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

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Phosphorylation of Grb2-Associated Binder 2 on Serine 623 by ERK MAPK Regulates Its Association with the Phosphatase SHP-2 and Decreases STAT5 Activation

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The tyrosine phosphatase SHP2 increases robustness and information transfer within IL-6-induced JAK/STAT signalling

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Paired immunoglobulin-like receptor B regulates platelet activation

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Qualitatively Different T Cell Phenotypic Responses to IL-2 versus IL-15 Are Unified by Identical Dependences on Receptor Signal Strength and Duration

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Cannabinoid 1 Receptor and Interleukin-6 Receptor Together Induce Integration of Protein Kinase and Transcription Factor Signaling to Trigger Neurite Outgrowth

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Cellular Stability of Serotonin N-Acetyltransferase Conferred by Phosphonodifluoromethylene Alanine (Pfa) Substitution for Ser-205

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SHP-2 is a novel target of Abl kinases during cell proliferation

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The protein tyrosine phosphatase SHP-2 is required for EGFRvIII oncogenic transformation in human glioblastoma cells

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SHP-1 expression accounts for resistance to imatinib treatment in Philadelphia chromosome–positive cells derived from patients with chronic myeloid leukemia

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Involvement of EphA2-mediated tyrosine phosphorylation of Shp2 in Shp2-regulated activation of extracellular signal-regulated kinase

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Antagonism between binding site affinity and conformational dynamics tunes alternative cis-interactions within Shp2

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Resistance to allosteric SHP2 inhibition in FGFR-driven cancers through rapid feedback activation of FGFR

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A Possible Approach to Site-Specific Insertion of Two Different Unnatural Amino Acids into Proteins in Mammalian Cells via Nonsense Suppression

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Autoimmune Disease–Associated Haplotypes of BLK Exhibit Lowered Thresholds for B Cell Activation and Expansion of Ig Class‐Switched B Cells

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Intrinsic Signaling Functions of the β4 Integrin Intracellular Domain

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SHP2 Mediates the Localized Activation of Fyn Downstream of the α6β4 Integrin To Promote Carcinoma Invasion

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Systems biology of IL-6, IL-12 family cytokines

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Src-Mediated Phosphorylation of the Tyrosine Phosphatase PRL-3 Is Required for PRL-3 Promotion of Rho Activation, Motility and Invasion

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Interaction of the tyrosine phosphatase SHP-2 with Gab2 regulates Rho-dependent activation of the c-fosserum response element by interleukin-2

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Resistance Mechanisms to SYK Inhibition in Acute Myeloid Leukemia

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Structure-Based Kinetic Models of Modular Signaling Protein Function: Focus on Shp2

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Shp2 acts downstream of SDF-1α/CXCR4 in guiding granule cell migration during cerebellar development

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S100A7-Downregulation Inhibits Epidermal Growth Factor-Induced Signaling in Breast Cancer Cells and Blocks Osteoclast Formation

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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

Shp2 Associates with and Enhances Nephrin Tyrosine Phosphorylation and Is Necessary for Foot Process Spreading in Mouse Models of Podocyte Injury

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Stepping out of the shadows: Oncogenic and tumor-promoting protein tyrosine phosphatases

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The Protein Tyrosine Phosphatase SHP-2 Regulates Interleukin-1-induced ERK Activation in Fibroblasts

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Crystallographic landscape of SHP2 provides molecular insights for SHP2 targeted drug discovery

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Phosphorylation of SHP-2 Regulates Interactions between the Endoplasmic Reticulum and Focal Adhesions to Restrict Interleukin-1-induced Ca2+ Signaling

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Protein Tyrosine Phosphatase SHP2 Mediates Chronic Insulin-Induced Endothelial Inflammation

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Corrigendum to “Hypoxia Impairs NK Cell Cytotoxicity through SHP-1-Mediated Attenuation of STAT3 and ERK Signaling Pathways”

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Chemical tags for site-specific fluorescent labeling of biomolecules

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Incorporation of Phosphorylated Tyrosine into Proteins: In Vitro Translation and Study of Phosphorylated IκB-α and Its Interaction with NF-κB

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Phosphotyrosine couples peptide binding and SHP2 activation via a dynamic allosteric network

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Raft-mediated Src Homology 2 Domain-containing Proteintyrosine Phosphatase 2 (SHP-2) Regulation in Microglia

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Inhibitory receptors on myeloid cells: New targets for therapy?

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Protein tyrosine phosphatase Shp2 deficiency in podocytes attenuates lipopolysaccharide-induced proteinuria

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PD-1 and CTLA-4 exert additive control of effector regulatory T cells at homeostasis

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SH2 Domain-Containing Protein-Tyrosine Phosphatases

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Geranylnaringenin (CG902) inhibits constitutive and inducible STAT3 activation through the activation of SHP-2 tyrosine phosphatase

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Model-driven experimental analysis of the function of SHP-2 in IL-6-induced Jak/STAT signaling

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Grb2 binding induces phosphorylation-independent activation of Shp2

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Overcoming Immune Checkpoint Therapy Resistance with SHP2 Inhibition in Cancer and Immune Cells: A Review of the Literature and Novel Combinatorial Approaches

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SHPS-1/SIRP1alpha contributes to interleukin-6 signalling.

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Chemical Strategies for Controlling Protein Folding and Elucidating the Molecular Mechanisms of Amyloid Formation and Toxicity

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Interplay between the tyrosine kinases Chk and Csk and phosphatase PTPRJ is critical for regulating platelets in mice

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Novel Functions of the Phosphatase SHP2 in the DNA Replication and Damage Checkpoints

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SHP2 is a downstream target of ZAP70 to regulate JAK1/STAT3 and ERK signaling pathways in mouse embryonic stem cells

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Deletion of the Angiotensin II Type 1a Receptor Prevents Atherosclerotic Plaque Rupture in Apolipoprotein E −/− Mice

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Targeting the EphB4 receptor tyrosine kinase sensitizes HER2-positive breast cancer cells to Lapatinib

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An Intracellular Multi-Effector Complex Mediates Somatostatin Receptor 1 Activation of Phospho-Tyrosine Phosphatase η

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Tyrosine phosphatase SHP‐2 regulates IL‐1 signaling in fibroblasts through focal adhesions

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Dysregulation of janus kinases and signal transducers and activators of transcription in cancer.

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Structural basis of how stress-induced MDMX phosphorylation activates p53

Chen, X., Gohain, N., Zhan, C., Lu, W.-Y., Pazgier, M., & Lu, W. (2015) · Oncogene · doi:10.1038/onc.2015.255 · Cited by 22

SHP2 tyrosine phosphatase stimulates CEBPA gene expression to mediate cytokine-dependent granulopoiesis

Zhang, L., & Friedman, A. D. (2011) · Blood · doi:10.1182/blood-2011-01-331157 · Cited by 23

SH2 Domain-Containing Protein Tyrosine Phosphatase 2 and Focal Adhesion Kinase Protein Interactions Regulate Pulmonary Endothelium Barrier Function

Chichger, H., Braza, J., Duong, H., & Harrington, E. O. (2014) · American Journal of Respiratory Cell and Molecular Biology · doi:10.1165/rcmb.2013-0489oc · Cited by 23

Regulation of allergic inflammatory responses by inhibitory receptors

Shik, D., & Munitz, A. (2010) · Clinical & Experimental Allergy · doi:10.1111/j.1365-2222.2010.03501.x · Cited by 22

Protein tyrosine phosphatase SHP2/PTPN11 mistargeting as a consequence of SH2-domain point mutations associated with Noonan Syndrome and leukemia

Müller, P. J., Rigbolt, K. T. G., Paterok, D., Piehler, J., Vanselow, J. T., Lasonder, E., Andersen, J., Schaper, F., & Sobota, R. M. (2013) · Journal of Proteomics · doi:10.1016/j.jprot.2013.04.005 · Cited by 22

The epidermal growth factor receptor ligand amphiregulin is a negative regulator of hepatic acute-phase gene expression

Pardo–Saganta, A., Latasa, M. U., Castillo, J., Alvarez–Asiain, L., Perugorria, M. J., Sarobe, P., Rodríguez‐Ortigosa, C. M., Prìeto, J., Berasain, C., Santamaría, M., et al. (2009) · Journal of Hepatology · doi:10.1016/j.jhep.2009.06.030 · Cited by 22

Ethacrynic acid inhibits STAT3 activity through the modulation of SHP2 and PTP1B tyrosine phosphatases in DU145 prostate carcinoma cells

Lee, Y.-J., Song, H., Yoon, Y. J., Park, S.-J., Kim, S., Han, D. C., & Kwon, B. (2020) · Biochemical Pharmacology · doi:10.1016/j.bcp.2020.113920 · Cited by 22

The Non-Receptor Protein Tyrosine Phosphatase PTPN6 Mediates a Positive Regulatory Approach From the Interferon Regulatory Factor to the JAK/STAT Pathway in Litopenaeus vannamei

Luo, M., Xu, X., Liu, X., Shen, W., Yang, L., Zhu, Z., Weng, S., He, J., & Zuo, H. (2022) · Frontiers in Immunology · doi:10.3389/fimmu.2022.913955 · Cited by 21

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

Phosphorylation of SHP2 at Tyr62 Enables Acquired Resistance to SHP2 Allosteric Inhibitors in FLT3-ITD–Driven AML

Pfeiffer, A., Franciosa, G., Locard‐Paulet, M., Piga, I., Reckzeh, K., Vemulapalli, V., Blacklow, S. C., Theilgaard‐Mönch, K., Jensen, L. J., & Olsen, J. V. (2022) · Cancer Research · doi:10.1158/0008-5472.can-21-0548 · Cited by 24

TNFα counteracts interleukin-10 anti-inflammatory pathway through the NOX2-Lyn-SHP-1 axis in human monocytes

Khemis, M. B., Liu, D., Pintard, C., Song, Z., Hurtado-Nédelec, M., Marie, J., Benna, J. E., & Dang, P. M. (2023) · Redox Biology · doi:10.1016/j.redox.2023.102898 · Cited by 20

Molecular mechanisms of natural killer cell regulation

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A role for SHPS-1/SIRPα1 in IL-1β- and TNFα-dependent signaling

Amin, A. R. M. R., Machida, K., Oshima, K., Oo, M. L., Thant, A. A., Senga, T., Matsuda, S., Akhand, A. A., Maeda, A., Kurosaki, T., et al. (2002) · Oncogene · doi:10.1038/sj.onc.1206018 · Cited by 20

Role of SHP2 protein tyrosine phosphatase in SERT inhibition by enteropathogenicE. coli(EPEC)

Singhal, M., Manzella, C. R., Soni, V. K., Alrefai, W. A., Saksena, S., Hecht, G. A., Dudeja, P. K., & Gill, R. K. (2017) · American Journal of Physiology-Gastrointestinal and Liver Physiology · doi:10.1152/ajpgi.00011.2017 · Cited by 19

Calpain-dependent cleavage of SHP-1 and SHP-2 is involved in the dephosphorylation of Jurkat T cells induced byEntamoeba histolytica

KIM, K. A., Lee, Y. A., & Shin, M. H. (2009) · Parasite Immunology · doi:10.1111/j.1365-3024.2009.01175.x · Cited by 19

Tyrosine phosphatases as key regulators of StAR induction and cholesterol transport: SHP2 as a potential tyrosine phosphatase involved in steroid synthesis

Cooke, M., Mele, P. G., Maloberti, P. M., Duarte, A., Poderoso, C., Orlando, U. D., Paz, C., Maciel, F. C., & Podesta, E. J. (2010) · Molecular and Cellular Endocrinology · doi:10.1016/j.mce.2010.11.030 · Cited by 17

A highly multiplexed quantitative phosphosite assay for biology and preclinical studies

Keshishian, H., McDonald, E. R., Mundt, F., Melanson, R., Krug, K., PORTER, D. A., Wallace, L., Forestier, D., Rabasha, B., Marlow, S., et al. (2021) · Molecular Systems Biology · doi:10.15252/msb.202010156 · Cited by 17

The Tyrosine Phosphatase Shp-2 Mediates Intracellular Signaling Initiated by Ret Mutants

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