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Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins
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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“Signal transducer and activator of transcription 3 (STAT3) belongs to the family of STAT transcription factors which mediate the cellular response to a variety of cytokines and growth factors including IL-6 (6-8”
From STAT3 Contributes to the Mitogenic Response of Hepatocytes during Liver Regeneration (2002) · cites this paper as [6]
In the citing paper
“Specifically, STAT1 and IRF5 have been shown to be involved in polarization and maintenance of an M1 phenotype while STAT6, IRF4, CREB-C/EBPβ, and PPARγ are involved in polarization and maintenance of an M2 phenotype [23–30].”
From Macrophage polarization: an opportunity for improved outcomes in biomaterials and regenerative medicine (2012) · cites this paper as [23]
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Phospholipid scramblases: An overview
Sahu, S. K., Gummadi, S. N., Manoj, N., & Aradhyam, G. K. (2007) · Archives of Biochemistry and Biophysics · doi:10.1016/j.abb.2007.04.002 · Cited by 211
De Domenico, I., Zhang, T. Y., Koening, C. L., Branch, R. W., London, N., Lo, E., Daynes, R. A., Kushner, J. P., Li, D., Ward, D. M., et al. (2010) · Journal of Clinical Investigation · doi:10.1172/jci42011 · Cited by 197
Signaling pathways involved in MDSC regulation
Trikha, P., & Carson, W. E. (2014) · Biochimica et Biophysica Acta (BBA) - Reviews on Cancer · doi:10.1016/j.bbcan.2014.04.003 · Cited by 207
“Gene knockout studies have helped elucidate various components of this pathway, which was originally discovered as part of the IFN signaling system [84].”
BackgroundA nuclear protein tyrosine phosphatase is required for the inactivation of Stat1
Haspel, R. L., & Darnell, J. E. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.18.10188 · Cited by 203
How cells respond to interferons revisited: From early history to current complexity
Stark, G. R. (2007) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2007.06.013 · Cited by 182
“Please see reviews [6,7] for descriptions and results of these experiments.”
BackgroundSelf-citationLiu, W.-J., Chang, Y.-S., Wang, A. H. ‐., Kou, G., & Lo, C. (2007) · Journal of Virology · doi:10.1128/jvi.01880-06 · Cited by 205
“Tyrosine-phosphorylated STATs form dimers or multimers, are transported into the nucleus, bind to the cognate DNA sequences, and activate gene expression (7, 10, 15, 31, 44).”
BackgroundPregnancy recognition signaling mechanisms in ruminants and pigs
Bazer, F. (2013) · Journal of Animal Science and Biotechnology · doi:10.1186/2049-1891-4-23 · Cited by 200
“(TYK2) pathway [1,7,8].”
Hepatitis C Virus Core Protein Blocks Interferon Signaling by Interaction with the STAT1 SH2 Domain
Lin, W., Kim, S. S., Yeung, E., Kamegaya, Y., Blackard, J., Kim, K. A., Holtzman, M., & Chung, R. (2006) · Journal of Virology · doi:10.1128/jvi.00459-06 · Cited by 200
“... previously demonstrated to be essential for STAT1 signaling, we examined the effect of HCV core transfection in STAT1-deficient U3A cells cotransfected with wild-type STAT1 construct pST1-Full (aa 1 to 750) or point mutant STAT1 constructs pST1- 428/9 M (putative DNA binding site), pST1-701 M (JAK kinase phosphory…”
BackgroundMethodProtein kinase inhibitors in the treatment of inflammatory and autoimmune diseases
Patterson, H., Nibbs, R., McInnes, I., & Siebert, S. (2014) · Clinical and Experimental Immunology · doi:10.1111/cei.12248 · Cited by 199
Kasembeli, M. M., Bharadwaj, U., Robinson, P., & Tweardy, D. J. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19082299 · Cited by 199
“Signal transducer and activator of transcription (STAT) 3 is one of a seven-member family of proteins that transduce peptide hormone signals from the cell surface to the nucleus [1].”
BackgroundInterferons: Signaling, antiviral and viral evasion
Bonjardim, C. A., Ferreira, P. C. P., & Kroon, E. G. (2009) · Immunology Letters · doi:10.1016/j.imlet.2008.11.002 · Cited by 196
“However, a recent report revealed that ISGF3 formation and translocation to the nucleus in response to IFN-␣ is dependent on the acetylation of all components of the heterotrimeric complex.”
BackgroundRedox Regulation of STAT1 and STAT3 Signaling
Butturini, E., de Prati, A. C., & Mariotto, S. (2020) · International Journal of Molecular Sciences · doi:10.3390/ijms21197034 · Cited by 214
Evaluation of potential Stat3-regulated genes in human breast cancer
Hsieh, F.-C., Cheng, G., & Lin, J. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.07.075 · Cited by 180
Kubota, T., Matsuoka, M., Chang, T.-H., Tailor, P. B., Sasaki, T., Tashiro, M., Kato, A., & Ozato, K. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804479200 · Cited by 174
Schroeder, A., Herrmann, A., Cherryholmes, G. A., Kowolik, C. M., Buettner, R., Pal, S. K., Yu, H., Müller‐Newen, G., & Jove, R. (2013) · Cancer Research · doi:10.1158/0008-5472.can-13-0594 · Cited by 192
“Upon STAT3 phosphorylation at Y705, STAT3 forms stable dimers and translocates to the nucleus, where it binds to its specific promoter sequences to induce target gene expression (9, 24).”
BackgroundThe Common Cytokine Receptor γ Chain Family of CytokinesPreprint
Lin, J., & Leonard, W. J. (2017) · Cold Spring Harbor Perspectives in Biology · doi:10.1101/cshperspect.a028449 · Cited by 215
Novel STAT1 Alleles in Otherwise Healthy Patients with Mycobacterial Disease
Chapgier, A. L. A., Boisson‐Dupuis, S., Jouanguy, E., Vogt, G., Feinberg, J. M., Prochnicka‐Chalufour, A., Casrouge, A., Yang, K., Soudais, C., Fieschi, C., et al. (2006) · PLoS Genetics · doi:10.1371/journal.pgen.0020131 · Cited by 200
Targeting the JAK/STAT Signaling Pathway Using Phytocompounds for Cancer Prevention and Therapy
Bose, S., Banerjee, S., Mondal, A., Chakraborty, U., Pumarol, J., Croley, C. R., & Bishayee, A. (2020) · Cells · doi:10.3390/cells9061451 · Cited by 219
“The dimer then translocates into the nucleus wherein the dimer gets attached to DNA and stimulates the expression of genes that are responsive to cytokines [33,34].”
BackgroundLife-threatening influenza pneumonitis in a child with inherited IRF9 deficiency
Hernandez, N., Melki, I., Jing, H., Habib, T., Huang, S. S. Y., Danielson, J. J., Kula, T., Drutman, S. B., Belkaya, S., Rattina, V., et al. (2018) · The Journal of Experimental Medicine · doi:10.1084/jem.20180628 · Cited by 215
“IRF9 also enables binding of the trimer to DNA, after its translocation to the nucleus (Veals et al., 1993; Darnell et al., 1994; Taniguchi et al., 2001; Stark and Darnell, 2012).”
BackgroundDo, D. V., Ueda, J., Messerschmidt, D. M., Lorthongpanich, C., Zhou, Y., Feng, B., Guo, G., Lin, P. J., Hossain, M. Z., Zhang, W., et al. (2013) · Genes & Development · doi:10.1101/gad.221176.113 · Cited by 184
“…recruitment of the Src homology-2 (SH2) domain and phosphorylation on Tyr705 residues of signal transducers and activators of transcription (STAT), a gene family originally described in the interferon-induced regulatory pathways (Fu et al. 1990, 1992; Schindler et al. 1992; Darnell et al. 1994).”
BackgroundBDNF Selectively Regulates GABA A Receptor Transcription by Activation of the JAK/STAT Pathway
Lund, I. V., Hu, Y., Raol, Y. H., Benham, R. S., Faris, R., Russek, S. J., & Brooks‐Kayal, A. R. (2008) · Science Signaling · doi:10.1126/scisignal.1162396 · Cited by 181
Interplay between interferon and other cytokine systems in bone metabolism
Takayanagi, H., Sato, K., Takaoka, A., & Taniguchi, T. (2005) · Immunological Reviews · doi:10.1111/j.0105-2896.2005.00337.x · Cited by 192
Understanding the therapeutic toolkit for inflammatory bowel disease
Vieujean, S., Jairath, V., Peyrin‐Biroulet, L., Dubinsky, M. C., Iacucci, M., Magro, F., & Danese, S. (2025) · Nature Reviews Gastroenterology & Hepatology · doi:10.1038/s41575-024-01035-7 · Cited by 210
“JAK, including JAK1, JAK2, JAK3 and TYK2, are enzymes linked to the intracellular domains of cytokine receptors 169 .”
Differential Regulation of Type I and Type III Interferon Signaling
Stanifer, M. L., Pervolaraki, K., & Boulant, S. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20061445 · Cited by 214
“Beside the canonical ISGF3 transcriptional complex made of STAT1:STAT2 heterodimer and of IRF9, almost all combination of STAT homo- and heterodimers can be found: STAT1:STAT1, STAT3:STAT3, STAT4:STAT4, STAT5:STAT5, STAT6:STAT6, STAT1:STAT2, STAT1:STAT3, STAT1:STAT4, STAT1:STAT5, STAT2:STAT3 STAT5:STAT6 [12,30,92,100,…”
BackgroundPatel, M. C., Debrosse, M., Smith, M. D., Dey, A., Huynh, W., Sarai, N., Heightman, T. D., Tamura, T., & Ozato, K. (2013) · Molecular and Cellular Biology · doi:10.1128/mcb.01180-12 · Cited by 182
“Given that a wide range of genes are stimulated by JAK/STAT pathways in addition to ISGs, regulating cell growth, development, and responses to various external signals, it is reasonable to assume that the pattern of NELF/DSIF occupancy revealed in this study may represent a fairly common feature (30, 31, 33, 51).”
BackgroundTerenzi, F., Hui, D. J., Merrick, W. C., & Sen, G. C. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m605771200 · Cited by 177
Gleave, M. E., & Monia, B. P. (2005) · Nature reviews. Cancer · doi:10.1038/nrc1631 · Cited by 384
“Following specific receptor stimulation and dimerization, activation of the Janus tyrosine kinases or SRC family members results in the phosphorylation and activation of STAT family member”
BackgroundThe complex STATes of astrocyte reactivity: How are they controlled by the JAK-STAT3 pathway?
Ceyzériat, K., Abjean, L., Carrillo-de Sauvage, M.-A., Ben Haim, L., & Escartin, C. (2016) · Neuroscience · doi:10.1016/j.neuroscience.2016.05.043 · Cited by 185
Review: ICSBP/IRF-8: Its Regulatory Roles in the Development of Myeloid Cells
Tamura, T., & Ozato, K. (2002) · Journal of Interferon & Cytokine Research · doi:10.1089/107999002753452755 · Cited by 183
Angelini, J., Talotta, R., Roncato, R., Fornasier, G., Barbiero, G., Cin, L. D., Brancati, S. B., & Scaglione, F. (2020) · Biomolecules · doi:10.3390/biom10071002 · Cited by 224
“IFN-α/β Type II JAK1 TYK2 STAT1 STAT2 STAT4 STAT3 naïve T lymphocytes, Th1 lymphocytes alopecia, rheumatoid arthritis, atopic dermatitis, systemic lupus erythematosus, ulcerative colitis, Crohn’s disease, ankylosing spondylitis [11,38,39,59,60]”
BackgroundPharmacology and therapeutic potential of interferons
George, P. M., Badiger, R., Alazawi, W., Foster, G. R., & Mitchell, J. A. (2012) · Pharmacology & Therapeutics · doi:10.1016/j.pharmthera.2012.03.006 · Cited by 182
Song, G., Liu, B., Li, Z., Wu, H. M., Wang, P., Zhao, K., Jiang, G., Zhang, L., & Gao, C. (2016) · Nature Immunology · doi:10.1038/ni.3588 · Cited by 201
Sinnreich, M. F., Wang, X., Yan, M., Duong, F. H. T., Poli, V., Hilton, D. J., Zhang, D., & Heim, M. H. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.00224-09 · Cited by 177
IFN-λ: Novel Antiviral Cytokines
Ank, N., West, H., & Paludan, S. R. (2006) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2006.26.373 · Cited by 193
“36 To some extent, the use of Stats explains the activities of a given cytokine.”
Kusaba, T., Nakayama, T., Yamazumi, K., Yakata, Y., Yoshizaki, A., Nagayasu, T., & Sekine, I. (2005) · Journal of Clinical Pathology · doi:10.1136/jcp.2004.023416 · Cited by 169
Roy, A., Srivastava, M., Saqib, U., Liu, D., Faisal, S. M., Sugathan, S., Bishnoi, S., & Baig, M. S. (2016) · International Immunopharmacology · doi:10.1016/j.intimp.2016.08.026 · Cited by 196
Yang, C. H., Yue, J., Fan, M., & Pfeffer, L. M. (2010) · Cancer Research · doi:10.1158/0008-5472.can-10-2579 · Cited by 179
Shimozaki, K., Nakajima, K., Hirano, T., & Nagata, S. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.40.25184 · Cited by 169
Berry, D. C., Jin, H., Majumdar, A., & Noy, N. (2011) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1011115108 · Cited by 204
Ramaswamy, M., Shi, L., Varga, S. M., Barik, S., Behlke, M. A., & Look, D. C. (2005) · Virology · doi:10.1016/j.virol.2005.09.009 · Cited by 165
Herbeuval, J., Hardy, A. W., Boasso, A., Anderson, S. A., Dolan, M. J., Dy, M., & Shearer, G. M. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0505251102 · Cited by 164
Jeon, Y. J., Yoo, H. M., & Chung, C. H. (2010) · Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease · doi:10.1016/j.bbadis.2010.02.006 · Cited by 175
“activator of transcription (STAT) signaling pathway [3].”
IL‐23‐mediated regulation of IL‐17 production in Helicobacter pylori‐infected gastric mucosa
Caruso, R., Fina, D., Paoluzi, O. A., Blanco, G. D. V., Stolfi, C., Rizzo, A., Caprioli, F., Sarra, M., Andrei, F., Fantini, M. C., et al. (2008) · European Journal of Immunology · doi:10.1002/eji.200737635 · Cited by 164
Galectin-3 Exerts Cytokine-Like Regulatory Actions through the JAK–STAT Pathway
Jeon, S., Yoon, H. J., Chang, C. Y., Koh, H. S., Jeon, S.-H., & Park, E. J. (2010) · The Journal of Immunology · doi:10.4049/jimmunol.1000154 · Cited by 176
“Because IFN-g receptor 1 (IFNGR1) has been shown to be responsible for ligand binding and activation of the JAK–STAT pathway (36), we questioned whether IFNGR1 could be associated with galectin-3–triggered phosphorylation of the JAK2-STAT cascade.”
BackgroundThe Role of JAK/STAT Pathway in Fibrotic Diseases: Molecular and Cellular Mechanisms
Liu, J., Wang, F., & Luo, F. (2023) · Biomolecules · doi:10.3390/biom13010119 · Cited by 188
“The JAK/signal transducer and activator of transcription (STAT) signaling pathway is a cascade of responses critical for the signal transduction of multiple cytokines and growth factors in vivo [6,7].”
BackgroundStat3 activation in human endometrial and cervical cancers
Chen, C.-L., Hsieh, F.-C., Lieblein, J., Brown, J., Chan, C., Wallace, J. A., Cheng, G., Hall, B. M., & Lin, J. (2007) · British Journal of Cancer · doi:10.1038/sj.bjc.6603597 · Cited by 171
“…www.bjcancer.com & 2007 Cancer Research UK Keywords: Stat3; endometrial cancer; cervical cancer; tissue microarray Signal transducer and activator of transcription signaling pathways are activated in response to cytokines and growth factors (Darnell et al, 1994; Zhong et al, 1994).”
BackgroundAlff, P. J., Gavrilovskaya, I. N., Gorbunova, E. E., Endriss, K., Chong, Y., Geimonen, E., Sen, N., Reich, N. C., & Mackow, E. R. (2006) · Journal of Virology · doi:10.1128/jvi.00508-06 · Cited by 152
“In response to IFN, IFN receptors activate JAK/STAT signaling pathways and direct transcription of interferon-stimulated genes (ISGs), which amplify the IFN response and disrupt viral transcription and translation (8, 9, 54).”
BackgroundGong, Y., Ishida-Takahashi, R., Villanueva, E. C., Fingar, D. C., Münzberg, H., & Myers, M. G. (2007) · Journal of Biological Chemistry · doi:10.1074/jbc.m702838200 · Cited by 173
Activation of p38 MAPK in CD4 T cells controls IL-17 production and autoimmune encephalomyelitis
Noubade, R., Krementsov, D. N., del Río, R., Thornton, T. M., Nagaleekar, V. K., Saligrama, N., Spitzack, A., Spach, K. M., Sabio, G., Davis, R. J., et al. (2011) · Blood · doi:10.1182/blood-2011-02-336552 · Cited by 167
Patel, D., Nan, Y., Shen, M., Ritthipichai, K., Zhu, X., & Zhang, Y. (2010) · Journal of Virology · doi:10.1128/jvi.00655-10 · Cited by 163
“Overexpression of NSP1 of PRRSV VR2385 inhibited expression of ISG15 and ISG56 and blocked nuclear translocation of STAT1, which suggests that NSP1 might be the viral protein responsible for the inhibition of IFN signaling.”
BackgroundInfluentialA Genomic Approach to Human Autoimmune Diseases
Pascual, V., Chaussabel, D., & Banchereau, J. (2010) · Annual Review of Immunology · doi:10.1146/annurev-immunol-030409-101221 · Cited by 152
“All nucleated cells express the type I IFN receptor (IFNAR) and respond to type I IFN with phosphorylation of STAT1 and STAT2, which ultimately leads to the transcription of interferon-responsive genes (83).”
BackgroundOlias, P., Etheridge, R. D., Zhang, Y., Holtzman, M. J., & Sibley, L. D. (2016) · Cell Host & Microbe · doi:10.1016/j.chom.2016.06.006 · Cited by 187
“…trafficking, and binding to a conserved motif known as the gamma-activated sequence (GAS), resulting in the transcription of many genes, including those important for immunity (Darnell et al., 1994; 72 Cell Host & Microbe 20, 72–82, July 13, 2016 ª 2016 Elsevier Inc. Schindler and Darnell, 1995).”
Kim, Y., Kim, H., Bae, S., Choi, J., Lim, S., Lee, N., Kong, J. M., Hwang, Y.-I., Kang, J. S., & Lee, W. J. (2013) · Immune Network · doi:10.4110/in.2013.13.2.70 · Cited by 186
“The phosphorylation of signal transducers and activators of transcription (STATs) is the critical signaling process after the dimerization of its receptors, when type I IFNs are increased (17,18).”
STAT proteins – Key regulators of anti-viral responses, inflammation, and tumorigenesis in the liver
Gao, B., Wang, H., Lafdil, F., & Feng, D. (2012) · Journal of Hepatology · doi:10.1016/j.jhep.2012.01.029 · Cited by 180
“The JAK–STAT pathway was identified in the early 1990s as a key signaling cascade mediating cytokine receptor-derived signals in mammals [1,2].”
BackgroundRegulation of JAK2 by miR-135a: prognostic impact in classic Hodgkin lymphoma
Navarro, A., Díaz, T., Martı́nez, A., Gayà, A., Pons, A., Gel, B., Codony, C., Ferrer, G., Martı́nez, C., Montserrat, E., et al. (2009) · Blood · doi:10.1182/blood-2009-02-204842 · Cited by 171
MyD88-mediated stabilization of interferon-γ-induced cytokine and chemokine mRNA
Sun, D., & Ding, A. H. (2006) · Nature Immunology · doi:10.1038/ni1308 · Cited by 210
“These inflammatory mediators are also induced by IFN-γ, which uses a signaling pathway involving Janus kinases and signal transducers and activators of transcription (STATs”
Melatonin in macrophage biology: Current understanding and future perspectives
Xia, Y., Chen, S., Zeng, S., Zhao, Y., Zhu, C., Deng, B., Zhu, G., Yin, Y., Wang, W., Hardeland, R., et al. (2018) · Journal of Pineal Research · doi:10.1111/jpi.12547 · Cited by 191
MicroRNA miR-21 Regulates the Metastatic Behavior of B16 Melanoma Cells
Yang, C. H., Yue, J., Pfeffer, S. R., Handorf, C. R., & Pfeffer, L. M. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.285098 · Cited by 186
JAK1 and Tyk2 Activation by the Homologous Polycythemia Vera JAK2 V617F Mutation
Staerk, J., Kallin, A., Demoulin, J., Vainchenker, W., & Constantinescu, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.c500358200 · Cited by 169
STAT3 and apoptosis challenges in cancer
Fathi, N., Rashidi, G., Khodadadi, A., Shahi, S., & Sharifi, S. (2018) · International Journal of Biological Macromolecules · doi:10.1016/j.ijbiomac.2018.05.121 · Cited by 191
Mechanisms of Fish Macrophage Antimicrobial Immunity
Grayfer, L., Kerimoğlu, B., Yaparla, A., Hodgkinson, J. W., Xie, J., & Belosevic, M. (2018) · Frontiers in Immunology · doi:10.3389/fimmu.2018.01105 · Cited by 191
“The assembly of this signaling complex (IFNγ:IFNGR1:IFNGR2) activates Janus kinases (Jak)-1 and -2 (124), upon which phosphorylation activates signal transducer of activation-1 (Stat1) transcription factor (125).”
BackgroundCancer Prevention with Promising Natural Products: Mechanisms of Action and Molecular Targets
Pratheeshkumar, P., Sreekala, C., Zhang, Z., Budhraja, A., Ding, S., Son, Y., Wang, X., Hitron, J. A., Hyun-Jung, K., Wang, L., et al. (2012) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/187152012803833035 · Cited by 180
Signal transducer and activator of transcription (STAT) signalling and T‐cell lymphomas
Mitchell, T. J., & John, S. (2005) · Immunology · doi:10.1111/j.1365-2567.2005.02091.x · Cited by 172
PD-L1/PD-1 Axis in Glioblastoma Multiforme
Litak, J., Mazurek, M., Grochowski, C., Kamieniak, P., & Roliński, J. (2019) · International Journal of Molecular Sciences · doi:10.3390/ijms20215347 · Cited by 187
Hepatitis C virus expression suppresses interferon signaling by degrading STAT1.
Lin, W., Choe, W., Hiasa, Y., Kamegaya, Y., Blackard, J., Schmidt, E., & Chung, R. (2005) · Gastroenterology · doi:10.1053/j.gastro.2005.02.006 · Cited by 165
STAT1 and Its Crucial Role in the Control of Viral Infections
Tolomeo, M., Cavalli, A., & Cascio, A. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23084095 · Cited by 187
Importance of Type I and III Interferons at Respiratory and Intestinal Barrier Surfaces
Stanifer, M. L., Guo, C., Doldan, P., & Boulant, S. (2020) · Frontiers in Immunology · doi:10.3389/fimmu.2020.608645 · Cited by 195
“Following type I IFN binding, STAT1–6 have all been shown to participate in the antiviral and anti-proliferative actions of these IFNs (65, 66).”
BackgroundRani, A., & Murphy, J. J. (2015) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2015.0054 · Cited by 179
“The first STATs to be cloned by Darnell and co-workers were the IFN-inducible 91-kDa STAT1and the 113-kDa STAT2 proteins [3, 7].”
Sharf, R., Meraro, D., Azriel, A., Thornton, A. M., Ozato, K., Petricoin, E. F., Larner, A. C., Schaper, F., Hauser, H., & Levi, B.-Z. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.15.9785 · Cited by 162
Giese, N. A., Gabriele, L., Doherty, T. M., Klinman, D. M., Tadesse-Heath, L., Contursi, C., Epstein, S. L., & Morse, H. C. (1997) · The Journal of Experimental Medicine · doi:10.1084/jem.186.9.1535 · Cited by 160
Domenico, I. D., Lo, E., Ward, D. M., & Kaplan, J. (2009) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0900453106 · Cited by 143
Mining for JAK–STAT mutations in cancer
Constantinescu, S. N., Girardot, M., & Pecquet, C. (2008) · Trends in Biochemical Sciences · doi:10.1016/j.tibs.2007.12.002 · Cited by 153
Metadata
- 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
- Published
- 1994-06-03
- Volume
- 264
- Issue
- 5164
- Pages
- 1415-1421
- ISSN
- 0036-8075 (ISSN-L)
- 1095-9203
- 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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