The DOI matches its Crossref record; 28 of the 28 references it cites were found in a registry or an index.
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.
Overview
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Integrity signals
Registry
Cites
Statistics
Verification
Claims the paper makes
The claims and statistics of this paper haven’t been checked yet.
Run the check — free, no account needed. It reads the open-access text and checks the sources it cites.
Claims other papers make about this one
Each is checked against this paper’s own text: does it say what the citing paper says it does?
The cited source says what the claim attributes to it.
In the citing paper
“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]
Self-check
Percentages, sums and reported differences re-computed from the paper’s own numbers.
The self-check needs the paper’s full text.
Citations
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
Sorted by citations
Items 101–200 of 400
Puhr, M., Santer, F. R., Neuwirt, H., Susani, M., Nemeth, J. A., Hobisch, A., Kenner, L., & Čulig, Z. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-0806 · Cited by 84
Linossi, E. M., & Nicholson, S. E. (2015) · Immunological Reviews · doi:10.1111/imr.12305 · Cited by 86
Dey, B. R., Furlanetto, R. W., & NISSLEY, P. S. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.3762 · Cited by 83
Matsumoto, A., Seki, Y.-I., Watanabe, R., Hayashi, K., Johnston, J. A., Harada, Y., Abe, R., Yoshimura, A., & Kubo, M. (2003) · The Journal of Experimental Medicine · doi:10.1084/jem.20020939 · Cited by 82
Self-citationMutational landscape of B‐cell post‐transplant lymphoproliferative disorders
Menter, T., Juškevičius, D., Alikian, M., Steiger, J., Dirnhofer, S., Tzankov, A., & Naresh, K. N. (2017) · British Journal of Haematology · doi:10.1111/bjh.14633 · Cited by 82
An activity-dependent determinant of synapse elimination in the mammalian brain
Yasuda, M., Nagappan-Chettiar, S., Johnson‐Venkatesh, E., & Umemori, H. (2021) · Neuron · doi:10.1016/j.neuron.2021.03.006 · Cited by 83
van de Geijn, G. M., Gits, J., Aarts, L. H. J., Heijmans‐Antonissen, C., & Touw, I. P. (2004) · Blood · doi:10.1182/blood-2003-08-2913 · Cited by 78
Qing, Y., Costa‐Pereira, A. P., Watling, D., & Stark, G. R. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m409863200 · Cited by 78
Regulation of CD4 + T‐cell polarization by suppressor of cytokine signalling proteins
Knosp, C. A., & Johnston, J. A. (2011) · Immunology · doi:10.1111/j.1365-2567.2011.03520.x · Cited by 80
Self-citationMujtaba, M. G., Flowers, L. O., Patel, C. B., Patel, R. A., Haider, M. I., & Johnson, H. M. (2005) · The Journal of Immunology · doi:10.4049/jimmunol.175.8.5077 · Cited by 77
Regulation of Janus kinases by SOCS proteins
Kershaw, N. J., Murphy, J. M., Lucet, I. S., Nicola, N. A., & Babon, J. J. (2013) · Biochemical Society Transactions · doi:10.1042/bst20130077 · Cited by 75
A three-dimensional model of Suppressor Of Cytokine Signalling 1 (SOCS-1)
Giordanetto, F., & Kroemer, R. T. (2003) · Protein Engineering Design and Selection · doi:10.1093/proeng/gzg015 · Cited by 76
Skjesol, A., Liebe, T., Iliev, D. B., Thomassen, E. I. S., Greiner-Tollersrud, L., Sobhkhez, M., Joensen, L. L., Secombes, C. J., & Jørgensen, J. B. (2014) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2014.02.009 · Cited by 75
Chung, A. S., Guan, Y. A., Yuan, Z., Albina, J. E., & Chin, Y. E. (2005) · Molecular and Cellular Biology · doi:10.1128/mcb.25.11.4716-4726.2005 · Cited by 75
Ali, O., Cerjak, D., Kent, J. W., James, R. G., Blangero, J., Carless, M. A., & Zhang, Y. (2016) · Epigenetics · doi:10.1080/15592294.2016.1216284 · Cited by 75
Terstegen, L., Gatsios, P., Bode, J. G., Schaper, F., Heinrich, P. C., & Graeve, L. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.m904148199 · Cited by 73
Morrison, A. C., Wilson, C. B., Ray, M., & Correll, P. H. (2004) · The Journal of Immunology · doi:10.4049/jimmunol.172.3.1825 · Cited by 73
Brender, C., Columbus, R., Metcalf, D., Handman, E., Starr, R., Huntington, N. D., Tarlinton, D. M., Ødum, N., Nicholson, S. E., Nicola, N. A., et al. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.13.6094-6103.2004 · Cited by 73
Moshapa, F. T., Riches‐Suman, K., & Palmer, T. M. (2019) · Cardiology Research and Practice · doi:10.1155/2019/9846312 · Cited by 76
Boyle, K., Egan, P. J., Rakar, S., Willson, T. A., Wicks, I. P., Metcalf, D., Hilton, D. J., Nicola, N. A., Alexander, W. S., Roberts, A. W., et al. (2007) · Blood · doi:10.1182/blood-2007-03-079178 · Cited by 74
Hanada, T., Yoshida, T., Kinjyo, I., Minoguchi, S., Yasukawa, H., Kato, S., Mimata, H., Nomura, Y., Seki, Y., Kubo, M., et al. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m106139200 · Cited by 72
Self-citationFXR ligands protect against hepatocellular inflammation via SOCS3 induction
Xu, Z., Huang, G., Gong, W., Zhou, P., Zhao, Y., Zhang, Y., Zeng, Y., Gao, M., Pan, Z., & He, F. (2012) · Cellular Signalling · doi:10.1016/j.cellsig.2012.04.015 · Cited by 71
Activation of the transcription factor NF-κB by the erythropoietin receptor
Bittorf, T., Büchse, T., Sasse, T., Jaster, R., & Brock, J. (2001) · Cellular Signalling · doi:10.1016/s0898-6568(01)00189-9 · Cited by 70
Regulation of the inflammatory response of vascular endothelial cells by EPAC1
Parnell, E., Smith, B. O., Palmer, T. M., Terrin, A., Zaccolo, M., & Yarwood, S. J. (2011) · British Journal of Pharmacology · doi:10.1111/j.1476-5381.2011.01808.x · Cited by 71
LIF signal in mouse embryonic stem cells
Ohtsuka, S., Nakai, Y., & Niwa, H. (2015) · JAK-STAT · doi:10.1080/21623996.2015.1086520 · Cited by 74
Regulation of Macrophage, Dendritic Cell, and Microglial Phenotype and Function by the SOCS Proteins
McCormick, S. M., & Heller, N. M. (2015) · Frontiers in Immunology · doi:10.3389/fimmu.2015.00549 · Cited by 69
Oh, S. T., & Gotlib, J. R. (2010) · Expert Review of Hematology · doi:10.1586/ehm.10.28 · Cited by 67
Cianciulli, A., Calvello, R., Porro, C., Trotta, T., & Panaro, M. A. (2017) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2017.07.005 · Cited by 59
Boyle, K., Zhang, J., Nicholson, S. E., Trounson, E., Babon, J. J., McManus, E. J., Nicola, N. A., & Robb, L. G. (2008) · Cellular Signalling · doi:10.1016/j.cellsig.2008.11.002 · Cited by 69
Sox6 enhances erythroid differentiation in human erythroid progenitors
Cantù, C., Ierardi, R., Alborelli, I., Fugazza, C., Cassinelli, L., Piconese, S., Bosè, F., Ottolenghi, S., Ferrari, G., & Ronchi, A. E. (2011) · Blood · doi:10.1182/blood-2010-04-282350 · Cited by 65
Roles of Stat3 and ERK in G‐CSF Signaling
Kamezaki, K., Shimoda, K., Numata, A., Haro, T., Kakumitsu, H., Yoshie, M., Yamamoto, M., Takeda, K., Matsuda, T., Akira, S., et al. (2005) · Stem Cells · doi:10.1634/stemcells.2004-0173a · Cited by 66
Uren, R. T., & Turnley, A. M. (2014) · Frontiers in Molecular Neuroscience · doi:10.3389/fnmol.2014.00039 · Cited by 70
Hirata, Y., Brems, H., Suzuki, M., Kanamori, M., Okada, M., Morita, R., Llano‐Rivas, I., Ose, T., Messiaen, L. M., Legius, E., et al. (2015) · Journal of Biological Chemistry · doi:10.1074/jbc.m115.703710 · Cited by 63
Self-citationZimmerer, J. M., Lesinski, G. B., Kondadasula, S. V., Karpa, V. I., Lehman, A., Ray‐Chaudhury, A., Becknell, B., & Carson, W. E. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.8.4832 · Cited by 62
Chen, W., Daines, M., & Hershey, G. K. K. (2004) · Journal of Allergy and Clinical Immunology · doi:10.1016/j.jaci.2004.06.042 · Cited by 66
Cell-Type-Specific Type I Interferon Antagonism Influences Organ Tropism of Murine Coronavirus
Zhao, L., Rose, K. M., Elliott, R., van Rooijen, N., & Weiss, S. R. (2011) · Journal of Virology · doi:10.1128/jvi.05075-11 · Cited by 63
Hebenstreit, D., Luft, P., Schmiedlechner, A., Regl, G., Frischauf, A., Aberger, F., Duschl, A., & Horejs‐Hoeck, J. (2003) · The Journal of Immunology · doi:10.4049/jimmunol.171.11.5901 · Cited by 63
Doti, N., Scognamiglio, P. L., Madonna, S., Scarponi, C., Ruvo, M., Perretta, G., Albanesi, C., & Marasco, D. (2011) · Biochemical Journal · doi:10.1042/bj20111647 · Cited by 63
Growth Hormone Receptor Regulation in Cancer and Chronic Diseases
Strous, G. J., Almeida, A. D. S., Putters, J., Schantl, J., Sędek, M., Slotman, J. A., Nespital, T., Hassink, G. C., & Mol, J. A. (2020) · Frontiers in Endocrinology · doi:10.3389/fendo.2020.597573 · Cited by 61
Structural Basis for Phosphotyrosine Recognition by Suppressor of Cytokine Signaling-3
Bergamin, E., Wu, J., & Hubbard, S. R. (2006) · Structure · doi:10.1016/j.str.2006.06.011 · Cited by 60
JAK/STAT3 signaling in cardiac fibrosis: a promising therapeutic target
Jiang, H., Yang, J., Li, T., Wang, X., Fan, Z., Ye, Q., & Du, Y. (2024) · Frontiers in Pharmacology · doi:10.3389/fphar.2024.1336102 · Cited by 68
The Role of Suppressors of Cytokine Signalling in Human Neoplasms
Sasi, W., Sharma, A. K., & Mokbel, K. (2014) · Molecular Biology International · doi:10.1155/2014/630797 · Cited by 60
Mazurkiewicz-Muñoz, A. M., Argetsinger, L. S., Kouadio, J.-L. K., Stensballe, A., Jensen, O. N., Cline, J. M., & Carter‐Su, C. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.01591-05 · Cited by 58
McCormick, S. M., Gowda, N. M., Fang, J., & Heller, N. M. (2016) · Journal of Biological Chemistry · doi:10.1074/jbc.m116.746164 · Cited by 56
SOCS1 is a critical checkpoint in immune homeostasis, inflammation and tumor immunity
Bidgood, G. M., Keating, N., Doggett, K., & Nicholson, S. E. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1419951 · Cited by 61
SOCS proteins in infectious diseases of mammals
Delgado-Ortega, M., Marc, D., Dupont, J., Trapp, S., Berri, M., & Meurens, F. (2012) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2012.11.008 · Cited by 61
Ben‐Zvi, T., Yayon, A., Gertler, A., & Ornan, E. M. (2006) · Journal of Cell Science · doi:10.1242/jcs.02740 · Cited by 56
Exercise-Induced Activation of STAT3 Signaling Is Increased with Age
Caldow, M. K., Carey, K. A., Ward, A. C., Farnfield, M. M., & Cameron‐Smith, D. (2008) · Rejuvenation Research · doi:10.1089/rej.2007.0643 · Cited by 57
Wiejak, J., Dunlop, J., Mackay, S. P., & Yarwood, S. J. (2013) · Biochemical Journal · doi:10.1042/bj20130481 · Cited by 55
Linossi, E. M., Chandrashekaran, I. R., Kolesnik, T. B., Murphy, J. M., Webb, A. I., Willson, T. A., Kedzierski, Ł., Bullock, A. N., Babon, J. J., Norton, R. S., et al. (2013) · PLoS ONE · doi:10.1371/journal.pone.0070536 · Cited by 54
Dhar, K., Rakesh, K., Pankajakshan, D., & Agrawal, D. K. (2013) · American Journal of Physiology-Heart and Circulatory Physiology · doi:10.1152/ajpheart.00570.2012 · Cited by 58
SOCS3 Drives Proteasomal Degradation of TBK1 and Negatively Regulates Antiviral Innate Immunity
Liu, D., Sheng, C., Gao, S., Yao, C., Li, J., Jiang, W., Chen, H., Wu, J., Pan, C., Chen, S., et al. (2015) · Molecular and Cellular Biology · doi:10.1128/mcb.00090-15 · Cited by 53
Neuwirt, H., Puhr, M., Cavarretta, I. T. R., Mitterberger, M., Hobisch, A., & Čulig, Z. (2007) · Endocrine Related Cancer · doi:10.1677/erc-07-0172 · Cited by 52
Yue, S., Wang, Z., Wang, L., Peng, Q., & Xue, B. (2020) · Animals · doi:10.3390/ani10061015 · Cited by 53
Leptin activates AMP-activated protein kinase in hepatic cells via a JAK2-dependent pathway
Uotani, S., Abe, T., & Yamaguchi, Y. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.10.015 · Cited by 56
JAK's SOCS: A Mechanism of Inhibition
Yoshimura, A., & Yasukawa, H. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.010 · Cited by 54
Self-citationHaan, S., Wüller, S., Kaczor, J., Rolvering, C., Nocker, T., Behrmann, I., & Haan, C. (2009) · Oncogene · doi:10.1038/onc.2009.155 · Cited by 51
Advances in understanding the pathogenesis of primary familial and congenital polycythaemia
Huang, L. J.-S., Shen, Y.-M. P., & Bulut, G. B. (2010) · British Journal of Haematology · doi:10.1111/j.1365-2141.2009.08069.x · Cited by 52
White, C. A., & Nicola, N. A. (2013) · JAK-STAT · doi:10.4161/jkst.25045 · Cited by 53
Ortmann, R., Cheng, T. P., Visconti, R., Frucht, D. M., & O’Shea, J. J. (2000) · Arthritis Research · doi:10.1186/ar66 · Cited by 50
Insulin decreases hepatic acute phase protein levels in severely burned children
Wu, X., Thomas, S. J., Herndon, D. N., Sanford, A. P., & Wolf, S. E. (2004) · Surgery · doi:10.1016/j.surg.2003.08.018 · Cited by 50
Leptin Signaling in the Control of Metabolism and Appetite: Lessons from Animal Models
Barrios-Correa, A. A., Estrada, J. A., & Contreras, I. (2018) · Journal of Molecular Neuroscience · doi:10.1007/s12031-018-1185-0 · Cited by 54
DrosophilaSOCS36E negatively regulates JAK/STAT pathway signaling via two separable mechanisms
Stec, W. J., Vidal, O. M., & Zeidler, M. P. (2013) · Molecular Biology of the Cell · doi:10.1091/mbc.e13-05-0275 · Cited by 48
Babon, J. J., Yao, S., DeSouza, D. P., Harrison, C. F., Fabri, L., Liepinsh, E., Scrofani, S. D. B., Baca, M., & Norton, R. S. (2005) · FEBS Journal · doi:10.1111/j.1742-4658.2005.05010.x · Cited by 48
SOCS-1 Localizes to the Microtubule Organizing Complex-Associated 20S Proteasome
Vuong, B. Q., Arenzana, T. L., Showalter, B. M., Losman, J. A., Chen, X. P., Mostecki, J. W., Banks, A. S., Limnander, A., Fernandez, N., & Rothman, P. B. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.20.9092-9101.2004 · Cited by 47
Eberle, M.-E., & Dalpke, A. H. (2012) · The Journal of Immunology · doi:10.4049/jimmunol.1103068 · Cited by 46
Numata, K., Kubo, M., Watanabe, H. A., Takagi, K., Mizuta, H., Okada, S., Kunkel, S. L., Ito, T., & Matsukawa, A. (2007) · The Journal of Immunology · doi:10.4049/jimmunol.178.6.3777 · Cited by 46
O’Connell, D., Bouazza, B., Kokalari, B., Amrani, Y., Khatib, A., Ganther, J. D., & Tliba, O. (2015) · American Journal of Physiology-Lung Cellular and Molecular Physiology · doi:10.1152/ajplung.00099.2015 · Cited by 46
A Comprehensive Survey of the Roles of Highly Disordered Proteins in Type 2 Diabetes
Du, Z., & Uversky, V. N. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18102010 · Cited by 47
Natural killer cells and anti-tumor immunity
Nicholson, S. E., Keating, N., & Belz, G. T. (2017) · Molecular Immunology · doi:10.1016/j.molimm.2017.12.002 · Cited by 46
Zhou, X., Gan, F., Hou, L., Liu, Z., Su, J., Lin, Z., Le, G., & Huang, K. (2019) · Journal of Agricultural and Food Chemistry · doi:10.1021/acs.jafc.8b07309 · Cited by 48
Mimetics of suppressor of cytokine signaling 3: Novel potential therapeutics in triple breast cancer
Manna, S. L., Lee, E.-M., Ouzounova, M., Natale, C. D., Novellino, E., Merlino, A., Körkaya, H., & Marasco, D. (2018) · International Journal of Cancer · doi:10.1002/ijc.31594 · Cited by 44
Integrative Signaling by Minimal Erythropoietin Receptor Forms and c-Kit
Pircher, T. J., Geiger, J. N., Zhang, D., Miller, C. P., Gaines, P. C. W., & Wojchowski, D. M. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m007473200 · Cited by 45
Shouda, T., Hiraoka, K., Komiya, S., Hamada, T., Zenmyo, M., Iwasaki, H., Isayama, T., Fukushima, N., Nagata, K., & Yoshimura, A. (2005) · Cancer Letters · doi:10.1016/j.canlet.2005.01.042 · Cited by 44
Self-citationExpression of SOCS1-7 and CIS mRNA in porcine tissues
Delgado-Ortega, M., Melo, S., & Meurens, F. (2011) · Veterinary Immunology and Immunopathology · doi:10.1016/j.vetimm.2011.08.002 · Cited by 45
Negative regulation of cytokine signaling and inflammatory diseases
Inagaki-Ohara, K. (2003) · Current Opinion in Pharmacology · doi:10.1016/s1471-4892(03)00070-5 · Cited by 41
Hanada, T., Kinjyo, I., Inagaki-Ohara, K., & Yoshimura, A. (2003) · Springer eBooks · doi:10.1007/s10254-003-0015-z · Cited by 43
Self-citationLiu, Y., Zhang, Z., Zhao, X., Yu, R., Zhang, X., Wu, S., Liu, J., Chi, X., Song, X., Fu, L., et al. (2014) · Viral Immunology · doi:10.1089/vim.2013.0127 · Cited by 43
Kershaw, N. J., Laktyushin, A., Nicola, N. A., & Babon, J. J. (2014) · Growth Factors · doi:10.3109/08977194.2013.877005 · Cited by 46
Structural insights into substrate recognition by the SOCS2 E3 ubiquitin ligase
Kung, W.-W., Ramachandran, S., Makukhin, N., Bruno, E., & Ciulli, A. (2019) · Nature Communications · doi:10.1038/s41467-019-10190-4 · Cited by 42
Stroß, C., Radtke, S., Clahsen, T., Gerlach, C., Volkmer, R., Schaper, F., Heinrich, P. C., & Hermanns, H. M. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m511212200 · Cited by 41
Yan, C., Cao, J., Wu, M., Zhang, W., Jiang, T., Yoshimura, A., & Gao, H. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.132084 · Cited by 41
Self-citationActivating mutations of the gp130/JAK/STAT pathway in human diseases
Lokau, J., & Garbers, C. (2018) · Advances in protein chemistry and structural biology · doi:10.1016/bs.apcsb.2018.11.007 · Cited by 41
SOCS3 regulates graft-versus-host disease
Hill, G. R., Kuns, R. D., Raffelt, N. C., Don, A. L. J., Olver, S. D., Markey, K. A., Wilson, Y. A., Tocker, J. E., Alexander, W. S., Clouston, A. D., et al. (2010) · Blood · doi:10.1182/blood-2009-12-259598 · Cited by 40
Mechanisms of SOCS3 Phosphorylation upon Interleukin-6 Stimulation
Sommer, U., Schmid, C., Sobota, R. M., Lehmann, U., Stevenson, N. J., Johnston, J. A., Schaper, F., Heinrich, P. C., & Haan, S. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m506008200 · Cited by 42
Self-citationPost-Receptor Inhibitors of the GHR-JAK2-STAT Pathway in the Growth Hormone Signal Transduction
Wójcik, M., Krawczyńska, A., Antushevich, H., & Herman, A. P. (2018) · International Journal of Molecular Sciences · doi:10.3390/ijms19071843 · Cited by 39
SOCS3 inhibiting migration of A549 cells correlates with PYK2 signaling in vitro
Zhang, S., Guo, D., Jiang, L., Zhang, Q., Qiu, X., & Wang, E. (2008) · BMC Cancer · doi:10.1186/1471-2407-8-150 · Cited by 38
Orth, J. H. C., Aktories, K., & Kubatzky, K. F. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m609018200 · Cited by 38
Hepatocyte growth control by SOCS1 and SOCS3
Khan, M. G. M., Ghosh, A., Variya, B. C., Santharam, M. A., Kandhi, R., Ramanathan, S., & Ilangumaran, S. (2019) · Cytokine · doi:10.1016/j.cyto.2019.154733 · Cited by 38
SOCS1: Regulator of T Cells in Autoimmunity and Cancer
Ilangumaran, S., Bobbala, D., & Ramanathan, S. (2017) · Current topics in microbiology and immunology · doi:10.1007/82_2017_63 · Cited by 37
SOCS: negative regulators of cytokine signaling for immune tolerance
Yoshimura, A., Ito, M., Mise‐Omata, S., & Ando, M. (2021) · International Immunology · doi:10.1093/intimm/dxab055 · Cited by 38
Self-citationMethylation and microRNA-mediated epigenetic regulation of SOCS3
Boosani, C. S., & Agrawal, D. K. (2015) · Molecular Biology Reports · doi:10.1007/s11033-015-3860-3 · Cited by 37
Williams, J. J. L., Munro, K. M., & Palmer, T. M. (2014) · Cells · doi:10.3390/cells3020546 · Cited by 38
Williams, J. J. L., Alotaiq, N., Mullen, W., Burchmore, R., Liu, L., Baillie, G. S., Schaper, F., Pilch, P. F., & Palmer, T. M. (2018) · Nature Communications · doi:10.1038/s41467-017-02585-y · Cited by 35
Maehr, T., Vecino, J. L. G., Wadsworth, S., Wang, T., & Secombes, C. J. (2014) · Molecular Immunology · doi:10.1016/j.molimm.2014.06.021 · Cited by 36
Dynamics of rumen gene expression, microbiome colonization, and their interplay in goats
Pan, X., Li, Z., Li, B., Zhao, C., Wang, Y., Chen, Y., & Jiang, Y. (2021) · BMC Genomics · doi:10.1186/s12864-021-07595-1 · Cited by 37
Wu, X., Herndon, D. N., & Wolf, S. E. (2003) · Shock · doi:10.1097/00024382-200304000-00004 · Cited by 36
Pharmacology of inhibitors of Janus kinases – Part 1: Pharmacokinetics
Eichner, A., & Wohlrab, J. (2022) · JDDG Journal der Deutschen Dermatologischen Gesellschaft · doi:10.1111/ddg.14921 · Cited by 35
van de Geijn, G. M., Gits, J., & Touw, I. P. (2004) · Journal of Leukocyte Biology · doi:10.1189/jlb.0104041 · Cited by 35
Gu, Q., Kong, Y., Yu, Z., Li, B., & Xiao, Y. (2011) · Biochimie · doi:10.1016/j.biochi.2011.02.009 · Cited by 36
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
About these checks
Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.
Statistics and arithmetic are recomputed, not judged.
Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.
What counts as a claim ›How we measure confidence ›How we check this ›
Are you an author, or do you see a problem with this page? Request a review