Double-edged roles of protein tyrosine phosphatase SHP2 in cancer and its inhibitors in clinical trials

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Mutations in PTPN11 implicate the SHP-2 phosphatase in leukemogenesis

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RAS nucleotide cycling underlies the SHP2 phosphatase dependence of mutant BRAF-, NF1- and RAS-driven cancers

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PTPN11 is the first identified proto-oncogene that encodes a tyrosine phosphatase

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Mutant KRAS-driven cancers depend on PTPN11/SHP2 phosphatase

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The molecular functions of Shp2 in the Ras/Mitogen-activated protein kinase (ERK1/2) pathway

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A Novel Positive Feedback Loop Mediated by the Docking Protein Gab1 and Phosphatidylinositol 3-Kinase in Epidermal Growth Factor Receptor Signaling

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Ptpn11/Shp2 Acts as a Tumor Suppressor in Hepatocellular Carcinogenesis

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SHP2 is required for growth of KRAS-mutant non-small-cell lung cancer in vivo

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Molecular mechanism for a role of SHP2 in epidermal growth factor receptor signaling

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Protein Kinases and Phosphatases in the Control of Cell Fate

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

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Dissection of signaling cascades through gp130 in vivo: reciprocal roles for STAT3- and SHP2-mediated signals in immune responses.

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An Shp2/SFK/Ras/Erk Signaling Pathway Controls Trophoblast Stem Cell Survival

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Tyrosine phosphatase SHP2 promotes breast cancer progression and maintains tumor-initiating cells via activation of key transcription factors and a positive feedback signaling loop

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Inhibition of SHP2-mediated dephosphorylation of Ras suppresses oncogenesis

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Identification of TNO155, an Allosteric SHP2 Inhibitor for the Treatment of Cancer

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SHP2 inhibition restores sensitivity in ALK-rearranged non-small-cell lung cancer resistant to ALK inhibitors

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SHP2 inhibition triggers anti-tumor immunity and synergizes with PD-1 blockade

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The tyrosine phosphatase SHP-2 is required for mediating phosphatidylinositol 3-kinase/Akt activation by growth factors

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Targeting SHP2 as a promising strategy for cancer immunotherapy

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Roles of Gab1 and SHP2 in Paxillin Tyrosine Dephosphorylation and Src Activation in Response to Epidermal Growth Factor

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Discovery of SHP2-D26 as a First, Potent, and Effective PROTAC Degrader of SHP2 Protein

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Protein Tyrosine Phosphatases: Structure, Function, and Implication in Human Disease

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Combinations with Allosteric SHP2 Inhibitor TNO155 to Block Receptor Tyrosine Kinase Signaling

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The COOH-terminal Tyrosine Phosphorylation Sites on IRS-1 Bind SHP-2 and Negatively Regulate Insulin Signaling

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Spectrum of mutations in PTPN11 and genotype–phenotype correlation in 96 patients with Noonan syndrome and five patients with cardio-facio-cutaneous syndrome

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Signal transducer and activator of transcription 3 is a major kinase-independent target of sorafenib in hepatocellular carcinoma

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Human somatic PTPN11 mutations induce hematopoietic-cell hypersensitivity to granulocyte-macrophage colony-stimulating factor

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Rel/NF-κB and IκB factors in oncogenesis

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Shp2 promotes liver cancer stem cell expansion by augmenting β‐catenin signaling and predicts chemotherapeutic response of patients

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PTPN11/Shp2 overexpression enhances liver cancer progression and predicts poor prognosis of patients

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Structural and Mechanistic Insights into LEOPARD Syndrome-Associated SHP2 Mutations

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Tyrosine phosphatase SHP2 inhibitors in tumor-targeted therapies

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Helicobacter pylori CagA Phosphorylation Status Determines the gp130-activated SHP2/ERK and JAK/STAT Signal Transduction Pathways in Gastric Epithelial Cells

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Modulation of the Nuclear Factor κb Pathway by Shp-2 Tyrosine Phosphatase in Mediating the Induction of Interleukin (Il)-6 by IL-1 or Tumor Necrosis Factor

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Mechanism of activating mutations and allosteric drug inhibition of the phosphatase SHP2

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Dual Allosteric Inhibition of SHP2 Phosphatase

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The tyrosine phosphatase SHP2 controls TGFβ-induced STAT3 signaling to regulate fibroblast activation and fibrosis

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Mediating ERK1/2 signaling rescues congenital heart defects in a mouse model of Noonan syndrome

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Leukemogenic Ptpn11 causes fatal myeloproliferative disorder via cell-autonomous effects on multiple stages of hematopoiesis

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Protein tyrosine phosphatase variants in human hereditary disorders and disease susceptibilities

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Allosteric Inhibitors of SHP2 with Therapeutic Potential for Cancer Treatment

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Genetic abnormalities and pathophysiology of MDS

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Allosteric SHP2 Inhibitor, IACS-13909, Overcomes EGFR-Dependent and EGFR-Independent Resistance Mechanisms toward Osimertinib

Sun, Y., Meyers, B. A., Czakó, B., Leonard, P. G., Mseeh, F., Harris, A. L., Wu, Q., Johnson, S. B., Parker, C. A., Cross, J. B., et al. (2020) · Cancer Research · doi:10.1158/0008-5472.can-20-1634 · Cited by 107

SHP-2 Positively Regulates Myogenesis by Coupling to the Rho GTPase Signaling Pathway

Kontaridis, M. I., Eminaga, S., Fornaro, M., Zito, C. I., Sordella, R., Settleman, J. E., & Bennett, A. M. (2004) · Molecular and Cellular Biology · doi:10.1128/mcb.24.12.5340-5352.2004 · Cited by 106

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 100

Live‐cell imaging of endogenous Ras‐GTP illustrates predominant Ras activation at the plasma membrane

Augsten, M., Pusch, R., Biskup, C., Rennert, K., Wittig, U., Beyer, K., Blume, A., Wetzker, R., Friedrich, K., & Rubio, I. (2006) · EMBO Reports · doi:10.1038/sj.embor.7400560 · Cited by 99

Diverse driving forces underlie the invariant occurrence of the T42A, E139D, I282V and T468M SHP2 amino acid substitutions causing Noonan and LEOPARD syndromes

Martinelli, S., Torreri, P., Tinti, M., Stella, L., Bocchinfuso, G., Flex, E., Grottesi, A., Ceccarini, M., Palleschi, A., Cesareni, G., et al. (2008) · Human Molecular Genetics · doi:10.1093/hmg/ddn099 · Cited by 97

SHP-2/PTPN11 mediates gliomagenesis driven by PDGFRA and INK4A/ARF aberrations in mice and humans

Liu, K.-W., Feng, H., Bachoo, R. M., Kazlauskas, A., Smith, E. M., Symes, K., Hamilton, R. L., Nagane, M., Nishikawa, R., Hu, B., et al. (2011) · Journal of Clinical Investigation · doi:10.1172/jci43690 · Cited by 92

Optimization of Fused Bicyclic Allosteric SHP2 Inhibitors

Bagdanoff, J. T., Chen, Z., Acker, M., Chen, Y., Chan, H., Dore, M., Firestone, B., Fodor, M., García‐Fortanet, J., Hentemann, M., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01725 · Cited by 92

Kinetic and Mechanistic Characterization of a Mammalian Protein-tyrosine Phosphatase, PTP1

Zhang, Z. (1995) · Journal of Biological Chemistry · doi:10.1074/jbc.270.19.11199 · Cited by 90

SHP-2 Regulates SOCS-1-mediated Janus Kinase-2 Ubiquitination/Degradation Downstream of the Prolactin Receptor

Ali, S., Nouhi, Z., Chughtai, N., & Ali, S. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m306758200 · Cited by 88

Molecular Basis of Gain-of-Function LEOPARD Syndrome-Associated SHP2 Mutations

Yu, Z.-H., Zhang, R.-Y., Walls, C. D., Chen, L., Zhang, S., Wu, L., Liu, S., & Zhang, Z.-Y. (2014) · Biochemistry · doi:10.1021/bi5002695 · Cited by 87

6-Amino-3-methylpyrimidinones as Potent, Selective, and Orally Efficacious SHP2 Inhibitors

Sarver, P., Acker, M., Bagdanoff, J. T., Chen, Z., Chen, Y.-N., Chan, H., Firestone, B., Fodor, M., Fortanet, J., Hao, H., et al. (2019) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.8b01726 · Cited by 87

Negative regulation of signal transducer and activator of transcription-3 signalling cascade by lupeol inhibits growth and induces apoptosis in hepatocellular carcinoma cells

Siveen, K. S., Nguyen, A. H., Lee, J. H., Li, F., Singh, S. S., Kumar, A. P., Low, G., Jha, S. K., Tergaonkar, V., Ahn, K. S., et al. (2014) · British Journal of Cancer · doi:10.1038/bjc.2014.422 · Cited by 86

Structural insights into Noonan/LEOPARD syndrome-related mutants of protein-tyrosine phosphatase SHP2 (PTPN11)

Qiu, W., Wang, X., Romanov, V., Hutchinson, A., Lin, A., Ruzanov, M., Battaile, K. P., PAI, E. F., Neel, B. G., & Chirgadze, N. Y. (2014) · BMC Structural Biology · doi:10.1186/1472-6807-14-10 · Cited by 86

Gain-of-function/Noonan syndrome SHP-2/ Ptpn11 mutants enhance calcium oscillations and impair NFAT signaling

Uhlén, P., Burch, P. M., Zito, C. I., Estrada, M., Ehrlich, B. E., & Bennett, A. M. (2006) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0510876103 · Cited by 86

Discovery of thalidomide-based PROTAC small molecules as the highly efficient SHP2 degraders

Yang, X., Wang, Z., Pei, Y., Song, N., Xu, L., Feng, B., Wang, H., Luo, X., Hu, X., Qiu, X., et al. (2021) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2021.113341 · Cited by 85

Leptin activates STAT and ERK2 pathways and induces gastric cancer cell proliferation

Pai, R., Lin, C. K., Tran, T., & Tarnawski, A. S. (2005) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2005.03.236 · Cited by 82

Novel PROTACs for degradation of SHP2 protein

Zheng, M., Liu, Y., Wu, C., Yang, K., Wang, Q., Zhou, Y., Chen, L., & Li, H. (2021) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2021.104788 · Cited by 81

Therapeutic potential of targeting SHP2 in human developmental disorders and cancers

Shen, D., Chen, W., Zhu, J., Wu, G., Shen, R., Xi, M., & Sun, H. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112117 · Cited by 79

Anticancer Activity of Sodium Stibogluconate in Synergy with IFNs

Yi, T., Pathak, M. K., Lindner, D. J., Ketterer, M. E., Farver, C. F., & Borden, E. C. (2002) · The Journal of Immunology · doi:10.4049/jimmunol.169.10.5978 · Cited by 70

Targeting a Cryptic Allosteric Site for Selective Inhibition of the Oncogenic Protein Tyrosine Phosphatase Shp2

Chio, C. M., Lim, C. S., & Bishop, A. C. (2014) · Biochemistry · doi:10.1021/bi5013595 · Cited by 66

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 65

Cytokine signalling via gp130 in gastric cancer

Howlett, M., Menheniott, T. R., Judd, L. M., & Giraud, A. (2009) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2009.07.009 · Cited by 65

Shp2 deletion in hepatocytes suppresses hepatocarcinogenesis driven by oncogenic β-Catenin, PIK3CA and MET

Liu, J. J., Li, Y., Chen, W. S., Liang, Y., Wang, G., Zong, M., Kaneko, K., Xu, R., Karin, M., & Feng, G. (2018) · Journal of Hepatology · doi:10.1016/j.jhep.2018.02.014 · Cited by 64

Strategies to overcome drug resistance using SHP2 inhibitors

Liu, M., Gao, S., Elhassan, R. M., Hou, X., & Fang, H. (2021) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2021.03.037 · Cited by 58

The protein tyrosine phosphatase, Shp2, positively contributes to FLT3-ITD-induced hematopoietic progenitor hyperproliferation and malignant disease in vivo

Nabinger, S. C., Li, X. J., Ramdas, B., He, Y., Zhang, X., Zeng, L., Richine, B. M., Bowling, J. D., Fukuda, S., Goenka, S., et al. (2012) · Leukemia · doi:10.1038/leu.2012.308 · Cited by 56

Growth hormone modulation of EGF-induced PI3K-Akt pathway in mice liver

Díaz, M. E., González, L., Miquet, J. G., Martinez, C. S., Sotelo, A. I., Bartke, A., & Turyn, D. (2011) · Cellular Signalling · doi:10.1016/j.cellsig.2011.10.001 · Cited by 54

Identification of an allosteric benzothiazolopyrimidone inhibitor of the oncogenic protein tyrosine phosphatase SHP2

LaRochelle, J. R., Fodor, M., Ellegast, J. M., Liu, X., Vemulapalli, V., Mohseni, M., Stams, T., Buhrlage, S. J., Stegmaier, K., LaMarche, M. J., et al. (2017) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2017.10.025 · Cited by 51

A critical role for SHP2 in STAT5 activation and growth factor–mediated proliferation, survival, and differentiation of human CD34+ cells

Li, L., Modi, H., McDonald, T., Rossi, J., Yee, J., & Bhatia, R. (2011) · Blood · doi:10.1182/blood-2010-06-288910 · Cited by 49

TIGIT, A Novel Therapeutic Target for Tumor Immunotherapy

Liu, X., Hou, M., & Liu, Y. (2016) · Immunological Investigations · doi:10.1080/08820139.2016.1237524 · Cited by 47

Medicinal chemistry strategies for the development of protein tyrosine phosphatase SHP2 inhibitors and PROTAC degraders

Tang, K., Jia, Y.-N., Yu, B., & Liu, H. (2020) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2020.112657 · Cited by 47

Constitutively Active SHP2 Cooperates with HoxA10 Overexpression to Induce Acute Myeloid Leukemia

Wang, H., Lindsey, S. C., Konieczna, I. M., Bei, L., Horvath, E., Huang, W., Saberwal, G. S., & Eklund, E. A. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804704200 · Cited by 46

A Cross-Species Study of PI3K Protein-Protein Interactions Reveals the Direct Interaction of P85 and SHP2

Breitkopf, S. B., Yang, X., Begley, M. J., Kulkarni, M. M., Chiu, Y., Turke, A. B., Lauriol, J., Yuan, M., Qi, J., Engelman, J. A., et al. (2016) · Scientific Reports · doi:10.1038/srep20471 · Cited by 45

The Allosteric Site on SHP2’s Protein Tyrosine Phosphatase Domain is Targetable with Druglike Small Molecules

Marsh-Armstrong, B. P., Fajnzylber, J. M., Korntner, S., Plaman, B. A., & Bishop, A. C. (2018) · ACS Omega · doi:10.1021/acsomega.8b02200 · Cited by 44

Regulation of SHP2 by PTEN/AKT/GSK-3β signaling facilitates IFN-γ resistance in hyperproliferating gastric cancer

Tseng, P., Huang, W., Chen, C., Sheu, B., Shan, Y., Tsai, C., Wang, C., Chen, S.-O., Hsieh, C.-Y., & Lin, C. (2012) · Immunobiology · doi:10.1016/j.imbio.2012.01.001 · Cited by 39

Expression and Clinical Significance of SHP2 in Gastric Cancer

Dong, S., Fq, L., Zhang, Q., Lv, K.-Z., Yang, H.-L., Gao, Y., & Yu, J.-R. (2012) · Journal of International Medical Research · doi:10.1177/030006051204000605 · Cited by 39

Shp2 Inhibits Proliferation of Esophageal Squamous Cell Cancer via Dephosphorylation of Stat3

Chen, Q., Han, T., Tang, H., Huang, K., Min, J., Li, J., Ding, X., & Xu, Z. (2017) · International Journal of Molecular Sciences · doi:10.3390/ijms18010134 · Cited by 38

Phosphatase-independent functions of SHP2 and its regulation by small molecule compounds

Guo, W., & Xu, Q. (2020) · Journal of Pharmacological Sciences · doi:10.1016/j.jphs.2020.06.002 · Cited by 38

Shipping out MEK inhibitor resistance with SHP2 inhibitors

Torres-Ayuso, P., & Brognard, J. (2018) · Cancer Discovery · doi:10.1158/2159-8290.cd-18-0915 · Cited by 37

SHP2 negatively regulates HLA-ABC and PD-L1 expression via STAT1 phosphorylation in prostate cancer cells

Liu, Z., Zhao, Y. Q., Fang, J., Cui, R., Xiao, Y., & Xu, Q. (2017) · Oncotarget · doi:10.18632/oncotarget.18591 · Cited by 35

Targeting SHP2 for EGFR inhibitor resistant non-small cell lung carcinoma

Xu, J., Zeng, L., Shen, W., Turchi, J. J., & Zhang, Z. (2013) · Biochemical and Biophysical Research Communications · doi:10.1016/j.bbrc.2013.09.028 · Cited by 34

A multifunctional cross-validation high-throughput screening protocol enabling the discovery of new SHP2 inhibitors

Song, Y., Zhao, M., Wu, Y., Yu, B., & Liu, H. (2020) · Acta Pharmaceutica Sinica B · doi:10.1016/j.apsb.2020.10.021 · Cited by 34

Shp2 SUMOylation promotes ERK activation and hepatocellular carcinoma development

Deng, R., Zhao, X., Qu, Y., Chen, C., Zhu, C., Zhang, H., Yuan, H., Jin, H. Z., Liu, X., Wang, Y., et al. (2015) · Oncotarget · doi:10.18632/oncotarget.3323 · Cited by 33

SHP2 promotes laryngeal cancer growth through the Ras/Raf/Mek/Erk pathway and serves as a prognostic indicator for laryngeal cancer.

Gu, J., Han, T., Ma, R., Zhu, Y.-L., Jia, Y., Du, J.-J., Chen, Y., Jiang, X.-J., Xie, X.-D., & Guo, X. (2014) · International Journal of Oncology · doi:10.3892/ijo.2013.2191 · Cited by 31

Syk kinase and Shp2 phosphatase inhibition cooperate to reduce FLT3-ITD-induced STAT5 activation and proliferation of acute myeloid leukemia

Richine, B. M., Virts, E. L., Bowling, J. D., Ramdas, B., Mali, R. S., Naoye, R., Liu, Z., Zhang, Z.-Y., Boswell, H. S., Kapur, R., et al. (2016) · Leukemia · doi:10.1038/leu.2016.131 · Cited by 26

SHP2 inhibitor specifically suppresses the stemness of KRAS-mutant non-small cell lung cancer cells

Jiang, L., Xu, W., Chen, Y., & Zhang, Y. (2019) · Artificial Cells Nanomedicine and Biotechnology · doi:10.1080/21691401.2019.1646748 · Cited by 26

Association of nuclear localization of SHP2 and YAP1 with unfavorable prognosis in non-small cell lung cancer

Chen, M., Wang, Y., Wu, D., Chen, C.-Y., & Lee, H. (2019) · Pathology - Research and Practice · doi:10.1016/j.prp.2019.01.027 · Cited by 25

The tyrosine phosphatase SHP‐2 regulates differentiation and apoptosis of individual primary T lymphocytes

Hoff, H., & Brunner-Weinzierl, M. C. (2007) · European Journal of Immunology · doi:10.1002/eji.200636240 · Cited by 22

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 prognostic significance of SHP2 and its binding protein Hook1 in non-small cell lung cancer

He, L., Li, Y., Huang, X., Cheng, H., Ke, Y., & Wang, L.-R. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s210223 · Cited by 19

Enhanced anti-melanoma efficacy of interferon alfa-2b via inhibition of Shp2

Win-Piazza, H., Schneeberger, V. E., Chen, L., Pernazza, D., Lawrence, H. R., Sebti, S. M., Lawrence, N. J., & Wu, J. (2012) · Cancer Letters · doi:10.1016/j.canlet.2012.01.034 · Cited by 18

Shp2 regulates migratory behavior and response to EGFR-TKIs through ERK1/2 pathway activation in non-small cell lung cancer cells

Sun, Y., Zhuo, Z., Xian, H., Chen, K., Yang, F., & Zhao, X. T. (2017) · Oncotarget · doi:10.18632/oncotarget.20249 · Cited by 18

Emerging chemical scaffolds with potential SHP2 phosphatase inhibitory capabilities – A comprehensive review

Tripathi, R. K. P., & Ayyannan, S. R. (2020) · Chemical Biology & Drug Design · doi:10.1111/cbdd.13807 · Cited by 18

Gain-Of-Function E76K-Mutant SHP2 Promotes Cell Proliferation, Metastasis, And Tumor Growth In Glioblastoma Through Activation Of The ERK/CREB Pathway

Yang, F., Xu, M., Wang, S., Song, L., Yu, D., Li, Y., Cao, R., Zhang, X., Chen, Z., Zhang, Q., et al. (2019) · OncoTargets and Therapy · doi:10.2147/ott.s222881 · Cited by 17

Small‐Molecule Inhibitors of Shp2 Phosphatase as Potential Chemotherapeutic Agents for Glioblastoma: A Minireview

Mitra, R., & Ayyannan, S. R. (2020) · ChemMedChem · doi:10.1002/cmdc.202000706 · Cited by 17

The second-sphere residue T263 is important for the function and catalytic activity of PTP1B via interaction with the WPD-loop

Xiao, P., Xiao, W., Wang, H., Fu, X.-L., Cui, F., Yu, X., Wen, S.-S., Bi, W., & Sun, J. (2014) · The International Journal of Biochemistry & Cell Biology · doi:10.1016/j.biocel.2014.10.004 · Cited by 16

Shp2 confers cisplatin resistance in small cell lung cancer via an AKT-mediated increase in CA916798

Yang, X., Tang, C., Luo, H., Wang, H., & Zhou, X. (2017) · Oncotarget · doi:10.18632/oncotarget.15641 · Cited by 16

Shp2 activation in bone marrow microenvironment mediates the drug resistance of B-cell acute lymphoblastic leukemia through enhancing the role of VCAM-1/VLA-4

Yu, K., Yin, Y., Ma, D., Lu, T., Wei, D., Xiong, J., Zhou, Z., Zhang, T., Zhang, S., Fang, Q., et al. (2020) · International Immunopharmacology · doi:10.1016/j.intimp.2019.106008 · Cited by 16

Low expression of SHP-2 is associated with less favorable prostate cancer outcomes

Tassidis, H., Brokken, L. J. S., Jirström, K., Bjartell, A. S., Ulmert, D., Härkönen, P. L., & Wingren, A. G. (2012) · Tumor Biology · doi:10.1007/s13277-012-0590-1 · Cited by 14

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

Gab2 is Essential for Transformation by FLT3‐ITD in Acute Myeloid Leukemia

Sies, K., Spohr, C., Gründer, A., Todorova, R., Uhl, F. M., Huber, J., Zeiser, R., Pahl, H. L., Becker, H., Aumann, K., et al. (2019) · HemaSphere · doi:10.1097/hs9.0000000000000184 · Cited by 7

Expressions of Src homology 2 domain-containing phosphatase and its clinical significance in laryngeal carcinoma

Dong, L., Li, G. Q., Tian, Z., Wang, Z. M., & Xu, K. (2013) · Genetics and Molecular Research · doi:10.4238/2013.october.7.6 · Cited by 6

An allosteric inhibitor of SHP2 effectively targets PDGFRα-driven glioblastoma

Tannous, B. A., & Badr, C. E. (2019) · Neuro-Oncology · doi:10.1093/neuonc/noz176 · Cited by 6

Combination strategies with PD-1/PD-L1 blockade: current advances and future directions

Yi, M., Zheng, X., Niu, M., Zhu, S., Ge, H., & Wu, K. (2022) · Molecular Cancer · doi:10.1186/s12943-021-01489-2 · Cited by 1,445

Small molecule inhibitors targeting the cancers

Liu, G., Chen, T., Zhang, X., Ma, X., & Shi, H. (2022) · MedComm · doi:10.1002/mco2.181 · Cited by 212

Progress on Ras/MAPK Signaling Research and Targeting in Blood and Solid Cancers

Dillon, M., Lopez, A. R., Lin, E., Sales, D., Perets, R., & Jain, P. (2021) · Cancers · doi:10.3390/cancers13205059 · Cited by 175

Targeting protein phosphatases for the treatment of inflammation-related diseases: From signaling to therapy

Pan, J., Zhou, L., Zhang, C., Xu, Q., & Sun, Y. (2022) · Signal Transduction and Targeted Therapy · doi:10.1038/s41392-022-01038-3 · Cited by 118

Strategies Targeting Protein Tyrosine Phosphatase SHP2 for Cancer Therapy

Song, Y., Wang, S., Zhao, M., Yang, X., & Yu, B. (2022) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.1c02008 · Cited by 101

Complex Roles of PTPN11/SHP2 in Carcinogenesis and Prospect of Targeting SHP2 in Cancer Therapy

Scheiter, A., Lu, L., Gao, L. H., & Feng, G. (2023) · Annual Review of Cancer Biology · doi:10.1146/annurev-cancerbio-062722-013740 · Cited by 13

A comprehensive review of SHP2 and its role in cancer

Asmamaw, M. D., Shi, X.-J., Zhang, L.-R., & Liu, H.-M. (2022) · Cellular Oncology · doi:10.1007/s13402-022-00698-1 · Cited by 119

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

SHP2-targeted cancer therapeutics: Structural insights, inhibitor development and emerging modalities

Zhang, Y., Zhu, C., Si, C., Lin, Y., Guo, Q., Zhou, H., & Yu, Z. (2026) · Bioorganic & Medicinal Chemistry · doi:10.1016/j.bmc.2026.118708 · Cited by 3

Protein Tyrosine Phosphatase SHP-2 as Drug Target

Somani, R. R., Madan, D., & Rai, P. (2016) · Mini-Reviews in Organic Chemistry · doi:10.2174/1570193x13666161017141804 · Cited by 2