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Cytokine‐inducible SH2 protein‐3 (CIS3/SOCS3) inhibits Janus tyrosine kinase by binding through the N‐terminal kinase inhibitory region as well as SH2 domain
Open accessAbstract
Background: The Janus family of protein tyrosine kinases (JAKs) regulate cellular processes involved in cell growth, differentiation and transformation through their association with cytokine receptors. We have recently identified the JAK‐binding protein, JAB that inhibits various cytokine‐dependent JAK signalling pathways. JAB inhibits JAK2 tyrosine kinase activity by binding to the kinase domain (JH1 domain) through the N‐terminal kinase inhibitory region (KIR) and the SH2 domain. The SH2 domain of JAB has been shown to bind to the phosphorylated Y1007 in the activation loop of JH1. We also identified another JAK‐binding protein, CIS3 (cytokine‐inducible SH2‐protein 3, or SOCS3) that inhibits signalling of various cytokines. However, the mechanism of JAK signal inhibition by CIS3 has not been clarified. Results: We showed that endogenous CIS3 bound to JAK2 in intact cells. The CIS3‐SH2 domain bound to the phosphorylated Y1007 of JH1, and inhibited tyrosine kinase activity through the N‐terminal KIR. Therefore, CIS3 and JAB inhibit JAK2 tyrosine kinase activity by an essentially similar mechanism. However, we found that the affinity of the SH2 domain of CIS3 to Y1007 was weaker than that of JAB. In contrast, the KIR of CIS3 showed stronger potential for both binding to JH1 and inhibition of JAK kinase activity than that of JAB. Consistent with this notion, chimeras containing CIS3‐KIR and JAB‐SH2 domain inhibited JAK2 kinase activity more efficiently than the wild‐type CIS3 or JAB. Conclusion: CIS3 inhibits JAK2 kinase activity by binding to the activation loop through the SH2 domain, and KIR is necessary for kinase inhibition. Although the inhibitory mechanism by CIS3 is similar to that by JAB, the contributions of the SH2 domain and KIR for binding are different between JAB and CIS3. Our study defined the inhibitory mechanism of CIS3 and provides a useful information for creating a novel tyrosine kinase inhibitor.
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“The suppressor of cytokine signaling (SOCS) family of proteins, especially SOCS1 and SOCS3, inhibit STAT3 in a cytokine-inducible manner by binding to and inhibiting upstream JAKs.13,14”
From Critical analysis of the potential for targeting STAT3 in human malignancy (2013) · cites this paper as [13]
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Cites
Darnell, J. E. (1997) · Science · doi:10.1126/science.277.5332.1630 · Cited by 3,979
A family of cytokine-inducible inhibitors of signalling
Starr, R., Willson, T. A., Viney, E. M., Murray, L. J. L., Rayner, J. R., Jenkins, B. J., Gonda, T. J., Alexander, W. S., Metcalf, D., Nicola, N. A., et al. (1997) · Nature · doi:10.1038/43206 · Cited by 2,066
A new protein containing an SH2 domain that inhibits JAK kinases
Endo, T. A., Masuhara, M., Yokouchi, M., Suzuki, R., Sakamoto, H., Mitsui, K., Matsumoto, A., Tanimura, S., Ohtsubo, M., Misawa, H., et al. (1997) · Nature · doi:10.1038/43213 · Cited by 1,408
Self-citationSTATs: Signal Transducers and Activators of Transcription
Ihle, J. N. (1996) · Cell · doi:10.1016/s0092-8674(00)81277-5 · Cited by 1,381
Ihle, J. N. (1995) · Nature · doi:10.1038/377591a0 · Cited by 1,201
Structure and function of a new STAT-induced STAT inhibitor
Naka, T., Narazaki, M., Hirata, M., Matsumoto, T., Minamoto, S., Aono, A., Nishimoto, N., Kajita, T., Taga, T., Yoshizaki, K., et al. (1997) · Nature · doi:10.1038/43219 · Cited by 1,040
Identification of SOCS-3 as a Potential Mediator of Central Leptin Resistance
Bjørbæk, C., Elmquist, J. K., Frantz, J. D., Shoelson, S. E., & Flier, J. S. (1998) · Molecular Cell · doi:10.1016/s1097-2765(00)80062-3 · Cited by 1,014
Yoshimura, A., Ohkubo, T., Kiguchi, T., Jenkins, N. A., Gilbert, D. J., Copeland, N. G., Hara, T., & Miyajima, A. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07281.x · Cited by 751
Self-citationCrystal Structure of a Tyrosine Phosphorylated STAT-1 Dimer Bound to DNA
Chen, X., Vinkemeier, U., Zhao, Y., Jeruzalmi, D., Darnell, J. E., Jr., & Kuriyan, J. (1998) · Cell · doi:10.1016/s0092-8674(00)81443-9 · Cited by 734
Twenty proteins containing a C-terminal SOCS box form five structural classes
Hilton, D. J., Richardson, R. T., Alexander, W. S., Viney, E. M., Willson, T. A., Sprigg, N. S., Starr, R., Nicholson, S. E., Metcalf, D., & Nicola, N. A. (1998) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.95.1.114 · Cited by 728
Cited by
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Items 201–300 of 400
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Cho‐Vega, J. H., Rassidakis, G. Z., Amin, H. M., Tsioli, P., Spurgers, K. B., Remache, Y. K., Vega, F., Goy, A. H., Gilles, F., & Medeiros, L. J. (2004) · Leukemia · doi:10.1038/sj.leu.2403495 · Cited by 33
Porphyromonas gingivalisand digestive system cancers
Zhou, Y., & Luo, G. (2019) · World Journal of Clinical Cases · doi:10.12998/wjcc.v7.i7.819 · Cited by 34
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Alston, C. I., & Dix, R. D. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00732 · Cited by 34
Woldman, I., Varinou, L., Ramsauer, K., Rapp, B., & Decker, T. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m105320200 · Cited by 37
Varghese, L. N., Ungureanu, D., Liau, N. P. D., Young, S. N., Laktyushin, A., Hammarén, H. M., Lucet, I. S., Nicola, N. A., Silvennoinen, O., Babon, J. J., et al. (2013) · Biochemical Journal · doi:10.1042/bj20131516 · Cited by 33
Preventive Role of Resveratrol Against Inflammatory Cytokines and Related Diseases
Rafe, T., Shawon, P. A., Salem, L., Chowdhury, N. I., Kabir, F., Zahur, S. M. B., Akhter, R., Noor, H. B., Mohib, M. M., & Sagor, M. A. T. (2019) · Current Pharmaceutical Design · doi:10.2174/1381612825666190410153307 · Cited by 33
Bruel, T., Guibon, R., Melo, S., Guillén, N., Salmon, H., Girard‐Misguich, F., & Meurens, F. (2010) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2009.12.017 · Cited by 36
Identification of a Novel, Small Molecule Partial Agonist for the Cyclic AMP Sensor, EPAC1
Parnell, E., McElroy, S. P., Wiejak, J., Baillie, G. L., Porter, A., Adams, D. R., Rehmann, H., Smith, B. O., & Yarwood, S. J. (2017) · Scientific Reports · doi:10.1038/s41598-017-00455-7 · Cited by 32
Gene methylation and silencing of SOCS 3 in mantle cell lymphoma
Molavi, O., Wang, P., Zak, Z., Gélébart, P., Belch, A. R., & Lai, R. L. (2013) · British Journal of Haematology · doi:10.1111/bjh.12262 · Cited by 34
Zeng, B., Li, H., Liu, Y., Zhang, Z., Zhang, Y., & Yang, R. (2008) · Cancer Research · doi:10.1158/0008-5472.can-07-6792 · Cited by 32
Heeg, K. M., & Dalpke, A. H. (2003) · Vaccine · doi:10.1016/s0264-410x(03)00202-0 · Cited by 32
Suppressor of Cytokine Signaling 3 Inhibits Breast Tumor Kinase Activation of STAT3
Gao, Y., Cimica, V., & Reich, N. C. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.334144 · Cited by 33
Sakamoto, H., Kinjyo, I., & Yoshimura, A. (2000) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428190009060318 · Cited by 31
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Touw, I. P., Palande, K. K., & Beekman, R. (2012) · Hematology/Oncology Clinics of North America · doi:10.1016/j.hoc.2012.10.002 · Cited by 32
Thanasaksiri, K., Hırono, I., & Kondo, H. (2016) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2016.09.018 · Cited by 31
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Dunbar, A. J., Bowman, R. L., Park, Y. C., O’Connor, K., Izzo, F., Myers, R. M., Karzai, A., Zaroogian, Z., Kim, W. J., Fernández-Maestre, I., et al. (2024) · Cancer Discovery · doi:10.1158/2159-8290.cd-22-0952 · Cited by 34
Fletcher, T. C., DiGiandomenico, A., & Hawiger, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.095216 · Cited by 33
A systems approach to understanding human rhinovirus and influenza virus infection
Kim, T., Bheda-Malge, A., Lin, Y., Sreekrishna, K., Adams, R. L., Robinson, M. K., Bascom, C. C., Tiesman, J. P., Isfort, R. J., & Gelinas, R. E. (2015) · Virology · doi:10.1016/j.virol.2015.08.014 · Cited by 34
Proteomic applications of protein quantification by isotope-dilution mass spectrometry
Mayya, V., & Han, D. K. M. (2006) · Expert Review of Proteomics · doi:10.1586/14789450.3.6.597 · Cited by 31
Reddy, P. N. G., Sargin, B., Choudhary, C., Stein, S., Grez, M., Müller‐Tidow, C., Berdel, W. E., Serve, H. L., & Brandts, C. (2012) · Blood · doi:10.1182/blood-2010-08-301416 · Cited by 31
Sobota, R. M., Müller, P. J., Heinrich, P. C., & Schaper, F. (2008) · Biochemical Journal · doi:10.1042/bj20071572 · Cited by 29
Mechanism of attenuation of leptin signaling under chronic ligand stimulation
Knobelspies, H., Zeidler, J., Hekerman, P., Bamberg‐Lemper, S., & Becker, W. B. (2010) · BMC Biochemistry · doi:10.1186/1471-2091-11-2 · Cited by 31
Yasukawa, H., Nagata, T., Oba, T., & Imaizumi, T. (2012) · JAK-STAT · doi:10.4161/jkst.22435 · Cited by 30
Self-citationPrediction and Experimental Validation of Novel STAT3 Target Genes in Human Cancer Cells
Oh, Y. M., Kim, J. K., Choi, Y., Choi, S., & Yoo, J.-Y. (2009) · PLoS ONE · doi:10.1371/journal.pone.0006911 · Cited by 28
LINC00893 inhibits the progression of prostate cancer through miR-3173-5p/SOCS3/JAK2/STAT3 pathway
Yu, C., Fan, Y., Zhang, Y., Liu, L., & Guo, G. (2022) · Cancer Cell International · doi:10.1186/s12935-022-02637-4 · Cited by 28
Suppressors of cytokine signaling (SOCS) and type 2 diabetes
Feng, X., Tang, H., Leng, J., & Jiang, Q. (2014) · Molecular Biology Reports · doi:10.1007/s11033-014-3079-8 · Cited by 28
Ungureanu, D., & Silvennoinen, O. (2005) · Science s STKE · doi:10.1126/stke.3042005pe49 · Cited by 28
Boyle, K., & Robb, L. G. (2007) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2007.02.003 · Cited by 28
Starr, R., Fuchsberger, M., Lau, L. S., Uldrich, A. P., Goradia, A., Willson, T. A., Verhagen, A. M., Alexander, W. S., & Smyth, M. J. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0901010 · Cited by 28
Duan, W., Xia, Z., Liu, M., Sun, Q., Lei, S., Wu, X., Meng, Q., & Leng, Y. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6941 · Cited by 28
Mansfield, K. L., Johnson, N., Cosby, S. L., Solomon, T., & Fooks, A. R. (2010) · Vector-Borne and Zoonotic Diseases · doi:10.1089/vbz.2009.0259 · Cited by 28
Metlakunta, A. S., Sahu, M., Yasukawa, H., Dhillon, S. S., Belsham, D. D., Yoshimura, A., & Sahu, A. (2011) · American Journal of Physiology-Regulatory, Integrative and Comparative Physiology · doi:10.1152/ajpregu.00794.2010 · Cited by 27
Self-citationNaudin, C., Chevalier, C., & Roche, S. (2016) · Oncotarget · doi:10.18632/oncotarget.6929 · Cited by 33
Wiejak, J., van Basten, B., Luchowska-Stańska, U., Hamilton, G. M., & Yarwood, S. J. (2018) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2018.11.004 · Cited by 25
Discovery of an exosite on the SOCS2-SH2 domain that enhances SH2 binding to phosphorylated ligands
Linossi, E. M., Li, K., Veggiani, G., Tan, C., Dehkhoda, F., Hockings, C., Calleja, D. J., Keating, N., Feltham, R., Brooks, A. J., et al. (2021) · Nature Communications · doi:10.1038/s41467-021-26983-5 · Cited by 26
Interferon Independent Non-Canonical STAT Activation and Virus Induced Inflammation
Nan, Y., Wu, C., & Zhang, Y. (2018) · Viruses · doi:10.3390/v10040196 · Cited by 26
Critical analysis of the potential for targeting STAT3 in human malignancy
Grandis, J., & Peyser (2013) · OncoTargets and Therapy · doi:10.2147/ott.s47903 · Cited by 24
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Qi, Y.-F., Huang, Y., Wang, H., Zhang, Y., Bao, Y., Sun, L., Wu, Y., Yu, C., Song, Z., Zheng, L., et al. (2013) · BMC Bioinformatics · doi:10.1186/1471-2105-14-41 · Cited by 27
Zhou, Q., Jiang, X., Wang, Z., Li, C., & Cui, Y. (2015) · Medical Oncology · doi:10.1007/s12032-015-0553-7 · Cited by 24
Guo, C.-J., Yang, L., Zhang, Y.-F., Wu, Y., Weng, S., Yu, X., & He, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041092 · Cited by 24
Heat Stress and Immune Function
Aggarwal, A., & Upadhyay, R. C. (2012) · Springer eBooks · doi:10.1007/978-81-322-0879-2_5 · Cited by 25
Stat3 Regulates Liver Progenitor Cell-Driven Liver Regeneration in Zebrafish
Khaliq, M., Ko, S., Liu, Y., Wang, H., Sun, Y., Solnica‐Krezel, L., & Shin, D. (2018) · Gene Expression · doi:10.3727/105221618x15242506133273 · Cited by 25
Wang, X., Jia, Y., Ren, J., Liu, H., Xiao, S., Wang, X., & Yang, Z. (2019) · Veterinary Microbiology · doi:10.1016/j.vetmic.2019.108460 · Cited by 24
Zhang, W., Wang, L., Wang, Q., Luo, X. G., Fang, D., Chen, Y., Pan, X., Man, J., Xia, Q., Jin, B., et al. (2011) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.276832 · Cited by 23
Suessmuth, Y., Elliott, J., Percy, M. J., Inami, M., Attal, H., Harrison, C. N., Inokuchi, K., McMullin, M., & Johnston, J. A. (2009) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.07860.x · Cited by 23
Self-citationSOCS‐3 antagonizes pro‐apoptotic effects of TRAIL and resveratrol in prostate cancer cells
Horndasch, M., & Čulig, Z. (2011) · The Prostate · doi:10.1002/pros.21353 · Cited by 23
Assmann, J. L. J. C., León, L. G., Stavast, C. J., van den Bogaerdt, S. E., Schilperoord‐Vermeulen, J., Sandberg, Y., Bellido, M., Erkeland, S. J., Feith, D. J., Loughran, T. P., et al. (2021) · Leukemia · doi:10.1038/s41375-021-01480-2 · Cited by 22
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Liu, Q., Liu, S., Shi, Y., Li, H., Hao, J., Xing, L., Cao, Y., & Duan, H. (2011) · American Journal of Nephrology · doi:10.1159/000329325 · Cited by 22
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Gao, A., & Dyke, T. E. V. (2014) · Frontiers in Immunology · doi:10.3389/fimmu.2013.00506 · Cited by 22
Wiejak, J., Dunlop, J., Gao, S., Borland, G., & Yarwood, S. J. (2012) · Molecular Pharmacology · doi:10.1124/mol.111.076976 · Cited by 22
Coope, A., Pascoal, L. B., da Silva, F. A. R., Botezelli, J. D., Ayrizono, M. D. L. S., Milanski, M., Camargo, M. G., Planell, N., Portovedo, M., Dias, C. B., et al. (2017) · International Journal of Inflammation · doi:10.1155/2017/7646859 · Cited by 22
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Bodur, Ç., Duensing, A. M., & Myers, M. G. (2025) · Genes & Development · doi:10.1101/gad.352550.124 · Cited by 24
Haan, C., Kroy, D. C., Wüller, S., Sommer, U., Nöcker, T., Rolvering, C., Behrmann, I., Heinrich, P. C., & Haan, S. (2009) · The Journal of Immunology · doi:10.4049/jimmunol.0800572 · Cited by 21
Ding, F., Liao, R., Chen, Y., Xie, G., Zhang, P., Shao, P. H., & Zhang, M. (2017) · Molecular Medicine Reports · doi:10.3892/mmr.2017.6630 · Cited by 23
The SOCS1 KIR and SH2 domain are both required for suppression of cytokine signaling in vivo
Doggett, K., Keating, N., Dehkhoda, F., Bidgood, G. M., Guzman, L. G. M., Leong, E., Kueh, A. J., Nicola, N. A., Kershaw, N. J., Babon, J. J., et al. (2023) · Cytokine · doi:10.1016/j.cyto.2023.156167 · Cited by 21
Kong, X., Sun, H., Pan, P., Li, D., Zhu, F., Chang, S., Xu, L., Li, Y., & Hou, T. (2017) · Scientific Reports · doi:10.1038/s41598-017-09586-3 · Cited by 21
Luan, X., Yang, W., Bai, X., Li, H., Li, H., Fan, W., Zhang, H., Liu, W., & Sun, L. (2021) · The FASEB Journal · doi:10.1096/fj.202101044rrr · Cited by 20
Chen, Y., Zhong, W., Xie, Z., Li, B., Li, H., Gao, K., & Ning, Z. (2022) · Virus Research · doi:10.1016/j.virusres.2022.198748 · Cited by 20
Hu, J. S., Lin, F., Yin, Y., Shang, Y., Xiao, Z., & Xu, W. (2023) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2023.106278 · Cited by 21
Kong, J., Liu, Y., Qian, M., Xing, L., & Gao, S. (2023) · Epidemiology and Infection · doi:10.1017/s0950268823000298 · Cited by 20
Molecular Signatures of Human Regulatory T Cells in Colorectal Cancer and Polyps
Johdi, N. A., Ait‐Tahar, K., Sagap, I., & Jamal, R. (2017) · Frontiers in Immunology · doi:10.3389/fimmu.2017.00620 · Cited by 21
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Barker, G., Parnell, E., van Basten, B., Buist, H., Adams, D., & Yarwood, S. J. (2017) · Journal of Cardiovascular Development and Disease · doi:10.3390/jcdd4040022 · Cited by 20
Ji, K., Yang, M., Jou, I., Shong, M., & Joe, E.-H. (2004) · Glia · doi:10.1002/glia.20059 · Cited by 20
Yu, F. (2011) · Oncology Reports · doi:10.3892/or.2011.1144 · Cited by 19
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da Silva, C. G., Revuelta‐Cervantes, J., Studer, P., & Ferran, C. J. (2014) · Advances in experimental medicine and biology · doi:10.1007/978-1-4939-0398-6_8 · Cited by 20
Clahsen, T., Lehmann, U., Stross, C., Hermanns, H., Volkmer‐Engert, R., Schneider-Mergener, J., Heinrich, P., & Schaper, F. (2005) · Cellular Signalling · doi:10.1016/j.cellsig.2004.09.016 · Cited by 20
Tsai, C.-H., Lee, Y., Li, C.-H., Cheng, Y., & Kang, J. (2019) · Cell Biology and Toxicology · doi:10.1007/s10565-019-09499-z · Cited by 18
The role of suppressors of cytokine signalling in thymopoiesis and T cell activation
Fletcher, J. G., & Starr, R. (2005) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2005.04.005 · Cited by 19
SOCS Proteins: Modulators of Neuroimmunoendocrine Functions: Impact on Corticotroph LIF Signaling
Auernhammer, C. J., Bousquet, C., Chesnokova, V., & Melmed, S. K. (2000) · Annals of the New York Academy of Sciences · doi:10.1111/j.1749-6632.2000.tb05431.x · Cited by 19
Yoshimura, A., Aki, D., & Ito, M. (2021) · Proceedings of the Japan Academy Series B · doi:10.2183/pjab.97.016 · Cited by 19
Self-citationPeriodontitis and progression of gastrointestinal cancer: current knowledge and future perspective
Nasiri, K., Moghaddam, M. A., Etajuri, E. A., Badkoobeh, A., Tavakol, O., Rafinejad, M., Mirhosseini, A. F., & Fathi, A. (2023) · Clinical & Translational Oncology · doi:10.1007/s12094-023-03162-0 · Cited by 19
Regulation of Macrophage Polarization by the STAT–SOCS Signaling Axis
Nicholson, S. E., & Murray, P. J. (2014) · Springer eBooks · doi:10.1007/978-1-4939-1311-4_24 · Cited by 17
Karki, P., Ke, Y., Zhang, C.-O., Li, Y., Tian, Y., Son, S., Yoshimura, A., Kaibuchi, K., Birukov, K. G., & Birukova, A. A. (2020) · Journal of Biological Chemistry · doi:10.1074/jbc.ra120.014232 · Cited by 18
Self-citationXiang, S., Liu, J., Dong, N., Shi, J., Xiao, Y.-Q., Wang, Y., Hu, X., Gong, L., & Wang, W. (2014) · Journal of Vascular Research · doi:10.1159/000355193 · Cited by 17
Regulation of multiple cytokine signalling pathways by SOCS3 is independent of SOCS2
Kiu, H., Greenhalgh, C. J., Thaus, A. L., Hilton, D. J., Nicola, N. A., Alexander, W. S., & Roberts, A. W. (2009) · Growth Factors · doi:10.3109/08977190903210954 · Cited by 17
Zhu, X., Bai, J., Liu, P., Wang, X., & Jiang, P. (2016) · Scientific Reports · doi:10.1038/srep32538 · Cited by 16
Oberbach, A., Schlichting, N. S., Heinrich, M., Till, H., Stolzenburg, J., & Neuhaus, J. (2012) · PLoS ONE · doi:10.1371/journal.pone.0041026 · Cited by 16
Moravcová, S., Červená, K., Pačesová, D., & Bendová, Z. (2015) · Journal of Neuroscience Research · doi:10.1002/jnr.23673 · Cited by 17
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Okamura, A., Iwata, N., Nagata, A., Tamekane, A., Shimoyama, M., Gomyo, H., Yakushijin, K., Urahama, N., Hamaguchi, M., Fukui, C., et al. (2004) · Blood · doi:10.1182/blood-2003-08-2768 · Cited by 16
Vanadate enhances leptin-induced activation of JAK/STAT pathway in CHO cells
Kita, A., Uotani, S., Kuwahara, H., Takahashi, R., Oshima, K., Yamasaki, H., Mizuguchi, H., Hayakawa, T., Nagayama, Y., Yamaguchi, Y., et al. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)00264-x · Cited by 16
Han, M., Li, Y., Wu, W., Zhang, Y., Yan, W., Luo, X., & Ning, Q. (2017) · Antiviral Research · doi:10.1016/j.antiviral.2017.10.003 · Cited by 15
Chronic exposure to methylmercury enhances the anorexigenic effects of leptin in C57BL/6J male mice
Ferrer, B., Prince, L. M., Tinkov, A. A., Santamarı́a, A., Farina, M., da Rocha, J. B. T., Bowman, A. B., & Aschner, M. (2020) · Food and Chemical Toxicology · doi:10.1016/j.fct.2020.111924 · Cited by 14
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O’Leary, E. E., Mazurkiewicz-Muñoz, A. M., Argetsinger, L. S., Maures, T. J., Huynh, H. T., & Carter‐Su, C. (2013) · Molecular Endocrinology · doi:10.1210/me.2011-1275 · Cited by 15
Unbiased identification of substrates for the Epac1-inducible E3 ubiquitin ligase component SOCS-3
Williams, J. J. L., & Palmer, T. M. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110629 · Cited by 15
Reuben, J. S., Dinh, L., Lee, J., Stateson, J., Kamara, H., Xiang, L., & Opperman, L. A. (2011) · Oral Surgery Oral Medicine Oral Pathology Oral Radiology and Endodontology · doi:10.1016/j.tripleo.2010.09.068 · Cited by 16
Suppressors of cytokine signaling proteins in innate and adaptive immune responses.
Dalpke, A. H., & Heeg, K. M. (2003) · PubMed · Cited by 14
Aziz, S. G., Aziz, S. G.-G., Khabbazi, A., & Alipour, S. (2020) · Biomarkers · doi:10.1080/1354750x.2020.1754912 · Cited by 13
Novel control of cAMP-regulated transcription in vascular endothelial cells
Milne, G. R., Palmer, T. M., & Yarwood, S. J. (2012) · Biochemical Society Transactions · doi:10.1042/bst20110606 · Cited by 13
Lehmann, U., Sommer, U., Smyczek, T., Hörtner, M., Frisch, W., Volkmer‐Engert, R., Heinrich, P., Schaper, F., & Haan, S. (2006) · Cellular Signalling · doi:10.1016/j.cellsig.2005.03.019 · Cited by 19
Wei, Y., Zhang, Z., She, N., Chen, X., Zhao, Y., & Zhang, J. (2019) · Physical Chemistry Chemical Physics · doi:10.1039/c9cp02257k · Cited by 13
Sk, M. F., Jonniya, N. A., Roy, R., & Kar, P. (2022) · The Journal of Physical Chemistry B · doi:10.1021/acs.jpcb.1c10733 · Cited by 12
Zhang, J., Li, F., Sun, P., Wang, J., Li, K., Zhao, Z., Bai, X., Cao, Y., Bao, H., Li, D., et al. (2022) · Veterinary Microbiology · doi:10.1016/j.vetmic.2022.109595 · Cited by 12
Merchant, S. (2021) · International review of cytology · doi:10.1016/bs.ircmb.2021.09.002 · Cited by 15
The Negative Regulation of JAK/STAT Signaling
Murphy, J. M., Tannahill, G. M., Hilton, D. J., & Greenhalgh, C. J. (2010) · Elsevier eBooks · doi:10.1016/b978-0-12-374145-5.00064-4 · Cited by 12
Chapter 3 Role of SOCS in Allergic and Innate Immune Responses
Cassel, S. L., & Rothman, P. B. (2009) · Advances in immunology · doi:10.1016/s0065-2776(09)03003-x · Cited by 12
STAT module can function as a biphasic amplitude filter
Mayya, V., & Loew, L. M. (2005) · Systems Biology · doi:10.1049/sb:20045037 · Cited by 11
Interleukin-15 cytokine checkpoints in natural killer cell anti-tumor immunity
Sudholz, H., Delconte, R. B., & Huntington, N. D. (2023) · Current Opinion in Immunology · doi:10.1016/j.coi.2023.102364 · Cited by 10
Johnson, J. A., Calo, S., Nair, L. T., IglayReger, H. B., Greenwald-Yarnell, M. L., Skorupski, J. C., Myers, M. G., & Bodary, P. F. (2012) · The Journal of Steroid Biochemistry and Molecular Biology · doi:10.1016/j.jsbmb.2012.06.002 · Cited by 10
The Acth Axis: Pathogenesis, Diagnosis and Treatment
Gaillard, R. C. (2003) · Endocrine updates · doi:10.1007/978-1-4615-0501-3 · Cited by 9
Fushimi, S., Ogino, T., Hara, J., Takahata, T., Wakabayashi, H., Watanabe, H., Arashima, Y., Kubo, M., & Matsukawa, A. (2009) · Clinical Immunology · doi:10.1016/j.clim.2009.08.015 · Cited by 10
Metadata
- Authors
- Sasaki, A., Yasukawa, H., Suzuki, A., Kamizono, S., Syoda, T., Kinjyo, I., Sasaki, M., Johnston, J. A., & Yoshimura, A.
- Affiliations
- Kurume University (JP)
- Corresponding author
- Yoshimura, Akihiko
- Venue
- Genes to Cells
- Publisher
- Wiley
- Published
- 1999-06
- Volume
- 4
- Issue
- 6
- Pages
- 339-351
- ISSN
- 1356-9597 (ISSN-L)
- 1365-2443
- OpenAlex
- W2008295144
- Cited by
- 398
- References
- 28
- Citations by year
- 2026: 5 · 2025: 6 · 2024: 8 · 2023: 11 · 2022: 13 · 2021: 13 · 2020: 13 · 2019: 17 · 2018: 15 · 2017: 15 · 2016: 8 · 2015: 17 · 2014: 19 · 2013: 18 · 2012: 29
- FWCI
- 5.24
- Type
- journal article
- Language
- en
- Open access
- bronze
- doi.org
- Locations
- Genes to Cells (publishedVersion)
- PubMed (publishedVersion)
- Funders
- Naito Foundation
- Sumitomo Foundation
- Kanae Foundation for the Promotion of Medical Science
- 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 › Molecular Biology › Receptor Mechanisms and Signaling
- Keywords
- SOCS3, JAK2, SH2 domain, jab, cytokine signaling, protein tyrosine kinase inhibitors, fusion protein
- MeSH terms
- Suppressor of Cytokine Signaling 3 Protein, Amino Acid Sequence, Enzyme Activation, Humans, Molecular Sequence Data, Phosphorylation, Protein Binding, Protein-Tyrosine Kinases, Proteins, Proto-Oncogene Proteins, Repressor Proteins, Transcription Factors, Signal Transduction, src Homology Domains, Suppressor of Cytokine Signaling Proteins, Janus Kinase 2
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