Role of SHP2 (PTPN11) in glycoprotein VI-dependent thrombus formation: Improved platelet responsiveness by the allosteric drug SHP099 in Noonan syndrome patients.
暂无分享,去创建一个
Ángel García | J. Heemskerk | Y. Henskens | M. Kuijpers | M. Te Loo | Delia I. Fernández | Jingnan Huang | Lidia Hermida-Nogueira | S. Veiras | M. Diender | Marijke J E Kuijpers | D. Fernández
[1] J. Heemskerk. More than reverting tyrosine kinases. , 2022, Blood.
[2] A. Sickmann,et al. Roles of Focal Adhesion Kinase PTK2 and Integrin αIIbβ3 Signaling in Collagen- and GPVI-Dependent Thrombus Formation under Shear , 2022, International journal of molecular sciences.
[3] A. Greinacher,et al. GPVI expression is linked to platelet size, age, and reactivity , 2022, Blood advances.
[4] Jiao Kong,et al. Recent advances in the discovery of protein tyrosine phosphatase SHP2 inhibitors. , 2022, RSC medicinal chemistry.
[5] Shu Wang,et al. Strategies Targeting Protein Tyrosine Phosphatase SHP2 for Cancer Therapy. , 2022, Journal of medicinal chemistry.
[6] M. Nijziel,et al. Comparison of inhibitory effects of irreversible and reversible Btk inhibitors on platelet function , 2021, EJHaem.
[7] G. Shapiro,et al. Initial results from a dose finding study of TNO155, a SHP2 inhibitor, in adults with advanced solid tumors. , 2021 .
[8] M. Peppelenbosch,et al. The role of phospho-tyrosine signaling in platelet biology and hemostasis. , 2020, Biochimica et biophysica acta. Molecular cell research.
[9] P. Hammerman,et al. Combinations with Allosteric SHP2 Inhibitor TNO155 to Block Receptor Tyrosine Kinase Signaling , 2020, Clinical Cancer Research.
[10] Michael K. Wendt,et al. SHP2 is a multifunctional therapeutic target in drug resistant metastatic breast cancer , 2020, Oncogene.
[11] Runling Wang,et al. Allosteric inhibitors of SHP2: an updated patent review (2015-2020). , 2020, Current medicinal chemistry.
[12] Xiao-Feng Xiong,et al. Tyrosine phosphatase SHP2 inhibitors in tumor-targeted therapies , 2020, Acta pharmaceutica Sinica. B.
[13] R. van Oerle,et al. Platelet-primed interactions of coagulation and anticoagulation pathways in flow-dependent thrombus formation , 2020, Scientific Reports.
[14] S. Nampoothiri,et al. Molecular and clinical studies in 107 Noonan syndrome affected individuals with PTPN11 mutations , 2020, BMC Medical Genetics.
[15] Haopeng Sun,et al. Therapeutic potential of targeting SHP2 in human developmental disorders and cancers. , 2020, European journal of medicinal chemistry.
[16] B. Neel,et al. Catalytic dysregulation of SHP2 leading to Noonan syndromes impacts on platelet signaling and functions. , 2019, Blood.
[17] Qiang Xu,et al. Targeting SHP2 as a promising strategy for cancer immunotherapy. , 2019, Pharmacological research.
[18] M. Loza,et al. A Comprehensive Tyrosine Phosphoproteomic Analysis Reveals Novel Components of the Platelet CLEC-2 Signaling Cascade , 2019, Thrombosis and Haemostasis.
[19] Y. Liu,et al. Platelet Shp2 negatively regulates thrombus stability under high shear stress , 2018, Journal of thrombosis and haemostasis : JTH.
[20] W. Ouwehand,et al. High-throughput elucidation of thrombus formation reveals sources of platelet function variability , 2018, Haematologica.
[21] Qiang Xu,et al. Tyrosine phosphatase SHP2 negatively regulates NLRP3 inflammasome activation via ANT1-dependent mitochondrial homeostasis , 2017, Nature Communications.
[22] Chunlei Liu,et al. ClinVar: improving access to variant interpretations and supporting evidence , 2017, Nucleic Acids Res..
[23] S. Pfister,et al. Recommendations for Cancer Surveillance in Individuals with RASopathies and Other Rare Genetic Conditions with Increased Cancer Risk , 2017, Clinical Cancer Research.
[24] Sarah L. Williams,et al. Allosteric Inhibition of SHP2: Identification of a Potent, Selective, and Orally Efficacious Phosphatase Inhibitor. , 2016, Journal of medicinal chemistry.
[25] Ping Zhu,et al. Allosteric inhibition of SHP2 phosphatase inhibits cancers driven by receptor tyrosine kinases , 2016, Nature.
[26] J. Heemskerk,et al. Platelet Control of Fibrin Distribution and Microelasticity in Thrombus Formation Under Flow , 2016, Arteriosclerosis, thrombosis, and vascular biology.
[27] M. Summar,et al. Malignancy in Noonan syndrome and related disorders , 2015, Clinical genetics.
[28] S. Rahmouni,et al. Perspective: Tyrosine phosphatases as novel targets for antiplatelet therapy. , 2015, Bioorganic & medicinal chemistry.
[29] Rachel Cavill,et al. Identification of platelet function defects by multi-parameter assessment of thrombus formation , 2014, Nature Communications.
[30] I. Martinelli,et al. Hemostatic Abnormalities in Noonan Syndrome , 2014, Pediatrics.
[31] H. ten Cate,et al. Additive roles of platelets and fibrinogen in whole-blood fibrin clot formation upon dilution as assessed by thromboelastometry , 2013, Thrombosis and Haemostasis.
[32] B. Neel,et al. Megakaryocyte-specific deletion of the protein-tyrosine phosphatases Shp1 and Shp2 causes abnormal megakaryocyte development, platelet production, and function. , 2013, Blood.
[33] S. Watson,et al. Mice Lacking the ITIM-Containing Receptor G6b-B Exhibit Macrothrombocytopenia and Aberrant Platelet Function , 2012, Science Signaling.
[34] L. Kiemeney,et al. Cancer risk in patients with Noonan syndrome carrying a PTPN11 mutation , 2011, European Journal of Human Genetics.
[35] D. Jackson,et al. CEACAM1 negatively regulates platelet-collagen interactions and thrombus growth in vitro and in vivo. , 2009, Blood.
[36] Y. Matsubara,et al. The RAS/MAPK syndromes: novel roles of the RAS pathway in human genetic disorders , 2008, Human mutation.
[37] I. van der Burgt,et al. Noonan Syndrome , 2019, Encyclopedia of Endocrine Diseases.
[38] R. Foà,et al. Diversity and functional consequences of germline and somatic PTPN11 mutations in human disease. , 2006, American journal of human genetics.
[39] M. V. van Zandvoort,et al. The Glycoprotein VI-Phospholipase C&ggr;2 Signaling Pathway Controls Thrombus Formation Induced by Collagen and Tissue Factor In Vitro and In Vivo , 2005, Arteriosclerosis, thrombosis, and vascular biology.
[40] J. Krieger,et al. Neurofibromatosis–Noonan syndrome: Molecular evidence of the concurrence of both disorders in a patient , 2005, American journal of medical genetics. Part A.
[41] H. Ohashi,et al. Functional analysis of PTPN11/SHP-2 mutants identified in Noonan syndrome and childhood leukemia , 2005, Journal of Human Genetics.
[42] John D. Minna,et al. Activating Mutations of the Noonan Syndrome-Associated SHP2/PTPN11 Gene in Human Solid Tumors and Adult Acute Myelogenous Leukemia , 2004, Cancer Research.
[43] B. Gelb,et al. Genetic evidence for lineage-related and differentiation stage-related contribution of somatic PTPN11 mutations to leukemogenesis in childhood acute leukemia. , 2004, Blood.
[44] S. Watson,et al. GPVI levels in platelets: relationship to platelet function at high shear. , 2003, Blood.
[45] J. Licht,et al. Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia , 2003, Nature Genetics.
[46] H. Ropers,et al. Spectrum of mutations in PTPN11 and genotype–phenotype correlation in 96 patients with Noonan syndrome and five patients with cardio-facio-cutaneous syndrome , 2003, European Journal of Human Genetics.
[47] Michael A. Patton,et al. Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome , 2001, Nature Genetics.
[48] T. Pawson,et al. Abnormal mesoderm patterning in mouse embryos mutant for the SH2 tyrosine phosphatase Shp‐2 , 1997, The EMBO journal.
[49] E. Mariman,et al. Clinical and molecular studies in a large Dutch family with Noonan syndrome. , 1994, American journal of medical genetics.
[50] R. Tsien,et al. A new generation of Ca2+ indicators with greatly improved fluorescence properties. , 1985, The Journal of biological chemistry.