Shp-2 Tyrosine Phosphatase Functions as a Negative Regulator of the Interferon-Stimulated Jak/STAT Pathway

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Therapeutic Targets of KRAS in Colorectal Cancer

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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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Photobiomodulation and the expression of genes related to the JAK/STAT signalling pathway in wounded and diabetic wounded cells

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TGF-beta1 suppresses IL-6-induced STAT3 activation through regulation of Jak2 expression in prostate epithelial cells.

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Ceacam1L Modulates STAT3 Signaling to Control the Proliferation of Glioblastoma-Initiating Cells

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Regulation of T-Cell Signaling by Post-Translational Modifications in Autoimmune Disease

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Phosphatases: Counterregulatory role in inflammatory cell signaling

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A novel VIP signaling pathway in T cells

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Expression of interferon alfa signaling components in human alcoholic liver disease

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Predicting resistance by selection of signaling pathways.

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LST1/A Is a Myeloid Leukocyte-specific Transmembrane Adaptor Protein Recruiting Protein Tyrosine Phosphatases SHP-1 and SHP-2 to the Plasma Membrane

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Human β-defensin 3 induces STAT1 phosphorylation, tyrosine phosphatase activity, and cytokine synthesis in T cells

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Pioneering therapies for post-infarction angiogenesis: Insight into molecular mechanisms and preclinical studies

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Elucidating the crosstalk mechanism between IFN-gamma and IL-6 via mathematical modelling

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Systemic treatment in EGFR-ALK NSCLC patients: second line therapy and beyond.

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Molecular Cloning and Expression Analysis of Three Suppressors of Cytokine Signaling Genes (SOCS5, SOCS6, SOCS7) in the Mealworm Beetle Tenebrio molitor

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MicroRNA Regulation of T-Cell Exhaustion in Cutaneous T Cell Lymphoma

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Annexin V Associates with the IFN-γ Receptor and Regulates IFN-γ Signaling

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Signal transduction activator of transcription 5 (STAT5) dysfunction in autoimmune monocytes and macrophages

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The differentiation and plasticity of Tc17 cells are regulated by CTLA-4-mediated effects on STATs

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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

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Molecular Regulation of Inducible Nitric Oxide Synthase

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Protein-tyrosine Phosphatases Are Involved in Interferon Resistance Associated with Insulin Resistance in HepG2 Cells and Obese Mice

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MHC Class I Molecules Exacerbate Viral Infection by Disrupting Type I Interferon Signaling

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Negative Regulation of Janus Kinases

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Interferon-α resistance can be reversed by inhibition of IFN-α-induced COX-2 expression potentially via STAT1 activation in A549 cells

Lee, J., Jung, H., Im, Y., Kim, J. D., Park, J., Kım, K., Kim, W. I., Ahn, J. S., Jung, C., Park, Y. M., et al. (2006) · Oncology Reports · doi:10.3892/or.15.6.1541 · Cited by 22

Loss of PTEN causes SHP2 activation, making lung cancer cells unresponsive to IFN-γ

Chen, C., Chiang, T.-H., Tseng, P., Wang, Y., & Lin, C. (2015) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2015.09.085 · Cited by 21

An increase in galectin-3 causes cellular unresponsiveness to IFN-γ-induced signal transduction and growth inhibition in gastric cancer cells

Tseng, P., Chen, C., Shan, Y., & Lin, C. (2016) · Oncotarget · doi:10.18632/oncotarget.7750 · Cited by 21

The biological function of SHP2 in human disease

Li, S. (2016) · Molecular Biology · doi:10.1134/s0026893316010118 · Cited by 20

Nuclear phosphatases and the proteasome in suppression of STAT1 activity in hepatocytes

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Glycogen synthase kinase‐3β indirectly facilitates interferon‐γ‐induced nuclear factor‐κB activation and nitric oxide biosynthesis

Kai, J.-I., Huang, W., Tsai, C., Chang, W., Chen, C., & Lin, C. (2010) · Journal of Cellular Biochemistry · doi:10.1002/jcb.22881 · Cited by 21

Initiation and maintenance of CNTF–Jak/STAT signaling in neurons is blocked by protein tyrosine phosphatase inhibitors

Jiao, J. (2003) · Molecular Brain Research · doi:10.1016/s0169-328x(03)00286-9 · Cited by 20

Molecular Regulation of Inducible Nitric Oxide Synthase

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IFN-β: A Contentious Player in Host–Pathogen Interaction in Tuberculosis

Sabir, N., Hussain, T. A., Shah, S. Z. A., Zhao, D., & Zhou, X. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18122725 · Cited by 21

Osteopontin Regulates Ubiquitin-Dependent Degradation of Stat1 in Murine Mammary Epithelial Tumor Cells

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Increased phosphorylation of AKT in high-risk gastric mucosa.

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Respiratory syncytial virus NS1 inhibits anti-viral Interferon-α-induced JAK/STAT signaling, by limiting the nuclear translocation of STAT1

Efstathiou, C., Zhang, Y., Kandwal, S., Fayne, D., Molloy, E. J., & Stevenson, N. J. (2024) · Frontiers in Immunology · doi:10.3389/fimmu.2024.1395809 · Cited by 20

Cross-Inhibition of Interferon-Induced Signals by GM-CSF Through a Block in Stat1 Activation

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IL-5-INDUCED JAB–JAK2 INTERACTION

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Interferon-γ

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Interstitial Cells of Cajal : Pathology , Injury and Repair = خلايا كاجال الخلالية : علم الأمراض و الإصابات و الإصلاح

Al‐Sajee, D., & Huizinga, J. D. (2012) · Sultan Qaboos University medical journal · doi:10.12816/0003165 · Cited by 17

SHP2 : The protein tyrosine phosphatase involved in chronic pulmonary inflammation and fibrosis

Chang, C., Lin, C., Chen, B.-C., Lin, P., & Chen, C. (2021) · IUBMB Life · doi:10.1002/iub.2559 · Cited by 17

The Jak-STAT Signal Transduction Pathway in Melanoma

Nicholas, C., & Gregory, B. (2011) · InTech eBooks · doi:10.5772/18876 · Cited by 19

Reciprocal regulation of TLR2-mediated IFN-β production by SHP2 and Gsk3β

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Autophagy facilitates cytokine-induced ICAM-1 expression

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SHP2 REGULATES IL-2 INDUCED MAPK ACTIVATION, BUT NOT Stat3 OR Stat5 TYROSINE PHOSPHORYLATION, IN CUTANEOUS T CELL LYMPHOMA CELLS

Brockdorff, J. L., Woetmann, A., Mustelin, T., Kaltoft, K., Zhang, Q., Wasik, M. A., Röpke, C., & Ødum, N. (2002) · Cytokine · doi:10.1006/cyto.2002.1986 · Cited by 16

Current treatment of cutaneous squamous cancer and molecular strategies for its sensitization to new target-based drugs

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AKT plays a crucial role in gastric cancer

Sasaki, T., Yamashita, Y., & Kuniyasu, H. (2015) · Oncology Letters · doi:10.3892/ol.2015.3260 · Cited by 15

Expression and significance of SHP-2 in human papillomavirus infected cervical cancer

Meng, F., Zhao, X., & Zhang, S. (2012) · Journal of Huazhong University of Science and Technology [Medical Sciences] · doi:10.1007/s11596-012-0044-4 · Cited by 14

Shp‐2 contributes to anti‐ RSV activity in human pulmonary alveolar epithelial cells by interfering with the IFN ‐α‐induced Jak/Stat1 pathway

Wang, S., Zheng, G., Zhao, L., Xu, F., & Qian, J. (2015) · Journal of Cellular and Molecular Medicine · doi:10.1111/jcmm.12629 · Cited by 14

Биологические функции shp2 при заболеваниях человека

Li, S., & Li, S. (2016) · Molecular Biology · doi:10.7868/s0026898416010110 · Cited by 14

S ignal T ransducers and A ctivators of T ranscription: I nsights into the M olecular B asis of O ral C ancer

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Cloning and characterisation of type I interferon receptor 1 in orange-spotted grouper (Epinephelus coioides) for response to nodavirus infection

Tang, Z. Z., Wang, T., Chen, Y.-M., & Chen, T.-Y. (2020) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2020.04.044 · Cited by 12

Ferroptosis triggers anti-tumor immunity via promoting chaperone-mediated autophagic degradation of SHP2

Zhu, J., Li, X., Chen, W., Zuo, Z., Gong, Q., Hu, J., Huang, K., Liu, W., Gu, Y., Xu, Q., et al. (2025) · Redox Biology · doi:10.1016/j.redox.2025.103796 · Cited by 12

Cyclooxygenase-2 Inhibitor Enhances Whereas Prostaglandin E2Inhibits the Production of Interferon-Induced Protein of 10 kDa in Epidermoid Carcinoma A431

Kanda, N., & Watanabe, S. (2002) · Journal of Investigative Dermatology · doi:10.1046/j.1523-1747.2002.19510.x · Cited by 12

Pathogenic signaling in multiple myeloma

Bolomsky, A., & Young, R. M. (2022) · Seminars in Oncology · doi:10.1053/j.seminoncol.2022.01.005 · Cited by 15

Reactive Oxygen Species and Epidermal Growth Factor Are Antagonistic Cues Controlling SHP-2 Dimerization

Nardozza, A. P., D’Orazio, M., Trapannone, R., Corallino, S., Filomeni, G., Tartaglia, M., Battistoni, A., Cesareni, G., & Castagnoli, L. (2012) · Molecular and Cellular Biology · doi:10.1128/mcb.06674-11 · Cited by 12

A small molecule inhibitor targeting SHP2 mutations for the lung carcinoma

Nian, Q., Zeng, J., Li, H., Chen, Y., Zhang, Z., Rodrigues‐Lima, F., Zhao, L., Feng, X., & Shi, J. (2021) · Chinese Chemical Letters · doi:10.1016/j.cclet.2021.01.002 · Cited by 12

Suppression of Interferon-α Treatment Response by Host Negative Factors in Hepatitis B Virus Infection

Wang, J., Du, L., & Tang, H. (2021) · Frontiers in Medicine · doi:10.3389/fmed.2021.784172 · Cited by 12

Expression Changes of ERK1/2, STAT3 and SHP-2 in Bone Marrow Cells from γ-ray Induced Leukemia Mice

Fu, Z., Huang, D., Cai, J., Chen, Q., Han, L., Li, B., Wang, F., & Gao, J. (2006) · Journal of Radiation Research · doi:10.1269/jrr.47.121 · Cited by 12

Jak2 Tyrosine Kinase: A Mediator of Both Housekeeping and Ligand-Dependent Gene Expression?

Wallace, T. A., & Sayeski, P. P. (2006) · Cell Biochemistry and Biophysics · doi:10.1385/cbb:44:2:213 · Cited by 12

Targeting Shp2 as a therapeutic strategy for neurodegenerative diseases

Pang, J., Cen, C.-Q., Tian, Y., Cao, X., Hao, L., Tao, X., & Cao, Z. (2025) · Translational Psychiatry · doi:10.1038/s41398-024-03222-1 · Cited by 12

Ethanol inhibition of Angiotensin II-stimulated Tyr705 and Ser727 STAT3 phosphorylation in cultured rat hepatocytes: Relevance to activation of p42/44 mitogen-activated protein kinase

Weng, Y.-I., Aroor, A. R., & Shukla, S. D. (2008) · Alcohol · doi:10.1016/j.alcohol.2008.02.004 · Cited by 11

Functional cross-talk between the cyclic AMP and Jak/STAT signaling pathways in vascular smooth muscle cells

Meloche, S., Pelletier, S. W., & Servant, M. J. (2000) · Springer eBooks · doi:10.1007/978-1-4615-4351-0_12 · Cited by 11

SHP-2 positively regulates adipogenic differentiation in 3T3-L1 cells

Uehara, T., Suzuki, K., Yamanaka, H., Kizaki, T., Sakurai, T., Ishibashi, Y., Ishida, H., & Ohno, H. (2007) · International Journal of Molecular Medicine · doi:10.3892/ijmm.19.6.895 · Cited by 11

SHP2-independent tyrosine dephosphorylation of cortactin and vinculin during infection with Helicobacter pylori

Knorr, J., Backert, S., & Tegtmeyer, N. (2020) · European Journal of Microbiology and Immunology · doi:10.1556/1886.2020.00001 · Cited by 11

STAT module can function as a biphasic amplitude filter

Mayya, V., & Loew, L. M. (2005) · Systems Biology · doi:10.1049/sb:20045037 · Cited by 11

Noonan Syndrome--Certitude Replaces Conjecture

Saenger, P. H. (2002) · The Journal of Clinical Endocrinology & Metabolism · doi:10.1210/jc.87.8.3527 · Cited by 11

Determining folding and binding properties of the C‐terminal SH2 domain of SHP2

Nardella, C., Malagrinò, F., Pagano, L., Rinaldo, S., Gianni, S., & Toto, A. (2021) · Protein Science · doi:10.1002/pro.4201 · Cited by 9

A shift in the IL-6/STAT3 signalling pathway imbalance towards the SHP2 pathway in severe asthma results in reduced proliferation process

Salem, I. H., Plante, S., GOUNNI, A. S., Rouabhia, M., & Chakir, J. (2017) · Cellular Signalling · doi:10.1016/j.cellsig.2017.12.001 · Cited by 10

HER-2/neu raises SHP-2, stops IFN-γ anti-proliferation in bladder cancer

Su, W.-P., Tu, I.-H., Hu, S.-W., Yeh, H.-H., Shieh, D., Chen, T.-Y., & Su, W. (2007) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2007.02.099 · Cited by 10

Functional cross-talk between the cyclic AMP and Jak/STAT signaling pathways in vascular smooth muscle cells

Meloche, S., Pelletier, S. W., & Servant, M. J. (2000) · Molecular and Cellular Biochemistry · doi:10.1023/a:1007140606333 · Cited by 10

Phosphopeptide binding to the N-SH2 domain of tyrosine phosphatase SHP2 correlates with the unzipping of its central β-sheet

Marasco, M., Kirkpatrick, J., Carlomagno, T., Hub, J. S., & Anselmi, M. (2024) · Computational and Structural Biotechnology Journal · doi:10.1016/j.csbj.2024.02.023 · Cited by 9

SHP‐2 phosphatase promotes cervical cancer cell proliferation through inhibiting interferon‐β production

Meng, F., Zhao, X., & Zhang, S. (2012) · Journal of obstetrics and gynaecology research · doi:10.1111/j.1447-0756.2012.01952.x · Cited by 9

Proteolysis-Targeting Chimera Molecules Targeting SHP2

Yu, D., Zheng, M., Liu, Y., Chen, L., & Li, H. (2022) · Future Medicinal Chemistry · doi:10.4155/fmc-2021-0324 · Cited by 9

Protein-protein interaction between caveolin-1 and SHP-2 is dependent on the N-SH2 domain of SHP-2

Park, H., Ahn, K. J., Kang, J. L., & Choi, Y. (2015) · BMB Reports · doi:10.5483/bmbrep.2015.48.3.249 · Cited by 9

The adaptor function of SHP-2 downstream of the prolactin receptor is required for the recruitment of p29, a substrate of SHP-2

Minoo, P., Chughtai, N., Campiglio, M., Stein-Gerlach, M., Lebrun, J. J., Ullrich, A., & Ali, S. (2003) · Cellular Signalling · doi:10.1016/s0898-6568(02)00122-5 · Cited by 9

Protein Post‐Translational Modification‐Mediated Control of Type I Interferon Cascade Signaling

Chen, X., Cheng, Q., Gong, F., & Zheng, H. (2025) · Medicine Bulletin · doi:10.1002/mdb2.70000 · Cited by 9

Setting sail: Maneuvering SHP2 activity and its effects in cancer

Welsh, C. L., Allen, S., & Madan, L. K. (2023) · Advances in cancer research · doi:10.1016/bs.acr.2023.03.003 · Cited by 9

STAT Activation in Malignancies: Roles in Tumor Progression and in the Generation of Antineoplastic Effects of IFNs

Wang, B. X., Platanias, L. C., & Fish, E. N. (2013) · Journal of Interferon & Cytokine Research · doi:10.1089/jir.2012.0154 · Cited by 9

The interplay between the immune system and viruses

Wubben, R., Efstathiou, C., & Stevenson, N. J. (2021) · Vitamins and hormones · doi:10.1016/bs.vh.2021.06.011 · Cited by 8

Transcription Factor Activation in Human Neutrophils

Cloutier, A., & McDonald, P. P. (2003) · KARGER eBooks · doi:10.1159/000071553 · Cited by 11

Role of Glycogen Synthase Kinase-3 in Interferon-γ-Mediated Immune Hepatitis

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SC-60, a Dimer-Based Sorafenib Derivative, Shows a Better Anti–Hepatocellular Carcinoma Effect than Sorafenib in a Preclinical Hepatocellular Carcinoma Model

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