Three-dimensional structure of the Stat3β homodimer bound to DNA

PROCHECK: a program to check the stereochemical quality of protein structures

Laskowski, R. A., MacArthur, M. W., Moss, D. S., & Thornton, J. M. (1993) · Journal of Applied Crystallography · doi:10.1107/s0021889892009944 · Cited by 24,581

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

Interferon activation of the transcription factor Stat91 involves dimerization through SH2-phosphotyrosyl peptide interactions

Shuai, K., Horvath, C. M., Huang, L. H. T., Qureshi, S. A., Cowburn, D., & Darnell, J. E. (1994) · Cell · doi:10.1016/0092-8674(94)90357-3 · Cited by 807

Structure of the DNA-binding domains from NFAT, Fos and Jun bound specifically to DNA

Chen, L., Glover, J. N. M., Hogan, P. G., Rao, A., & Harrison, S. C. (1998) · Nature · doi:10.1038/32100 · Cited by 521

STAT3β, a splice variant of transcription factor STAT3, is a dominant negative regulator of transcription

Caldenhoven, E., van Dijk, T. B., Solari, R., Armstrong, J., Raaijmakers, J. A. M., Lammers, J.-W. J., Koenderman, L., & de Groot, R. P. (1996) · Journal of Biological Chemistry · doi:10.1074/jbc.271.22.13221 · Cited by 373

Principles of interleukin (IL)-6-type cytokine signalling and its regulation

HEINRICH, P. C., BEHRMANN, I., HAAN, S., HERMANNS, H. M., MÜLLER-NEWEN, G., & SCHAPER, F. (2003) · Biochemical Journal · doi:10.1042/bj20030407 · Cited by 3,272

STATs: transcriptional control and biological impact

Levy, D. E., & Darnell, J. E. (2002) · Nature Reviews Molecular Cell Biology · doi:10.1038/nrm909 · Cited by 3,201

Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway

HEINRICH, P. C., BEHRMANN, I., MÜLLER-NEWEN, G., SCHAPER, F., & GRAEVE, L. (1998) · Biochemical Journal · doi:10.1042/bj3340297 · Cited by 2,130

STATs in oncogenesis

Bowman, T., Garcia, R., Turkson, J., & Jove, R. (2000) · Oncogene · doi:10.1038/sj.onc.1203527 · Cited by 1,743

Stattic: a small-molecule inhibitor of STAT3 activation and dimerization

Schust, J., Sperl, B., Hollis, A., Mayer, T. U., & Berg, T. (2006) · Chemistry & Biology · doi:10.1016/j.chembiol.2006.09.018 · Cited by 1,105

Stat3 Dimerization Regulated by Reversible Acetylation of a Single Lysine Residue

Yuan, Z.-L., Guan, Y.-J., Chatterjee, D., & Chin, Y. E. (2005) · Science · doi:10.1126/science.1105166 · Cited by 790

STAT3 signaling in immunity

Hillmer, E. J., Zhang, H., Li, H. S., & Watowich, S. S. (2016) · Cytokine & Growth Factor Reviews · doi:10.1016/j.cytogfr.2016.05.001 · Cited by 740

The JAK‐binding protein JAB inhibits Janus tyrosine kinase activity through binding in the activation loop

Yasukawa, H., Misawa, H., Sakamoto, H., Masuhara, M., Sasaki, A., Wakioka, T., Ohtsuka, S., Imaizumi, T., Matsuda, T., Ihle, J. N., et al. (1999) · The EMBO Journal · doi:10.1093/emboj/18.5.1309 · Cited by 719

The Stat family in cytokine signaling

Ihle, J. N. (2001) · Current Opinion in Cell Biology · doi:10.1016/s0955-0674(00)00199-x · Cited by 713

A Potent and Selective Small-Molecule Degrader of STAT3 Achieves Complete Tumor Regression In Vivo

Bai, L., Zhou, H., Xu, R., Zhao, Y., Chinnaswamy, K., McEachern, D., Chen, J., Yang, C.-Y., Liu, Z., Wang, M., et al. (2019) · Cancer Cell · doi:10.1016/j.ccell.2019.10.002 · Cited by 652

STAT proteins: novel molecular targets for cancer drug discovery

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

A low-molecular-weight compound discovered through virtual database screening inhibits Stat3 function in breast cancer cells

Song, H., Wang, R., Wang, S., & Lin, J. (2005) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0409894102 · Cited by 504

Biology and significance of the JAK/STAT signalling pathways

Kiu, H., & Nicholson, S. E. (2012) · Growth Factors · doi:10.3109/08977194.2012.660936 · Cited by 470

Novel roles of unphosphorylated STAT3 in oncogenesis and transcriptional regulation

Yang, J., Chatterjee-Kishore, M., Staugaitis, S. M., Nguyen, H., Schlessinger, K., Levy, D. E., & Stark, G. R. (2005) · Cancer Research · doi:10.1158/0008-5472.939.65.3 · Cited by 405

Activation of the androgen receptor N-terminal domain by interleukin-6 via MAPK and STAT3 signal transduction pathways.

Ueda, T., Bruchovsky, N., & Sadar, M. D. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108255200 · Cited by 381

Modulation of STAT signaling by STAT-interacting proteins

Shuai, K. (2000) · Oncogene · doi:10.1038/sj.onc.1203522 · Cited by 379

Tracking STAT nuclear traffic

Reich, N. C., & Liu, L. (2006) · Nature Reviews Immunology · doi:10.1038/nri1885 · Cited by 376

STAT signaling in head and neck cancer

Song, J. I., & Grandis, J. R. (2000) · Oncogene · doi:10.1038/sj.onc.1203483 · Cited by 374

DNA Binding Specificity of Different STAT Proteins

Ehret, G. B., Reichenbach, P., Schindler, U., Horvath, C. M., Fritz, S., Nabholz, M., & Bucher, P. (2001) · Journal of Biological Chemistry · doi:10.1074/jbc.m001748200 · Cited by 369

Roles of unphosphorylated STATs in signaling

Yang, J., & Stark, G. R. (2008) · Cell Research · doi:10.1038/cr.2008.41 · Cited by 347

Reversible methylation of promoter-bound STAT3 by histone-modifying enzymes

Yang, J., Huang, J., Dasgupta, M., Sears, N., Miyagi, M., Wang, B., Chance, M. R., Chen, X., Du, Y., Wang, Y., et al. (2010) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1016147107 · Cited by 340

First-in-Human Trial of a STAT3 Decoy Oligonucleotide in Head and Neck Tumors: Implications for Cancer Therapy

Sen, M., Thomas, S. M., Kim, S., Yeh, J. I., Ferris, R. L., Johnson, J. T., Duvvuri, U., Lee, J., Sahu, N., Joyce, S., et al. (2012) · Cancer Discovery · doi:10.1158/2159-8290.cd-12-0191 · Cited by 313

Autoregulation of pituitary corticotroph SOCS-3 expression: Characterization of the murine SOCS-3 promoter

Auernhammer, C. J., Bousquet, C., & Melmed, S. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.12.6964 · Cited by 284

Constitutively activated Stat3 protects fibroblasts from serum withdrawal and UV-induced apoptosis and antagonizes the proapoptotic effects of activated Stat1

Shen, Y., Devgan, G., Darnell, J. E., & Bromberg, J. F. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.98.4.1543 · Cited by 249

Structure-Based Discovery of SD-36 as a Potent, Selective, and Efficacious PROTAC Degrader of STAT3 Protein

Zhou, H., Bai, L., Xu, R., Zhao, Y., Chen, J., McEachern, D., Chinnaswamy, K., Wen, B., Dai, L., Kumar, P., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.9b01530 · Cited by 233

The STAT3 pathway as a therapeutic target in head and neck cancer: barriers and innovations

Geiger, J. L., Grandis, J. R., & Bauman, J. E. (2016) · Oral Oncology · doi:10.1016/j.oraloncology.2015.11.022 · Cited by 193

Arginine/Lysine-rich Nuclear Localization Signals Mediate Interactions between Dimeric STATs and Importin α5

Fagerlund, R., Melén, K., Kinnunen, L., & Julkunen, I. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m202943200 · Cited by 183

A novel small-molecule disrupts Stat3 SH2 domain–phosphotyrosine interactions and Stat3-dependent tumor processes

Zhang, X., Yue, P., Fletcher, S., Zhao, W., Gunning, P. T., & Turkson, J. (2010) · Biochemical Pharmacology · doi:10.1016/j.bcp.2010.01.001 · Cited by 179

The Structure of SOCS3 Reveals the Basis of the Extended SH2 Domain Function and Identifies an Unstructured Insertion That Regulates Stability

Babon, J. J., McManus, E. J., Yao, S., DeSouza, D. P., Mielke, L. A., Sprigg, N. S., Willson, T. A., Hilton, D. J., Nicola, N. A., Baca, M., et al. (2006) · Molecular Cell · doi:10.1016/j.molcel.2006.03.024 · Cited by 163

Loops Govern SH2 Domain Specificity by Controlling Access to Binding Pockets

Kaneko, T., Huang, H., Zhao, B., Li, L., Liu, H., Voss, C. K., Wu, C., Schiller, M. R., & Li, S. S.-C. (2010) · Science Signaling · doi:10.1126/scisignal.2000796 · Cited by 146

The coiled-coil domain of Stat3 is essential for its SH2 domain-mediated receptor binding and subsequent activation induced by epidermal growth factor and interleukin-6

Zhang, T., Kee, W. H., Seow, K. T., Fung, W., & Cao, X. (2000) · Molecular and Cellular Biology · doi:10.1128/mcb.20.19.7132-7139.2000 · Cited by 150

Mitochondrial Stat3, the need for design thinking

Yang, R., & Rincon, M. (2016) · International Journal of Biological Sciences · doi:10.7150/ijbs.15153 · Cited by 147

Real time analysis of STAT3 nucleocytoplasmic shuttling

Pranada, A. L., Metz, S., Herrmann, A., Heinrich, P. C., & Müller-Newen, G. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312530200 · Cited by 140

Stat3 Inhibitor Stattic Exhibits Potent Antitumor Activity and Induces Chemo- and Radio-Sensitivity in Nasopharyngeal Carcinoma

Pan, Y., Zhou, F., Zhang, R., & Claret, F. X. (2013) · PLoS ONE · doi:10.1371/journal.pone.0054565 · Cited by 132

Identification of a High-Affinity Phosphopeptide Inhibitor of Stat3

Ren, Z., Cabell, L. A., Schaefer, T. S., & McMurray, J. S. (2003) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(02)01050-8 · Cited by 128

Structure of the DNA-Bound T-Box Domain of Human TBX3, a Transcription Factor Responsible for Ulnar-Mammary Syndrome

Coll, M., Seidman, J. G., & Müller, C. W. (2002) · Structure · doi:10.1016/s0969-2126(02)00722-0 · Cited by 121

A Novel Sequence in the Coiled-coil Domain of Stat3 Essential for Its Nuclear Translocation

Ma, J., Zhang, T., Novotny-Diermayr, V., Tan, A. L. C., & Cao, X. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m304196200 · Cited by 110

Identification of novel direct Stat3 target genes for control of growth and differentiation

Snyder, M., Huang, X.-Y., & Zhang, J. J. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m706976200 · Cited by 108

Extended knobs-into-holes packing in classical and complex coiled-coil assemblies☆

Walshaw, J., & Woolfson, D. N. (2003) · Journal of Structural Biology · doi:10.1016/j.jsb.2003.10.014 · Cited by 104

Mitochondrial dysfunction induced by a SH2 domain-targeting STAT3 inhibitor leads to metabolic synthetic lethality in cancer cells

Genini, D., Brambilla, L., Laurini, E., Merulla, J., Civenni, G., Pandit, S., D'Antuono, R., Perez, L., Levy, D. E., Pricl, S., et al. (2017) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1615730114 · Cited by 106

IL-6 signaling via the STAT3/SOCS3 pathway: functional analysis of the conserved STAT3 N-domain

Zhang, L., Badgwell, D. B., Bevers, J. J., Schlessinger, K., Murray, P. J., Levy, D. E., & Watowich, S. S. (2006) · Molecular and Cellular Biochemistry · doi:10.1007/s11010-006-9137-3 · Cited by 89

S-Glutathionylation at Cys328 and Cys542 impairs STAT3 phosphorylation

Butturini, E., Darra, E., Chiavegato, G., Cellini, B., Cozzolino, F., Monti, M., Pucci, P., Dell’Orco, D., & Mariotto, S. (2014) · ACS Chemical Biology · doi:10.1021/cb500407d · Cited by 82

The role of the N-terminal domain in dimerization and nucleocytoplasmic shuttling of latent STAT3

Vogt, M., Domoszlai, T., Kleshchanok, D., Lehmann, S., Schmitt, A., Poli, V., Richtering, W., & Müller-Newen, G. (2011) · Journal of Cell Science · doi:10.1242/jcs.072520 · Cited by 80

A STAT3 dimer formed by inter-chain disulphide bridging during oxidative stress

Li, L., & Shaw, P. E. (2004) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2004.08.014 · Cited by 79

Anti-DNA autoantibodies and systemic lupus erythematosus

Blatt, N. B., & Glick, G. D. (1999) · Pharmacology & Therapeutics · doi:10.1016/s0163-7258(99)00022-4 · Cited by 60

Mutations in the linker domain affect phospho-STAT3 function and suggest targets for interrupting STAT3 activity

Mertens, C., Haripal, B., Klinge, S., & Darnell, J. E. (2015) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1515876112 · Cited by 59

Structural requirements for signal transducer and activator of transcription 3 binding to phosphotyrosine ligands containing the YXXQ motif

Shao, H., Xu, X., Mastrangelo, M.-A. A., Jing, N., Cook, R. G., Legge, G. B., & Tweardy, D. J. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m314037200 · Cited by 53

Investigation of the protein alkylation sites of the STAT3:STAT3 inhibitor Stattic by mass spectrometry

Heidelberger, S., Zinzalla, G., Antonow, D., Essex, S., Piku Basu, B., Palmer, J., Husby, J., Jackson, P. J. M., Rahman, K. M., Wilderspin, A. F., et al. (2013) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2013.05.066 · Cited by 52

Design of Conditionally Active STATs: Insights into STAT Activation and Gene Regulatory Function

Milocco, L. H., Haslam, J. A., Rosen, J., & Seidel, H. M. (1999) · Molecular and Cellular Biology · doi:10.1128/mcb.19.4.2913 · Cited by 52

Changes in signal transducer and activator of transcription 3 (STAT3) dynamics induced by complexation with pharmacological inhibitors of Src homology 2 (SH2) domain dimerization

Resetca, D., Haftchenary, S., Gunning, P. T., & Wilson, D. J. (2014) · Journal of Biological Chemistry · doi:10.1074/jbc.m114.595454 · Cited by 47

Signal integration and gene induction by a functionally distinct STAT3 phosphoform

Waitkus, M. S., Chandrasekharan, U. M., Willard, B., Tee, T. L., Hsieh, J. K., Przybycin, C. G., Rini, B. I., & DiCorleto, P. E. (2014) · Molecular and Cellular Biology · doi:10.1128/mcb.00034-14 · Cited by 45

Protein stabilization improves STAT3 function in autosomal dominant hyper-IgE syndrome

Bocchini, C. E., Nahmod, K., Katsonis, P., Kim, S., Kasembeli, M. M., Freeman, A., Lichtarge, O., Makedonas, G., & Tweardy, D. J. (2016) · Blood · doi:10.1182/blood-2016-02-702373 · Cited by 36

Allosteric communication across STAT3 domains associated with STAT3 function and disease-causing mutation

Namanja, A. T., Wang, J., Buettner, R., Colson, L., & Chen, Y. (2016) · Journal of Molecular Biology · doi:10.1016/j.jmb.2016.01.003 · Cited by 31

Design, synthesis, and evaluation of peptidomimetics containing Freidinger lactams as STAT3 inhibitors

Gomez, C., Bai, L., Zhang, J., Nikolovska-Coleska, Z., Chen, J., Yi, H., & Wang, S. (2009) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2009.01.091 · Cited by 26

Target specificity, in vivo pharmacokinetics, and efficacy of the putative STAT3 inhibitor LY5 in osteosarcoma, Ewing's sarcoma, and rhabdomyosarcoma

Yu, P. Y., Gardner, H. L., Roberts, R., Cam, H., Hariharan, S., Ren, L., LeBlanc, A. K., Xiao, H., Lin, J., Guttridge, D. C., et al. (2017) · PLOS ONE · doi:10.1371/journal.pone.0181885 · Cited by 17