Interleukin-6 signalling: More than Jaks and STATs

STATs in cancer inflammation and immunity: a leading role for STAT3

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The pro- and anti-inflammatory properties of the cytokine interleukin-6

Scheller, J., Chalaris, A., Schmidt-Arras, D., & Rose-John, S. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.01.034 · Cited by 3,212 · see citing works

Maximal activation of transcription by statl and stat3 requires both tyrosine and serine phosphorylation

Wen, Z., Zhong, Z., & Darnell, J. E. (1995) · Cell · doi:10.1016/0092-8674(95)90311-9 · Cited by 1,974 · see citing works

Liver Failure and Defective Hepatocyte Regeneration in Interleukin-6-Deficient Mice

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Crystal Structure of the Tyrosine Phosphatase SHP-2

Hof, P., Pluskey, S., Dhe‐Paganon, S., Eck, M. J., & Shoelson, S. E. (1998) · Cell · doi:10.1016/s0092-8674(00)80938-1 · Cited by 996 · see citing works

Choice of STATs and Other Substrates Specified by Modular Tyrosine-Based Motifs in Cytokine Receptors

Stahl, N., Farruggella, T. J., Boulton, T. G., Zhong, Z., Darnell, J. E., & Yancopoulos, G. D. (1995) · Science · doi:10.1126/science.7871433 · Cited by 979 · see citing works

Association and Activation of Jak-Tyk Kinases by CNTF-LIF-OSM-IL-6 β Receptor Components

Stahl, N., Boulton, T. G., Farruggella, T., Ip, N. Y., Davis, S., Witthuhn, B. A., Quelle, F. W., Silvennoinen, O., Barbieri, G., Pellegrini, S., et al. (1994) · Science · doi:10.1126/science.8272873 · Cited by 979 · see citing works

Serine phosphorylation of STATs

Decker, T., & Kovarik, P. (2000) · Oncogene · doi:10.1038/sj.onc.1203481 · Cited by 887 · see citing works

Association of Transcription Factor APRF and Protein Kinase Jak1 with the Interleukin-6 Signal Transducer gp130

Lütticken, C., Wegenka, U. M., Yuan, J., Buschmann, J., Schindler, C., Ziemiecki, A., Harpur, A. G., Wilks, A. F., Yasukawa, K., Taga, T., et al. (1994) · Science · doi:10.1126/science.8272872 · Cited by 814 · see citing works

IL-6 signal transduction and its physiological roles: the signal orchestration model

Kamimura, D., Ishihara, K., & Hirano, T. (2003) · Reviews of Physiology, Biochemistry and Pharmacology · doi:10.1007/s10254-003-0012-2 · Cited by 673 · see citing works

Two Signals Are Necessary for Cell Proliferation Induced by a Cytokine Receptor gp130: Involvement of STAT3 in Anti-Apoptosis

Fukada, T., Hibi, M., Yamanaka, Y., Takahashi-Tezuka, M., Fujitani, Y., Yamaguchi, T., Nakajima, K., & Hirano, T. (1996) · Immunity · doi:10.1016/s1074-7613(00)80501-4 · Cited by 652 · see citing works

STAT proteins: novel molecular targets for cancer drug discovery

Turkson, J., & Jove, R. (2000) · Oncogene · doi:10.1038/sj.onc.1204086 · Cited by 643 · see citing works

STAT3 Serine Phosphorylation by ERK-Dependent and -Independent Pathways Negatively Modulates Its Tyrosine Phosphorylation

Chung, J., Uchida, E., Grammer, T. C., & Blenis, J. (1997) · Molecular and Cellular Biology · doi:10.1128/mcb.17.11.6508 · Cited by 620 · see citing works

Inflammatory cytokines in cancer: tumour necrosis factor and interleukin 6 take the stage

Grivennikov, S. I., & Karin, M. (2011) · Annals of the Rheumatic Diseases · doi:10.1136/ard.2010.140145 · Cited by 560 · see citing works

Transcriptionally active Stat1 is required for the antiproliferative effects of both interferon alpha and interferon gamma.

Bromberg, J., Horvath, C. M., Wen, Z., Schreiber, R. D., & Darnell, J. E., Jr. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.15.7673 · Cited by 541 · see citing works

Germline gain-of-function mutations in RAF1 cause Noonan syndrome

Razzaque, A. M., Nishizawa, T., Komoike, Y., Yagi, H., Furutani, M., Amo, R., Kamisago, M., Momma, K., Katayama, H., Nakagawa, M., et al. (2007) · Nature Genetics · doi:10.1038/ng2078 · Cited by 501 · see citing works

The role of PI3K in immune cells

Koyasu, S. (2003) · Nature Immunology · doi:10.1038/ni0403-313 · Cited by 486 · see citing works

Two contact regions between Stat1 and CBP/p300 in interferon γ signaling

Zhang, J. J., Vinkemeier, U., Gu, W., Chakravarti, D., Horvath, C. M., & Darnell, J. E., Jr. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.26.15092 · Cited by 485 · see citing works

Reciprocal regulation of gastrointestinal homeostasis by SHP2 and STAT-mediated trefoil gene activation in gp130 mutant mice

Tebbutt, N. C., Giraud, A. S., Inglese, M., Jenkins, B., Waring, P., Clay, F. J., Malki, S., Alderman, B. M., Grail, D., Hollande, F., et al. (2002) · Nature Medicine · doi:10.1038/nm763 · Cited by 474 · see citing works

Suppressor of cytokine signaling-3 preferentially binds to the SHP-2-binding site on the shared cytokine receptor subunit gp130

Nicholson, S. E., De Souza, D., Fabri, L. J., Corbin, J., Willson, T. A., Zhang, J.-G., Silva, A., Asimakis, M., Farley, A., Nash, A. D., et al. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.100135197 · Cited by 456 · see citing works

A major role for the protein tyrosine kinase JAK1 in the JAK/STAT signal transduction pathway in response to interleukin‐6.

Guschin, D. Y., Rogers, N. C., Briscoe, J., Witthuhn, B. A., Watling, D., Horn, F., Pellegrini, S., Yasukawa, K., Heinrich, P. C., & Stark, G. R. (1995) · The EMBO Journal · doi:10.1002/j.1460-2075.1995.tb07128.x · Cited by 434 · see citing works

Complementation of a mutant cell line: central role of the 91 kDa polypeptide of ISGF3 in the interferon‐alpha and ‐gamma signal transduction pathways.

Müller, M., Laxton, C., Briscoe, J., Schindler, C., Improta, T., Darnell, J. E., Stark, G. R., & Kerr, I. M. (1993) · The EMBO Journal · doi:10.1002/j.1460-2075.1993.tb06106.x · Cited by 411 · see citing works

SOCS3 Exerts Its Inhibitory Function on Interleukin-6 Signal Transduction through the SHP2 Recruitment Site of gp130

Schmitz, J., Weissenbach, M., Haan, S., Heinrich, P. C., & Schaper, F. (2000) · Journal of Biological Chemistry · doi:10.1074/jbc.275.17.12848 · Cited by 388 · see citing works

Autocrine IL-6 signaling: a key event in tumorigenesis?

Grivennikov, S., & Karin, M. (2008) · Cancer Cell · doi:10.1016/j.ccr.2007.12.020 · Cited by 379 · see citing works

The IL-6/sIL-6R complex as a novel target for therapeutic approaches

Rose‐John, S., Waetzig, G. H., Scheller, J., Grötzinger, J., & Seegert, D. (2007) · Expert Opinion on Therapeutic Targets · doi:10.1517/14728222.11.5.613 · Cited by 362 · see citing works

Differential Activation of Acute Phase Response Factor/STAT3 and STAT1 via the Cytoplasmic Domain of the Interleukin 6 Signal Transducer gp130

Gerhartz, C., Heesel, B., Sasse, J., Hemmann, U., Landgraf, C., Schneider-Mergener, J., Horn, F., Heinrich, P., & Graeve, L. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12991 · Cited by 351 · see citing works

PTPN11 (Shp2) Mutations in LEOPARD Syndrome Have Dominant Negative, Not Activating, Effects

Kontaridis, M. I., Swanson, K. D., David, F. S., Barford, D., & Neel, B. G. (2005) · Journal of Biological Chemistry · doi:10.1074/jbc.m513068200 · Cited by 340 · see citing works

Hyperactivation of Stat3 in gp130 mutant mice promotes gastric hyperproliferation and desensitizes TGF-β signaling

Jenkins, B. J., Grail, D., Nheu, T., Najdovska, M., Wang, B., Waring, P., Inglese, M., McLoughlin, R. M., Jones, S. A., Topley, N., et al. (2005) · Nature Medicine · doi:10.1038/nm1282 · Cited by 308 · see citing works

Acquiring signalling specificity from the cytokine receptor gp130

Ernst, M. (2003) · Trends in Genetics · doi:10.1016/j.tig.2003.11.003 · Cited by 297 · see citing works

Gab1 Acts as an Adapter Molecule Linking the Cytokine Receptor gp130 to ERK Mitogen-Activated Protein Kinase

Takahashi-Tezuka, M., Yoshida, Y., Fukada, T., Ohtani, T., Yamanaka, Y., Nishida, K., Nakajima, K., Hibi, M., & Hirano, T. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.7.4109 · Cited by 286 · see citing works

Phosphorylation of the Stat1 Transactivation Domain Is Required for Full-Fledged IFN-γ-Dependent Innate Immunity

Varinou, L., Ramsauer, K., Karaghiosoff, M., Kolbe, T., Pfeffer, K., Müller, M., & Decker, T. (2003) · Immunity · doi:10.1016/s1074-7613(03)00322-4 · Cited by 284 · see citing works

Receptor-Specific Regulation of Phosphatidylinositol 3′-Kinase Activation by the Protein Tyrosine Phosphatase Shp2

Zhang, S. Q., Tsiaras, W. G., Araki, T., Wen, G., Minichiello, L., Klein, R., & Neel, B. G. (2002) · Molecular and Cellular Biology · doi:10.1128/mcb.22.12.4062-4072.2002 · Cited by 283 · see citing works

Role of Phosphoinositide 3-Kinase in Activation of Ras and Mitogen-Activated Protein Kinase by Epidermal Growth Factor

Wennström, S., & Downward, J. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.6.4279 · Cited by 279 · see citing works

Site-Specific Incorporation of a Phosphotyrosine Mimetic Reveals a Role for Tyrosine Phosphorylation of SHP-2 in Cell Signaling

Lu, W., Gong, D., Bar-Sagi, D., & Cole, P. A. (2001) · Molecular Cell · doi:10.1016/s1097-2765(01)00369-0 · Cited by 268 · see citing works

STAT3 orchestrates contradictory signals in cytokine-induced G1 to S cell-cycle transition

Fukada, T., Ohtani, T., Yoshida, Y., Shirogane, T., Nishida, K., Nakajima, K., Hibi, M., & Hirano, T. (1998) · The EMBO Journal · doi:10.1093/emboj/17.22.6670 · Cited by 247 · see citing works

SHP2 and SOCS3 Contribute to Tyr-759-dependent Attenuation of Interleukin-6 Signaling through gp130

Lehmann, U., Schmitz, J., Weissenbach, M., Sobota, R. M., Hörtner, M., Friederichs, K., Behrmann, I., Tsiaris, W., Sasaki, A., Schneider-Mergener, J., et al. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m210552200 · Cited by 236 · see citing works

Serine Phosphorylation and Negative Regulation of Stat3 by JNK

Lim, C. P., & Cao, X. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.43.31055 · Cited by 225 · see citing works

Protein Kinase C δ Associates with and Phosphorylates Stat3 in an Interleukin-6-dependent Manner*

Jain, N., Zhang, T., Wei, H.-K., Li, W.-Q., & Cao, X. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.34.24392 · Cited by 222 · see citing works

Systems-level interactions between insulin–EGF networks amplify mitogenic signaling

Borisov, N., Aksamitiene, E., Kiyatkin, A., Legewie, S., Berkhout, J., Maiwald, T., Kaimachnikov, N. P., Timmer, J., Hoek, J. B., & Kholodenko, B. N. (2009) · Molecular Systems Biology · doi:10.1038/msb.2009.19 · Cited by 222 · see citing works

A Novel Role for Gab1 and SHP2 in Epidermal Growth Factor-induced Ras Activation

Montagner, A., Yart, A., Dance, M., Perret, B., Salles, J., & Raynal, P. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m410012200 · Cited by 205 · see citing works

Conditional Inhibition of the Mitogen-activated Protein Kinase Cascade by Wortmannin

Duckworth, B. C., & Cantley, L. C. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.44.27665 · Cited by 200 · see citing works

Essential role of STAT3 in postnatal survival and growth revealed by mice lacking STAT3 serine 727 phosphorylation

Shen, Y., Schlessinger, K., Zhu, X., Meffre, E., Quimby, F., Levy, D. E., & Darnell, J. E. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.1.407-419.2004 · Cited by 200 · see citing works

Differential Activation of Acute Phase Response Factor/Stat3 and Stat1 via the Cytoplasmic Domain of the Interleukin 6 Signal Transducer gp130

Hemmann, U., Gerhartz, C., Heesel, B., Sasse, J., Kurapkat, G., Grötzinger, J., Wollmer, A., Zhong, Z., Darnell, J., Graeve, L., et al. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.12999 · Cited by 197 · see citing works

Noonan syndrome and related disorders: dysregulated RAS-mitogen activated protein kinase signal transduction

Gelb, B. D., & Tartaglia, M. (2006) · Human Molecular Genetics · doi:10.1093/hmg/ddl197 · Cited by 197 · see citing works

Scaffolding Protein Grb2-associated Binder 1 Sustains Epidermal Growth Factor-induced Mitogenic and Survival Signaling by Multiple Positive Feedback Loops

Kiyatkin, A., Aksamitiene, E., Markevich, N. I., Borisov, N. M., Hoek, J. B., & Kholodenko, B. N. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m600482200 · Cited by 195 · see citing works

Gastric cancer development in mice lacking the SHP2 binding site on the IL-6 family co-receptor gp130

Judd, L. M., Alderman, B. M., Howlett, M., Shulkes, A., Dow, C., Moverley, J., Grail, D., Jenkins, B. J., Ernst, M., & Giraud, A. S. (2003) · Gastroenterology · doi:10.1053/j.gastro.2003.10.066 · Cited by 180 · see citing works

Activation of the protein tyrosine phosphatase SHP2 via the interleukin-6 signal transducing receptor protein gp130 requires tyrosine kinase Jak1 and limits acute-phase protein expression

SCHAPER, F., GENDO, C., ECK, M., SCHMITZ, J., GRIMM, C., ANHUF, D., KERR, I. M., & HEINRICH, P. C. (1998) · Biochemical Journal · doi:10.1042/bj3350557 · Cited by 178 · see citing works

Interleukin-6/Glycoprotein 130-dependent Pathways Are Protective during Liver Regeneration

Wüestefeld, T., Klein, C., Streetz, K. L., Betz, U. A. K., Lauber, J., Buer, J., Manns, M. P., Müller, W., & Trautwein, C. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m208470200 · Cited by 176 · see citing works

Function, regulation and pathological roles of the Gab/DOS docking proteins

Wöhrle, F. U., Daly, R. J., & Brummer, T. (2009) · Cell Communication and Signaling · doi:10.1186/1478-811x-7-22 · Cited by 171 · see citing works

SHP-2 Is a Dual-specificity Phosphatase Involved in Stat1 Dephosphorylation at Both Tyrosine and Serine Residues in Nuclei

Wu, T., Hong, Y. K., Wang, X., Ling, M. Y., Dragoi, A. M., Chung, A. S., Campbell, A. G., Han, Z.-Y., Feng, G., & Chin, Y. E. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207536200 · Cited by 170 · see citing works

A Key Role for gp130 Expressed on Peripheral Sensory Nerves in Pathological Pain

Andratsch, M., Mair, N., Constantin, C., Scherbakov, N., Benetti, C., Quarta, S., Vogl, C., Sailer, C. A., Üçeyler, N., Brockhaus, J., et al. (2009) · Journal of Neuroscience · doi:10.1523/jneurosci.1822-09.2009 · Cited by 159 · see citing works

Exchange Protein Activated by Cyclic AMP (Epac)-Mediated Induction of Suppressor of Cytokine Signaling 3 (SOCS-3) in Vascular Endothelial Cells

Sands, W. A., Woolson, H. D., Milne, G. R., Rutherford, C. L., & Palmer, T. M. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00207-06 · Cited by 156 · see citing works

A Critical Role for Phosphoinositide 3-Kinase Upstream of Gab1 and SHP2 in the Activation of Ras and Mitogen-activated Protein Kinases by Epidermal Growth Factor

Yart, A., Laffargue, M., Mayeux, P., Chrétien, S., Peres, C., Tonks, N. K., Roche, S., Payrastre, B., Chap, H., & Raynal, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m006966200 · Cited by 147 · see citing works

Germ-line and somatic PTPN11 mutations in human disease

Tartaglia, M., & Gelb, B. D. (2005) · European Journal of Medical Genetics · doi:10.1016/j.ejmg.2005.03.001 · Cited by 141 · see citing works

STAT3 Is a Serine Kinase Target in T Lymphocytes

Ng, J., & Cantrell, D. A. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.39.24542 · Cited by 141 · see citing works

The protein tyrosine phosphatase SHP-2 negatively regulates ciliary neurotrophic factor induction of gene expression.

Symes, A., Stahl, N., Reeves, S. A., Farruggella, T., Servidei, T., Gearan, T., Yancopouloš, G., & Fink, J. (1997) · Current Biology · doi:10.1016/s0960-9822(06)00298-3 · Cited by 133 · see citing works

SnapShot: Network Motifs

Shoval, O., & Alon, U. S. (2010) · Cell · doi:10.1016/j.cell.2010.09.050 · Cited by 126 · see citing works

Ser727-dependent transcriptional activation by association of p300 with STAT3 upon IL-6 stimulation

Schuringa, J.-J., Schepers, H., Vellenga, E., & Kruijer, W. (2001) · FEBS Letters · doi:10.1016/s0014-5793(01)02354-7 · Cited by 124 · see citing works

Protein Tyrosine Phosphatase 2 (SHP-2) Moderates Signaling by gp130 but Is Not Required for the Induction of Acute-Phase Plasma Protein Genes in Hepatic Cells

Kim, H., Hawley, T. S., Hawley, R. G., & Baumann, H. (1998) · Molecular and Cellular Biology · doi:10.1128/mcb.18.3.1525 · Cited by 119 · see citing works

Concerted Functions of Gab1 and Shp2 in Liver Regeneration and Hepatoprotection

Bard-Chapeau, E. A., Yuan, J., Droin, N. M., Long, S., Zhang, E. E., Nguyen, T. V., & Feng, G. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.02253-05 · Cited by 115 · see citing works

Functional Effects of PTPN11 (SHP2) Mutations Causing LEOPARD Syndrome on Epidermal Growth Factor-Induced Phosphoinositide 3-Kinase/AKT/Glycogen Synthase Kinase 3β Signaling

Édouard, T., Combier, J., Nédélec, A., Bel-Vialar, S., Metrich, M., Conte-Auriol, F., Lyonnet, S., Parfait, B., Tauber, M., Salles, J., et al. (2010) · Molecular and Cellular Biology · doi:10.1128/mcb.00646-09 · Cited by 101 · see citing works

Interleukin-6-induced STAT3 transactivation and Ser727 phosphorylation involves Vav, Rac-1 and the kinase SEK-1/MKK-4 as signal transduction components

Schuringa, J. J., Jonk, L. J. C., Dokter, W. H. A., Vellenga, E., & Kruijer, W. (2000) · Biochemical Journal · doi:10.1042/bj3470089 · Cited by 99 · see citing works

Listeria monocytogenes Modulates Macrophage Cytokine Responses Through STAT Serine Phosphorylation and the Induction of Suppressor of Cytokine Signaling 3

Stoiber, D., Stockinger, S., Steinlein, P., Kovařík, J., & Decker, T. (2001) · The Journal of Immunology · doi:10.4049/jimmunol.166.1.466 · Cited by 96 · see citing works

The cytoplasmic tyrosine motifs in full-length glycoprotein 130 have different roles in IL-6 signal transduction

Schmitz, J., Dahmen, H., Grimm, C., Gendo, C., Müller-Newen, G., Heinrich, P. C., & Schaper, F. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.164.2.848 · Cited by 92 · see citing works

Pathologic consequences of STAT3 hyperactivation by IL-6 and IL-11 during hematopoiesis and lymphopoiesis

Jenkins, B. J., Roberts, A. W., Greenhill, C., Najdovska, M., Lundgren–May, T., Robb, L. G., Grail, D., & Ernst, M. (2006) · Blood · doi:10.1182/blood-2006-08-040352 · Cited by 90 · see citing works

The threshold of gp130-dependent STAT3 signaling is critical for normal regulation of hematopoiesis

Jenkins, B. J., Roberts, A. W., Najdovska, M., Grail, D., & Ernst, M. (2005) · Blood · doi:10.1182/blood-2004-09-3751 · Cited by 85 · see citing works

Sequential Activation of Rac-1, SEK-1/MKK-4, and Protein Kinase Cδ Is Required for Interleukin-6-induced STAT3 Ser-727 Phosphorylation and Transactivation

Schuringa, J. J., Dekker, L. V., Vellenga, E., & Kruijer, W. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m009821200 · Cited by 81 · see citing works

The Carboxyl-terminal Region of STAT3 Controls Gene Induction by the Mouse Haptoglobin Promoter

Kim, H., & Baumann, H. (1997) · Journal of Biological Chemistry · doi:10.1074/jbc.272.23.14571 · Cited by 68 · see citing works

Critical Role for Hematopoietic Cell Kinase (Hck)-mediated Phosphorylation of Gab1 and Gab2 Docking Proteins in Interleukin 6-induced Proliferation and Survival of Multiple Myeloma Cells

Podar, K., Mostoslavsky, G., Sattler, M., Tai, Y., Hayashi, T., Catley, L. P., Hideshima, T., Mulligan, R. C., Chauhan, D., & Anderson, K. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m305783200 · Cited by 67 · see citing works

The YXXQ motif in gp 130 is crucial for STAT3 phosphorylation at Ser727 through an H7-sensitive kinase pathway

Abe, K., Hirai, M., Mizuno, K., Higashi, N., Sekimoto, T., Miki, T., Hirano, T., & Nakajima, K. (2001) · Oncogene · doi:10.1038/sj.onc.1204461 · Cited by 65 · see citing works

Negative Regulation of Stat3 by Activating PTPN11 Mutants Contributes to the Pathogenesis of Noonan Syndrome and Juvenile Myelomonocytic Leukemia

Zhang, W., Chan, R. J., Chen, H., Yang, Z., He, Y., Zhang, X., Luo, Y., Yin, F., Moh, A., Miller, L., et al. (2009) · Journal of Biological Chemistry · doi:10.1074/jbc.m109.020495 · Cited by 63 · see citing works

Perspectives for the use of structural information and chemical genetics to develop inhibitors of Janus kinases

Haan, C., Behrmann, I., & Haan, S. (2010) · Journal of Cellular and Molecular Medicine · doi:10.1111/j.1582-4934.2010.01018.x · Cited by 63 · see citing works

Signaling through a Novel Domain of gp130 Mediates Cell Proliferation and Activation of Hck and Erk Kinases

Schaeffer, M., Schneiderbauer, M. M., Weidler, S., Tavares, R., Warmuth, M., de Vos, G., & Hallek, M. J. (2001) · Molecular and Cellular Biology · doi:10.1128/mcb.21.23.8068-8081.2001 · Cited by 62 · see citing works

Inhibition of IFN-γ-Induced STAT1 Tyrosine Phosphorylation by Human CMV Is Mediated by SHP2

Baron, M., & Davignon, J. (2008) · The Journal of Immunology · doi:10.4049/jimmunol.181.8.5530 · Cited by 61 · see citing works

Conditional Deletion of Shp2 in the Mammary Gland Leads to Impaired Lobulo-alveolar Outgrowth and Attenuated Stat5 Activation

Ke, Y., Lesperance, J., Zhang, E. E., Bard-Chapeau, E. A., Oshima, R. G., Muller, W. J., & Feng, G. (2006) · Journal of Biological Chemistry · doi:10.1074/jbc.m607325200 · Cited by 61 · see citing works

Syp Associates with gp130 and Janus Kinase 2 in Response to Interleukin-11 in 3T3-L1 Mouse Preadipocytes

Fuhrer, D. K., Feng, G., & Yang, Y. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.42.24826 · Cited by 61 · see citing works

Chemical Dissection of the Effects of Tyrosine Phosphorylation of SHP-2

Lu, W., Shen, K., & Cole, P. A. (2003) · Biochemistry · doi:10.1021/bi0340144 · Cited by 59 · see citing works

Signal Transduction of IL-6, Leukemia-Inhibitory Factor, and Oncostatin M: Structural Receptor Requirements for Signal Attenuation

Anhuf, D., Weißenbach, M., Schmitz, J., Sobota, R. M., Hermanns, H. M., Radtke, S., Linnemann, S., Behrmann, I., Heinrich, P. C., & Schaper, F. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.5.2535 · Cited by 57 · see citing works

A new mechanism for the regulation of Gab1 recruitment to the plasma membrane

Eulenfeld, R., & Schaper, F. (2009) · Journal of Cell Science · doi:10.1242/jcs.037226 · Cited by 57 · see citing works

PI3 kinase is important for Ras, MEK and Erk activation of Epo-stimulated human erythroid progenitors

Schmidt, E. K., Fichelson, S., & Feller, S. M. (2004) · BMC Biology · doi:10.1186/1741-7007-2-7 · Cited by 55 · see citing works

Signal Strength Dictates Phosphoinositide 3-Kinase Contribution to Ras/Extracellular Signal-Regulated Kinase 1 and 2 Activation via Differential Gab1/Shp2 Recruitment: Consequences for Resistance to Epidermal Growth Factor Receptor Inhibition

Sampaio, C. S., Dance, M., Montagner, A., Édouard, T., Malet, N., Perret, B., Yart, A., Salles, J., & Raynal, P. (2007) · Molecular and Cellular Biology · doi:10.1128/mcb.01318-07 · Cited by 54 · see citing works

How do Shp2 mutations that oppositely influence its biochemical activity result in syndromes with overlapping symptoms?

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Toll-like receptor 4 and myeloid differentiation factor 88 provide mechanistic insights into the cause and effects of interleukin-6 activation in mouse liver regeneration

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The STAT3 Inhibitor Galiellalactone Reduces IL6-Mediated AR Activity in Benign and Malignant Prostate Models

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Proteolytic control of Interleukin-11 and Interleukin-6 biology

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Activating mutations of the gp130/JAK/STAT pathway in human diseases

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Acrylamide inhibits cellular differentiation of human neuroblastoma and glioblastoma cells

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Subcutaneous tocilizumab in rheumatoid arthritis: findings from the common-framework phase 4 study programme TOZURA conducted in 22 countries

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STAT3 promotes survival of mutant photoreceptors in inherited photoreceptor degeneration models

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PM2.5 aggravates diabetes via the systemically activated IL-6-mediated STAT3/SOCS3 pathway in rats’ liver

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Interleukin-6 promotes primitive endoderm development in bovine blastocysts

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Effects of Interleukin-6 on STAT3-regulated signaling in oral cancer and as a prognosticator of patient survival

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Bone morphogenetic protein‐6 induces castration resistance in prostate cancer cells through tumor infiltrating macrophages

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Differentially expressed JAK-STAT signaling pathway genes and target microRNAs in the spleen of necrotic enteritis-afflicted chicken lines

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SOCS3 limits TNF and endotoxin-induced endothelial dysfunction by blocking a required autocrine interleukin-6 signal in human endothelial cells

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