A comprehensive review of SHP2 and its role in cancer

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SHP-1 and SHP-2 Associate with Immunoreceptor Tyrosine-Based Switch Motif of Programmed Death 1 upon Primary Human T Cell Stimulation, but Only Receptor Ligation Prevents T Cell Activation

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Kinase inhibitors: the road ahead

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Crystal Structure of the Tyrosine Phosphatase SHP-2

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Allosteric inhibition of SHP2 phosphatase inhibits cancers driven by receptor tyrosine kinases

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Small‐Molecule PROTACS: New Approaches to Protein Degradation

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Melanoma Cell-Intrinsic PD-1 Receptor Functions Promote Tumor Growth

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Phospholipase C-γ1 and phosphatidylinositol 3 kinase are the downstream mediators of the PDGF receptor's mitogenic signal

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Targeted protein degradation by PROTACs

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Sprouty1 and Sprouty2 provide a control mechanism for the Ras/MAPK signalling pathway

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Regulation of T Cell Receptor Signaling by Tyrosine Phosphatase SYP Association with CTLA-4

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Activation of a Phosphotyrosine Phosphatase by Tyrosine Phosphorylation

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Application of PD-1 Blockade in Cancer Immunotherapy

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Activating Mutations of the Noonan Syndrome-Associated <b> <i>SHP2/PTPN11</i> </b> Gene in Human Solid Tumors and Adult Acute Myelogenous Leukemia

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Germline gain-of-function mutations in RAF1 cause Noonan syndrome

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A new function for a phosphotyrosine phosphatase: linking GRB2-Sos to a receptor tyrosine kinase

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Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp‐2

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Shp2 regulates SRC family kinase activity and Ras/Erk activation by controlling Csk recruitment.

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RhoA Inactivation by p190RhoGAP Regulates Cell Spreading and Migration by Promoting Membrane Protrusion and Polarity

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A Novel Membrane Glycoprotein, SHPS-1, That Binds the SH2-Domain-Containing Protein Tyrosine Phosphatase SHP-2 in Response to Mitogens and Cell Adhesion

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Mutations in PTPN11 implicate the SHP-2 phosphatase in leukemogenesis

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Diversity and functional consequences of germline and somatic PTPN11 mutations in human disease

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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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PTPN11 (Shp2) Mutations in LEOPARD Syndrome Have Dominant Negative, Not Activating, Effects

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Ptpn11/Shp2 Acts as a Tumor Suppressor in Hepatocellular Carcinogenesis

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The SH2-containing protein-tyrosine phosphatase SH-PTP2 is required upstream of MAP kinase for early xenopus development

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

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SHP2 inhibition prevents adaptive resistance to MEK inhibitors in multiple cancer models

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Protein tyrosine phosphatases in the JAK/STAT pathway

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

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Cloning of p97/Gab2, the Major SHP2-Binding Protein in Hematopoietic Cells, Reveals a Novel Pathway for Cytokine-Induced Gene Activation

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Mice mutant for Egfr and Shp2 have defective cardiac semilunar valvulogenesis

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Diverse Biochemical Properties of Shp2 Mutants

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Potent Stimulation of SH-PTP2 Phosphatase Activity by Simultaneous Occupancy of Both SH2 Domains

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

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The role of Shp2 (PTPN11) in cancer

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The Tyrosine Phosphatase Shp2 in Development and Cancer

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Prognostic, therapeutic, and mechanistic implications of a mouse model of leukemia evoked by Shp2 (PTPN11) mutations

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Induction of Siglec-G by RNA Viruses Inhibits the Innate Immune Response by Promoting RIG-I Degradation

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Helicobacter pylori CagA Induces Ras-independent Morphogenetic Response through SHP-2 Recruitment and Activation

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Molecular mechanism of SHP2 activation by PD-1 stimulation

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Neuronal Shp2 tyrosine phosphatase controls energy balance and metabolism

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Targeting wild-type KRAS-amplified gastroesophageal cancer through combined MEK and SHP2 inhibition

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SHP2 inhibition diminishes KRASG12C cycling and promotes tumor microenvironment remodeling

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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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Leukaemogenic effects of Ptpn11 activating mutations in the stem cell microenvironment

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Cancer cell-derived exosomal circUSP7 induces CD8+ T cell dysfunction and anti-PD1 resistance by regulating the miR-934/SHP2 axis in NSCLC

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Functions of Shp2 in cancer

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PD-1/SHP-2 Inhibits Tc1/Th1 Phenotypic Responses and the Activation of T Cells in the Tumor Microenvironment

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Inhibition of SHP2-mediated dephosphorylation of Ras suppresses oncogenesis

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SHP-2 Phosphatase Negatively Regulates the TRIF Adaptor Protein-Dependent Type I Interferon and Proinflammatory Cytokine Production

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Protein tyrosine phosphatase SHP-2: A proto-oncogene product that promotes Ras activation

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How to make tubes: signaling by the Met receptor tyrosine kinase

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Gab-Family Adapter Proteins Act Downstream of Cytokine and Growth Factor Receptors and T- and B-Cell Antigen Receptors

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SHP2 and SOCS3 Contribute to Tyr-759-dependent Attenuation of Interleukin-6 Signaling through gp130

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SHP2 sails from physiology to pathology

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Tyrosyl phosphorylation of Shp2 is required for normal ERK activation in response to some, but not all, growth factors

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PROTACs: An Emerging Targeting Technique for Protein Degradation in Drug Discovery

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

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Ptpn11 deletion in a novel progenitor causes metachondromatosis by inducing hedgehog signalling

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SHP2 drives adaptive resistance to ERK signaling inhibition in molecularly defined subsets of ERK-dependent tumors

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Regulation of Early Events in Integrin Signaling by Protein Tyrosine Phosphatase SHP-2

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The 64-kDa protein that associates with the platelet-derived growth factor receptor beta subunit via Tyr-1009 is the SH2-containing phosphotyrosine phosphatase Syp.

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A Novel Role for Gab1 and SHP2 in Epidermal Growth Factor-induced Ras Activation

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Programmed cell death‐1 (PD‐1) checkpoint blockade in combination with a mammalian target of rapamycin inhibitor restrains hepatocellular carcinoma growth induced by hepatoma cell–intrinsic PD‐1

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Characterization of phosphotyrosine binding motifs in the cytoplasmic domain of B and T lymphocyte attenuator required for association with protein tyrosine phosphatases SHP-1 and SHP-2

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

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Therapeutic targeting of oncogenic tyrosine phosphatases

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Antigen-Presenting Cell-Intrinsic PD-1 Neutralizes PD-L1 in cis to Attenuate PD-1 Signaling in T Cells

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Induction of apoptosis in MDA-MB-231 breast cancer cells by a PARP1-targeting PROTAC small molecule

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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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Shp2, an SH2-containing Protein-tyrosine Phosphatase, Positively Regulates Receptor Tyrosine Kinase Signaling by Dephosphorylating and Inactivating the Inhibitor Sprouty

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

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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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SHP-2 Is a Dual-specificity Phosphatase Involved in Stat1 Dephosphorylation at Both Tyrosine and Serine Residues in Nuclei

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PTPN11 is a central node in intrinsic and acquired resistance to targeted cancer drugs

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Cytosolic Tyrosine Dephosphorylation of STAT5

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Structural reorganization of SHP2 by oncogenic mutations and implications for oncoprotein resistance to allosteric inhibition

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

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Infiltration of a mixture of immune cells may be related to good prognosis in patients with differentiated thyroid carcinoma

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A Deletion Mutation in the SH2-N Domain of Shp-2 Severely Suppresses Hematopoietic Cell Development

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The Phosphotyrosine Interactome of the Insulin Receptor Family and Its Substrates IRS-1 and IRS-2

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Targeting Protein Tyrosine Phosphatases for Anticancer Drug Discovery

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Tyrosine phosphatase SHP2 negatively regulates NLRP3 inflammasome activation via ANT1-dependent mitochondrial homeostasis

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Quantitative Interactomics in Primary T Cells Provides a Rationale for Concomitant PD-1 and BTLA Coinhibitor Blockade in Cancer Immunotherapy

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A Critical Role for Phosphoinositide 3-Kinase Upstream of Gab1 and SHP2 in the Activation of Ras and Mitogen-activated Protein Kinases by Epidermal Growth Factor

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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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Blockade of Tumor-Expressed PD-1 promotes lung cancer growth

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Structural and Mechanistic Insights into LEOPARD Syndrome-Associated SHP2 Mutations

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

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Germ-line and somatic PTPN11 mutations in human disease

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Therapeutic Potential of Targeting the Oncogenic SHP2 Phosphatase

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Tyrosine phosphatase SHP2 inhibitors in tumor-targeted therapies

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The protein tyrosine phosphatase Shp-2 regulates RhoA activity

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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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Dual Allosteric Inhibition of SHP2 Phosphatase

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

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PD-1 and BTLA regulate T cell signaling differentially and only partially through SHP1 and SHP2

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

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Biased Suppression of Hematopoiesis and Multiple Developmental Defects in Chimeric Mice Containing Shp-2 Mutant Cells

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The SH2 tyrosine phosphatase Shp2 is required for mammalian limb development

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Allosteric SHP2 inhibitors in cancer: Targeting the intersection of RAS, resistance, and the immune microenvironment

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Overexpression of Shp2 tyrosine phosphatase is implicated in leukemogenesis in adult human leukemia

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Role of the SHP-2 tyrosine phosphatase in cytokine-induced signaling and cellular response

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Requirement of Shp-2 tyrosine phosphatase in lymphoid and hematopoietic cell development

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SHP-2 and myeloid malignancies

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Reduced phosphatase activity of SHP‐2 in LEOPARD syndrome: Consequences for PI3K binding on Gab1

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SHP2 Tyrosine Phosphatase Converts Parafibromin/Cdc73 from a Tumor Suppressor to an Oncogenic Driver

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Role of SH-PTP2, a Protein-Tyrosine Phosphatase with Src Homology 2 Domains, in Insulin-Stimulated Ras Activation

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Tyrosine Phosphorylation of Jak2 in the JH2 Domain Inhibits Cytokine Signaling

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Targeted protein knockdown using small molecule degraders

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Loss-of-Function Mutations in PTPN11 Cause Metachondromatosis, but Not Ollier Disease or Maffucci Syndrome

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PD-1 Blunts the Function of Ovarian Tumor–Infiltrating Dendritic Cells by Inactivating NF-κB

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Phosphatases start shedding their stigma of undruggability

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SHP-2 and PD-L1 Inhibition Combined with Radiotherapy Enhances Systemic Antitumor Effects in an Anti–PD-1–Resistant Model of Non–Small Cell Lung Cancer

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

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Isolation of a distinct class of gain-of-function SHP-2 mutants with oncogenic RAS-like transforming activity from solid tumors

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

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Endothelial deletion of SHP2 suppresses tumor angiogenesis and promotes vascular normalization

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SHP2-mediated signaling cascade through gp130 is essential for LIF-dependent I CaL, [Ca2+]i transient, and APD increase in cardiomyocytes.

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YAP and TAZ, Hippo Signaling Targets, Act as a Rheostat for Nuclear SHP2 Function

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SHP‐2 regulates the phosphatidylinositide 3′‐kinase/Akt pathway and suppresses caspase 3‐mediated apoptosis

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Differentiated thyroid carcinomas may elude the immune system by B7H1 upregulation

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Allosteric Inhibition of SHP2 Stimulates Antitumor Immunity by Transforming the Immunosuppressive Environment

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Inhibition of SHP2 leads to mesenchymal to epithelial transition in breast cancer cells

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Sticking It to Cancer with Molecular Glue for SHP2

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Endogenous miR-204 Protects the Kidney against Chronic Injury in Hypertension and Diabetes

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Nuclear Protein Tyrosine Phosphatase Shp-2 Is One Important Negative Regulator of Nuclear Export of Telomerase Reverse Transcriptase

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Optimization of Fused Bicyclic Allosteric SHP2 Inhibitors

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SHP2 is up‐regulated in breast cancer cells and in infiltrating ductal carcinoma of the breast, implying its involvement in breast oncogenesis

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Tyrosine phosphatase activity in mitochondria: presence of Shp-2 phosphatase in mitochondria

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

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PTPN11 mutations in patients with LEOPARD syndrome: a French multicentric experience

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

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SHP-2, SH2-containing protein tyrosine phosphatase-21Due to the limitation of references we would like to apologize to all authors that contributed important results to the elucidation of the biological function of SHP-2 and could not be mentioned in this review.1

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

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Prolactin Induces SHP-2 Association with Stat5, Nuclear Translocation, and Binding to the β-Casein Gene Promoter in Mammary Cells

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Glycogen Synthase Kinase-3β Facilitates IFN-γ-Induced STAT1 Activation by Regulating Src Homology-2 Domain-Containing Phosphatase 2

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PD-1 blockade delays tumor growth by inhibiting an intrinsic SHP2/Ras/MAPK signalling in thyroid cancer cells

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Novel PROTACs for degradation of SHP2 protein

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Grb2 controls phosphorylation of FGFR2 by inhibiting receptor kinase and Shp2 phosphatase activity

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Targeting Protein Tyrosine Phosphatase SHP2 for Therapeutic Intervention

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ThePTPN11loss-of-function mutation Q510E-Shp2 causes hypertrophic cardiomyopathy by dysregulating mTOR signaling

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Tyrosine Phosphatase SHP-2 Binding to CTLA-4: Absence of Direct YVKM/YFIP Motif Recognition

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Therapeutic potential of targeting SHP2 in human developmental disorders and cancers

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Shp2-mediated molecular signaling in control of embryonic stem cell self-renewal and differentiation

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SHP-2 promoting migration and metastasis of MCF-7 with loss of E-cadherin, dephosphorylation of FAK and secretion of MMP-9 induced by IL-1 ?in vivo andin vitro

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A12 The SHP2 Inhibitor RMC-4630 in Patients with KRAS-Mutant Non-Small Cell Lung Cancer: Preliminary Evaluation of a First-in-Man Phase 1 Clinical Trial

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SHP2 blockade enhances anti-tumor immunity via tumor cell intrinsic and extrinsic mechanisms

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Catalytic-dependent and -independent roles of SHP-2 tyrosine phosphatase in interleukin-3 signaling

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Structural and Functional Consequences of Three Cancer-Associated Mutations of the Oncogenic Phosphatase SHP2

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Sprouty proteins are in vivo targets of Corkscrew/SHP-2 tyrosine phosphatases

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Role of SHP2 in hematopoiesis and leukemogenesis

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E3 ligase FBXW7 is critical for RIG-I stabilization during antiviral responses

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Selective inhibition of leukemia-associated SHP2E69K mutant by the allosteric SHP2 inhibitor SHP099

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Shp2 promotes metastasis of prostate cancer by attenuating the PAR3/PAR6/aPKC polarity protein complex and enhancing epithelial-to-mesenchymal transition

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The Tyrosine Phosphatase SHP2 Regulates Focal Adhesion Kinase to Promote EGF-Induced Lamellipodia Persistence and Cell Migration

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SHP2 promotes proliferation of breast cancer cells through regulating Cyclin D1 stability via the PI3K/AKT/GSK3β signaling pathway

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Angiotensin-II-induced apoptosis requires regulation of nucleolin and Bcl-xL by SHP-2 in primary lung endothelial cells

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Recent advances in targeting the “undruggable” proteins: from drug discovery to clinical trials

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Targeting the undruggables—the power of protein degraders

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SH2 Domains: Folding, Binding and Therapeutical Approaches

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Identification of GDC-1971 (RLY-1971), a SHP2 Inhibitor Designed for the Treatment of Solid Tumors

Taylor, A. M., Williams, B. R., Giordanetto, F., Kelley, E. H., Lescarbeau, A., Shortsleeves, K., Tang, Y., Walters, W. P., Arrazate, A., Bowman, C. M., et al. (2023) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.3c00483 · Cited by 51 · see citing works

Targeting KRAS in Pancreatic Ductal Adenocarcinoma: The Long Road to Cure

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Macrophage SHP2 Deficiency Alleviates Diabetic Nephropathy via Suppression of MAPK/NF-κB– Dependent Inflammation

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Emerging landscape of KRAS inhibitors in cancer treatment

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Optogenetics with Atomic Precision─A Comprehensive Review of Optical Control of Protein Function through Genetic Code Expansion

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Traditional Chinese medicine inhibits PD-1/PD-L1 axis to sensitize cancer immunotherapy: a literature review

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Pioneer in Molecular Biology: Conformational Ensembles in Molecular Recognition, Allostery, and Cell Function

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Allostery Frustrates the Experimentalist

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MUC1-C is necessary for SHP2 activation and BRAF inhibitor resistance in BRAF(V600E) mutant colorectal cancer

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Covalent-Allosteric Inhibitors: Do We Get the Best of Both Worlds?

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The roles of fused-cyclopropanes in medicinal chemistry: Insights from the past decade

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Protein–peptide docking with a rational and accurate diffusion generative model

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The Impact of ETV6-NTRK3 Oncogenic Gene Fusions on Molecular and Signaling Pathway Alterations

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LAIR1 drives glioma progression by nuclear focal adhesion kinase dependent expressions of cyclin D1 and immunosuppressive chemokines/cytokines

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The pathogenic T42A mutation in SHP2 rewires the interaction specificity of its N-terminal regulatory domain

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Targeted protein degradation using chimeric human E2 ubiquitin-conjugating enzymes

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A patent review of SHP2 allosteric inhibitors (2018-present)

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Discovery of a Novel Series of Potent SHP2 Allosteric Inhibitors

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Bivalent target-binding bioPROTACs induce potent degradation of oncogenic SHP2

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Combined Inhibition of PI3K and STAT3 signaling effectively inhibits bladder cancer growth

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Design, Synthesis and Antitumor Activity of a Novel Class of SHP2 Allosteric Inhibitors with a Furanyl Amide-Based Scaffold

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Targeting ERBB3 and AKT to overcome adaptive resistance in EML4-ALK-driven non-small cell lung cancer

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TET3-mediated DNA demethylation modification activates SHP2 expression to promote endometrial cancer progression through the EGFR/ERK pathway

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Modeling (not so) rare developmental disorders associated with mutations in the protein-tyrosine phosphatase SHP2

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Cancer‐derived non‐coding RNAs endow tumor microenvironment with immunosuppressive properties

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DeepPath: overcoming data scarcity for protein transition pathway prediction using physics-based deep learning

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Spatial interaction and functional status of CD68+SHP2+ macrophages in tumor microenvironment correlate with overall survival of NSCLC

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Combination therapy and dual-target inhibitors based on cyclin-dependent kinases (CDKs): Emerging strategies for cancer therapy

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How a single mutation alters the protein structure: a simulation investigation on protein tyrosine phosphatase SHP2

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New Directions for Advanced Targeting Strategies of EGFR Signaling in Cancer

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Cardiac Phenotype and Gene Mutations in RASopathies

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Targeting Shp2 as a therapeutic strategy for neurodegenerative diseases

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

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YinChen WuLing powder attenuates non-alcoholic steatohepatitis through the inhibition of the SHP2/PI3K/NLRP3 pathway

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Computational Elucidation of a Monobody Targeting the Phosphatase Domain of SHP2

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Setting sail: Maneuvering SHP2 activity and its effects in cancer

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Mechanisms of synergistic suppression of ALK-positive lung cancer cell growth by the combination of ALK and SHP2 inhibitors

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Protein kinase a suppresses antiproliferative effect of interferon-α in hepatocellular carcinoma by activation of protein tyrosine phosphatase SHP2

Sheng, Y., Lin, Y. H., Qiang, Z., Shen, X., He, Y., Li, L., Li, S., Zhang, G., & Wang, F. (2025) · Journal of Biological Chemistry · doi:10.1016/j.jbc.2025.108195 · Cited by 7 · see citing works

Synthetic Lethality of SHP2 and XIAP Suppresses Proliferation and Metastasis in KRAS‐mutant Nonsmall Cell Lung Cancer

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Synthetic Biology for Designing Allostery and Its Potential Biomedical Applications

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Curcumin inhibits proliferation of hepatocellular carcinoma cells by blocking PTPN1 and PTPN11 expression

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Allosteric SHP2 inhibition enhances regorafenib's effectiveness in colorectal cancer treatment

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An intramolecular energetic network regulates ligand recognition in a SH2 domain

Nardella, C., Pagano, L., Pennacchietti, V., Felice, M. D., Matteo, S. D., Diop, A., Malagrinò, F., Marcocci, L., Pietrangeli, P., Gianni, S., et al. (2023) · Protein Science · doi:10.1002/pro.4729 · Cited by 7 · see citing works

PTPN11 is a potential biomarker for type 2 diabetes mellitus complicated with colorectal cancer

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Baliosperoid A attenuates lipopolysaccharide-induced acute lung injury by targeting SHP2 to inhibit inflammation and oxidative stress

Li, Y., Zhao, L., Liu, Z., Chen, Y., Li, X., Zhu, D., & Liu, L. (2024) · Bioorganic Chemistry · doi:10.1016/j.bioorg.2024.107982 · Cited by 6 · see citing works

Allosteric SHP2 inhibitors suppress lung cancer cell migration by inhibiting non-canonical activation of EphA2 via the ERK-RSK signaling pathway

Nguyen, K., Zhou, Y., Yokoyama, S., Sasaki, S., Yano, S., Hayashi, R., Koizumi, K., Hayakawa, Y., & Sakurai, H. (2025) · Scientific Reports · doi:10.1038/s41598-025-20770-8 · Cited by 6 · see citing works

Experiment-guided molecular simulations define a heterogeneous structural ensemble for the PTPN11 tandem SH2 domains

Marasco, M., Kirkpatrick, J., Carlomagno, T., Hub, J. S., & Anselmi, M. (2023) · Chemical Science · doi:10.1039/d3sc00746d · Cited by 6 · see citing works

Development of Novel Phosphonodifluoromethyl-Containing Phosphotyrosine Mimetics and a First-In-Class, Potent, Selective, and Bioavailable Inhibitor of Human CDC14 Phosphatases

Dong, J., Jassim, B. A., Milholland, K. L., Qu, Z., Bai, Y., Miao, Y., Miao, J., Ma, Y., Lin, J., Hall, M. C., et al. (2024) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.4c00149 · Cited by 6 · see citing works

Proximity-labeling proteomics reveals remodeled interactomes and altered localization of pathogenic SHP2 variants

van Vlimmeren, A. E., Tang, L. C., Jiang, Z., Iyer, A., Voleti, R., Krismer, K., Gaublomme, J. T., Jovanović, M., & Shah, N. H. (2025) · EMBO Reports · doi:10.1038/s44319-025-00674-4 · Cited by 5 · see citing works

DOT1L suppressed the proliferation of osteosarcoma cell line via modulating SYK/EGFR/P53 and SHP2-induced STING-NLRP3-pyroptosis signaling

Hu, F. (2025) · Scientific Reports · doi:10.1038/s41598-025-05221-8 · Cited by 5 · see citing works

Molecular Docking and Target‐Specific Binding Profiles of Benzosuberane‐Based Compounds

Saragatsis, M. A., Kinsella, G. K., Curtin, J. F., & Zhang, T. (2025) · ChemMedChem · doi:10.1002/cmdc.202500365 · Cited by 5 · see citing works

Mechanism of SHP2 activation by bis-Tyr-phosphorylated Gab1

Machner, L., Shaikhqasem, A., Gruber, T., Hamdi, F., Breithaupt, C., Kniest, J., Wiebe, F., Lewitzky, M., Parthier, C., Kyrilis, F. L., et al. (2025) · Structure · doi:10.1016/j.str.2025.11.018 · Cited by 5 · see citing works

Regulation and activity of the phosphatase SHP2: SH2 domains, dephosphorylation activity, and beyond

Pierotti, C. L., & Köhn, M. (2026) · Biochemical Society Transactions · doi:10.1042/bst20253102 · Cited by 5 · see citing works

SHP2 inhibition displays efficacy as a monotherapy and in combination with JAK2 inhibition in preclinical models of myeloproliferative neoplasms

Pandey, G., Mazzacurati, L., Rowsell, T. M., Horvat, N. P., Amin, N. E., Zhang, G., Akuffo, A. A., Colin, C., Haura, E. B., Kuykendall, A. T., et al. (2024) · American Journal of Hematology · doi:10.1002/ajh.27282 · Cited by 6 · see citing works

Discovery of novel substituted pyridine carboxamide derivatives as potent allosteric SHP2 inhibitors

Lv, X., Li, P., Chen, Z., Huang, S., Zhang, S., Ji, B., Liu, J., Du, T., Zhang, T., Chen, X., et al. (2024) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2024.116830 · Cited by 5 · see citing works

Synergistic effects of BTN3A1, SHP2, CD274, and STAT3 gene polymorphisms on the risk of systemic lupus erythematosus: a multifactorial dimensional reduction analysis

Tang, Y., Xu, W., Fu, L., Liu, X.-Y., & Huang, A. (2023) · Clinical Rheumatology · doi:10.1007/s10067-023-06765-8 · Cited by 6 · see citing works

IL-17 receptor goes solo in autoimmune inflammation

Bittner, S., & Zipp, F. (2023) · Immunity · doi:10.1016/j.immuni.2023.08.007 · Cited by 5 · see citing works

Identification of new small molecule allosteric SHP2 inhibitor through pharmacophore-based virtual screening, molecular docking, molecular dynamics simulation studies, synthesis and in vitro evaluation

Mitra, R., Kumar, S., & Ayyannan, S. R. (2023) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2023.2291733 · Cited by 5 · see citing works

A Novel Gain-of-Signal Assay to Detect Targeted Protein Degradation

Hoffman, M., Cheah, K. M., & Wittrup, K. D. (2024) · ACS Synthetic Biology · doi:10.1021/acssynbio.3c00447 · Cited by 5 · see citing works

Targeting SHP2 with Natural Products: Exploring Saponin-Based Allosteric Inhibitors and Their Therapeutic Potential

Moon, D. (2025) · Current Issues in Molecular Biology · doi:10.3390/cimb47050309 · Cited by 4 · see citing works

Emerging opportunities to treat drug-resistant breast cancer: Discovery of novel small-molecule inhibitors against different targets

Chen, R., Zhou, Z.-L., Meng, X., Lei, Y., Wang, D., & Wang, Y. (2025) · Frontiers in Pharmacology · doi:10.3389/fphar.2025.1578342 · Cited by 4 · see citing works

SHP2: A Redox-Sensitive Regulator Linking Immune Checkpoint Inhibitor Therapy to Cancer Treatment and Vascular Risk

Moreno, S. F. L., Lenz, S. A., Casso-Chapa, B., Paniagua-Bojorges, A., Kim, J. H., Palaskas, N. L., Nead, K. T., Samanthapudi, V. S. K., Mejia, G. F., Hoang, O. N., et al. (2025) · Antioxidants · doi:10.3390/antiox14121388 · Cited by 4 · see citing works

Phosphatase SHP2 pathogenic mutations enhance activity by altering conformational sampling

Glaser, A., Padua, R. A. P., Ojoawo, A. M., Sullivan, C., & Kern, D. (2026) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.2513851123 · Cited by 4 · see citing works

Folding and Binding Kinetics of the Tandem of SH2 Domains from SHP2

Pagano, L., Pennacchietti, V., Malagrinò, F., Felice, M. D., Toso, J., Puglisi, E., Gianni, S., & Toto, A. (2024) · International Journal of Molecular Sciences · doi:10.3390/ijms25126566 · Cited by 4 · see citing works

SHP2 regulates the HIF-1 signaling pathway in the decidual human endometrial stromal cells

Ouyang, L., Gao, X., Yang, R., Zhou, P., Cai, H., Tian, Y., Wang, H., Kong, S., & Lu, Z. (2025) · Biology of Reproduction · doi:10.1093/biolre/ioaf019 · Cited by 4 · see citing works

Deletion of the tyrosine phosphatase Shp2 in cervical cancer cells promotes reprogramming of glutamine metabolism

Gao, X., Kang, J., Li, X., Chen, C., & Luo, D. (2023) · The FASEB Journal · doi:10.1096/fj.202202078rr · Cited by 4 · see citing works

Relationship between SHP2 gene polymorphisms and systemic lupus erythematosus risk

Li, R., Zhou, L., Yang, C., Xu, W., & Huang, A. (2023) · International Journal of Rheumatic Diseases · doi:10.1111/1756-185x.14761 · Cited by 4 · see citing works

PZR promotes tumorigenicity of lung cancer cells by regulating cell migration and invasion via modulating oxidative stress and cell adhesion

Fu, Y., Sui, Y., Zhao, Y., Jiang, J., Wang, X., Cui, J., Fu, X., Xing, S., & Zhao, Z. J. (2023) · Aging · doi:10.18632/aging.204771 · Cited by 4 · see citing works

Molecular recognition of ITIM/ITSM domains with SHP2 and their allosteric effect

Yan, C., Ouyang, W., Liu, L., Tang, L., Zhang, Z., Yue, X., Liang, L., Hu, J., & Luo, T. L. (2023) · Physical Chemistry Chemical Physics · doi:10.1039/d3cp03923d · Cited by 4 · see citing works

Novel insight into mechanisms of ROS1 catalytic activation via loss of the extracellular domain

Jones, K. L., Keddy, C., Jenkins, C., Nicholson, K. S., Shinde, U. P., & Davare, M. A. (2024) · Scientific Reports · doi:10.1038/s41598-024-71687-7 · Cited by 3 · see citing works

Targeting Glycolysis for Spinal Cord Injury: Regulatory Mechanisms and Therapeutic Prospects.

Qian, S., Shi, C., Wang, B., Guo, Y., Dan, L., Dang, Z., Zhao, X.-W., Gao, F., Yang, Y., Shen, J., et al. (2025) · ACS Chemical Neuroscience · doi:10.1021/acschemneuro.5c00604 · Cited by 3 · see citing works

Exploring the allosteric effect of SHP2 Tyr62 phosphorylation on the emergence of acquired resistance to allosteric inhibitor SHP099

Du, T., Gu, L., Xu, S., Zhang, J., Qiu, X., Liu, W., Zheng, G., Li, B., Zhou, B., & Li, M.-Y. (2025) · Journal of Biomolecular Structure and Dynamics · doi:10.1080/07391102.2025.2507815 · Cited by 2 · see citing works

Novel azabicyclic series of potent SHP2 allosteric inhibitors

Sferrazza, A., Rossetti, I., Fabbrini, D., Torrente, E., Relitti, N., Ferrigno, F., Fezzardi, P., Iaccarino, C., Bisbocci, M., Cellucci, A., et al. (2025) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/j.bmcl.2025.130383 · Cited by 2 · see citing works

Mapping of PTP1B, TCPTP, SHP2, and Putative Substrates Reveals Novel Networks in Glomerular Podocytes

LeBleu, G., Hsu, M.-F., Ito, Y., Liang, S., Ma, K., Meng, T., & Haj, F. G. (2026) · Journal of Cellular Physiology · doi:10.1002/jcp.70128 · Cited by 2 · see citing works

Balancing the Edge: Phosphatases as Homeostatic Buffers of Oncogenic Kinase Signaling in Cancer

Ehm, P. A. H. (2026) · Kinases and Phosphatases · doi:10.3390/kinasesphosphatases4010004 · Cited by 2 · see citing works

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 2 · see citing works

Computational study on the binding mechanism of allosteric drug TNO155 inhibiting SHP2E76A

Yang, L., Zhao, H., Yuan, F., Chen, M., Ma, N., Yin, Z., Liu, H., & Guo, Y. (2024) · Molecular Diversity · doi:10.1007/s11030-024-10881-1 · Cited by 2 · see citing works

Effects of changes in SHP2 expression on liver fibrosis by influencing the apoptosis of hepatic stellate cells

Hao, L., Ji, J., Jiang, M., Song, J., Chen, P., Zhan, Z., Miao, X., Gao, Y., Wang, W., & Liu, T. (2024) · Apmis · doi:10.1111/apm.13487 · Cited by 2 · see citing works

SHP2 promotes the epithelial-mesenchymal transition in triple negative breast cancer cells by regulating β-catenin

Qian, S., Zhu, J., Han, Q., Cheng, H., & Zhou, H. (2025) · Journal of Cancer Research and Clinical Oncology · doi:10.1007/s00432-025-06097-x · Cited by 2 · see citing works

Structure-guided expansion strategy unveils potent allosteric SHP2 inhibitors with synergistic efficacy against AML through MCL-1 co-targeting

Zhang, M., Wu, S., Liu, M., Li, H., Wang, L., Duan, F., Han, R., Shan, C., Jiang, Z., Liao, J., et al. (2025) · European Journal of Medicinal Chemistry · doi:10.1016/j.ejmech.2025.117988 · Cited by 1 · see citing works

PZR: Advances in research from cellular signaling Hub to emerging therapeutic targets

Wang, H. P., Sha, W., Fu, Y., & Wang, H. (2025) · Cellular Signalling · doi:10.1016/j.cellsig.2025.112061 · Cited by 1 · see citing works

Design, synthesis, and antiproliferative evaluation of dihydropyrimidinone-pyrazole derivatives as potential SHP2 inhibitors via in silico target prediction

Kou, S., Peng, X., Li, S., Yi, H. L., Sun, L., & Li, Z. (2026) · Future Medicinal Chemistry · doi:10.1080/17568919.2025.2599594 · Cited by 1 · see citing works

Progression and perspectives in disease modeling for Juvenile myelomonocytic leukemia

Fu, S., Guo, Y., Peng, Z., Zhang, D., Chang, Z., Xiao, Y., Zhang, Q., Yu, L., Chen, C., Chen, Y., et al. (2024) · Medical Oncology · doi:10.1007/s12032-024-02549-5 · Cited by 1 · see citing works

High-throughput biochemical phenotyping of SHP2 variants reveals the molecular basis of diseases and allosteric drug inhibitionPreprint

Lee, A. A., Mokhtari, D. A., Egan, E. D., Blacklow, S. C., Herschlag, D., & Fordyce, P. M. (2026) · bioRxiv (Cold Spring Harbor Laboratory) · doi:10.64898/2026.03.30.715055 · Cited by 1 · see citing works

Crystallization and preliminary diffraction analysis of the T2I·L262F double mutant form of SHP2

Lee, H. S., Ku, B., Shin, H., & Kim, S. J. (2022) · Korean Society for Structural Biology · doi:10.34184/kssb.2022.10.4.69

THE FEATURES AND ROLE OF SHP2 PROTEIN IN POSTNATAL MUSCLE DEVELOPMENT

Aphkhazava, D., Tuphinashvili, T., Sulashvili, N., & Nozadze, M. (2023) · doi:10.52340/spectri.2023.01

Impact of SHP2 tyrosine phosphorylation on the development of acquired resistance to allosteric SHP2 inhibitors

Franciosa, G., & Olsen, J. V. (2023) · Oncotarget · doi:10.18632/oncotarget.28392

Therapeutic Effect of Shp2 Inhibition Combined with Regorafenib in Advanced Colorectal CancerPreprint

Han, X., Wang, W., Zhang, W., Zhu, L., Xu, L., Li, X., Xu, Q., Guo, W., & Gu, Y. (2023) · SSRN Electronic Journal · doi:10.2139/ssrn.4534174

Analysis of the clinical characteristics and prognosis of adult de novo acute myeloid leukemia (none APL) with PTPN11 mutations

Li, S., Liu, Y., Zhu, Y., Zhou, J., & Hua, H. (2023) · Open Medicine · doi:10.1515/med-2023-0830

Author's Reply: “Aquaporin 1 in cancer: Oncogene or a tumor suppressor?”

Zhuang, M.-Q., Zhou, H., & Zhou, Y.-B. (2023) · Digestive and Liver Disease · doi:10.1016/j.dld.2023.11.003

Discovery of Novel Substituted Pyridine Carboxamide Derivatives as Potent and Selective Shp2 Allosteric InhibitorsPreprint

Lv, X., Li, P., Chen, Z., Huang, S., Du, T., Ji, B., Zhang, S., Liu, J., Zhang, T., Chen, X., et al. (2024) · SSRN Electronic Journal · doi:10.2139/ssrn.4871858

Bioinformatic analysis of neuropeptide related genes in patients diagnosed with invasive breast carcinoma

Yay, F., & Ayan, D. (2024) · Computers in Biology and Medicine · doi:10.1016/j.compbiomed.2024.109304

Research Progress of SHP2 Modulator in Anti-Tumor Biological Mechanism

Guo, J. (2025) · BIO Web of Conferences · doi:10.1051/bioconf/202517402019

SHP2 happens, just sail with it: the role of the protein tyrosine phosphatase SHP2 in autoimmune and autoinflammatory diseases

Sommer, S. L., & Kontaridis, M. I. (2025) · Current Opinion in Physiology · doi:10.1016/j.cophys.2025.100833

Discovery of Potent and Orally bioavailable Benzoazepinamine-Based SHP2 Allosteric Inhibitors for the Treatment of Inflammatory Diseases

Jiang, W., Hou, Q., Hua, D., Zeng, Y., Huang, C., Luo, G., Li, K., Jin, Z., Chen, X., Li, W., et al. (2025) · Journal of Medicinal Chemistry · doi:10.1021/acs.jmedchem.5c01578

MiR-590 Targets SHP2 to Promote Cervical Cancer Proliferation and Tumor Formation through Regulation of the JAK-STAT Signaling PathwayPreprint

Li, Y., Li, X., Diao, Y., Weng, X., Zhang, L., Zhu, X., & Sun, P. (2025) · Research Square · doi:10.21203/rs.3.rs-8106230/v1

CBX2 promoted oral squamous cell carcinoma via increasing CEP55/NF-κB/METTL3/SHP2 signaling induced metastasis/proliferation and angiogenesis

Ma, S., Wang, Z., LI, C., Liu, Z., & Zhang, X. (2025) · Scientific Reports · doi:10.1038/s41598-025-31475-3

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

Song, Y., Zhao, M., Zhang, H., & Yu, B. (2022) · Pharmacology &amp; Therapeutics · doi:10.1016/j.pharmthera.2021.107966 · Cited by 125 · see citing works

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 8 · see citing works

Small-molecule Modulators Targeting SHP2 for Cancer Therapy

Chen, Y., Mi, D., & Li, Y. (2022) · Anti-Cancer Agents in Medicinal Chemistry · doi:10.2174/1871520622666220921093052 · Cited by 16 · see citing works

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 2 · see citing works

Protein Tyrosine Phosphatase SHP-2 and its Relation with Cancer

Rocha, S. F. L. D. S., de Salles, C. M. C., & Sant’Anna, C. M. R. (2017) · Revista Virtual de Química · doi:10.21577/1984-6835.20170078