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Therapeutic Targeting of the Proinflammatory IL-6-JAK/STAT Signalling Pathways Responsible for Vascular Restenosis in Type 2 Diabetes Mellitus

Moshapa, F. T., Riches‐Suman, K., & Palmer, T. M. (2019) · Cardiology Research and Practice · doi:10.1155/2019/9846312 · Cited by 72 · see citing works

The SOCS box of suppressor of cytokine signaling-3 contributes to the control of G-CSF responsiveness in vivo

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 72 · see citing works

Suppressor of Cytokine Signaling 2 Is a Feedback Inhibitor of TLR-Induced Activation in Human Monocyte-Derived Dendritic Cells

Posselt, G., Schwarz, H., Duschl, A., & Horejs‐Hoeck, J. (2011) · The Journal of Immunology · doi:10.4049/jimmunol.1003348 · Cited by 71 · see citing works

Structural Basis for c-KIT Inhibition by the Suppressor of Cytokine Signaling 6 (SOCS6) Ubiquitin Ligase

Zadjali, F., Pike, A. C. W., Vesterlund, M., Sun, J., Wu, C., Li, S. S. ‐., Rönnstrand, L., Knapp, S., Bullock, A. N., & Flores‐Morales, A. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m110.173526 · Cited by 70 · see citing works

SOCS1 and SOCS3 Target IRF7 Degradation To Suppress TLR7-Mediated Type I IFN Production of Human Plasmacytoid Dendritic Cells

Yu, C., Peng, W., Schlee, M., Barchet, W., Eis‐Hübinger, A. M., Kolanus, W., Geyer, M., Schmitt, S., Steinhagen, F., Oldenburg, J., et al. (2018) · The Journal of Immunology · doi:10.4049/jimmunol.1700510 · Cited by 70 · see citing works

Deletion of the SOCS box of suppressor of cytokine signaling 3 (SOCS3) in embryonic stem cells reveals SOCS box-dependent regulation of JAK but not STAT phosphorylation

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 66 · see citing works

SOCS3 in immune regulation of inflammatory bowel disease and inflammatory bowel disease-related cancer

Li, Y., de Haar, C. G., Peppelenbosch, M. P., & van der Woude, C. J. (2012) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2012.04.005 · Cited by 63 · see citing works

Decoding inflammation, its causes, genomic responses, and emerging countermeasures

Hawiger, J., & Zienkiewicz, J. (2019) · Scandinavian Journal of Immunology · doi:10.1111/sji.12812 · Cited by 62 · see citing works

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 · see citing works

SOCS-JAK-STAT inhibitors and SOCS mimetics as treatment options for autoimmune uveitis, psoriasis, lupus, and autoimmune encephalitis

Pandey, R., Bakay, M. A., & Hakonarson, H. H. (2023) · Frontiers in Immunology · doi:10.3389/fimmu.2023.1271102 · Cited by 58 · see citing works

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 58 · see citing works

Suppressor of cytokine signaling 3 inhibits head kidney macrophage activation and cytokine expression in Scophthalmus maximus

Zhang, M., Xiao, Z., & Sun, L. (2010) · Developmental & Comparative Immunology · doi:10.1016/j.dci.2010.09.006 · Cited by 57 · see citing works

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 58 · see citing works

Expression of suppressor of cytokine signaling genes in human elderly and Alzheimer’s disease brains and human microglia

Walker, D. G., Whetzel, A. M., & Lue, L. (2014) · Neuroscience · doi:10.1016/j.neuroscience.2014.09.052 · Cited by 56 · see citing works

Suppressor of Cytokine Signaling (SOCS) 5 Utilises Distinct Domains for Regulation of JAK1 and Interaction with the Adaptor Protein Shc-1

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 · see citing works

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 · see citing works

Understanding SOCS protein specificity

Linossi, E. M., Calleja, D. J., & Nicholson, S. E. (2018) · Growth Factors · doi:10.1080/08977194.2018.1518324 · Cited by 53 · see citing works

JAK's SOCS: A Mechanism of Inhibition

Yoshimura, A., & Yasukawa, H. (2012) · Immunity · doi:10.1016/j.immuni.2012.01.010 · Cited by 51 · see citing works

Calpastatin Counteracts Pathological Angiogenesis by Inhibiting Suppressor of Cytokine Signaling 3 Degradation in Vascular Endothelial Cells

Miyazaki, T., Taketomi, Y., Saito, Y., Hosono, T., Lei, X., Kim‐Kaneyama, J., Arata, S., Takahashi, H., Murakami, M., & Miyazaki, A. (2015) · Circulation Research · doi:10.1161/circresaha.116.305363 · Cited by 51 · see citing works

SOCS3

White, C. A., & Nicola, N. A. (2013) · JAK-STAT · doi:10.4161/jkst.25045 · Cited by 52 · see citing works

Antigen Presentation by Dendritic Cells in Tumors Is Disrupted by Altered Metabolism that Involves Pyruvate Kinase M2 and Its Interaction with SOCS3

Zhang, Z., Liu, Q., Che, Y., Yuan, X., Dai, L., Zeng, B., Jiao, G., Zhang, Y., Wu, X., Yu, Y., et al. (2009) · Cancer Research · doi:10.1158/0008-5472.can-09-2970 · Cited by 49 · see citing works

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 · see citing works

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 46 · see citing works

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 · see citing works

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 45 · see citing works

Suppressor of Cytokine Signaling 3: Emerging Role Linking Central Insulin Resistance and Alzheimer’s Disease

Cao, L., Wang, Z., & Wan, W. (2018) · Frontiers in Neuroscience · doi:10.3389/fnins.2018.00417 · Cited by 45 · see citing works

The N‐terminal domains of SOCS proteins: A conserved region in the disordered N‐termini of SOCS4 and 5

Feng, Z., Chandrashekaran, I. R., Low, A., Speed, T. P., Nicholson, S. E., & Norton, R. S. (2011) · Proteins Structure Function and Bioinformatics · doi:10.1002/prot.23252 · Cited by 44 · see citing works

Expression 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 44 · see citing works

SOCS1 and SOCS3 as key checkpoint molecules in the immune responses associated to skin inflammation and malignant transformation

Morelli, M., Madonna, S., & Albanesi, C. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1393799 · Cited by 46 · see citing works

Reconstruction of an active SOCS3-based E3 ubiquitin ligase complexin vitro: identification of the active components and JAK2 and gp130 as substrates

Kershaw, N. J., Laktyushin, A., Nicola, N. A., & Babon, J. J. (2014) · Growth Factors · doi:10.3109/08977194.2013.877005 · Cited by 42 · see citing works

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 41 · see citing works

Mammalian Protein-Protein Interaction Trap (MAPPIT) Analysis of STAT5, CIS, and SOCS2 Interactions with the Growth Hormone Receptor

Uyttendaele, I., Lemmens, I. H., Verhee, A., de Smet, A.-S., Vandekerckhove, J. S., Lavens, D., Peelman, F., & Tavernier, J. H. (2007) · Molecular Endocrinology · doi:10.1210/me.2006-0541 · Cited by 39 · see citing works

SOCS1 and its Potential Clinical Role in Tumor

Ying, J., Qiu, X., Yu, L., & Zhang, M. (2019) · Pathology & Oncology Research · doi:10.1007/s12253-019-00612-5 · Cited by 37 · see citing works

Role of Ubiquitylation in Controlling Suppressor of Cytokine Signalling 3 (SOCS3) Function and Expression

Williams, J. J. L., Munro, K. M., & Palmer, T. M. (2014) · Cells · doi:10.3390/cells3020546 · Cited by 37 · see citing works

Cloning of common carp SOCS-3 gene and its expression during embryogenesis, GH-transgene and viral infection

Xiao, Z., Liu, H., Fu, J.-P., Hu, W., Wang, Y., & Guo, Q. (2009) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2009.11.012 · Cited by 36 · see citing works

Interaction of suppressor of cytokine signalling 3 with cavin-1 links SOCS3 function and cavin-1 stability

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 · see citing works

Loss of Expression and Function of SOCS3 Is an Early Event in HNSCC: Altered Subcellular Localization as a Possible Mechanism Involved in Proliferation, Migration and Invasion

Rossa, C., Sommer, G., Spolidório, L. C., Rosenzweig, S. A., Watson, D. K., & Kirkwood, K. L. (2012) · PLoS ONE · doi:10.1371/journal.pone.0045197 · Cited by 35 · see citing works

Cyclic Peptidyl Inhibitors of Grb2 and Tensin SH2 Domains Identified from Combinatorial Libraries

Zhang, Y., Zhou, S., Wavreille, A., DeWille, J. W., & Pei, D. (2008) · Journal of Combinatorial Chemistry · doi:10.1021/cc700185g · Cited by 35 · see citing works

Krüppel-like factor 4 is widely expressed in the mouse male and female reproductive tract and responds as an immediate early gene to activation of the protein kinase A in TM4 Sertoli cells

Godmann, M., Kosan, C., & Behr, R. (2010) · Reproduction · doi:10.1530/rep-09-0531 · Cited by 35 · see citing works

SOCS-mediated immunomodulation of natural killer cells

Keating, N., & Nicholson, S. E. (2018) · Cytokine · doi:10.1016/j.cyto.2018.03.033 · Cited by 34 · see citing works

Socs3 maintains the specificity of biological responses to cytokine signals during granulocyte and macrophage differentiation

Croker, B. A., Mielke, L. A., Wormald, S., Metcalf, D., Kiu, H., Alexander, W. S., Hilton, D. J., & Roberts, A. W. (2008) · Experimental Hematology · doi:10.1016/j.exphem.2008.02.008 · Cited by 33 · see citing works

SOCS and Herpesviruses, With Emphasis on Cytomegalovirus Retinitis

Alston, C. I., & Dix, R. D. (2019) · Frontiers in Immunology · doi:10.3389/fimmu.2019.00732 · Cited by 34 · see citing works

Epithelial induction of porcine suppressor of cytokine signaling 2 (SOCS2) gene expression in response to Entamoeba histolytica

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 33 · see citing works

Potential Roles of Suppressor of Cytokine Signaling in Wound Healing

Feng, Y., Sanders, A. J., Morgan, L. D., Harding, K. G., & Jiang, W. G. (2016) · Regenerative Medicine · doi:10.2217/rme.16.4 · Cited by 33 · see citing works

Inhibitory effects of suppressor of cytokine signaling 3 on inflammatory cytokine expression and migration and proliferation of IL-6/IFN-γ-induced vascular smooth muscle cells

Xiang, S., Dong, N.-G., Liu, J.-P., Wang, Y., Shi, J.-W., Wei, Z., Hu, X., & Gong, L. (2013) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-013-1168-x · Cited by 33 · see citing works

Through a glass less darkly: apoptosis and the germinal center response to antigen

Peperzak, V., Vikstrom, I. B., & Tarlinton, D. M. (2012) · Immunological Reviews · doi:10.1111/j.1600-065x.2012.01123.x · Cited by 32 · see citing works

Suppressor of Cytokine Signaling 3 Inhibits Breast Tumor Kinase Activation of STAT3*

Gao, Y.-W., Cimica, V., & Reich, N. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m111.334144 · Cited by 34 · see citing works

Extended Anti-inflammatory Action of a Degradation-resistant Mutant of Cell-penetrating Suppressor of Cytokine Signaling 3

Fletcher, T. C., DiGiandomenico, A., & Hawiger, J. (2010) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.095216 · Cited by 32 · see citing works

Genetics of pelvic organ prolapse: crossing the bridge between bench and bedside in urogynecologic research

Bortolini, M. A. T., & Rizk, D. E. E. (2011) · International Urogynecology Journal · doi:10.1007/s00192-011-1502-4 · Cited by 29 · see citing works

Proteomimetics of Natural Regulators of JAK–STAT Pathway: Novel Therapeutic Perspectives

Manna, S. L., Benedictis, I. D., & Marasco, D. (2022) · Frontiers in Molecular Biosciences · doi:10.3389/fmolb.2021.792546 · Cited by 29 · see citing works

The negative regulatory roles of suppressor of cytokine signaling proteins in myeloid signaling pathways

Wormald, S., & Hilton, D. J. (2007) · Current Opinion in Hematology · doi:10.1097/00062752-200701000-00004 · Cited by 29 · see citing works

SOCS proteins and their roles in the development of glioblastoma (Review)

Dai, L., Li, Z., Liang, W., Hu, W., Zhou, S., Yang, Z., Tao, Y., Hou, X., Xing, Z., Mao, J., et al. (2021) · Oncology Letters · doi:10.3892/ol.2021.13123 · Cited by 28 · see citing works

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 25 · see citing works

Detection of Protein-Protein Interactions by Far-Western Blotting

Machida, K., & Mayer, B. J. (2009) · Methods in molecular biology · doi:10.1007/978-1-59745-542-8_34 · Cited by 26 · see citing works

Intracellular Delivery of a Cell-Penetrating SOCS1 that Targets IFN-γ Signaling

DiGiandomenico, A., Wylezinski, L. S., & Hawiger, J. (2009) · Science Signaling · doi:10.1126/scisignal.1162191 · Cited by 24 · see citing works

Unravelling the druggability and immunological roles of the SOCS-family proteins

Lynch, D. M., Forrester, B., Webb, T., & Ciulli, A. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1449397 · Cited by 25 · see citing works

A new polycythaemia vera‐associated SOCS3 SH2 mutant (SOCS3F136L) cannot regulate erythropoietin responses

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 · see citing works

Structure and Functional Characterization of the Conserved JAK Interaction Region in the Intrinsically Disordered N-Terminus of SOCS5

Chandrashekaran, I. R., Mohanty, B., Linossi, E. M., Dagley, L. F., Leung, E. W. W., Murphy, J. M., Babon, J. J., Nicholson, S. E., & Norton, R. S. (2015) · Biochemistry · doi:10.1021/acs.biochem.5b00619 · Cited by 21 · see citing works

Phosphorylation of SOCS1 Inhibits the SOCS1–p53 Tumor Suppressor Axis

Saint‐Germain, E., Mignacca, L., Huot, G., Acevedo, M., Moineau‐Vallée, K., Calabrese, V., Bourdeau, V., Rowell, M., Ilangumaran, S., Lessard, F., et al. (2019) · Cancer Research · doi:10.1158/0008-5472.can-18-1503 · Cited by 19 · see citing works

A Concise Review of MicroRNA Exploring the Insights of MicroRNA Regulations in Bacterial, Viral and Metabolic Diseases

Naveed, A., ur-Rahman, S., Abdullah, S., & Naveed, M. A. (2017) · Molecular Biotechnology · doi:10.1007/s12033-017-0034-7 · Cited by 19 · see citing works

Secondary structure assignment of mouse SOCS3 by NMR defines the domain boundaries and identifies an unstructured insertion in the SH2 domain

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 · see citing works

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 · see citing works

SH2 Domains from Suppressor of Cytokine Signaling-3 and Protein Tyrosine Phosphatase SHP-2 Have Similar Binding Specificities

Souza, D. P. D., Fabri, L., Nash, A. D., Hilton, D. J., Nicola, N. A., & Baca, M. (2002) · Biochemistry · doi:10.1021/bi0259507 · Cited by 106 · see citing works

Grasp a pTyr-Peptide by Its SOCS

Hirano, T., & Murakami, M. (2006) · Developmental Cell · doi:10.1016/j.devcel.2006.04.011 · Cited by 8 · see citing works

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 25 · see citing works