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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Background
Potential therapeutic targets of the JAK2/STAT3 signaling pathway in triple-negative breast cancer
Lin, L., Fei, X., Chen, L., Yao, L., & Lei, X. (2024) · Frontiers in Oncology · doi:10.3389/fonc.2024.1381251 · Cited by 52
“The JAK2/STAT3 signaling pathway is ubiquitously expressed in cells and vital in physiological functions (91), such as cell proliferation, differentiation, apoptosis, and immune regulation (92).”
Background
The role of mitochondria in the resistance of melanoma to PD-1 inhibitors
Du, F., Yang, L.-H., Liu, J., Wang, J., Fan, L., Duangmano, S., Liu, H., Liu, M., Wang, J., Zhong, X., et al. (2023) · Journal of Translational Medicine · doi:10.1186/s12967-023-04200-9 · Cited by 47
Targeting type I interferons in systemic lupus erythematous
Bruera, S., Chavula, T., Madan, R., & Agarwal, S. K. (2023) · Frontiers in Pharmacology · doi:10.3389/fphar.2022.1046687 · Cited by 44
“Extensive complementary work by James Darnell, Ian Kerr and George Stark established the JAK-STAT signaling as the major pathway through which type 1 IFNs mediate their effects (Darnell et al., 1994).”
Background
Emerging Roles of Type-I Interferons in Neuroinflammation, Neurological Diseases, and Long-Haul COVID
Tan, P.-H., Ji, J., Hsing, C., Tan, R., & Ji, R. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms232214394 · Cited by 55
African Swine Fever Virus pI215L Inhibits Type I Interferon Signaling by Targeting Interferon Regulatory Factor 9 for Autophagic Degradation
Li, L., Fu, J., Li, J., Guo, S., Chen, Q., Zhang, Y., Liu, Z., Tan, C., Chen, H., & Wang, X. (2022) · Journal of Virology · doi:10.1128/jvi.00944-22 · Cited by 45
“The expression and phosphorylation of JAK1, TYK2, STAT1, and STAT2 were unaffected by ASFV pI215L (Fig.”
BackgroundMethodInfluential
The RLK protein TaCRK10 activates wheat high-temperature seedling-plant resistance to stripe rust through interacting with TaH2A.1.
Wang, J.-H., Wang, J.-J., Li, J., Shang, H., Chen, X.-M., & Hu, X.-P. (2021) · The Plant Journal · doi:10.1111/tpj.15513 · Cited by 44
STAT3 pathway as a molecular target for resveratrol in breast cancer treatment
Kohandel, Z., Farkhondeh, T., Aschner, M., Pourbagher‐Shahri, A. M., & Samarghandian, S. (2021) · Cancer Cell International · doi:10.1186/s12935-021-02179-1 · Cited by 51
“The involvement of STAT3 in the development, metastasis, multidrug resistance, and proliferation of cancer has been subject to extensive research [15, 16].”
Background
Disentangling molecular mechanisms regulating sensitization of interferon alpha signal transduction
Kok, F., Rosenblatt, M., Teusel, M., Nizharadze, T., Magalhães, V. G., Dächert, C., Maiwald, T., Vlasov, A., Wäsch, M., Tyufekchieva, S., et al. (2020) · Molecular Systems Biology · doi:10.15252/msb.20198955 · Cited by 44
Ruxolitinib synergistically enhances the anti-tumor activity of paclitaxel in human ovarian cancer
Han, E. S., Wen, W. X., Dellinger, T. H., Wu, J., Lu, S. A., Jove, R., & Yim, J. H. (2018) · Oncotarget · doi:10.18632/oncotarget.24368 · Cited by 51
“In response to cytokine stimulation, STAT3 is phosphorylated at Tyr705 by Janus family kinases (JAK) [8, 9].”
Background
Biflorin, Isolated from the Flower Buds ofSyzygium aromaticumL., Suppresses LPS-Induced Inflammatory Mediators via STAT1 Inactivation in Macrophages and Protects Mice from Endotoxin Shock
Lee, H., Shin, J., Lee, W., Ryu, B., Jang, D. S., & Lee, K. (2016) · Journal of Natural Products · doi:10.1021/acs.jnatprod.5b00609 · Cited by 48
The Interferon-Induced Mx2 Inhibits Porcine Reproductive and Respiratory Syndrome Virus Replication
Wang, H.-Y., Bai, J., Fan, B., Li, Y.-F., Zhang, Q., & Jiang, P. (2016) · Journal of Interferon and Cytokine Research · doi:10.1089/jir.2015.0077 · Cited by 44
EFTUD2 Is a Novel Innate Immune Regulator Restricting Hepatitis C Virus Infection through the RIG-I/MDA5 Pathway
Zhu, C., Xiao, F., Hong, J., Wang, K., Liu, X., Cai, D., Fusco, D. N., Zhao, L., Jeong, S. W., Brisac, C., et al. (2015) · Journal of Virology · doi:10.1128/jvi.00364-15 · Cited by 45
“The binding of IFN to its receptor leads to the activation of receptor-associated Janus-activated kinase 1 (JAK1) and tyrosine kinase 2 (Tyk2) (45, 46).”
Background
Decreased STAT4 indicates poor prognosis and enhanced cell proliferation in hepatocellular carcinoma
Wang, G. (2015) · World Journal of Gastroenterology · doi:10.3748/wjg.v21.i13.3983 · Cited by 43
Novel Thiosemicarbazones Regulate the Signal Transducer and Activator of Transcription 3 (STAT3) Pathway: Inhibition of Constitutive and Interleukin 6–Induced Activation by Iron Depletion
Lui, G. Y. L., Kovačević, Ž., Menezes, S. V., Kalinowski, D. S., Merlot, A. M., Sahni, S., & Richardson, D. R. (2015) · Molecular Pharmacology · doi:10.1124/mol.114.096529 · Cited by 45
“…and transcription of target genes (e.g., Bcl-2, cyclin D1, and c-myc) that promote cell proliferation, survival, migration, apoptosis inhibition, and immune evasion (Darnell et al., 1994; Ihle, 1995; Sasse et al., 1997; Zushi et al., 1998; Bromberg et al., 1999;Wang et al., 2004; Xie et al., 2004).”
Background
Ubiquitin-Specific Peptidase USP22 Negatively Regulates the STAT Signaling Pathway by Deubiquitinating SIRT1
Ao, N., Liu, Y., Feng, H., Bian, X., Li, Z., Gu, B., Zhao, X., & Liu, Y. (2014) · Cellular Physiology and Biochemistry · doi:10.1159/000362964 · Cited by 49
STAT1-caspase 3 pathway in the apoptotic process associated with steroid-induced necrosis of the femoral head
Xu, X., Wen, H. L., Hu, Y., Yu, H., Zhang, Y. L., Chen, C., & Pan, X. (2014) · Journal of Molecular Histology · doi:10.1007/s10735-014-9571-6 · Cited by 51
Dynamic trafficking of STAT5 depends on an unconventional nuclear localization signal
Shin, H., & Reich, N. (2013) · Journal of Cell Science · doi:10.1242/jcs.123042 · Cited by 44
“The family of signal transducers and activators of transcription (STATs) exemplifies signaling molecules that can sense changes at the plasma membrane and subsequently redirect gene expression (Darnell et al., 1994; Levy and Darnell, 2002; Schindler et al., 2007).”
Background
Developmental differences in IFN signaling affect GATA1s-induced megakaryocyte hyperproliferation
Woo, A. J., Wieland, K., Huang, H., Akie, T. E., Piers, T., Kim, J., & Cantor, A. B. (2013) · Journal of Clinical Investigation · doi:10.1172/jci40609 · Cited by 48
“Binding of IFN-α/β to its heterodimeric receptors, IFNAR1 and IFNAR2, leads to activation of the JAK-STAT pathway, with JAK1/ TYK2 and STAT1/STAT2 being the most important contributors (35, 36).”
Interferon-α (IFNα) neurotoxicity
Fritz-French, C., & Tyor, W. R. (2012) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2012.01.001 · Cited by 46
PIAS3 negatively regulates RANKL-mediated osteoclastogenesis directly in osteoclast precursors and indirectly via osteoblasts
Hikata, T., Takaishi, H., Takito, J., Hakozaki, A., Furukawa, M., Uchikawa, S., Kimura, T., Okada, Y., Matsumoto, M., Yoshimura, A., et al. (2008) · Blood · doi:10.1182/blood-2008-06-162594 · Cited by 45
Phase 1/2 Clinical Trial of Interferon α2b and Weekly Liposome-encapsulated All-trans Retinoic Acid in Patients With Advanced Renal Cell Carcinoma
Boorjian, S. A., Milowsky, M. I., Kaplan, J., Albert, M., Cobham, M. V., Coll, D. M., Mongan, N. P., Shelton, G., Petrylak, D. P., Gudas, L. J., et al. (2007) · Journal of Immunotherapy · doi:10.1097/cji.0b013e31805449a8 · Cited by 52
“Median relapse-free interval (mo) (range)* 66 (12-168) 10.”
Digesting the Role of JAK-STAT and Cytokine Signaling in Oral and Gastric Cancers
Ni, Y., Low, J. T., Silke, J., & O’Reilly, L. A. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.835997 · Cited by 47
Targeting EphA2 suppresses hepatocellular carcinoma initiation and progression by dual inhibition of JAK1/STAT3 and AKT signaling
Wang, H., Hou, W., Perera, A., Bettler, C., Beach, J. R., Ding, X., Li, J., Denning, M. F., Dhanarajan, A. R., Cotler, S. J., et al. (2021) · Cell Reports · doi:10.1016/j.celrep.2021.108765 · Cited by 47
“Although knockdown of EphA2 did not affect STAT3 mRNA expression levels in HCC cells (Figure S5A), EphA2 knockdown in HCC cells suppressed phosphorylation of STAT3 at Tyr705 (Figure 5B), which is critical for STAT3 activation (Darnell et al., 1994).”
JMJD4-demethylated RIG-I prevents hepatic steatosis and carcinogenesis
Li, Z., Zhou, Y., Jia, K., Yang, Y., Zhang, L., Wang, S., Dong, Y., Wang, M., Li, Y., Lu, S., et al. (2022) · Journal of Hematology & Oncology · doi:10.1186/s13045-022-01381-6 · Cited by 44
Tumor-associated macrophages in classical Hodgkin lymphoma: hormetic relationship to outcome
Werner, L. C., Dreyer, J. H., Hartmann, D., Barros, M. H. M., Büttner-Herold, M. J., Grittner, U., & Niedobitek, G. (2020) · Scientific Reports · doi:10.1038/s41598-020-66010-z · Cited by 48
Antiviral and Inflammatory Cellular Signaling Associated with Enterovirus 71 Infection
Jin, Y., Zhang, R., Wu, W., & Duan, G. (2018) · Viruses · doi:10.3390/v10040155 · Cited by 48
“The binding of IFN-α/β to the type I IFN receptors or IFN-γ to the type II IFN receptors results in the rapid autophosphorylation and activation of Janus-activated kinase (Jak)/signal transducer and activator of transcription (STAT) pathways [37].”
Background
An Activating Mutation in STAT3 Results in Neonatal Diabetes Through Reduced Insulin Synthesis
Velayos, T., Martínez, R., Alonso, M., García‐Etxebarria, K., Aguayo, A., Camarero, C., Urrutia, I., de la Piscina, I. M., Barrio, R., Santín, I., et al. (2017) · Diabetes · doi:10.2337/db16-0867 · Cited by 48
“The Identified STAT3 Mutation Leads to Increased STAT3 Activity but Does Not Affect STAT3 Phosphorylation The transcription factor STAT3 is activated by phosphorylation at tyrosine 705, which induces dimerization, nuclear translocation, and DNA binding (21).”
Background
miR-124 functions as a tumor suppressor in the endometrial carcinoma cell line HEC-1B partly by suppressing STAT3
Li, Y., Zhang, Z., Liu, X., Huang, T., He, W., Shen, Y., Liu, X., Hong, K., & Cao, Q. (2013) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-013-1913-2 · Cited by 39
“Activation by inflammatory cytokines like interleukin-6 (IL-6), IL-11, and interferon (IFN), as well as by lipopolysaccharide (LPS) induces STAT3 tyrosine-705 phosphorylation and dimer formation, cytoplasmic-to-nuclear shuttling, recognition of STAT3-specific DNA-binding elements, and transcriptional activation of tar…”
FGF2 regulates melanocytes viability through the STAT3-transactivated PAX3 transcription
Dong, L., Li, Y., Cao, J., Liu, F., Pier, E., Chen, J., Xu, Z., Chen, C., Wang, R.-A., & Cui, R. (2011) · Cell Death and Differentiation · doi:10.1038/cdd.2011.132 · Cited by 43
STAT3 is involved in phosphatidic acid-induced Bcl-2 expression in HeLa cells
Choi, H., Lee, J. H., Park, S., Cho, J. H., & Han, J. (2009) · Experimental & Molecular Medicine · doi:10.3858/emm.2009.41.2.012 · Cited by 43
Identification of human thioredoxin as a novel IFN-gamma-induced factor: Mechanism of induction and its role in cytokine production
Kim, S.-H., Oh, J., Choi, J., Jang, J.-Y., Kang, M.-W., & Lee, C.-E. (2008) · BMC Immunology · doi:10.1186/1471-2172-9-64 · Cited by 43
“The analysis of the signal pathways induced by IFN-γ in monocytic cells revealed that, in addition to the well-known Jak1/Stat1 pathways [35], IFN-γ generates strong activating signals for Akt, Erk and p38 MAPK within 15 to 60 min (Fig 4A).”
Background
Abrogation of Viral Interleukin-6 (vIL-6)-Induced Signaling by Intracellular Retention and Neutralization of vIL-6 with an Anti-vIL-6 Single-Chain Antibody Selected by Phage Display
Kovaleva, M., Bußmeyer, I., Rabe, B., Grötzinger, J., Sudarman, E., Eichler, J., Conrad, U., Rose‐John, S., & Scheller, J. (2006) · Journal of Virology · doi:10.1128/jvi.00420-06 · Cited by 41
“Dimerization of gp130 leads to the activation of kinases of the JAK family and of the STAT1 and STAT3 transcriptional activators (19, 76).”
Background
Hypericum perforatum attenuates the development of carrageenan-induced lung injury in mice
Menegazzi, M., Paola, R. D., Mazzon, E., Muià, C., Genovese, T., Crisafulli, C., Suzuki, H., & Cuzzocrea, S. (2005) · Free Radical Biology and Medicine · doi:10.1016/j.freeradbiomed.2005.08.034 · Cited by 43
Immature monocyte derived dendritic cells gene expression profile in response to Virus-Like Particles stimulation
Aricò, E., Wang, E., Tornesello, M., Tagliamonte, M., Lewis, G., Marincola, F., Buonaguro, F., & Buonaguro, L. (2005) · Journal of Translational Medicine · doi:10.1186/1479-5876-3-45 · Cited by 43
“STAT2 is activated upon the binding of type-I IFN, the major component of the innate immune system, to its receptor and participates to the formation of interferonstimulated gene factor 3 (ISGF3) complex, composed of STAT1, STAT2, and IFN regulatory factor 9, which promotes serial synthesis of selected proteins that i…”
Background
Effects of overexpression of pancreatic derived factor (FAM3B) in isolated mouse islets and insulin-secreting betaTC3 cells.
Cao, X.-P., Yang, J.-C., Burkhardt, B. R., Gao, Z., Wong, R., Greene, S. R., Wu, J.-M., & Wolf, B. (2005) · American Journal of Physiology. Endocrinology and Metabolism · doi:10.1152/ajpendo.00113.2005 · Cited by 43
“The STAT family has numerous isoforms, and they are necessary components of cytokine receptor signaling (9).”
Background
Two Gamma Interferon-Activated Site-Like Elements in the Human Cytomegalovirus Major Immediate-Early Promoter/Enhancer Are Important for Viral Replication
Netterwald, J., Yang, S.-J., Wang, W.-J., Ghanny, S., Cody, M. J., Soteropoulos, P., Tian, B., Dunn, W., Liu, F.-Y., & Zhu, H. (2005) · Journal of Virology · doi:10.1128/jvi.79.8.5035-5046.2005 · Cited by 43
“While it is clear from this study that the two VRS1 elements in the MIEP/E are important for major IE expression and viral growth in HFF cells at a low MOI, we propose that the HCMV-initiated signal transduction pathway, which leads to the activation of ISGs, directly regulates major IE expression through the VRS1 sit…”
BackgroundInfluential
Activation of Mitogen-activated Protein Kinase Kinase (MKK) 3 and MKK6 by Type I Interferons
Li, Y., Batra, S., Sassano, A., Majchrzak, B., Levy, D. E., Gaestel, M., Fish, E. N., Davis, R. J., & Platanias, L. C. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m410972200 · Cited by 37
Role of prostaglandin E2 in macrophage polarization: Insights into atherosclerosis
Wang, W., Liang, M., Wang, L., Bei, W., Rong, X., Xu, J., & Guo, J. (2022) · Biochemical Pharmacology · doi:10.1016/j.bcp.2022.115357 · Cited by 46
OTUB2 exerts tumor-suppressive roles via STAT1-mediated CALML3 activation and increased phosphatidylserine synthesis
Chang, W., Luo, Q., Wu, X., Nan, Y., Zhao, P., Zhang, L., Luo, A., Jiao, W., Zhu, Q., Fu, Y., et al. (2022) · Cell Reports · doi:10.1016/j.celrep.2022.111561 · Cited by 41
Crosstalk of the Androgen Receptor with Transcriptional Collaborators: Potential Therapeutic Targets for Castration-Resistant Prostate Cancer
Obinata, D., Takayama, K., Takahashi, S., & Inoue, S. (2017) · Cancers · doi:10.3390/cancers9030022 · Cited by 50
Quantitative proteomic analysis reveals that transmissible gastroenteritis virus activates the JAK-STAT1 signaling pathway.
An, K., Fang, L.-R., Luo, R., Wang, D., Xie, L.-L., Yang, J., Chen, H.-C., & Xiao, S.-B. (2014) · Journal of Proteome Research · doi:10.1021/pr500173p · Cited by 42
Host STAT2/type I interferon axis controls tumor growth
Yue, C., Xu, J., Estioko, M. D. T., Kotredes, K. P., Lopez-Otalora, Y., Hilliard, B. A., Baker, D. P., Gallucci, S., & Gamero, A. M. (2014) · International Journal of Cancer · doi:10.1002/ijc.29004 · Cited by 38
Three important components in the regeneration of the cavernous nerve: brain-derived neurotrophic factor, vascular endothelial growth factor and the JAK/STAT signaling pathway.
Zhang, H.-Y., Jin, X.-B., & Lue, T. F. (2011) · Asian Journal of Andrology · doi:10.1038/aja.2010.162 · Cited by 39
A novel virus-inducible enhancer of the interferon-β gene with tightly linked promoter and enhancer activities
Banerjee, A. R., Kim, Y. J., & Kim, T. H. (2014) · Nucleic Acids Research · doi:10.1093/nar/gku1018 · Cited by 39
“This element, a known component of the antiviral response (30), shared 10 out of 11 identical bases between human and mouse.”
BackgroundInfluential
The JAK-inhibitor, JAB/SOCS-1 selectively inhibits cytokine-induced, but not v-Src induced JAK–STAT activation
Iwamoto, T., Senga, T., Naito, Y., Matsuda, S., Miyake, Y., Yoshimura, A., & Hamaguchi, M. (2000) · Oncogene · doi:10.1038/sj.onc.1203829 · Cited by 36
Signalling Pathways Activated by All- trans -Retinoic Acid in Acute Promyelocytic Leukemia Cells
Kambhampati, S., Verma, A., Li, Y., Parmar, S., Sassano, A., & Platanias, L. (2004) · Leukemia & Lymphoma · doi:10.1080/10428190410001722053 · Cited by 29
Interferon γ (IFNγ) Signaling via Mechanistic Target of Rapamycin Complex 2 (mTORC2) and Regulatory Effects in the Generation of Type II Interferon Biological Responses
Kroczynska, B., Rafidi, R. L., Majchrzak-Kita, B., Kosciuczuk, E. M., Blyth, G. T., Jemielity, J., Warminska, Z., Saleiro, D., Mehrotra, S., Arslan, A. D., et al. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.664995 · Cited by 29
Alternative activation of macrophages by prostacyclin synthase ameliorates alcohol induced liver injury
Pan, X.-Y., Wang, L., You, H.-M., Cheng, M., Yang, Y., Huang, C., & Li, J. (2021) · Laboratory Investigation · doi:10.1038/s41374-021-00531-7 · Cited by 26
“ylation and subsequent dimerization of (STAT)1 [10].”
Inhibition of Janus Kinase 2 and Signal Transduction and Activator of Transcription 3 Protect Against Cecal Ligation and Puncture-Induced Multiple Organ Damage and Mortality
Hui, L., Yao, Y., Wang, S., Yu, Y., Dong, N., Li, H., & Sheng, Z. (2009) · Journal of Trauma: Injury, Infection & Critical Care · doi:10.1097/ta.0b013e318164d05f · Cited by 42
“For example, interferon (IFN)- employs the JAK/STAT pathway for its signal transduction to augment the innate immune response initiated by LPS, TNF- , or IL-1, and proinflammatory effect of IL-6 is mainly mediated by STAT1/3.4,5 Thus, blockade of JAK/STAT pathway at the right time as well as in the appropriate point p…”
BackgroundInfluential
Biological Hallmarks and Emerging Strategies to Target STAT3 Signaling in Multiple Myeloma
Zhou, J., & Chng, W.-J. (2022) · Cells · doi:10.3390/cells11060941 · Cited by 22
“Janus tyrosine kinases (JAKs)-STAT pathway was originally discovered in the context of interleukin-mediated inflammatory response [15].”
Background
Necdin, a negative growth regulator, is a novel STAT3 target gene down-regulated in human cancer
Haviland, R., Eschrich, S., Bloom, G., Ma, Y., Minton, S., Jove, R., & Cress, W. D. (2011) · PLoS ONE · doi:10.1371/journal.pone.0024923 · Cited by 19
Equid Herpesvirus 1 targets the sensitization and induction steps to inhibit the type I interferon response in equine endothelial cells.
Oladunni, F. S., Sarkar, S., Reedy, S., Balasuriya, U. B. R., Horohov, D. W., & Chambers, T. M. (2019) · Journal of Virology · doi:10.1128/jvi.01342-19 · Cited by 18
STAT1 Regulates the Homeostatic Component of Visual Cortical Plasticity via an AMPA Receptor-Mediated Mechanism
Nagakura, I., Van Wart, A., Petravicz, J., Tropea, D., & Sur, M. (2014) · Journal of Neuroscience · doi:10.1523/jneurosci.0189-14.2014 · Cited by 18
MAPK signaling during Müller glial cell development in retina explant cultures
Zhang, S. S.-M., Li, H., Huang, P., Lou, L. X., Fu, X.-Y., & Barnstable, C. J. (2010) · Journal of Ocular Biology, Diseases, and Informatics · doi:10.1007/s12177-011-9064-8 · Cited by 7
“After phosphorylation, the activated STAT proteins dimerize in the cytoplasm and then translocate to the nucleus where they can modulate transcription [20].”
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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