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Negative Regulation of Stat3 by Activating PTPN11 Mutants Contributes to the Pathogenesis of Noonan Syndrome and Juvenile Myelomonocytic Leukemia

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Mutated Ptpn11 alters leukemic stem cell frequency and reduces the sensitivity of acute myeloid leukemia cells to Mcl1 inhibition

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SHP2 forecast for the immune system: fog gradually clearing.

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Germline Mutations in Components of the Ras Signaling Pathway in Noonan Syndrome and Related Disorders

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PU.1, Interferon Regulatory Factor (IRF) 2, and the Interferon Consensus Sequence-binding Protein (ICSBP/IRF8) Cooperate to Activate NF1 Transcription in Differentiating Myeloid Cells

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

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SHP-2 in Lymphocytes' Cytokine and Inhibitory Receptor Signaling

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Recent advances in the pathogenesis and management of juvenile myelomonocytic leukaemia

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Activating PTPN11 mutations play a minor role in pediatric and adult solid tumors

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Effects of a Leukemia-associated Gain-of-Function Mutation of SHP-2 Phosphatase on Interleukin-3 Signaling

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Inhibition of the Gab2/PI3K/mTOR signaling ameliorates myeloid malignancy caused by Ptpn11 (Shp2) gain-of-function mutations

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

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Targeting Protein Tyrosine Phosphatase SHP2 for the Treatment of PTPN11 -Associated Malignancies

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Induction of a Tumor-associated Activating Mutation in Protein Tyrosine Phosphatase Ptpn11 (Shp2) Enhances Mitochondrial Metabolism, Leading to Oxidative Stress and Senescence

Zheng, H., Li, S., Hsu, P., & Qu, C. (2013) · Journal of Biological Chemistry · doi:10.1074/jbc.m113.462291 · Cited by 48 · see citing works

How do Shp2 mutations that oppositely influence its biochemical activity result in syndromes with overlapping symptoms?

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Noonan Syndrome-associated SHP-2/Ptpn11 Mutants Enhance SIRPα and PZR Tyrosyl Phosphorylation and Promote Adhesion-mediated ERK Activation

Eminaga, S., & Bennett, A. M. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m801382200 · Cited by 46 · see citing works

SHP2 Is a Target of the Immunosuppressant Tautomycetin

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SHP2E76K mutant promotes lung tumorigenesis in transgenic mice

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Identification of Small Molecular Weight Inhibitors of Src Homology 2 Domain-Containing Tyrosine Phosphatase 2 (SHP-2) via in Silico Database Screening Combined with Experimental Assay

Yu, W., Guvench, O., MacKerell, A. D., & Qu, C. (2008) · Journal of Medicinal Chemistry · doi:10.1021/jm800229d · Cited by 43 · see citing works

SHP-2 phosphatase is required for hematopoietic cell transformation by Bcr-Abl

Chen, J., Yu, W., Daino, H., Broxmeyer, H. E., Druker, B. J., & Qu, C. (2006) · Blood · doi:10.1182/blood-2006-04-019141 · Cited by 42 · see citing works

Leukemia-Associated, Constitutively Active Mutants of SHP2 Protein Tyrosine Phosphatase Inhibit <i>NF1</i> Transcriptional Activation by the Interferon Consensus Sequence Binding Protein

Huang, W., Saberwal, G., Horvath, E., Zhu, C., Lindsey, S., & Eklund, E. A. (2006) · Molecular and Cellular Biology · doi:10.1128/mcb.00036-06 · Cited by 41 · see citing works

Protein-tyrosine Phosphatase Shp2 Positively Regulates Macrophage Oxidative Burst

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

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Activating PTPN11 mutants promote hematopoietic progenitor cell-cycle progression and survival

Yang, Z., Li, Y., Yin, F., & Chan, R. J. (2008) · Experimental Hematology · doi:10.1016/j.exphem.2008.04.016 · Cited by 41 · see citing works

Counteracting Effects Operating on Src Homology 2 Domain-containing Protein-tyrosine Phosphatase 2 (SHP2) Function Drive Selection of the Recurrent Y62D and Y63C Substitutions in Noonan Syndrome*

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PI3K p110δ uniquely promotes gain-of-function Shp2-induced GM-CSF hypersensitivity in a model of JMML.

Goodwin, C. B., Li, X.-J., Mali, R., Chan, G., Kang, M. W., Liu, Z.-Y., Vanhaesebroeck, B., Neel, B., Loh, M., Lannutti, B., et al. (2014) · Blood · doi:10.1182/blood-2013-10-535104 · Cited by 39 · see citing works

Activating Mutations in Protein Tyrosine Phosphatase Ptpn11 (Shp2) Enhance Reactive Oxygen Species Production That Contributes to Myeloproliferative Disorder

Xu, D., Zheng, H., Yu, W.-M., & Qu, C. (2013) · PLoS ONE · doi:10.1371/journal.pone.0063152 · Cited by 37 · see citing works

Impact of PTPN11 mutations on clinical outcome analyzed in 1529 patients with acute myeloid leukemia

Stasik, S., Eckardt, J., Krämer, M., Röllig, C., Krämer, A., Scholl, S., Hochhaus, A., Crysandt, M. M., Brümmendorf, T. H., Naumann, R., et al. (2021) · Blood Advances · doi:10.1182/bloodadvances.2021004631 · Cited by 36 · see citing works

Protein Tyrosine Phosphatase SHP2 Mediates Chronic Insulin-Induced Endothelial Inflammation

Giri, H., Muthuramu, I., Dhar, M., Rathnakumar, K., Ram, U., & Dixit, M. (2012) · Arteriosclerosis Thrombosis and Vascular Biology · doi:10.1161/atvbaha.111.239251 · Cited by 37 · see citing works

Childhood Myelodysplastic Syndrome: Focus on the Approach to Diagnosis and Treatment of Juvenile Myelomonocytic Leukemia

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Noonan Syndrome/Leukemia-associated Gain-of-function Mutations in SHP-2 Phosphatase (PTPN11) Enhance Cell Migration and Angiogenesis

Wang, S., Yu, W., Zhang, W., McCrae, K. R., Neel, B. G., & Qu, C. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m804129200 · Cited by 37 · see citing works

p38 MAPK inhibition suppresses the TLR-hypersensitive phenotype in FANCC- and FANCA-deficient mononuclear phagocytes

Anur, P., Yates, J. E., Garbati, M. R., Vanderwerf, S. M., Keeble, W. W., Rathbun, K. R., Hays, L. E., Tyner, J. W., Svahn, J., Cappelli, E., et al. (2012) · Blood · doi:10.1182/blood-2011-06-354647 · Cited by 36 · see citing works

SH2 Domain-Containing Protein-Tyrosine Phosphatases

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Shp-2 heterozygous hematopoietic stem cells have deficient repopulating ability due to diminished self-renewal

Chan, R. J., Li, Y., Hass, M. N., Walter, A., Voorhorst, C. S., Shelley, W. C., Yang, Z., Orschell, C. M., & Yöder, M. C. (2006) · Experimental Hematology · doi:10.1016/j.exphem.2006.04.017 · Cited by 32 · see citing works

Gain‐of‐function mutation in PTPN11 in histiocytic sarcomas of Bernese Mountain Dogs

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Targeting SHP2 phosphatase in hematological malignancies

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Increased c-Jun Expression and Reduced GATA2 Expression Promote Aberrant Monocytic Differentiation Induced by Activating PTPN11 Mutants

Yang, Z., Kondo, T., Voorhorst, C. S., Nabinger, S. C., Ndong, L., Yin, F., Chan, E. M., Yu, M., Würstlin, O., Kratz, C. P., et al. (2009) · Molecular and Cellular Biology · doi:10.1128/mcb.01330-08 · Cited by 31 · see citing works

Noonan Syndrome, the Ras–MAPK Signalling Pathway and Short Stature

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Structural and functional effects of disease‐causing amino acid substitutions affecting residues Ala72 and Glu76 of the protein tyrosine phosphatase SHP‐2

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The Austrian biodatabase for chronic myelomonocytic leukemia (ABCMML)

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Angiopoietin‐2 mediates thrombin‐induced monocyte adhesion and endothelial permeability

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Novel approaches to diagnosis and treatment of Juvenile Myelomonocytic Leukemia

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

Dráber, P., Štěpánek, O., Hrdinka, M., Drobek, A., Chmátal, L., Mala, L., Ormsby, T., Angelisová, P., Hořejšı́, V., & Brdička, T. (2012) · Journal of Biological Chemistry · doi:10.1074/jbc.m112.339143 · Cited by 24 · see citing works

Juvenile myelomonocytic leukaemia-associated mutation in Cbl promotes resistance to apoptosis via the Lyn-PI3K/AKT pathway

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A tyrosine phosphatase SHP2 gain-of-function mutation enhances malignancy of breast carcinoma

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After 95 years, it's time to eRASe JMML

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SHP-2 tyrosine phosphatase in human diseases.

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Genetic disruption of the PI3K regulatory subunits, p85 , p55 , and p50 , normalizes mutant PTPN11-induced hypersensitivity to GM-CSF

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Correlation of RAS-Pathway Mutations and Spontaneous Myeloid Colony Growth with Progression and Transformation in Chronic Myelomonocytic Leukemia—A Retrospective Analysis in 337 Patients

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PTPN11 Mutations E76K, D61V, and D61Y Induce Hypersensitivity of Hematopoietic Progenitors to GM-CSF and IL-3.

Chan, R. J., Li, Y., & Leedy, M. B. (2004) · Blood · doi:10.1182/blood.v104.11.2559.2559

Activating PTPN11 Mutants Promote Myelomonocytic Differentiation Due to Altered Hematopoietic Lineage-Specific Transcription Factor Expression.

Chan, R. J., Voorhorst, C. S., Kondo, T., & Hashino, E. (2005) · Blood · doi:10.1182/blood.v106.11.3519.3519 · Cited by 1 · see citing works

Phosphatidylinositol-3-Kinase p110d Uniquely Promotes Gain-Of-Function PTPN11-Induced GM-CSF Hypersensitivity In a Model Of Juvenile Myelomonocytic Leukemia

Goodwin, C. B., Mali, R. S., Chan, G., Neel, B. G., Lannutti, B. J., Kapur, R., & Chan, R. J. (2013) · Blood · doi:10.1182/blood.v122.21.3678.3678

Biochemical Dissection of SHP-2 and C-CBL in Juvenile Myelomonocytic Leukemia

Shin, D. H. (2012) · eScholarship (California Digital Library)

Functional analysis of leukemia-associated PTPN11 mutations in primary hematopoietic cells

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