transporter LIV‐1 are associated with a better outcome of breast cancer patients
Kasper, G., Weiser, A. A., Rump, A., Sparbier, K., Dahl, E., Hartmann, A., Wild, P. J., Schwidetzky, U., Castaños‐Vélez, E., & Lehmann, K. E. (2005) · International Journal of Cancer · doi:10.1002/ijc.21235 · Cited by 84
Interferon–α Delays S–Phase Progression in Human Hepatocellular Carcinoma Cells Via Inhibition of Specific Cyclin–Dependent Kinases
Murphy, D. B., Detjen, K. M., Welzel, M., Wiedenmann, B. J., & Rosewicz, S. (2001) · Hepatology · doi:10.1053/jhep.2001.21749 · Cited by 84
Hedyotis diffusa Willd Inhibits Colorectal Cancer Growth in Vivo via Inhibition of STAT3 Signaling Pathway
Cai, Q., Lin, J., Wei, L., Zhang, L., Wang, L., Zhan, Y., Zeng, J., Xu, W., Shen, A., Hong, Z., et al. (2012) · International Journal of Molecular Sciences · doi:10.3390/ijms13056117 · Cited by 83
Naturally occurring dominant-negative Stat5 suppresses transcriptional activity of estrogen receptors and induces apoptosis in T47D breast cancer cells
Yamashita, H., Iwase, H., Toyama, T., & Fujii, Y. (2003) · Oncogene · doi:10.1038/sj.onc.1206277 · Cited by 83
Deregulation of Stat5 expression and activation causes mammary tumors in transgenic mice
Iavnilovitch, E., Cardiff, R. D., Groner, B., & Barash, I. (2004) · International Journal of Cancer · doi:10.1002/ijc.20484 · Cited by 82
Atractylenolide I Induces Apoptosis and Suppresses Glycolysis by Blocking the JAK2/STAT3 Signaling Pathway in Colorectal Cancer Cells
Li, Y., Wang, Y., Liu, Z., Guo, X., Miao, Z., & Ma, S. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2020.00273 · Cited by 82
Cell type-specific characterization of nuclear DNA contents within complex tissues and organs
Zhang, C., Gong, F. C., Lambert, G. M., & Galbraith, D. W. (2005) · Plant Methods · doi:10.1186/1746-4811-1-7 · Cited by 81
T-Cell Immunity in Acute Coronary Syndromes
Weyand, C. M., Goronzy, J. J., Liuzzo, G., Kopecky, S. L., Holmes, D. R., & Frye, R. L. (2001) · Mayo Clinic Proceedings · doi:10.4065/76.10.1011 · Cited by 81
Stat proteins and oncogenesis
Bromberg, J. (2002) · Journal of Clinical Investigation · doi:10.1172/jci200215617 · Cited by 81
Self-citation
Sequential Activation of Rac-1, SEK-1/MKK-4, and Protein Kinase Cδ Is Required for Interleukin-6-induced STAT3 Ser-727 Phosphorylation and Transactivation
Schuringa, J. J., Dekker, L. V., Vellenga, E., & Kruijer, W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009821200 · Cited by 83
MSK1 and JNKs mediate phosphorylation of STAT3 in UVA-irradiated mouse epidermal JB6 cells
Zhang, Y., Liu, G., & Dong, Z. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106044200 · Cited by 81
Growth inhibition of human hepatocellular carcinoma cells by blocking STAT3 activation with decoy-ODN
Sun, X., Zhang, J., Wang, L., & Tian, Z. (2008) · Cancer Letters · doi:10.1016/j.canlet.2007.12.009 · Cited by 80
Leptin Receptor Signaling Supports Cancer Cell Metabolism through Suppression of Mitochondrial Respiration in Vivo
Park, J., Kusminski, C. M., Chua, S. C., & Scherer, P. E. (2010) · American Journal Of Pathology · doi:10.2353/ajpath.2010.100595 · Cited by 80
Correlation between p-STAT3 overexpression and prognosis in lung cancer: A systematic review and meta-analysis
Tong, M., Wang, J., Jiang, N., Pan, H., & Li, D. (2017) · PLoS ONE · doi:10.1371/journal.pone.0182282 · Cited by 80
STAT3 activation is required for Asp816 mutant c-Kit induced tumorigenicity
Ning, Z.-Q., Li, J., McGuinness, M., & Arceci, R. J. (2001) · Oncogene · doi:10.1038/sj.onc.1204590 · Cited by 80
Monocytes present age-related changes in phospholipid concentration and decreased energy metabolism
Saare, M., Tserel, L., Haljasmägi, L., Taalberg, E., Peet, N., Eimre, M., Vetik, R., Kingo, K., Saks, K., Tamm, R., et al. (2020) · Aging Cell · doi:10.1111/acel.13127 · Cited by 79
Scoparone Exerts Anti-Tumor Activity against DU145 Prostate Cancer Cells via Inhibition of STAT3 Activity
Kim, J.-K., Kim, J.-Y., Kim, H.-J., Park, K., Harris, R. A., Cho, W., Lee, J.-T., & Lee, I. K. (2013) · PLoS ONE · doi:10.1371/journal.pone.0080391 · Cited by 81
A novel SHP-1/Grb2–dependent mechanism of negative regulation of cytokine-receptor signaling: contribution of SHP-1 C-terminal tyrosines in cytokine signaling
Minoo, P., Zadeh, M. M., Rottapel, R. K., Lebrun, J. J., & Ali, S. (2003) · Blood · doi:10.1182/blood-2003-07-2617 · Cited by 79
STAT3-RANTES Autocrine Signaling Is Essential for Tamoxifen Resistance in Human Breast Cancer Cells
Yi, E. H., Lee, C. S., Lee, J., Lee, Y. J., Shin, M. K., Cho, C., Kang, K. W., Lee, S. E., Han, W., Noh, D., et al. (2012) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-12-0217 · Cited by 79
Differential Effects of Interleukin-2 and Interleukin-15 versus Interleukin-21 on CD4+ Cutaneous T-Cell Lymphoma Cells
Marzec, M., Halasa, K., Kasprzycka, M., Wysocka, M., Liu, X., Tobias, J. W., Baldwin, D. A., Zhang, Q., Ødum, N., Rook, A. H., et al. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-2403 · Cited by 78
Regulation of STAT3-mediated signaling by LMW-DSP2
Sekine, Y., Tsuji, S., Ikeda, O., Sato, N., Aoki, N., Aoyama, K., Sugiyama, K., & Matsuda, T. (2006) · Oncogene · doi:10.1038/sj.onc.1209578 · Cited by 78

Authors: Bromberg, J., & Darnell, J. E.
Affiliations: Rockefeller University (US)
ORCID: Bromberg, Jacqueline
Venue: Oncogene
Publisher: Springer Science and Business Media LLC
Published: 2000-05-25
Volume: 19
Issue: 21
Pages: 2468-2473
ISSN: 0950-9232 (ISSN-L)
1476-5594
DOI: 10.1038/sj.onc.1203476
OpenAlex: W1977681992
Cited by: 1,201
References: 66
Citations by year: 2026: 10 · 2025: 22 · 2024: 21 · 2023: 24 · 2022: 37 · 2021: 40 · 2020: 46 · 2019: 41 · 2018: 42 · 2017: 51 · 2016: 46 · 2015: 49 · 2014: 59 · 2013: 67 · 2012: 56
FWCI: 6.32
Type: journal article
Language: en
Open access: closed
Licence: www.springer.com/tdm (tdm)
www.springer.com/tdm (vor)
Locations: Oncogene (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Protein Tyrosine Phosphatases
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: STAT proteins, transcriptional regulation, cytokine signaling, JAK kinases, tyrosine phosphorylation, STAT1, STAT3, STAT5, cell cycle progression, apoptosis, tumor suppressor, cell transformation, carcinogenesis, transcriptional coactivator
MeSH terms: Animals, Cell Division, Cell Transformation, Neoplastic, DNA-Binding Proteins, Gene Expression Regulation, Humans, Milk Proteins, Neoplasms, Structure-Activity Relationship, Transcription, Genetic, Trans-Activators, STAT1 Transcription Factor, STAT3 Transcription Factor, STAT5 Transcription Factor

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

The role of STATs in transcriptional control and their impact on cellular function

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks