Cited by 6,080Cytokine Signaling Pathways and Interactionsinterferon and immune responsesNF-κB Signaling Pathways

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Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins

Darnell, James E., Kerr, lan M., Stark, George R.·1994·Science

DOI 10.1126/science.8197455

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Abstract

Through the study of transcriptional activation in response to interferon alpha (IFN-alpha) and interferon gamma (IFN-gamma), a previously unrecognized direct signal transduction pathway to the nucleus has been uncovered: IFN-receptor interaction at the cell surface leads to the activation of kinases of the Jak family that then phosphorylate substrate proteins called STATs (signal transducers and activators of transcription). The phosphorylated STAT proteins move to the nucleus, bind specific DNA elements, and direct transcription. Recognition of the molecules involved in the IFN-alpha and IFN-gamma pathway has led to discoveries that a number of STAT family members exist and that other polypeptide ligands also use the Jak-STAT molecules in signal transduction.

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BackgroundInfluential
Mechanisms of mRNA translation of interferon stimulated genes
Joshi, S. S., Kaur, S., Kroczyńska, B., & Platanias, L. C. (2010) · Cytokine · doi:10.1016/j.cyto.2010.03.019 · Cited by 45
KAP1 regulates type I interferon/STAT1-mediated IRF-1 gene expression
Kamitani, S., Ohbayashi, N., Ikeda, O., Togi, S., Muromoto, R., Sekine, Y., Ohta, K., Ishiyama, H., & Matsuda, T. (2008) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2008.03.104 · Cited by 49
“The intracellular processing of cytokine signals entails the activation and nuclear translocation of STAT family transcription factors [1-3].”
Background
Binding of SH2-B Family Members within a Potential Negative Regulatory Region Maintains JAK2 in an Active State
Kurzer, J. H., Saharinen, P., Silvennoinen, O., & Carter-Su, C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00570-06 · Cited by 51
“brane to transcription within the nucleus (3).”
Background
Signal Transducer and Activator of Transcription Factor 1 Mediates Apoptosis Induced by Hepatitis C Virus and HIV Envelope Proteins in Hepatocytes
Balasubramanian, A., Ganju, R. K., & Groopman, J. E. (2006) · The Journal of Infectious Diseases · doi:10.1086/505708 · Cited by 45
“It has been demonstrated that STAT is activated by the upstream receptor kinases [46, 47] and/or nonreceptor kinases [48, 49].”
Background
JC virus induces altered patterns of cellular gene expression: Interferon-inducible genes as major transcriptional targets
Verma, S., Ziegler, K., Ananthula, P., Co, J. K. G., Frisque, R. J., Yanagihara, R. T., & Nerurkar, V. R. (2005) · Virology · doi:10.1016/j.virol.2005.10.012 · Cited by 51
Purpurin suppresses atopic dermatitis via TNF-α/IFN-γ-induced inflammation in HaCaT cells
Oh, J., Kim, S., Kwon, O., Kim, J., Oh, S., Han, S., Park, J., & Ahn, K. (2022) · International Journal of Immunopathology and Pharmacology · doi:10.1177/03946320221111135 · Cited by 54
“The STAT protein is the main signaling pathway for various factors and cytokines.31 The STAT family has seven members, of which STAT1 and STAT3 are responsible for the distribution of IFN-γ via JAK1.”
Background
PLTP regulates STAT3 and NFκB in differentiated THP1 cells and human monocyte-derived macrophages
Vuletic, S., Dong, W., Wolfbauer, G., Tang, C., & Albers, J. J. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.06.013 · Cited by 50
Cytokines in the Management of High Risk or Advanced Breast Cancer: An Update and Expectation
Carpi, A., Nicolini, A., Antonelli, A., Ferrari, P., & Rossi, G. (2009) · Current Cancer Drug Targets · doi:10.2174/156800909790192392 · Cited by 49
STAT1-dependent and STAT1-independent gene expression in murine immune cells following stimulation with interferon-alpha
Zimmerer, J. M., Lesinski, G., Radmacher, M., Ruppert, A., & Carson, W. E. I. (2007) · Cancer Immunology and Immunotherapy · doi:10.1007/s00262-007-0329-9 · Cited by 50
“The J. M. Zimmerer Integrated Biological Sciences Graduate Program, The Ohio State University Comprehensive Cancer Center, Columbus, OH 43210, USA J. M. Zimmerer · G. B. Lesinski · W. E. Carson III Human Cancer Genetics Program Department of Molecular Virology, Immunology, and Medical Genetics, The Ohio State Universi…”
Background
Cross-talk among gp130 Cytokines in Adipocytes*
Zvonić, S., Baugh, J., Arbour-Reily, P., Mynatt, R., & Stephens, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m508020200 · Cited by 50
The use of structural biology in Janus kinase targeted drug discovery
L. Alicea-Velazquez, N., & J. Boggon, T. (2011) · Current Drug Targets · doi:10.2174/138945011794751528 · Cited by 53
“The Signal Transducers and Activators of Transcription (STAT) are then recruited to the receptor tail, become phosphorylated and translocate to the nucleus to regulate transcription [4] (Fig.”
Background
Lycium barbarum polysaccharide alleviates dextran sodium sulfate-induced inflammatory bowel disease by regulating M1/M2 macrophage polarization via the STAT1 and STAT6 pathways
Wang, J., Gao, H., Xie, Y., Wang, P., Li, Y., Zhao, J., Wang, C., Ma, X., Wang, Y., Mao, Q., et al. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2023.1044576 · Cited by 46
“Whereas, IL-4/IL-13 activates the STAT6 pathway (Darnell et al., 1994; Kis et al., 2011) and promotes M2-like polarization of macrophage (Ding et al.”
Background
STAT3 ameliorates cognitive deficits via regulation of NMDAR expression in an Alzheimer's disease animal model
Wan, H., Hong, X.-Y., Zhao, Z., Li, T., Zhang, B., Liu, Q. R., Zhao, S. P., Wang, J., Shen, X., & Liu, G. (2021) · Theranostics · doi:10.7150/thno.56541 · Cited by 56
“It’s well known that STATs play a role in development, cell growth and differentiation, proliferation, immune responses, cell survival and apoptosis [5-12].”
Background
Translating JAKs to Jakinibs
Gadina, M., Chisolm, D. A., Philips, R. L., McInness, I. B., Changelian, P. S., & O’Shea, J. J. (2020) · The Journal of Immunology · doi:10.4049/jimmunol.1901477 · Cited by 67
“A critical discovery in understanding cytokine signaling was the identification of another class of JAK substrates by members of Jim Darnell’s laboratory (15, 16), the tyrosine-phosphorylated”
Background
Schisandrin B exhibits potent anticancer activity in triple negative breast cancer by inhibiting STAT3
Dai, X.-X., Yin, C.-T., Guo, G., Zhang, Y., Zhao, C., Qian, J.-C., Wang, O.-C., Zhang, X.-H., & Liang, G. (2018) · Toxicology and Applied Pharmacology · doi:10.1016/j.taap.2018.09.005 · Cited by 49
Identification of Hub Genes and Key Pathways Associated with Two Subtypes of Diffuse Large B-Cell Lymphoma Based on Gene Expression Profiling via Integrated Bioinformatics
Liu, Z., Meng, J., Li, X., Zhu, F., Liu, T., Wu, G., & Zhang, L. (2018) · BioMed Research International · doi:10.1155/2018/3574534 · Cited by 47
Mixed Lineage Kinase 3 Mediates the Induction of CXCL10 by a STAT1‐Dependent Mechanism During Hepatocyte Lipotoxicity
Tomita, K., Kabashima, A., Freeman, B. L., Bronk, S. F., Hirsova, P., & Ibrahim, S. H. (2017) · Journal of Cellular Biochemistry · doi:10.1002/jcb.25973 · Cited by 53
“Additionally, within the conventional JAK-STAT pathway, STAT1 Ser727 phosphorylation occurs in the nucleus after STAT1 Tyr701 activating phosphorylation to increase STAT1 transcriptional efficacy [Darnell et al., 1994].”
Background
SENP1 regulates IFN-γ−STAT1 signaling through STAT3−SOCS3 negative feedback loop
Yu, T., Zuo, Y., Cai, R., Huang, X., Wu, S., Zhang, C., Chin, Y. E., Li, D., Zhang, Z., Xia, N., et al. (2016) · Journal of Molecular Cell Biology · doi:10.1093/jmcb/mjw042 · Cited by 52
“…JAK2 auto-phosphorylation, and followed by phosphorylation of an IFNγR1 tyrosine residue, which serves as a docking site predominantly for STAT1 (Darnell et al., 1994; Sakatsume et al., 1995; Bach et al., 1996; Kaplan et al., 1996; Bach et al., 1997; Pestka et al., 2004; Platanias, 2005;…”
BackgroundInfluential
A novel anti-viral role for STAT3 in IFN-α signalling responses
Mahony, R., Gargan, S., Roberts, K., Bourke, N. M., Keating, S., Bowie, A., O'Farrelly, C., & Stevenson, N. (2016) · Cellular and Molecular Life Sciences · doi:10.1007/s00018-016-2435-3 · Cited by 49
“STAT1 and STAT2 are well-established mediators of the anti-viral response, which bind IFN regulatory factor (IRF)9, thus forming the IFN-stimulated gene factor (ISGF)3 complex ([14]; [44]).”
Background
Live Cell Analysis and Mathematical Modeling Identify Determinants of Attenuation of Dengue Virus 2’-O-Methylation Mutant
Schmid, B., Rinas, M., Ruggieri, A., Acosta, E. G., Bartenschlager, M., Reuter, A., Fischl, W., Harder, N., Bergeest, J.-P., Floßdorf, M., et al. (2015) · PLoS Pathogens · doi:10.1371/journal.ppat.1005345 · Cited by 55
“Upon release from infected cells, IFNs signal in an autocrine and paracrine manner, causing the expression of antiviral IFN-stimulated genes (ISGs) in target cells via phosphorylation of STAT1 and STAT2 [18 – 20].”
Investigational therapies targeting signal transducer and activator of transcription 3 for the treatment of cancer
Santoni, M., Massari, F., Re, M. D., Ciccarese, C., Piva, F., Principato, G., Montironi, R., Santini, D., Danesi, R., Tortora, G., et al. (2015) · Expert Opinion on Investigational Drugs · doi:10.1517/13543784.2015.1020370 · Cited by 49
“Twenty years ago, the signal transducer and activator of transcription (STAT) proteins and their activating Janus kinases (JAKs) were discovered as mediators of interferon signaling [1].”
Pentoxifylline inhibits melanoma tumor growth and angiogenesis by targeting STAT3 signaling pathway
Kamran, M. Z., & Gude, R. P. (2013) · Biomedicine & Pharmacotherapy · doi:10.1016/j.biopha.2013.03.020 · Cited by 50
Stat2 loss leads to cytokine-independent, cell-mediated lethality in LPS-induced sepsis
Alazawi, W., Heath, H., Waters, J. A., Woodfin, A., O'Brien, A. J., Scarzello, A. J., Ma, B., Lopez-Otalora, Y., Jacobs, M., Petts, G., et al. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221652110 · Cited by 44
Regulation of Actin Dynamics by Protein Kinase R Control of Gelsolin Enforces Basal Innate Immune Defense
Irving, A. T., Wang, D., Vasilevski, O., Latchoumanin, O., Kozer, N., Clayton, A. H. A., Szczepny, A., Morimoto, H., Xu, D., Williams, B. R. G., et al. (2012) · Immunity · doi:10.1016/j.immuni.2012.02.020 · Cited by 53
“70 Engagement of IFN receptors (IFNRs) activate Janus kinase (JAK)-signal transducer and 71 activator of transcription (STAT) signaling pathways, leading to transcriptional induction 72 of IFN-stimulated genes (ISGs) and ultimately the generation of ISG products which are 73 critical in order for the IFN-biological re…”
Background
Molecular signatures of peripheral blood mononuclear cells during chronic interferon-α treatment: relationship with depression and fatigue
Felger, J. C., Cole, S. W., Pace, T. W. W., Hu, F., Woolwine, B. J., Doho, G., Raison, C. L., & Miller, A. H. (2011) · Psychological Medicine · doi:10.1017/s0033291711002868 · Cited by 56
“…receptors expressed on immune cells to activate Janus kinase/ signal transducers and activators of transcription (JAK/STAT) and tyrosine kinase signaling, which then increase the expression of cytokines and immunoregulatory genes (Darnell et al. 1994 ; Haque & Williams, 1998 ; Pfeffer et al. 1998).”
Interleukin-29 Binds to Melanoma Cells Inducing Jak-STAT Signal Transduction and Apoptosis
Guenterberg, K. D., Grignol, V. P., Raig, E. T., Zimmerer, J. M., Chan, A. N., Blaskovits, F. M., Young, G. S., Nuovo, G. J., Mundy-Bosse, B. L., Lesinski, G. B., et al. (2010) · Molecular Cancer Therapeutics · doi:10.1158/1535-7163.mct-09-0461 · Cited by 51
“These STAT proteins (STAT1α, STAT2) are phosphorylated by the Janus kinases and subsequently form high-affinity DNA binding complexes that rapidly translocate to the cell nucleus to drive the expression of IFN-responsive genes (3, 4).”
Background
The Alpha/Beta Interferon Receptor Provides Protection against Influenza Virus Replication but Is Dispensable for Inflammatory Response Signaling
Goodman, A. G., Zeng, H., Proll, S. C., Peng, X., Cillóniz, C., Carter, V. S., Korth, M. J., Tumpey, T. M., & Katze, M. G. (2009) · Journal of Virology · doi:10.1128/jvi.01595-09 · Cited by 42
“and activating the JAK-STAT pathway (7).”
Live cell imaging of interleukin-6-induced targeting of “transcription factor” STAT3 to sequestering endosomes in the cytoplasm
Xu, F., Mukhopadhyay, S., & Sehgal, P. B. (2007) · American Journal of Physiology-Cell Physiology · doi:10.1152/ajpcell.00220.2007 · Cited by 49
“The experimental conditions were as follows, with the number of independent replications per variable in parentheses: 20 ␮M geldanamycin (GA) (7 replications); 100 ␮g/ml nocodazole (7); 10 ␮M staurosporine (ST) (6); 100 ␮M genistein (4); 20 ␮M cytochalasin B (CytB) (4); 50 ␮M MG132 (2); 20 ␮M filipin III (3); 200 nM l…”
Influential
Identification of CXCL11 as a STAT3-Dependent Gene Induced by IFN
Yang, C. H., Wei, L., Pfeffer, S. R., Du, Z., Murti, A., Valentine, W. J., Zheng, Y., & Pfeffer, L. M. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.2.986 · Cited by 46
“Phosphorylation of STAT proteins at a critical tyrosine residue is necessary for their appropriate transactivation function as transcription factors (2).”
Background
MUC1 Induced by Epstein-Barr Virus Latent Membrane Protein 1 Causes Dissociation of the Cell-Matrix Interaction and Cellular Invasiveness via STAT Signaling
Kondo, S., Yoshizaki, T., Wakisaka, N., Horikawa, T., Murono, S., Jang, K., Joab, I., Furukawa, M., & Pagano, J. (2006) · Journal of Virology · doi:10.1128/jvi.02222-06 · Cited by 49
“by on January 30, 2010 jvi.asm.org Downloaded from a single tyrosine, typically in response to extracellular ligands ( 9 , 42).”
Background
CXCL12 Signaling Is Independent of Jak2 and Jak3*
Moriguchi, M., Hissong, B., Gadina, M., Yamaoka, K., Tiffany, H., Murphy, P. M., Candotti, F., & O'Shea, J. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m414219200 · Cited by 49
Cardiovascular safety, cancer and Jak-inhibitors: Differences to be highlighted
Benucci, M., Damiani, A., Infantino, M. G., Manfredi, M., Lari, B., Grossi, V., Gobbi, F. L., & Sarzi‐Puttini, P. (2022) · Pharmacological Research · doi:10.1016/j.phrs.2022.106359 · Cited by 52
Role of JAK-STAT and PPAR-Gamma Signalling Modulators in the Prevention of Autism and Neurological Dysfunctions
Khera, R., Mehan, S., Kumar, S., Sethi, P., Bhalla, S., & Prajapati, A. (2022) · Molecular Neurobiology · doi:10.1007/s12035-022-02819-1 · Cited by 57
ORF3a Protein of Severe Acute Respiratory Syndrome Coronavirus 2 Inhibits Interferon-Activated Janus Kinase/Signal Transducer and Activator of Transcription Signaling via Elevating Suppressor of Cytokine Signaling 1
Wang, R., Yang, X., Chang, M., Xue, Z., Wang, W., Bai, L., Zhao, S., & Liu, E. (2021) · Frontiers in Microbiology · doi:10.3389/fmicb.2021.752597 · Cited by 49
Steamed Panax notoginseng Attenuates Anemia in Mice With Blood Deficiency Syndrome via Regulating Hematopoietic Factors and JAK-STAT Pathway
Zhang, Z., Zhang, Y., Gao, M., Cui, X.-M., Yang, Y., van Duijn, B., Wang, M., Hu, Y., Wang, C.-X., & Xiong, Y. (2020) · Frontiers in Pharmacology · doi:10.3389/fphar.2019.01578 · Cited by 48
Dependency on the TYK2/STAT1/MCL1 axis in anaplastic large cell lymphoma
Prutsch, N., Gurnhofer, E., Suske, T., Liang, H.-C., Schlederer, M., Roos, S., Wu, L. C., Simonitsch‐Klupp, I., Alvarez-Hernandez, A., Kornauth, C., et al. (2018) · Leukemia · doi:10.1038/s41375-018-0239-1 · Cited by 52
“To compare the TYK2-specific (Bayer-18 or TYK2) and the pan-JAK inhibitor, JAK inhibitor 1 or Ruxolitinib, we treated ALCL cells for 3 h, and then stimulated the cells for 10 min with Interferon-alpha (IFN-α), which is known to induce TYK2 and JAK1 activity [1, 27].”
Functional activities of interferon gamma in large yellow croaker Larimichthys crocea
Yang, S., Li, Q., Mu, Y.-N., Ao, J.-Q., & Chen, X.-H. (2017) · Fish and Shellfish Immunology · doi:10.1016/j.fsi.2017.09.051 · Cited by 48
Cigarette smoke–induced MMP2 and MMP9 secretion from aortic vascular smooth cells is mediated via the Jak/Stat pathway
Ghosh, A., Pechota, A., Coleman, D. M., Upchurch, G. R., & Eliason, J. L. (2014) · Human Pathology · doi:10.1016/j.humpath.2014.11.003 · Cited by 48
“Members of the Stat protein family function as cytoplasmic signaling molecules as well as transcription factors [23].”
Background
Platelet-Derived Growth Factor-B (PDGF-B) Induced by Hypoxia Promotes the Survival of Pulmonary Arterial Endothelial Cells through the PI3K/Akt/Stat3 Pathway
Li, L., Xu, M., Li, X., Lv, C., Zhang, X., Yu, H., Zhang, M., Fu, Y., Meng, H., & Zhou, J. (2015) · Cellular Physiology and Biochemistry · doi:10.1159/000369709 · Cited by 44
Hyperglycemia and angiotensin II cooperate to enhance collagen I deposition by cardiac fibroblasts through a ROS-STAT3-dependent mechanism
Fiaschi, T., Magherini, F., Gamberi, T., Lucchese, G., Faggian, G. G., Modesti, A., & Modesti, P. A. (2014) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2014.07.009 · Cited by 47
Hepatocellular alterations and dysregulation of oncogenic pathways in the liver of transgenic mice overexpressing growth hormone
Miquet, J. G., Freund, T., Martinez, C. S., González, L., Díaz, M. E., Micucci, G. P., Zotta, E., Boparai, R. K., Bartke, A., Turyn, D., et al. (2013) · Cell Cycle · doi:10.4161/cc.24026 · Cited by 48
The NS1 protein of influenza A virus suppresses interferon-regulated activation of antigen-presentation and immune-proteasome pathways
Tisoncik-Go, J., Billharz, R., Burmakina, S., Belisle, S. E., Proll, S. C., Korth, M. J., García‐Sastre, A., & Katze, M. G. (2011) · Journal of General Virology · doi:10.1099/vir.0.032060-0 · Cited by 46
Emerging Strategies to Strengthen the Anti-Tumour Activity of Type I Interferons: Overcoming Survival Pathways
Caraglia, M., Marra, M., Tagliaferri, P., Lamberts, S. W. J., Zappavigna, S., Misso, G., Cavagnini, F., Facchini, G., Abbruzzese, A., Hofland, L. J., et al. (2009) · Current Cancer Drug Targets · doi:10.2174/156800909789056980 · Cited by 49
Gene (mRNA) expression in canine atopic dermatitis: microarray analysis
Merryman‐Simpson, A. E., Wood, S. H., Fretwell, N., Jones, P. G., McLaren, W. M., McEwan, N. A., Clements, D. N., Carter, S. D., Ollier, W., & Nuttall, T. J. (2008) · Veterinary Dermatology · doi:10.1111/j.1365-3164.2008.00653.x · Cited by 45
BRCA1 Regulates IFN-γ Signaling through a Mechanism Involving the Type I IFNs
Buckley, N. E., Hosey, A. M., Gorski, J. J., Purcell, J. W., Mulligan, J. M., Harkin, D. P., & Mullan, P. B. (2007) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-06-0250 · Cited by 49
“kinases, followed by phosphorylation and dimerization of STAT1 (27, 28).”
Background
Direct role of NF‐κB activation in Toll‐like receptor‐triggered HLA‐DRA expression
Lee, K., Lee, Y., Kim, D., & Kwon, H. (2006) · European Journal of Immunology · doi:10.1002/eji.200535577 · Cited by 45
Lysine vitcylation is a vitamin C-derived protein modification that enhances STAT1-mediated immune response
He, X., Wang, Q., Cheng, X., Wang, W., Li, Y., Nan, Y., Wu, J., Xiu, B., Jiang, T., Bergholz, J. S., et al. (2025) · Cell · doi:10.1016/j.cell.2025.01.043 · Cited by 57
New and Upcoming Topical Treatments for Atopic Dermatitis: A Review of the Literature
Sideris, N., Paschou, E., Bakirtzi, K., Kiritsi, D., Papadimitriou, I., Tsentemeidou, A., Sotiriou, E., & Vakirlis, E. (2022) · Journal of Clinical Medicine · doi:10.3390/jcm11174974 · Cited by 52
The regulation of shrimp metabolism by the white spot syndrome virus (WSSV)
Kumar, R., Huang, J., Ng, Y. S., Chen, C.-Y., & Wang, H. (2021) · Reviews in Aquaculture · doi:10.1111/raq.12643 · Cited by 50
Rac1 modulates the formation of primordial follicles by facilitating STAT3-directed Jagged1, GDF9 and BMP15 transcription in mice
Zhao, L., Du, X., Huang, K., Zhang, T., Teng, Z., Niu, W., Wang, C., & Xia, G. (2016) · Scientific Reports · doi:10.1038/srep23972 · Cited by 59
“To elucidate how essential oocyte-enriched genes are regulated at the mRNA level, we focused our attention on STAT3, which can up-regulate transcription of many genes by binding to their promoters 40 .”
Persistent activation of STAT 3 by PIM 2‐driven positive feedback loop for epithelial‐mesenchymal transition in breast cancer
Uddin, N., Kim, R., Yoo, K.-C., Kim, Y., Cui, Y., Kim, I., Suh, Y., & Lee, S. (2015) · Cancer Science · doi:10.1111/cas.12668 · Cited by 49
Immunoregulatory cytokine networks: 60 years of learning from murine cytomegalovirus
Biron, C. A., & Tarrio, M. L. (2015) · Medical Microbiology and Immunology · doi:10.1007/s00430-015-0412-3 · Cited by 51
Inhibition of Janus kinase/signal transducer and activator of transcription (JAK/STAT) signalling pathway in rheumatoid synovial fibroblasts using small molecule compounds
Migita, K., Izumi, Y., Torigoshi, T., Satomura, K., Izumi, M., Nishino, Y., Jiuchi, Y., Nakamura, M., Kozuru, H., Nonaka, F., et al. (2013) · Clinical and Experimental Immunology · doi:10.1111/cei.12190 · Cited by 47
Hendra and Nipah infection: Emerging paramyxoviruses
Aljofan, M. (2013) · Virus Research · doi:10.1016/j.virusres.2013.08.002 · Cited by 58
Hantavirus Regulation of Type I Interferon Responses
Matthys, V. S., & Mackow, E. R. (2012) · Advances in Virology · doi:10.1155/2012/524024 · Cited by 49
“JAKs phosphorylate Signal Transduction and activators of transcription (STAT) factors, further activating downstream signaling pathways that lead to IFN induction and directing the production of many interferon-stimulated genes (ISGs) [78, 79].”
Background
The Role of Interferon Regulatory Factor-1 (IRF1) in Overcoming Antiestrogen Resistance in the Treatment of Breast Cancer
Schwartz, J., Shajahan‐Haq, A. N., & Clarke, R. C. (2011) · International Journal of Breast Cancer · doi:10.4061/2011/912102 · Cited by 42
“The IRF DBD has a helix-turn-helix architecture that recognizes a specific DNA sequence corresponding to the IFN-stimulated response element (ISRE; G(A)AAAG/CT/CGAAAG/CT/C) [21].”
Background
Metabolites and JAK/STAT pathway were involved in the liver and spleen damage in male Wistar rats fed with mequindox
Wang, X., Huang, X., Ihsan, A., Liu, Z., Huang, L., Zhang, H.-H., Zhang, H.-F., Zhou, W., Liu, Q., Xue, X., et al. (2010) · Toxicology · doi:10.1016/j.tox.2010.12.001 · Cited by 47
Nuclear β-Arrestin1 Functions as a Scaffold for the Dephosphorylation of STAT1 and Moderates the Antiviral Activity of IFN-γ
Mo, W., Zhang, L., Yang, G., Zhai, J., Hu, Z., Chen, Y., Chen, X., Hui, L., Huang, R., & Hu, G. (2008) · Molecular Cell · doi:10.1016/j.molcel.2008.06.017 · Cited by 51
“STAT1, a member of STAT family, is essential for gene activation in response to IFN-g stimulation ( Darnell et al., 1994; Durbin et al., 1996).”
Background
Mouse cytomegalovirus inhibits beta interferon (IFN-β) gene expression and controls activation pathways of the IFN-β enhanceosome
Le‐Trilling, V. T. K., Trilling, M., Zimmermann, A., & Hengel, H. (2008) · Journal of General Virology · doi:10.1099/vir.0.83538-0 · Cited by 40
“ISGF3 binds to IFN-stimulated response elements (ISRE), located in the promoter region of IFNinducible target genes mediating IFN effector functions (Darnell et al., 1994).”
Interferon-gamma-induced dephosphorylation of STAT3 and apoptosis are dependent on the mTOR pathway
FANG, P., Hwa, V., & Rosenfeld, R. G. (2006) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.12.011 · Cited by 45
Type I Interferons Trigger Systemic, Partial Lymphocyte Activation in Response to Viral Infection
Alsharifi, M., Lobigs, M., Regner, M., Lee, E., Koskinen, A. M. L., & Müllbacher, A. (2005) · Journal of Immunology · doi:10.4049/jimmunol.175.7.4635 · Cited by 47
“All IFN-I subtypes bind to a common cell surface receptor (5, 6) and play an important role in host protection following infection by a variety of viruses (2, 7–9).”
Background
RANK ligand and interferon gamma differentially regulate cathepsin gene expression in pre-osteoclastic cells
Pang, M., Martinez, A. F., Jacobs, J., Balkan, W., & Troen, B. R. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.12.005 · Cited by 44
SUMOylation of KLF4 promotes IL-4 induced macrophage M2 polarization
Wang, K., Zhou, W., Cai, Q., Cheng, J., Cai, R., & Xing, R. (2017) · Cell Cycle · doi:10.1080/15384101.2016.1269045 · Cited by 49
Genetic and Epigenetic Causes of Pituitary Adenomas
Chang, M., Yang, C., Bao, X., & Wang, R. (2021) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.596554 · Cited by 58
“Signal Transducer and Activator of Transcription 3 STAT3 is a member of the STAT family, and participates in cellular responses to cytokines and growth factors (67).”
Background
Discovery of a Janus Kinase Inhibitor Bearing a Highly Three-Dimensional Spiro Scaffold: JTE-052 (Delgocitinib) as a New Dermatological Agent to Treat Inflammatory Skin Disorders
Noji, S., Hara, Y., Miura, T., Yamanaka, H., Maeda, K., Hori, A., Yamamoto, H., Obika, S., Inoue, M., Hase, Y., et al. (2020) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.0c00450 · Cited by 59
Intermittent hypoxia mediated by TSP1 dependent on STAT3 induces cardiac fibroblast activation and cardiac fibrosis
Bao, Q., Zhang, B., Suo, Y., Liu, C., Yang, Q., Zhang, K., Yuan, M., Yuan, M., Zhang, Y., & Li, G. (2020) · eLife · doi:10.7554/elife.49923 · Cited by 59
“Since the phosphorylation status of STAT3 is related to its transcriptional activity (Darnell et al., 1994; Ihle, 1995), we determined the phosphorylation of STAT3 at multiple sites as well as the phosphorylation of JAKs in mPCFs under IH.”
Background
The Ancient Chinese Decoction Yu-Ping-Feng Suppresses Orthotopic Lewis Lung Cancer Tumor Growth Through Increasing M1 Macrophage Polarization and CD4+ T Cell Cytotoxicity
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Background

Authors: Darnell, J. E., Kerr, L. M., & Stark, G. R.
Affiliations: Rockefeller University (US)
Case Comprehensive Cancer Center (US)
ORCID: Stark, George R.
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1994-06-03
Volume: 264
Issue: 5164
Pages: 1415-1421
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.8197455
OpenAlex: W2029275361
Cited by: 6,080
References: 85
Citations by year: 2026: 84 · 2025: 139 · 2024: 175 · 2023: 170 · 2022: 183 · 2021: 177 · 2020: 162 · 2019: 155 · 2018: 121 · 2017: 166 · 2016: 148 · 2015: 152 · 2014: 160 · 2013: 207 · 2012: 188
FWCI: 28.59
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Immunology and Microbiology › Immunology › interferon and immune responses
Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › NF-κB Signaling Pathways
Keywords: JAK/STAT signaling, interferon-alpha, interferon-gamma, signal transduction, STAT proteins, transcriptional activation, JAK kinases, interferon receptor, nuclear translocation, DNA binding
MeSH terms: Amino Acid Sequence, Animals, Base Sequence, Cell Line, DNA-Binding Proteins, Genes, Genetic Complementation Test, Humans, Interferon-gamma, Molecular Sequence Data, Mutation, Protein-Tyrosine Kinases, Regulatory Sequences, Nucleic Acid, Transcription Factors, Signal Transduction, Transcriptional Activation, Interferon-alpha, Interferon-Stimulated Gene Factor 3, Interferon-Stimulated Gene Factor 3, gamma Subunit

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Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins

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