References analysis of the Wikipedia article "PTPN11" in the Japanese version

doi.org (Global: 2^nd place; Japanese: 6^th place)

“Mapping a gene for Noonan syndrome to the long arm of chromosome 12”. Nat. Genet. 8 (4): 357–60. (December 1994). doi:10.1038/ng1294-357. PMID 7894486.

“Identification of a human Src homology 2-containing protein-tyrosine-phosphatase: a putative homolog of Drosophila corkscrew”. Proc. Natl. Acad. Sci. U.S.A. 89 (23): 11239–43. (December 1992). doi:10.1073/pnas.89.23.11239. PMC 50525. PMID 1280823.

“Whole-genome sequencing of a single proband together with linkage analysis identifies a Mendelian disease gene”. PLoS Genet. 6 (6): e1000991. (June 2010). doi:10.1371/journal.pgen.1000991. PMC 2887469. PMID 20577567.

“Germline gain-of-function mutations in SOS1 cause Noonan syndrome”. Nat. Genet. 39 (1): 70–4. (January 2007). doi:10.1038/ng1926. PMID 17143285.

“PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects”. J. Biol. Chem. 281 (10): 6785–92. (March 2006). doi:10.1074/jbc.M513068200. PMID 16377799.

“Activating mutations of the noonan syndrome-associated SHP2/PTPN11 gene in human solid tumors and adult acute myelogenous leukemia”. Cancer Res. 64 (24): 8816–20. (December 2004). doi:10.1158/0008-5472.CAN-04-1923. PMID 15604238.

“High NPM1 mutant allele burden at diagnosis predicts unfavorable outcomes in de novo AML”. Blood 131 (25): 2816–2825. (May 2018). doi:10.1182/blood-2018-01-828467. PMC 6265642. PMID 29724895.

“Ptpn11/Shp2 acts as a tumor suppressor in hepatocellular carcinogenesis”. Cancer Cell 19 (5): 629–39. (May 2011). doi:10.1016/j.ccr.2011.03.023. PMC 3098128. PMID 21575863.

“Helicobacter pylori CagA: a new paradigm for bacterial carcinogenesis”. Cancer Science 96 (12): 835–843. (2005). doi:10.1111/j.1349-7006.2005.00130.x. PMID 16367902.

“Oncogenic mechanisms of the Helicobacter pylori CagA protein”. Nature Reviews Cancer 4 (9): 688–94. (September 2004). doi:10.1038/nrc1433. PMID 15343275.

“c-Cbl-dependent monoubiquitination and lysosomal degradation of gp130”. Mol. Cell. Biol. 28 (15): 4805–18. (Aug 2008). doi:10.1128/MCB.01784-07. PMC 2493370. PMID 18519587.

“SHP-1 binds and negatively modulates the c-Kit receptor by interaction with tyrosine 569 in the c-Kit juxtamembrane domain”. Mol. Cell. Biol. 18 (4): 2089–99. (April 1998). doi:10.1128/MCB.18.4.2089. PMC 121439. PMID 9528781.

“Platelet-endothelial cell adhesion molecule-1 (CD31), a scaffolding molecule for selected catenin family members whose binding is mediated by different tyrosine and serine/threonine phosphorylation”. J. Biol. Chem. 275 (28): 21435–43. (July 2000). doi:10.1074/jbc.M001857200. PMID 10801826.

“Differential association of cytoplasmic signalling molecules SHP-1, SHP-2, SHIP and phospholipase C-gamma1 with PECAM-1/CD31”. FEBS Lett. 450 (1–2): 77–83. (April 1999). doi:10.1016/S0014-5793(99)00446-9. PMID 10350061.

“Recruitment and activation of SHP-1 protein-tyrosine phosphatase by human platelet endothelial cell adhesion molecule-1 (PECAM-1). Identification of immunoreceptor tyrosine-based inhibitory motif-like binding motifs and substrates”. J. Biol. Chem. 273 (43): 28332–40. (October 1998). doi:10.1074/jbc.273.43.28332. PMID 9774457.

“The protein-tyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation. Evidence for a mechanistic link between PECAM-1- and integrin-mediated cellular signaling”. J. Biol. Chem. 272 (11): 6986–93. (March 1997). doi:10.1074/jbc.272.11.6986. PMID 9054388.

“The carboxyl-terminal region of biliary glycoprotein controls its tyrosine phosphorylation and association with protein-tyrosine phosphatases SHP-1 and SHP-2 in epithelial cells”. J. Biol. Chem. 274 (1): 335–44. (Jan 1999). doi:10.1074/jbc.274.1.335. PMID 9867848.

“Phosphotyrosine interactome of the ErbB-receptor kinase family”. Mol. Syst. Biol. 1 (1): E1–E13. (2005). doi:10.1038/msb4100012. PMC 1681463. PMID 16729043.

“Association of SH2 domain protein tyrosine phosphatases with the epidermal growth factor receptor in human tumor cells. Phosphatidic acid activates receptor dephosphorylation by PTP1C”. J. Biol. Chem. 270 (36): 21277–84. (Sep 1995). doi:10.1074/jbc.270.36.21277. PMID 7673163.

“The 'Shp'ing news: SH2 domain-containing tyrosine phosphatases in cell signaling”. Trends in Biochemical Sciences 28 (6): 284–293. (June 2003). doi:10.1016/S0968-0004(03)00091-4. ISSN 0968-0004. PMID 12826400.

“Potential involvement of FRS2 in insulin signaling”. Endocrinology 141 (2): 621–8. (Feb 2000). doi:10.1210/endo.141.2.7298. PMID 10650943.

“Identification of SNT/FRS2 docking site on RET receptor tyrosine kinase and its role for signal transduction”. Oncogene 20 (16): 1929–38. (Apr 2001). doi:10.1038/sj.onc.1204290. PMID 11360177.

“Binding of Shp2 tyrosine phosphatase to FRS2 is essential for fibroblast growth factor-induced PC12 cell differentiation”. Mol. Cell. Biol. 18 (7): 3966–73. (Jul 1998). doi:10.1128/MCB.18.7.3966. PMC 108981. PMID 9632781.

“Protein kinase C-alpha and protein kinase C-epsilon are required for Grb2-associated binder-1 tyrosine phosphorylation in response to platelet-derived growth factor”. J. Biol. Chem. 277 (26): 23216–22. (Jun 2002). doi:10.1074/jbc.M200605200. PMID 11940581.

“Determination of Gab1 (Grb2-associated binder-1) interaction with insulin receptor-signaling molecules”. Mol. Endocrinol. 12 (7): 914–23. (Jul 1998). doi:10.1210/mend.12.7.0141. PMID 9658397.

“Phosphatidylinositol 3-kinase regulates glycosylphosphatidylinositol hydrolysis through PLC-gamma(2) activation in erythropoietin-stimulated cells”. Cell. Signal. 14 (10): 869–78. (October 2002). doi:10.1016/S0898-6568(02)00036-0. PMID 12135708.

“PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2”. EMBO J. 21 (1–2): 72–82. (January 2002). doi:10.1093/emboj/21.1.72. PMC 125816. PMID 11782427.

“Gab2, a new pleckstrin homology domain-containing adapter protein, acts to uncouple signaling from ERK kinase to Elk-1”. J. Biol. Chem. 274 (28): 19649–54. (July 1999). doi:10.1074/jbc.274.28.19649. PMID 10391903.

“A yeast two-hybrid study of human p97/Gab2 interactions with its SH2 domain-containing binding partners”. FEBS Lett. 495 (3): 148–53. (April 2001). doi:10.1016/S0014-5793(01)02373-0. PMID 11334882.

Wolf, I.; Jenkins, B. J.; Liu, Y.; Seiffert, M.; Custodio, J. M.; Young, P.; Rohrschneider, L. R. (2002). “Gab3, a New DOS/Gab Family Member, Facilitates Macrophage Differentiation”. Molecular and Cellular Biology 22 (1): 231–244. doi:10.1128/MCB.22.1.231-244.2002. ISSN 0270-7306. PMC 134230. PMID 11739737. "and associates transiently with the SH2 domain-containing proteins p85 and SHP2"

“SHP2 and SOCS3 contribute to Tyr-759-dependent attenuation of interleukin-6 signaling through gp130”. J. Biol. Chem. 278 (1): 661–71. (January 2003). doi:10.1074/jbc.M210552200. PMID 12403768.

“Signal transduction of IL-6, leukemia-inhibitory factor, and oncostatin M: structural receptor requirements for signal attenuation”. Journal of Immunology 165 (5): 2535–43. (Sep 2000). doi:10.4049/jimmunol.165.5.2535. PMID 10946280.

“Transmembrane domain of gp130 contributes to intracellular signal transduction in hepatic cells”. J. Biol. Chem. 272 (49): 30741–7. (Dec 1997). doi:10.1074/jbc.272.49.30741. PMID 9388212.

“Molecular characterization of specific interactions between SHP-2 phosphatase and JAK tyrosine kinases”. J. Biol. Chem. 272 (2): 1032–7. (January 1997). doi:10.1074/jbc.272.2.1032. PMID 8995399.

“Beta-chemokine receptor CCR5 signals through SHP1, SHP2, and Syk”. J. Biol. Chem. 275 (23): 17263–8. (Jun 2000). doi:10.1074/jbc.M000689200. PMID 10747947.

“Protein-tyrosine-phosphatase SHPTP2 couples platelet-derived growth factor receptor beta to Ras”. Proc. Natl. Acad. Sci. U.S.A. 91 (15): 7335–9. (Jul 1994). doi:10.1073/pnas.91.15.7335. PMC 44394. PMID 8041791.

“Direct binding of Shc, Grb2, SHP-2 and p40 to the murine granulocyte colony-stimulating factor receptor”. Biochim. Biophys. Acta 1448 (1): 70–6. (Nov 1998). doi:10.1016/S0167-4889(98)00120-7. PMID 9824671.

“Induced direct binding of the adapter protein Nck to the GTPase-activating protein-associated protein p62 by epidermal growth factor”. Oncogene 15 (15): 1823–32. (Oct 1997). doi:10.1038/sj.onc.1201351. PMID 9362449.

“Fyn kinase-directed activation of SH2 domain-containing protein-tyrosine phosphatase SHP-2 by Gi protein-coupled receptors in Madin-Darby canine kidney cells”. J. Biol. Chem. 274 (18): 12401–7. (Apr 1999). doi:10.1074/jbc.274.18.12401. PMID 10212213.

“Flt3 signaling involves tyrosyl-phosphorylation of SHP-2 and SHIP and their association with Grb2 and Shc in Baf3/Flt3 cells”. J. Leukoc. Biol. 65 (3): 372–80. (Mar 1999). doi:10.1002/jlb.65.3.372. PMID 10080542.

“Epidermal growth factor induces coupling of protein-tyrosine phosphatase 1D to GRB2 via the COOH-terminal SH3 domain of GRB2”. J. Biol. Chem. 271 (35): 20981–4. (Aug 1996). doi:10.1074/jbc.271.35.20981. PMID 8702859.

“Mutation of the SHP-2 binding site in growth hormone (GH) receptor prolongs GH-promoted tyrosyl phosphorylation of GH receptor, JAK2, and STAT5B”. Mol. Endocrinol. 14 (9): 1338–50. (September 2000). doi:10.1210/me.14.9.1338. PMID 10976913.

“Grb10 identified as a potential regulator of growth hormone (GH) signaling by cloning of GH receptor target proteins”. J. Biol. Chem. 273 (26): 15906–12. (June 1998). doi:10.1074/jbc.273.26.15906. PMID 9632636.

“Constitutively active SHP2 cooperates with HoxA10 overexpression to induce acute myeloid leukemia.”. J Biol Chem 284 (4): 2549–67. (Jan 2009). doi:10.1074/jbc.M804704200. PMC 2629090. PMID 19022774.

“Insulin receptor kinase phosphorylates protein tyrosine phosphatase containing Src homology 2 regions and modulates its PTPase activity in vitro”. Biochem. Biophys. Res. Commun. 199 (2): 780–5. (Mar 1994). doi:10.1006/bbrc.1994.1297. PMID 8135823.

“Adapter function of protein-tyrosine phosphatase 1D in insulin receptor/insulin receptor substrate-1 interaction”. J. Biol. Chem. 270 (49): 29189–93. (Dec 1995). doi:10.1074/jbc.270.49.29189. PMID 7493946.

“Concerted activity of tyrosine phosphatase SHP-2 and focal adhesion kinase in regulation of cell motility”. Mol. Cell. Biol. 19 (4): 3125–35. (Apr 1999). doi:10.1128/mcb.19.4.3125. PMC 84106. PMID 10082579.

“Localization of the insulin-like growth factor I receptor binding sites for the SH2 domain proteins p85, Syp, and GTPase activating protein”. J. Biol. Chem. 270 (32): 19151–7. (Aug 1995). doi:10.1074/jbc.270.32.19151. PMID 7642582.

“The COOH-terminal tyrosine phosphorylation sites on IRS-1 bind SHP-2 and negatively regulate insulin signaling”. J. Biol. Chem. 273 (41): 26908–14. (Oct 1998). doi:10.1074/jbc.273.41.26908. PMID 9756938.

“Tyrosine 425 within the activated erythropoietin receptor binds Syp, reduces the erythropoietin required for Syp tyrosine phosphorylation, and promotes mitogenesis”. Blood 87 (11): 4495–501. (June 1996). doi:10.1182/blood.V87.11.4495.bloodjournal87114495. PMID 8639815.

“SHPTP2 serves adapter protein linking between Janus kinase 2 and insulin receptor substrates”. Biochem. Biophys. Res. Commun. 228 (1): 122–7. (November 1996). doi:10.1006/bbrc.1996.1626. PMID 8912646.

“FDF03, a novel inhibitory receptor of the immunoglobulin superfamily, is expressed by human dendritic and myeloid cells”. Journal of Immunology 165 (3): 1197–209. (Aug 2000). doi:10.4049/jimmunol.165.3.1197. PMID 10903717.

“LAIR-1, a novel inhibitory receptor expressed on human mononuclear leukocytes”. Immunity 7 (2): 283–90. (Aug 1997). doi:10.1016/S1074-7613(00)80530-0. PMID 9285412.

“Structural and functional consequences of tyrosine phosphorylation in the LRP1 cytoplasmic domain”. J. Biol. Chem. 283 (23): 15656–64. (June 2008). doi:10.1074/jbc.M709514200. PMC 2414285. PMID 18381291.

“Negative regulation of Ros receptor tyrosine kinase signaling. An epithelial function of the SH2 domain protein tyrosine phosphatase SHP-1”. J. Cell Biol. 152 (2): 325–34. (Jan 2001). doi:10.1083/jcb.152.2.325. PMC 2199605. PMID 11266449.

“SHP2 mediates the protective effect of interleukin-6 against dexamethasone-induced apoptosis in multiple myeloma cells”. J. Biol. Chem. 275 (36): 27845–50. (September 2000). doi:10.1074/jbc.M003428200. PMID 10880513.

“Molecular dissection of the signaling and costimulatory functions of CD150 (SLAM): CD150/SAP binding and CD150-mediated costimulation”. Blood 99 (3): 957–65. (Feb 2000). doi:10.1182/blood.V99.3.957. PMID 11806999.

“Structural basis for the interaction of the free SH2 domain EAT-2 with SLAM receptors in hematopoietic cells”. EMBO J. 20 (21): 5840–52. (Nov 2001). doi:10.1093/emboj/20.21.5840. PMC 125701. PMID 11689425.

“Erythropoietin and IL-3 induce tyrosine phosphorylation of CrkL and its association with Shc, SHP-2, and Cbl in hematopoietic cells”. Biochem. Biophys. Res. Commun. 239 (2): 412–7. (Oct 1997). doi:10.1006/bbrc.1997.7480. PMID 9344843.

“Cytosolic tyrosine dephosphorylation of STAT5. Potential role of SHP-2 in STAT5 regulation”. J. Biol. Chem. 275 (1): 599–604. (Jan 2000). doi:10.1074/jbc.275.1.599. PMID 10617656.

“Prolactin induces SHP-2 association with Stat5, nuclear translocation, and binding to the beta-casein gene promoter in mammary cells”. J. Biol. Chem. 277 (34): 31107–14. (Aug 2002). doi:10.1074/jbc.M200156200. PMID 12060651.

nih.gov (Global: 4^th place; Japanese: 24^th place)

pubmed.ncbi.nlm.nih.gov

“Mapping a gene for Noonan syndrome to the long arm of chromosome 12”. Nat. Genet. 8 (4): 357–60. (December 1994). doi:10.1038/ng1294-357. PMID 7894486.

“Germline gain-of-function mutations in SOS1 cause Noonan syndrome”. Nat. Genet. 39 (1): 70–4. (January 2007). doi:10.1038/ng1926. PMID 17143285.

“PTPN11 (Shp2) mutations in LEOPARD syndrome have dominant negative, not activating, effects”. J. Biol. Chem. 281 (10): 6785–92. (March 2006). doi:10.1074/jbc.M513068200. PMID 16377799.

“Ptpn11/Shp2 acts as a tumor suppressor in hepatocellular carcinogenesis”. Cancer Cell 19 (5): 629–39. (May 2011). doi:10.1016/j.ccr.2011.03.023. PMC 3098128. PMID 21575863.

“Helicobacter pylori CagA: a new paradigm for bacterial carcinogenesis”. Cancer Science 96 (12): 835–843. (2005). doi:10.1111/j.1349-7006.2005.00130.x. PMID 16367902.

“Oncogenic mechanisms of the Helicobacter pylori CagA protein”. Nature Reviews Cancer 4 (9): 688–94. (September 2004). doi:10.1038/nrc1433. PMID 15343275.

“c-Cbl-dependent monoubiquitination and lysosomal degradation of gp130”. Mol. Cell. Biol. 28 (15): 4805–18. (Aug 2008). doi:10.1128/MCB.01784-07. PMC 2493370. PMID 18519587.

“The ubiquitously expressed Syp phosphatase interacts with c-kit and Grb2 in hematopoietic cells”. J. Biol. Chem. 269 (40): 25206–11. (October 1994). PMID 7523381.

“Phosphotyrosine interactome of the ErbB-receptor kinase family”. Mol. Syst. Biol. 1 (1): E1–E13. (2005). doi:10.1038/msb4100012. PMC 1681463. PMID 16729043.

“Potential involvement of FRS2 in insulin signaling”. Endocrinology 141 (2): 621–8. (Feb 2000). doi:10.1210/endo.141.2.7298. PMID 10650943.

“PKB-mediated negative feedback tightly regulates mitogenic signalling via Gab2”. EMBO J. 21 (1–2): 72–82. (January 2002). doi:10.1093/emboj/21.1.72. PMC 125816. PMID 11782427.

“Beta-chemokine receptor CCR5 signals through SHP1, SHP2, and Syk”. J. Biol. Chem. 275 (23): 17263–8. (Jun 2000). doi:10.1074/jbc.M000689200. PMID 10747947.

“The insulin receptor substrate 1 associates with the SH2-containing phosphotyrosine phosphatase Syp”. J. Biol. Chem. 268 (16): 11479–81. (Jun 1993). PMID 8505282.

“LAIR-1, a novel inhibitory receptor expressed on human mononuclear leukocytes”. Immunity 7 (2): 283–90. (Aug 1997). doi:10.1016/S1074-7613(00)80530-0. PMID 9285412.

“Activation of the SH2-containing phosphotyrosine phosphatase SH-PTP2 by its binding site, phosphotyrosine 1009, on the human platelet-derived growth factor receptor”. J. Biol. Chem. 268 (29): 21478–81. (Oct 1993). PMID 7691811.

“Cytosolic tyrosine dephosphorylation of STAT5. Potential role of SHP-2 in STAT5 regulation”. J. Biol. Chem. 275 (1): 599–604. (Jan 2000). doi:10.1074/jbc.275.1.599. PMID 10617656.

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PTPN11 (Japanese Wikipedia)

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worldcat.org (Global: 5^th place; Japanese: 19^th place)

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PTPN11 (Japanese Wikipedia)

books.google.com (Global: 3rd place; Japanese: 61st place)

doi.org (Global: 2nd place; Japanese: 6th place)

ensembl.org (Global: 1,626th place; Japanese: 2,625th place)

May2017.archive.ensembl.org

nih.gov (Global: 4th place; Japanese: 24th place)

pubmed.ncbi.nlm.nih.gov

pmc.ncbi.nlm.nih.gov

ncbi.nlm.nih.gov

wikipedia.org (Global: low place; Japanese: low place)

en.wikipedia.org

worldcat.org (Global: 5th place; Japanese: 19th place)

search.worldcat.org

books.google.com (Global: 3^rd place; Japanese: 61^st place)

doi.org (Global: 2^nd place; Japanese: 6^th place)

ensembl.org (Global: 1,626^th place; Japanese: 2,625^th place)

nih.gov (Global: 4^th place; Japanese: 24^th place)

worldcat.org (Global: 5^th place; Japanese: 19^th place)