ReviewCancer science2009
Protein tyrosine phosphatase SHP-2: a proto-oncogene product that promotes Ras activation.
Review in Cancer science, 2009. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 116 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
116 citing papers in PubMed, 235 citations in OpenAlex.
- Allosteric PROTACs: Expanding the Horizon of Targeted Protein Degradation.Journal of the American Chemical Society · 2026Review
- Topical Trichosanthis Radix Water Extract Attenuates Atopic Dermatitis-Like Skin Inflammation: Marker Standardization, Network Pharmacology, and Preclinical Validation.Mediators of inflammation · 2026Article
- SFX-01 is therapeutic against myeloproliferative disorders caused by activating mutations in Shp2.EMBO molecular medicine · 2025Article
- First Results of Migoprotafib, a Potent and Highly Selective Src Homology-2 Domain-Containing Phosphatase 2 Inhibitor in Patients with Advanced Solid Tumors.Molecular cancer therapeutics · 2025Article
- Computational Elucidation of a Monobody Targeting the Phosphatase Domain of SHP2.Biomolecules · 2025Article
- KRAS inhibitors: resistance drivers and combinatorial strategies.Trends in cancer · 2025Review
- Ferrocenyl-Substituted Curcumin Derivatives as Potential SHP-2 Inhibitors for Anticolorectal Cancer: Design, Synthesis andACS omega · 2024Article
- Multipartite Fluorogenic Sensors for Monitoring Tyrosine Phosphatase Activity.Chembiochem : a European journal of chemical biology · 2024Article
- Integrating Vascular Phenotypic and Proteomic Analysis in an Open Microfluidic Platform.ACS nano · 2024Article
- Non-Receptor Tyrosine Kinases: Their Structure and Mechanistic Role in Tumor Progression and Resistance.Cancers · 2024Review
- Zebrafish Congenital Heart Disease Models: Opportunities and Challenges.International journal of molecular sciences · 2024Review
- RNA-Seq Analysis Reveals Altered Expression of Cell Adhesion-Related Genes Following PZR Knockout in Lung Cancer Cells.Applied biochemistry and biotechnology · 2024Article
- Tyrosine phosphataseFrontiers in immunology · 2024Review
- The clinical features and prognostic implications of PTPN11 mutation in adult patients with acute myeloid leukemia in China.Cancer medicine · 2023Article
- New insights into RAS in head and neck cancer.Biochimica et biophysica acta. Reviews on cancer · 2023Review
- Identification of CD133eLife · 2023Article
- RETRACTED: Protein Tyrosine Phosphatase Non-Receptor 11 (International journal of molecular sciences · 2023Article
- Kinase Inhibitors in Genetic Diseases.International journal of molecular sciences · 2023Review
- Setting sail: Maneuvering SHP2 activity and its effects in cancer.Advances in cancer research · 2023Review
- Measuring Protein Tyrosine Phosphatase Activity Dependent on SH2 Domain-Mediated Regulation.Methods in molecular biology (Clifton, N.J.) · 2023Article
56 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
SHP-2 is a cytoplasmic protein tyrosine phosphatase (PTP) that contains two Src homology 2 (SH2) domains. Although PTPs are generally considered to be negative regulators on the basis of their ability to oppose the effects of protein tyrosine kinases, SHP-2 is unusual in that it promotes the activation of the Ras-MAPK signaling pathway by receptors for various growth factors and cytokines. The molecular basis for the activation of SHP-2 is also unique: In the basal state, the NH(2)-terminal SH2 domain of SHP-2 interacts with the PTP domain, resulting in autoinhibition of PTP activity; the binding of SHP-2 via its SH2 domains to tyrosine-phosphorylated growth factor receptors or docking proteins, however, results in disruption of this intramolecular interaction, leading to exposure of the PTP domain and catalytic activation. Indeed, SHP-2 proteins with artificial mutations in the NH(2)-terminal SH2 domain have been shown to act as dominant active mutants in vitro. Such activating mutations of PTPN11 (human SHP-2 gene) were subsequently identified in individuals with Noonan syndrome, a human developmental disorder that is sometimes associated with juvenile myelomonocytic leukemia. Furthermore, somatic mutations of PTPN11 were found to be associated with pediatric leukemia. SHP-2 is also thought to participate in the development of other malignant disorders, but in a manner independent of such activating mutations. Biochemical and functional studies of SHP-2 and genetic analysis of PTPN11 in human disorders have thus converged to provide new insight into the pathogenesis of cancer as well as potential new targets for cancer treatment.
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Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.