Cited by 982Cytokine Signaling Pathways and InteractionsGenomics and Chromatin DynamicsPsoriasis: Treatment and Pathogenesis

The DOI matches its Crossref record; 17 of the 17 references it cites were found in a registry or an index.

Specific Inhibition of Stat3 Signal Transduction by PIAS3

Chung, Chan D., Liao, Jiayu, Liu, Bin, Rao, Xiaoping, Jay, Philippe, Berta, Philippe, Shuai, Ke·1997·Science

DOI 10.1126/science.278.5344.1803

Open this paper in CoChat — free account

Abstract

The signal transducer and activator of transcription-3 (Stat3) protein is activated by the interleukin 6 (IL-6) family of cytokines, epidermal growth factor, and leptin. A protein named PIAS3 (protein inhibitor of activated STAT) that binds to Stat3 was isolated and characterized. The association of PIAS3 with Stat3 in vivo was only observed in cells stimulated with ligands that cause the activation of Stat3. PIAS3 blocked the DNA-binding activity of Stat3 and inhibited Stat3-mediated gene activation. Although Stat1 is also phosphorylated in response to IL-6, PIAS3 did not interact with Stat1 or affect its DNA-binding or transcriptional activity. The results indicate that PIAS3 is a specific inhibitor of Stat3.

Integrity signals

Registry

Crossref · 10.1126/science.278.5344.1803

Cites

17 of 17 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

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?

Positional cloning of the mouse obese gene and its human homologue
Zhang, Y., Proenca, R., Maffei, M., Barone, M., Leopold, L., & Friedman, J. M. (1994) · Nature · doi:10.1038/372425a0 · Cited by 13,419
Jak-STAT Pathways and Transcriptional Activation in Response to IFNs and Other Extracellular Signaling Proteins
Darnell, J. E., Kerr, L. M., & Stark, G. R. (1994) · Science · doi:10.1126/science.8197455 · Cited by 6,080
Stat3: a STAT Family Member Activated by Tyrosine Phosphorylation in Response to Epidermal Growth Factor and Interleukin-6
Zhong, Z., Wen, Z., & Darnell, J. E. (1994) · Science · doi:10.1126/science.8140422 · Cited by 2,070
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
TRANSCRIPTIONAL RESPONSES TO POLYPEPTIDE LIGANDS: The JAK-STAT Pathway
Schindler, C., & Darnell, J. E. (1995) · Annual Review of Biochemistry · doi:10.1146/annurev.bi.64.070195.003201 · Cited by 1,808
Targeted disruption of the mouse Stat3 gene leads to early embryonic lethality
Takeda, K., Noguchi, K., Shi, W., Tanaka, T., Matsumoto, M., Yoshida, N., Kishimoto, T., & Akira, S. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.8.3801 · Cited by 1,323
Cytokine receptor signalling
Ihle, J. N. (1995) · Nature · doi:10.1038/377591a0 · Cited by 1,201
Leptin activation of Stat3 in the hypothalamus of wild-type and ob/ob mice but not db/db mice.
Vaisse, C., Halaas, J. L., Horvath, C. M., Darnell, J. E., Stoffel, M., & Friedman, J. M. (1996) · Nature Genetics · doi:10.1038/ng0996-95 · Cited by 1,086
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
Molecular cloning of APRF, a novel IFN-stimulated gene factor 3 p91-related transcription factor involved in the gp130-mediated signaling pathway
Akira, S., Nishio, Y., Inoue, M., Wang, X.-J., We, S., Matsusaka, T., Yoshida, K., Sudo, T., Naruto, M., & Kishimoto, T. (1994) · Cell · doi:10.1016/0092-8674(94)90235-6 · Cited by 1,019

Show all 17 references

Research works printed but not linked: 2

Leveillard T., Verma I. M., Gene Expr. 3, 135 (1993).
Chen C. A., Okayama H., Biotechniques 6, 632 (1988).

Sorted by citations

Items 501–600 of 982

GSTP1 negatively regulates Stat3 activation in epidermal growth factor signaling
Kou, X., Chen, N., Feng, Z., Luo, L., & Yin, Z. (2012) · Oncology Letters · doi:10.3892/ol.2012.1098 · Cited by 36
Regulation of IL-6 Signaling by p53: STAT3- and STAT5-Masking in p53-Val135-Containing Human Hepatoma Hep3B Cell Lines
Rayanade, R. J., Ndubuisi, M. I., Etlinger, J. D., & Sehgal, P. B. (1998) · The Journal of Immunology · doi:10.4049/jimmunol.161.1.325 · Cited by 35
Activation and inactivation of signal transducers and activators of transcription by ciliary neurotrophic factor in neuroblastoma cells
Kaur, N., Wohlhueter, A. L., & Halvorsen, S. W. (2002) · Cellular Signalling · doi:10.1016/s0898-6568(01)00280-7 · Cited by 35
Discovery of a Highly Potent and Orally Bioavailable STAT3 Dual Phosphorylation Inhibitor for Pancreatic Cancer Treatment
He, P., Bian, A., Miao, Y., Jin, W., Chen, H., He, J., Li, L., Sun, Y., Ye, J., Liu, M., et al. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.2c01554 · Cited by 34
The Intracellular Delivery of a Recombinant Peptide Derived from the Acidic Domain of PIAS3 Inhibits STAT3 Transactivation and Induces Tumor Cell Death
Borghouts, C., Tittmann, H., Delis, N., Kirchenbauer, M., Brill, B., & Groner, B. (2010) · Molecular Cancer Research · doi:10.1158/1541-7786.mcr-09-0417 · Cited by 34
SOCS-mediated immunomodulation of natural killer cells
Keating, N., & Nicholson, S. E. (2018) · Cytokine · doi:10.1016/j.cyto.2018.03.033 · Cited by 36
STAT transcription factors in normal and cancer stem cells.
Dorritie, K., Redner, R., & Johnson, D. E. (2014) · Advances in Biological Regulation · doi:10.1016/j.jbior.2014.05.004 · Cited by 34
A Human Skin Model Recapitulates Systemic Sclerosis Dermal Fibrosis and Identifies COL22A1 as a TGFβ Early Response Gene that Mediates Fibroblast to Myofibroblast Transition
Watanabe, T., Baker Frost, D., Mlakar, L., Heywood, J., da Silveira, W. A., Hardiman, G., & Feghali-Bostwick, C. (2019) · Genes · doi:10.3390/genes10020075 · Cited by 33
Interleukin-22 Inhibits Respiratory Syncytial Virus Production by Blocking Virus-Mediated Subversion of Cellular Autophagy
Das, S., Croix, C. M. S., Good, M. L., Chen, J., Zhao, J., Hu, S., Ross, M., Myerburg, M. M., Pilewski, J. M., Williams, J. V., et al. (2020) · iScience · doi:10.1016/j.isci.2020.101256 · Cited by 34
PIAS proteins are involved in the SUMO-1 modification, intracellular translocation and transcriptional repressive activity of RET finger protein
Matsuura, T., Shimono, Y., Kawai, K., Murakami, H., Urano, T., Niwa, Y., Goto, H., & Takahashi, M. (2005) · Experimental Cell Research · doi:10.1016/j.yexcr.2005.04.022 · Cited by 33
Intracellular signalling and antiviral effects of interferons
Heim, M. H. (2000) · Digestive and Liver Disease · doi:10.1016/s1590-8658(00)80831-2 · Cited by 33
Paired Stat6 C-Terminal Transcription Activation Domains Required Both for Inhibition of an IFN-Responsive Promoter and Trans- Activation
Goenka, S., Youn, J., Dzurek, L. M., Schindler, U., Yu‐Lee, L., & Boothby, M. R. (1999) · The Journal of Immunology · doi:10.4049/jimmunol.163.9.4663 · Cited by 33
Regulators of growth hormone signaling
Finidori, J. (2000) · Vitamins and hormones · doi:10.1016/s0083-6729(00)59004-9 · Cited by 33
Down-regulation of ATBF1 activates STAT3 signaling via PIAS3 in pacing-induced HL-1 atrial myocytes
Jiang, Q., Ni, B., Shi, J., Han, Z., Qi, R., Xu, W., Wang, D., Wang, D. W., & Chen, M. (2014) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2014.05.041 · Cited by 32
It takes two to tango: Ubiquitin and SUMO in the DNA damage response
Bologna, S., & Ferrari, S. M. (2013) · Frontiers in Genetics · doi:10.3389/fgene.2013.00106 · Cited by 33
Transcriptional Regulation in Neutrophils: Teaching Old Cells New Tricks
McDonald, P. P. (2004) · Advances in immunology · doi:10.1016/s0065-2776(04)82001-7 · Cited by 32
TRIM8 regulates Nanog via Hsp90β-mediated nuclear translocation of STAT3 in embryonic stem cells
Okumura, F., Okumura, A. J., Matsumoto, M., Nakayama, K. I., & Hatakeyama, S. (2011) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2011.05.013 · Cited by 32
Role of interleukin-6 in Barrett’s esophagus pathogenesis
Dvorak, K. (2013) · World Journal of Gastroenterology · doi:10.3748/wjg.v19.i15.2307 · Cited by 31
IL-6 signaling by STAT3 participates in the change from hyperplasia to neoplasia in NRP-152 and NRP-154 rat prostatic epithelial cells
Barton, B. E., Murphy, T. F., Adem, P. V., Watson, R. A., Irwin, R. J., & Huang, H. F. S. (2001) · BMC Cancer · doi:10.1186/1471-2407-1-19 · Cited by 32
Angiotensin II (AngII) induces the expression of suppressor of cytokine signaling (SOCS)-3 in rat hypothalamus - a mechanism for desensitization of AngII signaling
Torsoni, M. A., Carvalheira, J. B. C., Calegari, V. C., Bezerra, R. M. N., Saad, M., Gontijo, J. A. R., & Velloso, L. A. (2004) · Journal of Endocrinology · doi:10.1677/joe.0.1810117 · Cited by 32
Functional Potentiation of Leptin-Signal Transducer and Activator of Transcription 3 Signaling by the Androgen Receptor
Fan, W., Yanase, T., Nishi, Y., Chiba, S., Okabe, T., Nomura, M., Yoshimatsu, H., Kato, S., Takayanagi, R., & Nawata, H. (2008) · Endocrinology · doi:10.1210/en.2008-0431 · Cited by 32
Nuclear Localization of Duplin, a β-Catenin-binding Protein, Is Essential for Its Inhibitory Activity on the Wnt Signaling Pathway
Kobayashi, M., Kishida, S., Fukui, A., Michiue, T., Miyamoto, Y., Okamoto, T., Yoneda, Y., Asashima, M., & Kikuchi, A. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m108433200 · Cited by 31
Dendritic Cell-Based Tumor Vaccines and Antigen Presentation Attenuators
Evel-Kabler, K., & Chen, S. (2006) · Molecular Therapy · doi:10.1016/j.ymthe.2006.02.009 · Cited by 32
The Janus Kinase Inhibitor, JAB/SOCS-1, Is an Interferon-γ Inducible Gene and Determines the Sensitivity to Interferons
Sakamoto, H., Kinjyo, I., & Yoshimura, A. (2000) · Leukemia & lymphoma/Leukemia and lymphoma · doi:10.3109/10428190009060318 · Cited by 31
Upregulation of SOCS-3 and PIAS-3 Impairs IL-12-Mediated Interferon-Gamma Response in CD56+ T Cells in HCV-Infected Heroin Users
Ye, L., Wang, X., Metzger, D. S., Riedel, E., Montaner, L. J., & Ho, W. (2010) · PLoS ONE · doi:10.1371/journal.pone.0009602 · Cited by 32
Deficiency of β-arrestin1 ameliorates collagen-induced arthritis with impaired T H 17 cell differentiation
Li, J., Wei, B. K., Guo, A., Liu, C., Huang, S., Du, F., Fan, W., Bao, C., & Pei, G. (2013) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.1221608110 · Cited by 31
Two patterns of thrombopoietin signaling suggest no coupling between platelet production and thrombopoietin reactivity in thrombocytopenia-absent radii syndrome
Fiedler, J., Strauß, G., Wannack, M., Schwiebert, S., Seidel, K., Henning, K., Klopocki, E., Schmugge, M., Gaedicke, G., & Schulze, H. (2011) · Haematologica · doi:10.3324/haematol.2011.049619 · Cited by 31
Role of STAT3 Transcription Factor in Pathogenesis of Bronchial Asthma
Аркадьевич, Н. А., Shilovskiy, I. P., Barvinskaia, E. D., Викторович, К. А., Sundukova, M. S., & Khaitov, M. R. (2021) · Biochemistry (Moscow) · doi:10.1134/s0006297921110122 · Cited by 32
Organogenesis and tumorigenesis: Insight from the JAK/STAT pathway in the Drosophila eye
Wang, Y., & Huang, M. (2010) · Developmental Dynamics · doi:10.1002/dvdy.22394 · Cited by 31
Computational models of the JAK1/2-STAT1 signaling
Gambin, A., Charzyńska, A., Ellert‐Miklaszewska, A., & Rybiński, M. (2013) · JAK-STAT · doi:10.4161/jkst.24672 · Cited by 31
PIASy-mediated repression of the Ets-1 is independent of its sumoylation
Nishida, T., Terashima, M., & Fukami, K. (2006) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2006.05.065 · Cited by 33
Expression of the E3 SUMO-1 ligases PIASx and PIAS1 during spermatogenesis in the rat
Yan, W., Santti, H., Jänne, O. A., Palvimo, J. J., & Toppari, J. (2003) · Gene Expression Patterns · doi:10.1016/s1567-133x(03)00045-0 · Cited by 31
Cells Previously Desensitized to Type 1 Interferons Display Different Mechanisms of Activation of Stat-dependent Gene Expression from Naïve Cells
Sakamoto, S., Qin, J., Navarro, A., Gamero, A., Potla, R., Yi, T., Zhu, W., Baker, D. P., Feldman, G., & Larner, A. C. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m309631200 · Cited by 31
Identifying a common molecular mechanism for inhibition of MITF and STAT3 by PIAS3
Levy, C., Lee, Y. N., Nechushtan, H., Schueler‐Furman, O., Sonnenblick, A., Hacohen, S., & Razin, E. (2005) · Blood · doi:10.1182/blood-2005-08-3325 · Cited by 36
The Growth Hormone-binding Protein Is a Location-dependent Cytokine Receptor Transcriptional Enhancer
Graichen, R., Sandstedt, J., Goh, E. L. K., Isaksson, O. G. P., Törnell, J., & Lobie, P. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m207546200 · Cited by 31
Importin Alpha2-Interacting Proteins with Nuclear Roles During Mammalian Spermatogenesis1
Ly-Huynh, J. D., Lieu, K. G., Major, A. T., Whiley, P. A. F., Holt, J. E., Loveland, K. L., & Jans, D. A. (2011) · Biology of Reproduction · doi:10.1095/biolreprod.111.091686 · Cited by 30
The Evolving Picture of Microdeletion/Microduplication Syndromes in the Age of Microarray Analysis: Variable Expressivity and Genomic Complexity
Deak, K. L., Horn, S. R. G.-V., & Rehder, C. W. (2011) · Clinics in Laboratory Medicine · doi:10.1016/j.cll.2011.08.008 · Cited by 30
Identification of Drosophila Genes Modulating Janus Kinase/Signal Transducer and Activator of Transcription Signal Transduction
Mukherjee, T., Schäfer, U., & Zeidler, M. P. (2005) · Genetics · doi:10.1534/genetics.105.046904 · Cited by 30
The SUMO Ubiquitin-Protein Isopeptide Ligase Family Member Miz1/PIASxβ/Siz2 Is a Transcriptional Cofactor for TFII-I
Tussié-Luna, M. I., Michel, B., Hakre, S., & Roy, A. L. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m207635200 · Cited by 30
Resveratrol Enhances Temozolomide Efficacy in Glioblastoma Cells through Downregulated MGMT and Negative Regulators-Related STAT3 Inactivation
Wu, M., Song, D., Li, H. Z., Ahmad, N., Xu, H., Yang, X., Wang, Q., Cheng, X., Deng, S., & Shu, X. H. (2023) · International Journal of Molecular Sciences · doi:10.3390/ijms24119453 · Cited by 29
PIAS3, SHP2 and SOCS3 Expression patterns in Cervical Cancers: Relevance with activation and resveratrol-caused inactivation of STAT3 signaling
Zhang, P., Yang, B., Yao, Y.-Y., Zhong, L., Chen, X.-Y., Kong, Q., Wu, M., Li, C., Li, H., & Liu, J. (2015) · Gynecologic Oncology · doi:10.1016/j.ygyno.2015.09.087 · Cited by 29
Expression Profile in Omental and Subcutaneous Adipose Tissue from Lean and Obese Subjects. Repression of Lipolytic and Lipogenic Genes
del Pozo, C. H., Calvo, R. M., Vesperinas, G., Gómez‐Ambrosi, J., Frühbeck, G., Rubio, M. Á., & Obregón, M.-J. (2010) · Obesity Surgery · doi:10.1007/s11695-010-0246-4 · Cited by 29
miR‐199a‐5p promotes proliferation and metastasis and epithelial‐mesenchymal transition through targeting PIAS3 in cervical carcinoma
Qu, D., Yang, Y., & Huang, X. (2019) · Journal of Cellular Biochemistry · doi:10.1002/jcb.28631 · Cited by 29
TEL/ETV6 Is a Signal Transducer and Activator of Transcription 3 (Stat3)-induced Repressor of Stat3 Activity
Schick, N., Oakeley, E. J., Hynes, N. E., & Badache, A. (2004) · Journal of Biological Chemistry · doi:10.1074/jbc.m312581200 · Cited by 29
A novel nuclear zinc finger protein EZI enhances nuclear retention and transactivation of STAT3
Nakayama, K., Kim, K., & Miyajima, A. (2002) · The EMBO Journal · doi:10.1093/emboj/cdf596 · Cited by 29
MicroRNA-155 and cancer metastasis: Regulation of invasion, migration, and epithelial-to-mesenchymal transition
Moutabian, H., Radi, U. K., Saleman, A. Y., Adil, M., Zabibah, R. S., Chaitanya, M., Saadh, M. J., Jawad, M. J., Hazrati, E., Bagheri, H., et al. (2023) · Pathology - Research and Practice · doi:10.1016/j.prp.2023.154789 · Cited by 30
A novel microRNA regulates osteoclast differentiation via targeting protein inhibitor of activated STAT3 (PIAS3)
Liu, T., Qin, A.-P., Liao, B., Shao, H., Guo, L., Xie, G., Li, Y., & Jiang, T.-J. (2014) · Bone · doi:10.1016/j.bone.2014.07.004 · Cited by 28
Chronic IL-6 Administration Desensitizes IL-6 Response in Liver, Causes Hyperleptinemia and Aggravates Steatosis in Diet-Induced-Obese Mice
Gavito, A., Bautista, D., Suárez, J., Badran, S., Arco, R., Pavón, F. J., Serrano, A., Rivera, P., Decara, J. M., Cuesta, A. L., et al. (2016) · PLoS ONE · doi:10.1371/journal.pone.0157956 · Cited by 28
Differentially expressed JAK-STAT signaling pathway genes and target microRNAs in the spleen of necrotic enteritis-afflicted chicken lines
Truong, A. D., Rengaraj, D., Hong, Y., Hoang, C. T., Hong, Y. H., & Lillehoj, H. S. (2017) · Research in Veterinary Science · doi:10.1016/j.rvsc.2017.05.018 · Cited by 28
Anemoside B4 protects against chronic relapsing colitis in mice by modulating inflammatory response, colonic transcriptome and the gut microbiota
Han, Q., Deng, L.-R., Zou, M., Tang, H.-Z., Huang, C.-Y., Chen, F., Tomlinson, B., & Li, Y. (2022) · Phytomedicine · doi:10.1016/j.phymed.2022.154416 · Cited by 29
PIAS3 expression in squamous cell lung cancer is low and predicts overall survival
Abbas, R., McColl, K. S., Kresak, A. M., Yang, M., Chen, Y., Fu, P., Wildey, G. M., & Dowlati, A. (2015) · Cancer Medicine · doi:10.1002/cam4.372 · Cited by 28
The influence of ageing on the insulin signalling system in rat lacrimal and salivary glands
Rocha, E. M., Carvalho, C. R. D. O., Saad, M. J. A., & Velloso, L. A. (2003) · Acta Ophthalmologica Scandinavica · doi:10.1111/j.1395-3907.2003.00162.x · Cited by 28
TGF-beta1 suppresses IL-6-induced STAT3 activation through regulation of Jak2 expression in prostate epithelial cells.
Staršíchová, A., Lincová, E., Pernicová, Z., Kozubík, A., & Souček, K. (2010) · Cellular Signalling · doi:10.1016/j.cellsig.2010.06.014 · Cited by 28
PIAS1 negatively modulates virus triggered type I IFN signaling by blocking the DNA binding activity of IRF3
Li, R. P., Pan, Y., Shi, D., Zhang, Y., & Zhang, J. (2013) · Antiviral Research · doi:10.1016/j.antiviral.2013.09.001 · Cited by 28
The cancer/testis antigen MAGEC2 promotes amoeboid invasion of tumor cells by enhancing STAT3 signaling
Song, X., Hao, J., Wang, J., Guo, C., Wang, Y., He, Q., Tang, H., Qin, X., Li, Y., Zhang, Y., et al. (2016) · Oncogene · doi:10.1038/onc.2016.314 · Cited by 28
Interleukins and STAT Signaling
Haque, S. J., & Sharma, P. (2006) · Vitamins and hormones · doi:10.1016/s0083-6729(06)74007-9 · Cited by 28
A role for growth hormone and prolactin in leukaemia and lymphoma?
Hooghe, R. J., Merchav, S., Gaïdano, G., Naessens, F., & Matera, L. (1998) · Cellular and Molecular Life Sciences · doi:10.1007/s000180050238 · Cited by 28
Cross-talk between α1B-Adrenergic Receptor (α1BAR) and Interleukin-6 (IL-6) Signaling Pathways
Nguyen, V.-A. T., & Gao, B. (1999) · Journal of Biological Chemistry · doi:10.1074/jbc.274.50.35492 · Cited by 27
Deficient Stat3 DNA-binding is associated with high Pias3 expression and a positive anti-apoptotic balance in human end-stage alcoholic and hepatitis C cirrhosis
Stärkel, P., Saeger, C. D., Leclercq, I. A., Strain, A. J., & Horsmans, Y. (2005) · Journal of Hepatology · doi:10.1016/j.jhep.2005.03.024 · Cited by 28
Signaling Through Gp130: Toward a General Scenario of Cytokine Action
Fukada, T., Yoshida, Y., Nishida, K., Ohtani, T., Shirogane, T., Hibi, M., & Hirano, T. (1999) · Growth Factors · doi:10.3109/08977199909103518 · Cited by 28
Neuronal activity‐dependent STAT 3 localization to nucleus is dependent on Tyr‐705 and Ser‐727 phosphorylation in rat hippocampal neurons
Murase, S., & McKay, R. D. G. (2013) · European Journal of Neuroscience · doi:10.1111/ejn.12412 · Cited by 26
Natural Sesquiterpene Lactones Enhance Chemosensitivity of Tumor Cells through Redox Regulation of STAT3 Signaling
Butturini, E., de Prati, A. C., Boriero, D., & Mariotto, S. (2019) · Oxidative Medicine and Cellular Longevity · doi:10.1155/2019/4568964 · Cited by 29
Sumoylation of Rta of Epstein–Barr virus is preferentially enhanced by PIASxβ
Liu, S., Wang, W., Hong, Y., Chuang, J., Lu, P., & Chang, L.-K. (2006) · Virus Research · doi:10.1016/j.virusres.2006.01.004 · Cited by 27
Elongin B/C Recruitment Regulates Substrate Binding by CIS
Piessevaux, J., Ceuninck, L. D., Catteeuw, D., Peelman, F., & Tavernier, J. H. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m803742200 · Cited by 26
Modulation of Intracellular Restriction Factors Contributes to Methamphetamine- Mediated Enhancement of Acquired Immune Deficiency Syndrome Virus Infection of Macrophages
Wang, X., Wang, Y., Li, Y., Li, J., Zhou, Y., Sakarcan, S., & Ho, W. (2012) · Current HIV Research · doi:10.2174/157016212802138797 · Cited by 27
Mitochondrial GRIM-19 as a potential therapeutic target for STAT3-dependent carcinogenesis of gastric cancer
Huang, Y., Yang, M., Hu, H., Zhao, X., Bao, L., Huang, D., Song, L., & Li, Y. (2016) · Oncotarget · doi:10.18632/oncotarget.9167 · Cited by 27
MiR-9-5p and miR-106a-5p dysregulated in CD4+ T-cells of multiple sclerosis patients and targeted essential factors of T helper17/regulatory T-cells differentiation.
Majd, M., Hosseini, A., Ghaedi, K., Kiani‐Esfahani, A., Tanhaei, S., Shiralian-Esfahani, H., Rahnamaee, S. Y., Mowla, S. J., & Nasr‐Esfahani, M. H. (2018) · PubMed Central · doi:10.22038/ijbms.2018.25382.6275 · Cited by 27
Distinct signal transduction processes by IL-4 and IL-13 and influences from the Q551R variant of the human IL-4 receptor alpha chain
Kruse, S., Braun, S. L., & Deichmann, K. A. (2002) · Respiratory Research · doi:10.1186/rr174 · Cited by 27
Inhibition of Signal Transducer and Activator Transcription Factor 3 in Rats with Acute Hepatic Failure
Kamohara, Y., Sugiyama, N., Mizuguchi, T., Inderbitzin, D., Lilja, H., Middleton, Y., Neuman, T., Demetriou, A. A., & Rózga, J. (2000) · Biochemical and Biophysical Research Communications · doi:10.1006/bbrc.2000.2881 · Cited by 26
TRIM32 promotes radioresistance by disrupting TC45-STAT3 interaction in triple-negative breast cancer
Ma, Y., Zhang, H., Chen, C., Liu, L., Ding, T., Wang, Y., Ma, D., Ling, X., Chen, X., Li, J., et al. (2022) · Oncogene · doi:10.1038/s41388-022-02204-1 · Cited by 26
Leishmania intercepts IFN-γR signaling at multiple levels in macrophages
Gurjar, D., Patra, S. K., Bodhale, N. P., Lenka, N., & Saha, B. (2022) · Cytokine · doi:10.1016/j.cyto.2022.155956 · Cited by 28
The transcriptional responsiveness of LKB1 to STAT-mediated signaling is differentially modulated by prolactin in human breast cancer cells
Linher‐Melville, K., & Singh, G. (2014) · BMC Cancer · doi:10.1186/1471-2407-14-415 · Cited by 25
Machine learning techniques to discover genes with potential prognosis role in Alzheimer’s disease using different biological sources
Martínez-Ballesteros, M., García-Heredia, J. M., Nepomuceno-Chamorro, I. A., & Riquelme, J. C. (2016) · Information Fusion · doi:10.1016/j.inffus.2016.11.005 · Cited by 24
Interleukin-6-resistant melanoma cells exhibit reduced activation of STAT3 and lack of inhibition of cyclin E-associated kinase activity.
Böhm, M., Schulte, U., Funk, J. O., Raghunath, M., Behrmann, I., Kortylewski, M., Heinrich, P. C., Kues, T., Luger, T., & Schwarz, T. (2001) · Journal of Investigative Dermatology · doi:10.1046/j.0022-202x.2001.01372.x · Cited by 24
Termination of IL‐6‐induced STAT activation is independent of receptor internalization but requires de novo protein synthesis
Thiel, S., Sommer, U., Kortylewski, M., Haan, C., Behrmann, I., Heinrich, P. C., & Graeve, L. (2000) · FEBS Letters · doi:10.1016/s0014-5793(00)01276-x · Cited by 29
PIASxβ is a key regulator of osterix transcriptional activity and matrix mineralization in osteoblasts
Ali, M. M., Yoshizawa, T., Ishibashi, O., Matsuda, A., Ikegame, M., Shimomura, J., Mera, H., Nakashima, K., & Kawashima, H. (2007) · Journal of Cell Science · doi:10.1242/jcs.005090 · Cited by 26
Leptin and the Adipocyte Endocrine System
Diamond, F., & Eichler, D. C. (2002) · Critical Reviews in Clinical Laboratory Sciences · doi:10.1080/10408360290795565 · Cited by 27
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
Cytokine-induced tumor suppressors: A GRIM story
Kalvakolanu, D. V., Nallar, S. C., & Kalakonda, S. (2010) · Cytokine · doi:10.1016/j.cyto.2010.03.009 · Cited by 25
Tumor Suppressor LKB1 Inhibits Activation of Signal Transducer and Activator of Transcription 3 (STAT3) by Thyroid Oncogenic Tyrosine Kinase Rearranged in Transformation (RET)/Papillary Thyroid Carcinoma (PTC)
Kim, D. W., Chung, H. K., Park, K. C., Hwang, J. H., Jo, Y. S., Chung, J., Kalvakolanu, D. V., Resta, N., & Shong, M. (2007) · Molecular Endocrinology · doi:10.1210/me.2007-0269 · Cited by 25
Suppression of STAT3 Activity by Duplin, Which Is a Negative Regulator of the Wnt Signal
Yamashina, K., Yamamoto, H., Chayama, K., Nakajima, K., & Kikuchi, A. (2006) · The Journal of Biochemistry · doi:10.1093/jb/mvj033 · Cited by 25
Down-regulation of SHP1 and up-regulation of negative regulators of JAK/STAT signaling in HTLV-1 transformed cell lines and freshly transformed human peripheral blood CD4+ T-Cells
Cheng, J., Zhang, D., Zhou, C., & Marasco, W. A. (2003) · Leukemia Research · doi:10.1016/s0145-2126(03)00158-9 · Cited by 25
Association of 2',5'-Oligoadenylate Synthetase with the Prolactin (PRL) Receptor: Alteration in PRL-Inducible Stat1 (Signal Transducer and Activator of Transcription 1) Signaling to the IRF-1 (Interferon-Regulatory Factor 1) Promoter
McAveney, K. M., Book, M. L., Ling, P., Chebath, J., & Yu‐Lee, L. (2000) · Molecular Endocrinology · doi:10.1210/me.14.2.295 · Cited by 25
CELLULAR SIGNALLING PATHWAYS: NEW TARGETS IN LEUKAEMIA THERAPY
Ravandi, F., Talpaz, M., Kantarjian, H. M., & Estrov, Z. E. (2002) · British Journal of Haematology · doi:10.1046/j.1365-2141.2002.03236.x · Cited by 25
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
“Members of the protein inhibitor of activated STAT (PIAS) family, especially PIAS3, are small ubiquitin-like modifier-E3 ligases that bind specifically to STAT3 and abrogate its activity.(15) The SOCS and PIAS families together constitute major mechanisms by which STAT3 activity is downregulated quickly following stim…”
The role of transcription factors in atrial fibrillation.
Zhou, M., Liao, Y., & Tu, X. (2015) · Europe PMC (PubMed Central) · doi:10.3978/j.issn.2072-1439.2015.01.21 · Cited by 23
DNMT3a promotes proliferation by activating the STAT3 signaling pathway and depressing apoptosis in pancreatic cancer
Jing, W., Song, N., Liu, Y., Qu, X., Qi, Y., Li, C., Hou, K., Che, X., & Yang, X.-H. (2019) · Cancer Management and Research · doi:10.2147/cmar.s201610 · Cited by 24
Dysregulation of janus kinases and signal transducers and activators of transcription in cancer.
Costa‐Pereira, A. P., Bonito, N. A., & Seckl, M. J. (2011) · Europe PMC (PubMed Central) · Cited by 24
Bruton's tyrosine kinase prevents activation of the anti‐apoptotic transcription factor STAT3 and promotes apoptosis in neoplastic B‐cells and B‐cell precursors exposed to oxidative stress
Uckun, F. M., Özer, Z., & Vassilev, A. O. (2007) · British Journal of Haematology · doi:10.1111/j.1365-2141.2006.06468.x · Cited by 25
Stimulation of the JAK/STAT pathway by LIF and OSM in the human granulosa cell line COV434
Pastuschek, J., Poetzsch, J., Prieto, D. M. M., Schleußner, E., Markert, U. R., & Georgiev, G. (2015) · Journal of Reproductive Immunology · doi:10.1016/j.jri.2015.03.002 · Cited by 25
A Role for Protein Inhibitor of Activated STAT1 (PIAS1) in Lipogenic Regulation through SUMOylation-independent Suppression of Liver X Receptors
Zhang, Y., Gan, Z., Huang, P., Zhou, L., Mao, T., Shao, M., Jiang, X., Chen, Y., Ying, H., Cao, M.-N., et al. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.403139 · Cited by 24
Reactive Oxygen Species, SUMOylation, and Endothelial Inflammation
Le, N., Corsetti, J. P., Sparks, J. D., Sparks, C. E., Fujiwara, K., & Abe, J. (2012) · International Journal of Inflammation · doi:10.1155/2012/678190 · Cited by 24
Interaction of PIAS1 with PRRS virus nucleocapsid protein mediates NF-κB activation and triggers proinflammatory mediators during viral infection
Ke, H.-Z., Lee, S., Kim, J., Liu, H.-C. S., & Yoo, D. (2019) · Scientific Reports · doi:10.1038/s41598-019-47495-9 · Cited by 22
Regulation of Cytokine Receptor Signaling by Nuclear Hormone Receptors: A New Paradigm for Receptor Interaction
Leung, K. (2004) · DNA and Cell Biology · doi:10.1089/1044549041562285 · Cited by 24
Genetic Interactions of STAT3 and Anticancer Drug Development
Fang, B. (2014) · Cancers · doi:10.3390/cancers6010494 · Cited by 25
MicroRNA Regulation of T-Cell Exhaustion in Cutaneous T Cell Lymphoma
Han, Z., Estephan, R. J., Wu, X., Su, C., Yuan, Y., Qin, H., Kil, S. H., Morales, C. J., Schmolze, D. B., Sanchez, J. F., et al. (2021) · Journal of Investigative Dermatology · doi:10.1016/j.jid.2021.08.447 · Cited by 23
CUEDC2 (CUE Domain-containing 2) and SOCS3 (Suppressors of Cytokine Signaling 3) Cooperate to Negatively Regulate Janus Kinase 1/Signal Transducers and Activators of Transcription 3 Signaling
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
HIC1 interacts with and modulates the activity of STAT3
Lin, Y.-M., Wang, C.-M., Jeng, J., Leprince, D., & Shih, H. (2013) · Cell Cycle · doi:10.4161/cc.25365 · Cited by 24
Molecular interactions between STAT3 and protein inhibitor of activated STAT3, and androgen receptor
Yamamoto, T., Sato, N., Sekine, Y., Yumioka, T., Imoto, S., Junicho, A., Fuse, H., & Matsuda, T. (2003) · Biochemical and Biophysical Research Communications · doi:10.1016/s0006-291x(03)01026-x · Cited by 24
Suppressor of cytokine signalling protein SOCS1 and UBP43 regulate the expression of type I interferon-stimulated genes in human microvascular endothelial cells infected with Rickettsia conorii
Colonne, P. M., Sahni, A., & Sahni, S. (2013) · Journal of Medical Microbiology · doi:10.1099/jmm.0.054502-0 · Cited by 23

Authors: Chung, C. D., Liao, J., Liu, B., Rao, X., Jay, P., Berta, P., & Shuai, K.
Affiliations: University of California, Los Angeles (US)
Corresponding author: Chung, Chan D.
Liao, Jiayu
Shuai, Ke
ORCID: Liao, Jiayu
Liu, Bin
Jay, Philippe
Shuai, Ke
Venue: Science
Publisher: American Association for the Advancement of Science (AAAS)
Published: 1997-12-05
Volume: 278
Issue: 5344
Pages: 1803-1805
ISSN: 0036-8075 (ISSN-L)
1095-9203
DOI: 10.1126/science.278.5344.1803
OpenAlex: W1993520606
Cited by: 980
References: 17
Citations by year: 2026: 8 · 2025: 10 · 2024: 11 · 2023: 18 · 2022: 21 · 2021: 27 · 2020: 29 · 2019: 26 · 2018: 28 · 2017: 23 · 2016: 26 · 2015: 30 · 2014: 41 · 2013: 47 · 2012: 35
FWCI: 18.70
Type: journal article
Language: en
Open access: closed
Locations: Science (publishedVersion)
PubMed (publishedVersion)
Funders: National Institutes of Health (1r01ai039612-01)
National Cancer Institute (T32CA09056, T32CA009056)
National Institute of Allergy and Infectious Diseases (AI39612)
Topics: Life Sciences › Immunology and Microbiology › Immunology › Cytokine Signaling Pathways and Interactions
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics and Chromatin Dynamics
Life Sciences › Immunology and Microbiology › Immunology › Psoriasis: Treatment and Pathogenesis
Keywords: STAT3, PIAS3, signal transduction inhibition, interleukin-6 family cytokines, epidermal growth factor, leptin, STAT1, transcriptional regulation
MeSH terms: Amino Acid Sequence, Animals, Carrier Proteins, Cell Line, DNA, DNA-Binding Proteins, Gene Expression Regulation, Humans, Molecular Sequence Data, Phosphoproteins, Phosphorylation, Recombinant Fusion Proteins, Transfection, Tumor Cells, Cultured, Tumor Necrosis Factor-alpha, Signal Transduction, Transcriptional Activation, Trans-Activators, Interleukin-6, NF-kappa B, Interferon-alpha, Phosphotyrosine, Intracellular Signaling Peptides and Proteins, STAT1 Transcription Factor, STAT3 Transcription Factor, Protein Inhibitors of Activated STAT, Interferon Regulatory Factor-1, Mice

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

Specific Inhibition of Stat3 Signal Transduction by PIAS3

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks