메뉴 건너뛰기




Volumn 34, Issue 30, 2015, Pages 3885-3894

Genetic alterations of protein tyrosine phosphatases in human cancers

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN TYROSINE PHOSPHATASE; PROTEIN TYROSINE PHOSPHATASE NON RECEPTOR 1; PROTEIN TYROSINE PHOSPHATASE NON RECEPTOR 11; PROTEIN TYROSINE PHOSPHATASE NON RECEPTOR 13; PROTEIN TYROSINE PHOSPHATASE NON RECEPTOR 14; PROTEIN TYROSINE PHOSPHATASE RECEPTOR B; PROTEIN TYROSINE PHOSPHATASE RECEPTOR D; PROTEIN TYROSINE PHOSPHATASE RECEPTOR J; PROTEIN TYROSINE PHOSPHATASE RECEPTOR K; PROTEIN TYROSINE PHOSPHATASE RECEPTOR M; PROTEIN TYROSINE PHOSPHATASE RECEPTOR T; UNCLASSIFIED DRUG;

EID: 84937823809     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2014.326     Document Type: Review
Times cited : (58)

References (126)
  • 1
    • 79551632876 scopus 로고    scopus 로고
    • Protein kinase signaling networks in cancer
    • Brognard J, Hunter T. Protein kinase signaling networks in cancer. Curr Opin Genet Dev 2011; 21: 4-11.
    • (2011) Curr Opin Genet Dev , vol.21 , pp. 4-11
    • Brognard, J.1    Hunter, T.2
  • 3
    • 2442648882 scopus 로고    scopus 로고
    • Mutational analysis of the tyrosine phosphatome in colorectal cancers
    • Wang Z, Shen D, Parsons DW, Bardelli A, Sager J, Szabo S et al. Mutational analysis of the tyrosine phosphatome in colorectal cancers. Science 2004; 304: 1164-1166.
    • (2004) Science , vol.304 , pp. 1164-1166
    • Wang, Z.1    Shen, D.2    Parsons, D.W.3    Bardelli, A.4    Sager, J.5    Szabo, S.6
  • 5
    • 58249138122 scopus 로고    scopus 로고
    • Largescale structural analysis of the classical human protein tyrosine phosphatome
    • Barr AJ, Ugochukwu E, Lee WH, King ON, Filippakopoulos P, Alfano I et al. Largescale structural analysis of the classical human protein tyrosine phosphatome. Cell 2009; 136: 352-363.
    • (2009) Cell , vol.136 , pp. 352-363
    • Barr, A.J.1    Ugochukwu, E.2    Lee, W.H.3    King, O.N.4    Filippakopoulos, P.5    Alfano, I.6
  • 6
    • 33750299450 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases: From genes, to function, to disease
    • Tonks NK. Protein tyrosine phosphatases: from genes, to function, to disease. Nat Rev Mol Cell Biol 2006; 7: 833-846.
    • (2006) Nat Rev Mol Cell Biol , vol.7 , pp. 833-846
    • Tonks, N.K.1
  • 7
    • 4043181214 scopus 로고    scopus 로고
    • Cancer genes and the pathways they control
    • Vogelstein B, Kinzler KW. Cancer genes and the pathways they control. Nat Med 2004; 10: 789-799.
    • (2004) Nat Med , vol.10 , pp. 789-799
    • Vogelstein, B.1    Kinzler, K.W.2
  • 8
    • 84892928970 scopus 로고    scopus 로고
    • Frequent mutation of receptor protein tyrosine phosphatases provides a mechanism for STAT3 hyperactivation in head and neck cancer
    • Lui VW, Peyser ND, Ng PK, Hritz J, Zeng Y, Lu Y et al. Frequent mutation of receptor protein tyrosine phosphatases provides a mechanism for STAT3 hyperactivation in head and neck cancer. Proc Natl Acad Sci USA 2014; 111: 1114-1119.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 1114-1119
    • Lui, V.W.1    Peyser, N.D.2    Ng, P.K.3    Hritz, J.4    Zeng, Y.5    Lu, Y.6
  • 10
    • 84875758730 scopus 로고    scopus 로고
    • Lessons from the cancer genome
    • Garraway LA, Lander ES. Lessons from the cancer genome. Cell 2013; 153: 17-37.
    • (2013) Cell , vol.153 , pp. 17-37
    • Garraway, L.A.1    Lander, E.S.2
  • 11
    • 77249128431 scopus 로고    scopus 로고
    • Identification and functional characterization of paxillin as a target of protein tyrosine phosphatase receptor T
    • Zhao Y, Zhang X, Guda K, Lawrence E, Sun Q, Watanabe T et al. Identification and functional characterization of paxillin as a target of protein tyrosine phosphatase receptor T. Proc Natl Acad Sci USA 2010; 107: 2592-2597.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 2592-2597
    • Zhao, Y.1    Zhang, X.2    Guda, K.3    Lawrence, E.4    Sun, Q.5    Watanabe, T.6
  • 12
    • 84873030748 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase receptor-like genes are frequently hypermethylated in sporadic colorectal cancer
    • Laczmanska I, Karpinski P, Bebenek M, Sedziak T, Ramsey D, Szmida E et al. Protein tyrosine phosphatase receptor-like genes are frequently hypermethylated in sporadic colorectal cancer. J Hum Genet 2013; 58: 11-15.
    • (2013) J Hum Genet , vol.58 , pp. 11-15
    • Laczmanska, I.1    Karpinski, P.2    Bebenek, M.3    Sedziak, T.4    Ramsey, D.5    Szmida, E.6
  • 13
    • 84996565552 scopus 로고    scopus 로고
    • Large-scale characterization of DNA methylation changes in human gastric carcinomas with and without metastasis
    • Liu Z, Zhang J, Gao Y, Pei L, Zhou J, Gu L et al. Large-scale characterization of DNA methylation changes in human gastric carcinomas with and without metastasis. Clin Cancer Res 2014; 20: 4598-4612.
    • (2014) Clin Cancer Res , vol.20 , pp. 4598-4612
    • Liu, Z.1    Zhang, J.2    Gao, Y.3    Pei, L.4    Zhou, J.5    Gu, L.6
  • 14
    • 77954091358 scopus 로고    scopus 로고
    • Characterization of the adhesive properties of the type IIb subfamily receptor protein tyrosine phosphatases
    • Becka S, Zhang P, Craig SE, Lodowski DT, Wang Z, Brady-Kalnay SM. Characterization of the adhesive properties of the type IIb subfamily receptor protein tyrosine phosphatases. Cell Commun Adhes 2010; 17: 34-47.
    • (2010) Cell Commun Adhes , vol.17 , pp. 34-47
    • Becka, S.1    Zhang, P.2    Craig, S.E.3    Lodowski, D.T.4    Wang, Z.5    Brady-Kalnay, S.M.6
  • 15
    • 33749235133 scopus 로고    scopus 로고
    • Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT)
    • Besco JA, Hooft van Huijsduijnen R, Frostholm A, Rotter A. Intracellular substrates of brain-enriched receptor protein tyrosine phosphatase rho (RPTPrho/PTPRT). Brain Res 2006; 1116: 50-57.
    • (2006) Brain Res , vol.1116 , pp. 50-57
    • Besco, J.A.1    Hooft Van Huijsduijnen, R.2    Frostholm, A.3    Rotter, A.4
  • 16
    • 51649129150 scopus 로고    scopus 로고
    • Tumor-derived extracellular mutations of PTPRT/PTP{rho} are defective in cell adhesion
    • Yu J, Becka S, Zhang P, Zhang X, Brady-Kalnay SM, Wang Z. Tumor-derived extracellular mutations of PTPRT/PTP{rho} are defective in cell adhesion. Mol Cancer Res 2008; 6: 1106-1113.
    • (2008) Mol Cancer Res , vol.6 , pp. 1106-1113
    • Yu, J.1    Becka, S.2    Zhang, P.3    Zhang, X.4    Brady-Kalnay, S.M.5    Wang, Z.6
  • 17
    • 77951106136 scopus 로고    scopus 로고
    • Cancerderived mutations in the fibronectin III repeats of PTPRT/PTPrho inhibit cell-cell aggregation
    • Zhang P, Becka S, Craig SE, Lodowski DT, Brady-Kalnay SM, Wang Z. Cancerderived mutations in the fibronectin III repeats of PTPRT/PTPrho inhibit cell-cell aggregation. Cell Commun Adhes 2009; 16: 146-153.
    • (2009) Cell Commun Adhes , vol.16 , pp. 146-153
    • Zhang, P.1    Becka, S.2    Craig, S.E.3    Lodowski, D.T.4    Brady-Kalnay, S.M.5    Wang, Z.6
  • 18
    • 34247189533 scopus 로고    scopus 로고
    • Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T
    • Zhang X, Guo A, Yu J, Possemato A, Chen Y, Zheng W et al. Identification of STAT3 as a substrate of receptor protein tyrosine phosphatase T. PNAS 2007; 104: 4060-4064.
    • (2007) PNAS , vol.104 , pp. 4060-4064
    • Zhang, X.1    Guo, A.2    Yu, J.3    Possemato, A.4    Chen, Y.5    Zheng, W.6
  • 19
    • 20944441928 scopus 로고    scopus 로고
    • Validating Stat3 in cancer therapy
    • Darnell JE. Validating Stat3 in cancer therapy. Nat Med 2005; 11: 595-596.
    • (2005) Nat Med , vol.11 , pp. 595-596
    • Darnell, J.E.1
  • 20
    • 80054697272 scopus 로고    scopus 로고
    • Cross-talk between phospho-STAT3 and PLC{gamma}1 plays a critical role in colorectal tumorigenesis
    • Zhang P, Zhao Y, Zhu X, Sedwick D, Zhang X, Wang Z. Cross-talk between phospho-STAT3 and PLC{gamma}1 plays a critical role in colorectal tumorigenesis. Mol Cancer Res 2011; 9: 1418-1428.
    • (2011) Mol Cancer Res , vol.9 , pp. 1418-1428
    • Zhang, P.1    Zhao, Y.2    Zhu, X.3    Sedwick, D.4    Zhang, X.5    Wang, Z.6
  • 21
    • 84903272515 scopus 로고    scopus 로고
    • PTPRT regulates high-fat diet-induced obesity and insulin resistance
    • Feng X, Scott A, Wang Y, Wang L, Zhao Y, Doerner S et al. PTPRT regulates high-fat diet-induced obesity and insulin resistance. PLoS ONE 2014; 9: e100783.
    • (2014) PLoS ONE , vol.9 , pp. e100783
    • Feng, X.1    Scott, A.2    Wang, Y.3    Wang, L.4    Zhao, Y.5    Doerner, S.6
  • 22
    • 84872197471 scopus 로고    scopus 로고
    • Regulation of dendritic arborization by BCR Rac1 GTPase-activating protein, a substrate of PTPRT
    • Park AR, Oh D, Lim SH, Choi J, Moon J, Yu DY et al. Regulation of dendritic arborization by BCR Rac1 GTPase-activating protein, a substrate of PTPRT. J Cell Sci 2012; 125: 4518-4531.
    • (2012) J Cell Sci , vol.125 , pp. 4518-4531
    • Park, A.R.1    Oh, D.2    Lim, S.H.3    Choi, J.4    Moon, J.5    Yu, D.Y.6
  • 23
    • 84883784489 scopus 로고    scopus 로고
    • PTPRT regulates the interaction of Syntaxinbinding protein 1 with Syntaxin 1 through dephosphorylation of specific tyrosine residue
    • Lim SH, Moon J, Lee M, Lee JR. PTPRT regulates the interaction of Syntaxinbinding protein 1 with Syntaxin 1 through dephosphorylation of specific tyrosine residue. Biochem Biophys Res Commun 2013; 439: 40-46.
    • (2013) Biochem Biophys Res Commun , vol.439 , pp. 40-46
    • Lim, S.H.1    Moon, J.2    Lee, M.3    Lee, J.R.4
  • 25
    • 34249111848 scopus 로고    scopus 로고
    • Allelic imbalances and microdeletions affecting the PTPRD gene in cutaneous squamous cell carcinomas detected using single nucleotide polymorphism microarray analysis
    • Purdie KJ, Lambert SR, Teh MT, Chaplin T, Molloy G, Raghavan M et al. Allelic imbalances and microdeletions affecting the PTPRD gene in cutaneous squamous cell carcinomas detected using single nucleotide polymorphism microarray analysis. Genes Chromosomes Cancer 2007; 46: 661-669.
    • (2007) Genes Chromosomes Cancer , vol.46 , pp. 661-669
    • Purdie, K.J.1    Lambert, S.R.2    Teh, M.T.3    Chaplin, T.4    Molloy, G.5    Raghavan, M.6
  • 26
    • 77949347976 scopus 로고    scopus 로고
    • A catalog of genes homozygously deleted in human lung cancer and the candidacy of PTPRD as a tumor suppressor gene
    • Kohno T, Otsuka A, Girard L, Sato M, Iwakawa R, Ogiwara H et al. A catalog of genes homozygously deleted in human lung cancer and the candidacy of PTPRD as a tumor suppressor gene. Genes Chromosomes Cancer 2010; 49: 342-352.
    • (2010) Genes Chromosomes Cancer , vol.49 , pp. 342-352
    • Kohno, T.1    Otsuka, A.2    Girard, L.3    Sato, M.4    Iwakawa, R.5    Ogiwara, H.6
  • 27
    • 78650944685 scopus 로고    scopus 로고
    • High resolution ArrayCGH and expression profiling identifies PTPRD and PCDH17/PCH68 as tumor suppressor gene candidates in laryngeal squamous cell carcinoma
    • Giefing M, Zemke N, Brauze D, Kostrzewska-Poczekaj M, Luczak M, Szaumkessel M et al. High resolution ArrayCGH and expression profiling identifies PTPRD and PCDH17/PCH68 as tumor suppressor gene candidates in laryngeal squamous cell carcinoma. Genes Chromosomes Cancer 2011; 50: 154-166.
    • (2011) Genes Chromosomes Cancer , vol.50 , pp. 154-166
    • Giefing, M.1    Zemke, N.2    Brauze, D.3    Kostrzewska-Poczekaj, M.4    Luczak, M.5    Szaumkessel, M.6
  • 28
    • 33749993417 scopus 로고    scopus 로고
    • The consensus coding sequences of human breast and colorectal cancers
    • Sjoblom T, Jones S, Wood LD, Parsons DW, Lin J, Barber TD et al. The consensus coding sequences of human breast and colorectal cancers. Science 2006; 314: 268-274.
    • (2006) Science , vol.314 , pp. 268-274
    • Sjoblom, T.1    Jones, S.2    Wood, L.D.3    Parsons, D.W.4    Lin, J.5    Barber, T.D.6
  • 31
    • 67249088143 scopus 로고    scopus 로고
    • The tyrosine phosphatase PTPRD is a tumor suppressor that is frequently inactivated and mutated in glioblastoma and other human cancers
    • Veeriah S, Brennan C, Meng S, Singh B, Fagin JA, Solit DB et al. The tyrosine phosphatase PTPRD is a tumor suppressor that is frequently inactivated and mutated in glioblastoma and other human cancers. Proc Natl Acad Sci USA 2009; 106: 9435-9440.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 9435-9440
    • Veeriah, S.1    Brennan, C.2    Meng, S.3    Singh, B.4    Fagin, J.A.5    Solit, D.B.6
  • 32
    • 84901854064 scopus 로고    scopus 로고
    • Loss of the tyrosine phosphatase PTPRD leads to aberrant STAT3 activation and promotes gliomagenesis
    • Ortiz B, Fabius AW, Wu WH, Pedraza A, Brennan CW, Schultz N et al. Loss of the tyrosine phosphatase PTPRD leads to aberrant STAT3 activation and promotes gliomagenesis. Proc Natl Acad Sci USA 2014; 111: 8149-8154.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 8149-8154
    • Ortiz, B.1    Fabius, A.W.2    Wu, W.H.3    Pedraza, A.4    Brennan, C.W.5    Schultz, N.6
  • 33
    • 84880823765 scopus 로고    scopus 로고
    • Germline PTPRD mutations in Ewing sarcoma: Biologic and clinical implications
    • Jiang Y, Janku F, Subbiah V, Angelo LS, Naing A, Anderson PM et al. Germline PTPRD mutations in Ewing sarcoma: biologic and clinical implications. Oncotarget 2013; 4: 884-889.
    • (2013) Oncotarget , vol.4 , pp. 884-889
    • Jiang, Y.1    Janku, F.2    Subbiah, V.3    Angelo, L.S.4    Naing, A.5    Anderson, P.M.6
  • 34
    • 79953284982 scopus 로고    scopus 로고
    • Tyrosine phosphatase PTPRD suppresses colon cancer cell migration in coordination with CD44
    • Funato K, Yamazumi Y, Oda T, Akiyama T. Tyrosine phosphatase PTPRD suppresses colon cancer cell migration in coordination with CD44. Exp Ther Med 2011; 2: 457-463.
    • (2011) Exp Ther Med , vol.2 , pp. 457-463
    • Funato, K.1    Yamazumi, Y.2    Oda, T.3    Akiyama, T.4
  • 35
    • 0038641656 scopus 로고    scopus 로고
    • MIM-B, a putative metastasis suppressor protein, binds to actin and to protein tyrosine phosphatase delta
    • Woodings JA, Sharp SJ, Machesky LM. MIM-B, a putative metastasis suppressor protein, binds to actin and to protein tyrosine phosphatase delta. Biochem J 2003; 371: 463-471.
    • (2003) Biochem J , vol.371 , pp. 463-471
    • Woodings, J.A.1    Sharp, S.J.2    Machesky, L.M.3
  • 36
    • 84856436143 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase receptor delta acts as a neuroblastoma tumor suppressor by destabilizing the aurora kinase A oncogene
    • Meehan M, Parthasarathi L, Moran N, Jefferies CA, Foley N, Lazzari E et al. Protein tyrosine phosphatase receptor delta acts as a neuroblastoma tumor suppressor by destabilizing the aurora kinase A oncogene. Mol Cancer 2012; 11: 6.
    • (2012) Mol Cancer , vol.11 , pp. 6
    • Meehan, M.1    Parthasarathi, L.2    Moran, N.3    Jefferies, C.A.4    Foley, N.5    Lazzari, E.6
  • 39
    • 0037442987 scopus 로고    scopus 로고
    • Novel tumor suppressor loci on 6q22-23 in primary central nervous system lymphomas
    • Nakamura M, Kishi M, Sakaki T, Hashimoto H, Nakase H, Shimada K et al. Novel tumor suppressor loci on 6q22-23 in primary central nervous system lymphomas. Cancer Res 2003; 63: 737-741.
    • (2003) Cancer Res , vol.63 , pp. 737-741
    • Nakamura, M.1    Kishi, M.2    Sakaki, T.3    Hashimoto, H.4    Nakase, H.5    Shimada, K.6
  • 40
    • 84877837684 scopus 로고    scopus 로고
    • Tumor derived mutations of protein tyrosine phosphatase receptor type k affect its function and alter sensitivity to chemotherapeutics in glioma
    • Agarwal S, Al-Keilani MS, Alqudah MA, Sibenaller ZA, Ryken TC, Assem M. Tumor derived mutations of protein tyrosine phosphatase receptor type k affect its function and alter sensitivity to chemotherapeutics in glioma. PLoS ONE 2013; 8: e62852.
    • (2013) PLoS ONE , vol.8 , pp. e62852
    • Agarwal, S.1    Al-Keilani, M.S.2    Alqudah, M.A.3    Sibenaller, Z.A.4    Ryken, T.C.5    Assem, M.6
  • 41
    • 30044436233 scopus 로고    scopus 로고
    • Receptor-type proteintyrosine phosphatase-kappa regulates epidermal growth factor receptor function
    • Xu Y, Tan LJ, Grachtchouk V, Voorhees JJ, Fisher GJ. Receptor-type proteintyrosine phosphatase-kappa regulates epidermal growth factor receptor function. J Biol Chem 2005; 280: 42694-42700.
    • (2005) J Biol Chem , vol.280 , pp. 42694-42700
    • Xu, Y.1    Tan, L.J.2    Grachtchouk, V.3    Voorhees, J.J.4    Fisher, G.J.5
  • 43
    • 39849103401 scopus 로고    scopus 로고
    • PTPRK negatively regulates transcriptional activity of wild type and mutated oncogenic beta-catenin and affects membrane distribution of beta-catenin/E-cadherin complexes in cancer cells
    • Novellino L, De Filippo A, Deho P, Perrone F, Pilotti S, Parmiani G et al. PTPRK negatively regulates transcriptional activity of wild type and mutated oncogenic beta-catenin and affects membrane distribution of beta-catenin/E-cadherin complexes in cancer cells. Cell Signal 2008; 20: 872-883.
    • (2008) Cell Signal , vol.20 , pp. 872-883
    • Novellino, L.1    De Filippo, A.2    Deho, P.3    Perrone, F.4    Pilotti, S.5    Parmiani, G.6
  • 44
    • 18944382074 scopus 로고    scopus 로고
    • Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function
    • Wang SE, Wu FY, Shin I, Qu S, Arteaga CL. Transforming growth factor {beta} (TGF-{beta})-Smad target gene protein tyrosine phosphatase receptor type kappa is required for TGF-{beta} function. Mol Cell Biol 2005; 25: 4703-4715.
    • (2005) Mol Cell Biol , vol.25 , pp. 4703-4715
    • Wang, S.E.1    Wu, F.Y.2    Shin, I.3    Qu, S.4    Arteaga, C.L.5
  • 45
    • 38049105629 scopus 로고    scopus 로고
    • Down-regulation of the TGF-beta target gene, PTPRK, by the Epstein-Barr virus encoded EBNA1 contributes to the growth and survival of Hodgkin lymphoma cells
    • Flavell JR, Baumforth KR, Wood VH, Davies GL, Wei W, Reynolds GM et al. Down-regulation of the TGF-beta target gene, PTPRK, by the Epstein-Barr virus encoded EBNA1 contributes to the growth and survival of Hodgkin lymphoma cells. Blood 2008; 111: 292-301.
    • (2008) Blood , vol.111 , pp. 292-301
    • Flavell, J.R.1    Baumforth, K.R.2    Wood, V.H.3    Davies, G.L.4    Wei, W.5    Reynolds, G.M.6
  • 46
    • 78650895502 scopus 로고    scopus 로고
    • Galectin-3 binding protein promotes cell motility in colon cancer by stimulating the shedding of protein tyrosine phosphatase kappa by proprotein convertase 5
    • Kim YS, Jung JA, Kim HJ, Ahn YH, Yoo JS, Oh S et al. Galectin-3 binding protein promotes cell motility in colon cancer by stimulating the shedding of protein tyrosine phosphatase kappa by proprotein convertase 5. Biochem Biophys Res Commun 2011; 404: 96-102.
    • (2011) Biochem Biophys Res Commun , vol.404 , pp. 96-102
    • Kim, Y.S.1    Jung, J.A.2    Kim, H.J.3    Ahn, Y.H.4    Yoo, J.S.5    Oh, S.6
  • 47
    • 0003001467 scopus 로고    scopus 로고
    • Protein tyrosine phosphatases
    • In: Beckerle M (ed). Oxford University Press: Oxford, UK
    • Brady-Kalnay SM. Protein tyrosine phosphatases. In: Beckerle M (ed). Cell Adhesion: Frontiers in Molecular Biology, vol 39. Oxford University Press: Oxford, UK, 217-258.
    • Cell Adhesion: Frontiers in Molecular Biology , vol.39 , pp. 217-258
    • Brady-Kalnay, S.M.1
  • 48
    • 78751490759 scopus 로고    scopus 로고
    • Cancer cells cut homophilic cell adhesion molecules and run
    • Craig SE, Brady-Kalnay SM. Cancer cells cut homophilic cell adhesion molecules and run. Cancer Res 2011; 71: 303-309.
    • (2011) Cancer Res , vol.71 , pp. 303-309
    • Craig, S.E.1    Brady-Kalnay, S.M.2
  • 49
    • 0027296921 scopus 로고
    • Homophilic binding of PTP mu, a receptortype protein tyrosine phosphatase, can mediate cell-cell aggregation
    • Brady-Kalnay SM, Flint AJ, Tonks NK. Homophilic binding of PTP mu, a receptortype protein tyrosine phosphatase, can mediate cell-cell aggregation. J Cell Biol 1993; 122: 961-972.
    • (1993) J Cell Biol , vol.122 , pp. 961-972
    • Brady-Kalnay, S.M.1    Flint, A.J.2    Tonks, N.K.3
  • 50
    • 0027938304 scopus 로고
    • Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTP mu
    • Brady-Kalnay SM, Tonks NK. Identification of the homophilic binding site of the receptor protein tyrosine phosphatase PTP mu. J Biol Chem 1994; 269: 28472-28477.
    • (1994) J Biol Chem , vol.269 , pp. 28472-28477
    • Brady-Kalnay, S.M.1    Tonks, N.K.2
  • 52
    • 0037192854 scopus 로고    scopus 로고
    • Expression of the receptor protein-tyrosine phosphatase, PTPmu, restores E-cadherin-dependent adhesion in human prostate carcinoma cells
    • Hellberg CB, Burden-Gulley SM, Pietz GE, Brady-Kalnay SM. Expression of the receptor protein-tyrosine phosphatase, PTPmu, restores E-cadherin-dependent adhesion in human prostate carcinoma cells. J Biol Chem 2002; 277: 11165-11173.
    • (2002) J Biol Chem , vol.277 , pp. 11165-11173
    • Hellberg, C.B.1    Burden-Gulley, S.M.2    Pietz, G.E.3    Brady-Kalnay, S.M.4
  • 53
    • 0033517060 scopus 로고    scopus 로고
    • Association of the HGF/SF receptor, c-met, with the cellsurface adhesion molecule, E-cadherin, and catenins in human tumor cells
    • Hiscox S, Jiang WG. Association of the HGF/SF receptor, c-met, with the cellsurface adhesion molecule, E-cadherin, and catenins in human tumor cells. Biochem Biophys Res Commun 1999; 261: 406-411.
    • (1999) Biochem Biophys Res Commun , vol.261 , pp. 406-411
    • Hiscox, S.1    Jiang, W.G.2
  • 54
    • 0035805519 scopus 로고    scopus 로고
    • The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts
    • Mourton T, Hellberg CB, Burden-Gulley SM, Hinman J, Rhee A, Brady-Kalnay SM. The PTPmu protein-tyrosine phosphatase binds and recruits the scaffolding protein RACK1 to cell-cell contacts. J Biol Chem 2001; 276: 14896-14901.
    • (2001) J Biol Chem , vol.276 , pp. 14896-14901
    • Mourton, T.1    Hellberg, C.B.2    Burden-Gulley, S.M.3    Hinman, J.4    Rhee, A.5    Brady-Kalnay, S.M.6
  • 56
    • 78651326871 scopus 로고    scopus 로고
    • Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration
    • Phillips-Mason PJ, Kaur H, Burden-Gulley SM, Craig SE, Brady-Kalnay SM. Identification of phospholipase C gamma1 as a protein tyrosine phosphatase mu substrate that regulates cell migration. J Cell Biochem 2011; 112: 39-48.
    • (2011) J Cell Biochem , vol.112 , pp. 39-48
    • Phillips-Mason, P.J.1    Kaur, H.2    Burden-Gulley, S.M.3    Craig, S.E.4    Brady-Kalnay, S.M.5
  • 57
    • 85046979797 scopus 로고    scopus 로고
    • Should i stay or should i go? Shedding of RPTPs in cancer cells switches signals from stabilizing cell-cell adhesion to driving cell migration
    • Phillips-Mason PJ, Craig SE, Brady-Kalnay SM. Should I stay or should I go? Shedding of RPTPs in cancer cells switches signals from stabilizing cell-cell adhesion to driving cell migration. Cell Adhesion Migration 2011; 5: 298-305.
    • (2011) Cell Adhesion Migration , vol.5 , pp. 298-305
    • Phillips-Mason, P.J.1    Craig, S.E.2    Brady-Kalnay, S.M.3
  • 59
    • 84904422369 scopus 로고    scopus 로고
    • A protease storm cleaves a cell-cell adhesion molecule in cancer: Multiple proteases converge to regulate PTPmu in glioma cells
    • Phillips-Mason PJ, Craig SE, Brady-Kalnay SM. A protease storm cleaves a cell-cell adhesion molecule in cancer: multiple proteases converge to regulate PTPmu in glioma cells. J Cell Biochem 2014; 115: 1609-1623.
    • (2014) J Cell Biochem , vol.115 , pp. 1609-1623
    • Phillips-Mason, P.J.1    Craig, S.E.2    Brady-Kalnay, S.M.3
  • 60
    • 77951687837 scopus 로고    scopus 로고
    • A novel molecular diagnostic of glioblastomas: Detection of an extracellular fragment of protein tyrosine phosphatase mu
    • Burden-Gulley SM, Gates TJ, Burgoyne AM, Cutter JL, Lodowski DT, Robinson S et al. A novel molecular diagnostic of glioblastomas: detection of an extracellular fragment of protein tyrosine phosphatase mu. Neoplasia 2010; 12: 305-316.
    • (2010) Neoplasia , vol.12 , pp. 305-316
    • Burden-Gulley, S.M.1    Gates, T.J.2    Burgoyne, A.M.3    Cutter, J.L.4    Lodowski, D.T.5    Robinson, S.6
  • 61
    • 0038118340 scopus 로고    scopus 로고
    • LOH of PTPRJ occurs early in colorectal cancer and is associated with chromosomal loss of 18q12-21
    • Ruivenkamp C, Hermsen M, Postma C, Klous A, Baak J, Meijer G et al. LOH of PTPRJ occurs early in colorectal cancer and is associated with chromosomal loss of 18q12-21. Oncogene 2003; 22: 3472-3474.
    • (2003) Oncogene , vol.22 , pp. 3472-3474
    • Ruivenkamp, C.1    Hermsen, M.2    Postma, C.3    Klous, A.4    Baak, J.5    Meijer, G.6
  • 62
    • 26444460889 scopus 로고    scopus 로고
    • Allelic association of the human homologue of the mouse modifier Ptprj with breast cancer
    • Lesueur F, Pharoah PD, Laing S, Ahmed S, Jordan C, Smith PL et al. Allelic association of the human homologue of the mouse modifier Ptprj with breast cancer. Hum Mol Genet 2005; 14: 2349-2356.
    • (2005) Hum Mol Genet , vol.14 , pp. 2349-2356
    • Lesueur, F.1    Pharoah, P.D.2    Laing, S.3    Ahmed, S.4    Jordan, C.5    Smith, P.L.6
  • 63
    • 9144262524 scopus 로고    scopus 로고
    • The tyrosine phosphatase PTPRJ/DEP-1 genotype affects thyroid carcinogenesis
    • Iuliano R, Le Pera I, Cristofaro C, Baudi F, Arturi F, Pallante P et al. The tyrosine phosphatase PTPRJ/DEP-1 genotype affects thyroid carcinogenesis. Oncogene 2004; 23: 8432-8438.
    • (2004) Oncogene , vol.23 , pp. 8432-8438
    • Iuliano, R.1    Le Pera, I.2    Cristofaro, C.3    Baudi, F.4    Arturi, F.5    Pallante, P.6
  • 65
    • 84875078146 scopus 로고    scopus 로고
    • Highresolution loss of heterozygosity screening implicates PTPRJ as a potential tumor suppressor gene that affects susceptibility to Non-Hodgkin's lymphoma
    • Aya-Bonilla C, Green MR, Camilleri E, Benton M, Keane C, Marlton P et al. Highresolution loss of heterozygosity screening implicates PTPRJ as a potential tumor suppressor gene that affects susceptibility to Non-Hodgkin's lymphoma. Genes Chromosomes Cancer 2013; 52: 467-479.
    • (2013) Genes Chromosomes Cancer , vol.52 , pp. 467-479
    • Aya-Bonilla, C.1    Green, M.R.2    Camilleri, E.3    Benton, M.4    Keane, C.5    Marlton, P.6
  • 66
    • 33745628055 scopus 로고    scopus 로고
    • Loss of heterozygosity in human aberrant crypt foci (ACF), a putative precursor of colon cancer
    • Luo L, Shen GQ, Stiffler KA, Wang QK, Pretlow TG, Pretlow TP. Loss of heterozygosity in human aberrant crypt foci (ACF), a putative precursor of colon cancer. Carcinogenesis 2006; 27: 1153-1159.
    • (2006) Carcinogenesis , vol.27 , pp. 1153-1159
    • Luo, L.1    Shen, G.Q.2    Stiffler, K.A.3    Wang, Q.K.4    Pretlow, T.G.5    Pretlow, T.P.6
  • 68
    • 33745714241 scopus 로고    scopus 로고
    • The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins
    • Iervolino A, Iuliano R, Trapasso F, Viglietto G, Melillo RM, Carlomagno F et al. The receptor-type protein tyrosine phosphatase J antagonizes the biochemical and biological effects of RET-derived oncoproteins. Cancer Res 2006; 66: 6280-6287.
    • (2006) Cancer Res , vol.66 , pp. 6280-6287
    • Iervolino, A.1    Iuliano, R.2    Trapasso, F.3    Viglietto, G.4    Melillo, R.M.5    Carlomagno, F.6
  • 69
    • 33749817962 scopus 로고    scopus 로고
    • DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients
    • Balavenkatraman KK, Jandt E, Friedrich K, Kautenburger T, Pool-Zobel BL, Ostman A et al. DEP-1 protein tyrosine phosphatase inhibits proliferation and migration of colon carcinoma cells and is upregulated by protective nutrients. Oncogene 2006; 25: 6319-6324.
    • (2006) Oncogene , vol.25 , pp. 6319-6324
    • Balavenkatraman, K.K.1    Jandt, E.2    Friedrich, K.3    Kautenburger, T.4    Pool-Zobel, B.L.5    Ostman, A.6
  • 70
    • 8844236892 scopus 로고    scopus 로고
    • Restoration of receptor-type protein tyrosine phosphatase eta function inhibits human pancreatic carcinoma cell growth in vitro and in vivo
    • Trapasso F, Yendamuri S, Dumon KR, Iuliano R, Cesari R, Feig B et al. Restoration of receptor-type protein tyrosine phosphatase eta function inhibits human pancreatic carcinoma cell growth in vitro and in vivo. Carcinogenesis 2004; 25: 2107-2114.
    • (2004) Carcinogenesis , vol.25 , pp. 2107-2114
    • Trapasso, F.1    Yendamuri, S.2    Dumon, K.R.3    Iuliano, R.4    Cesari, R.5    Feig, B.6
  • 71
    • 0034458955 scopus 로고    scopus 로고
    • Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kip1)
    • Trapasso F, Iuliano R, Boccia A, Stella A, Visconti R, Bruni P et al. Rat protein tyrosine phosphatase eta suppresses the neoplastic phenotype of retrovirally transformed thyroid cells through the stabilization of p27(Kip1). Mol Cell Biol 2000; 20: 9236-9246.
    • (2000) Mol Cell Biol , vol.20 , pp. 9236-9246
    • Trapasso, F.1    Iuliano, R.2    Boccia, A.3    Stella, A.4    Visconti, R.5    Bruni, P.6
  • 72
    • 0036649023 scopus 로고    scopus 로고
    • Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers
    • Ruivenkamp CA, van Wezel T, Zanon C, Stassen AP, Vlcek C, Csikos T et al. Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers. Nat Genet 2002; 31: 295-300.
    • (2002) Nat Genet , vol.31 , pp. 295-300
    • Ruivenkamp, C.A.1    Van Wezel, T.2    Zanon, C.3    Stassen, A.P.4    Vlcek, C.5    Csikos, T.6
  • 73
    • 33745457190 scopus 로고    scopus 로고
    • Genetic ablation of Ptprj, a mouse cancer susceptibility gene, results in normal growth and development and does not predispose to spontaneous tumorigenesis
    • Trapasso F, Drusco A, Costinean S, Alder H, Aqeilan RI, Iuliano R et al. Genetic ablation of Ptprj, a mouse cancer susceptibility gene, results in normal growth and development and does not predispose to spontaneous tumorigenesis. DNA Cell Biol 2006; 25: 376-382.
    • (2006) DNA Cell Biol , vol.25 , pp. 376-382
    • Trapasso, F.1    Drusco, A.2    Costinean, S.3    Alder, H.4    Aqeilan, R.I.5    Iuliano, R.6
  • 74
    • 76549099086 scopus 로고    scopus 로고
    • Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative regulators of PKB/Akt activation in Ras-mutated cancer cells
    • Omerovic J, Clague MJ, Prior IA. Phosphatome profiling reveals PTPN2, PTPRJ and PTEN as potent negative regulators of PKB/Akt activation in Ras-mutated cancer cells. Biochem J 2010; 426: 65-72.
    • (2010) Biochem J , vol.426 , pp. 65-72
    • Omerovic, J.1    Clague, M.J.2    Prior, I.A.3
  • 75
    • 84867752182 scopus 로고    scopus 로고
    • Isolation and functional characterization of peptide agonists of PTPRJ, a tyrosine phosphatase receptor endowed with tumor suppressor activity
    • Paduano F, Ortuso F, Campiglia P, Raso C, Iaccino E, Gaspari M et al. Isolation and functional characterization of peptide agonists of PTPRJ, a tyrosine phosphatase receptor endowed with tumor suppressor activity. ACS Chem Biol 2012; 7: 1666-1676.
    • (2012) ACS Chem Biol , vol.7 , pp. 1666-1676
    • Paduano, F.1    Ortuso, F.2    Campiglia, P.3    Raso, C.4    Iaccino, E.5    Gaspari, M.6
  • 76
    • 79953187287 scopus 로고    scopus 로고
    • Proteintyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling
    • Arora D, Stopp S, Bohmer SA, Schons J, Godfrey R, Masson K et al. Proteintyrosine phosphatase DEP-1 controls receptor tyrosine kinase FLT3 signaling. J Biol Chem 2011; 286: 10918-10929.
    • (2011) J Biol Chem , vol.286 , pp. 10918-10929
    • Arora, D.1    Stopp, S.2    Bohmer, S.A.3    Schons, J.4    Godfrey, R.5    Masson, K.6
  • 77
    • 84874101235 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase receptor type J is regulated by the pVHL-HIF axis in clear cell renal cell carcinoma
    • Casagrande S, Ruf M, Rechsteiner M, Morra L, Brun-Schmid S, von Teichman A et al. The protein tyrosine phosphatase receptor type J is regulated by the pVHL-HIF axis in clear cell renal cell carcinoma. J Pathol 2013; 229: 525-534.
    • (2013) J Pathol , vol.229 , pp. 525-534
    • Casagrande, S.1    Ruf, M.2    Rechsteiner, M.3    Morra, L.4    Brun-Schmid, S.5    Von Teichman, A.6
  • 78
    • 84872763413 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase PTPRJ is negatively regulated by microRNA-328
    • Paduano F, Dattilo V, Narciso D, Bilotta A, Gaudio E, Menniti M et al. Protein tyrosine phosphatase PTPRJ is negatively regulated by microRNA-328. FEBS J 2013; 280: 401-412.
    • (2013) FEBS J , vol.280 , pp. 401-412
    • Paduano, F.1    Dattilo, V.2    Narciso, D.3    Bilotta, A.4    Gaudio, E.5    Menniti, M.6
  • 80
    • 33847636046 scopus 로고    scopus 로고
    • Vascular endothelial tyrosine phosphatase (VE-PTP)-null mice undergo vasculogenesis but die embryonically because of defects in angiogenesis
    • Dominguez MG, Hughes VC, Pan L, Simmons M, Daly C, Anderson K et al. Vascular endothelial tyrosine phosphatase (VE-PTP)-null mice undergo vasculogenesis but die embryonically because of defects in angiogenesis. Proc Natl Acad Sci USA 2007; 104: 3243-3248.
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 3243-3248
    • Dominguez, M.G.1    Hughes, V.C.2    Pan, L.3    Simmons, M.4    Daly, C.5    Anderson, K.6
  • 81
    • 33745107561 scopus 로고    scopus 로고
    • Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development
    • Baumer S, Keller L, Holtmann A, Funke R, August B, Gamp A et al. Vascular endothelial cell-specific phosphotyrosine phosphatase (VE-PTP) activity is required for blood vessel development. Blood 2006; 107: 4754-4762.
    • (2006) Blood , vol.107 , pp. 4754-4762
    • Baumer, S.1    Keller, L.2    Holtmann, A.3    Funke, R.4    August, B.5    Gamp, A.6
  • 83
    • 70349319448 scopus 로고    scopus 로고
    • Transcriptional profiling reveals a critical role for tyrosine phosphatase VE-PTP in regulation of VEGFR2 activity and endothelial cell morphogenesis
    • Mellberg S, Dimberg A, Bahram F, Hayashi M, Rennel E, Ameur A et al. Transcriptional profiling reveals a critical role for tyrosine phosphatase VE-PTP in regulation of VEGFR2 activity and endothelial cell morphogenesis. FASEB J 2009; 23: 1490-1502.
    • (2009) FASEB J , vol.23 , pp. 1490-1502
    • Mellberg, S.1    Dimberg, A.2    Bahram, F.3    Hayashi, M.4    Rennel, E.5    Ameur, A.6
  • 84
    • 84855493801 scopus 로고    scopus 로고
    • Dissociation of VE-PTP from VE-cadherin is required for leukocyte extravasation and for VEGF-induced vascular permeability in vivo
    • Broermann A, Winderlich M, Block H, Frye M, Rossaint J, Zarbock A et al. Dissociation of VE-PTP from VE-cadherin is required for leukocyte extravasation and for VEGF-induced vascular permeability in vivo. J Exp Med 2011; 208: 2393-2401.
    • (2011) J Exp Med , vol.208 , pp. 2393-2401
    • Broermann, A.1    Winderlich, M.2    Block, H.3    Frye, M.4    Rossaint, J.5    Zarbock, A.6
  • 85
    • 84877788239 scopus 로고    scopus 로고
    • VE-PTP regulates VEGFR2 activity in stalk cells to establish endothelial cell polarity and lumen formation
    • Hayashi M, Majumdar A, Li X, Adler J, Sun Z, Vertuani S et al. VE-PTP regulates VEGFR2 activity in stalk cells to establish endothelial cell polarity and lumen formation. Nat Commun 2013; 4: 1672.
    • (2013) Nat Commun , vol.4 , pp. 1672
    • Hayashi, M.1    Majumdar, A.2    Li, X.3    Adler, J.4    Sun, Z.5    Vertuani, S.6
  • 86
    • 84883174690 scopus 로고    scopus 로고
    • Effects of vascular-endothelial protein tyrosine phosphatase inhibition on breast cancer vasculature and metastatic progression
    • Goel S, Gupta N, Walcott BP, Snuderl M, Kesler CT, Kirkpatrick ND et al. Effects of vascular-endothelial protein tyrosine phosphatase inhibition on breast cancer vasculature and metastatic progression. J Natl Clin Inst 2013; 105: 1188-1201.
    • (2013) J Natl Clin Inst , vol.105 , pp. 1188-1201
    • Goel, S.1    Gupta, N.2    Walcott, B.P.3    Snuderl, M.4    Kesler, C.T.5    Kirkpatrick, N.D.6
  • 87
    • 84862129375 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase SHP-2 (PTPN11) in hematopoiesis and leukemogenesis
    • Liu X, Qu CK. Protein tyrosine phosphatase SHP-2 (PTPN11) in hematopoiesis and leukemogenesis. J Singnal Transduct 2011; 2011: 195239.
    • (2011) J Singnal Transduct , vol.2011 , pp. 195239
    • Liu, X.1    Qu, C.K.2
  • 88
    • 18344385476 scopus 로고    scopus 로고
    • Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome
    • Tartaglia M, Mehler EL, Goldberg R, Zampino G, Brunner HG, Kremer H et al. Mutations in PTPN11, encoding the protein tyrosine phosphatase SHP-2, cause Noonan syndrome. Nat Genet 2001; 29: 465-468.
    • (2001) Nat Genet , vol.29 , pp. 465-468
    • Tartaglia, M.1    Mehler, E.L.2    Goldberg, R.3    Zampino, G.4    Brunner, H.G.5    Kremer, H.6
  • 89
    • 0038278866 scopus 로고    scopus 로고
    • Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia
    • Tartaglia M, Niemeyer CM, Fragale A, Song X, Buechner J, Jung A et al. Somatic mutations in PTPN11 in juvenile myelomonocytic leukemia, myelodysplastic syndromes and acute myeloid leukemia. Nat Genet 2003; 34: 148-150.
    • (2003) Nat Genet , vol.34 , pp. 148-150
    • Tartaglia, M.1    Niemeyer, C.M.2    Fragale, A.3    Song, X.4    Buechner, J.5    Jung, A.6
  • 91
    • 84861875277 scopus 로고    scopus 로고
    • PTPN11-associated mutations in the heart: Has LEOPARD changed Its RASpots
    • Lauriol J, Kontaridis MI. PTPN11-associated mutations in the heart: has LEOPARD changed Its RASpots? Trends Cardiovasc Med 2011; 21: 97-104.
    • (2011) Trends Cardiovasc Med , vol.21 , pp. 97-104
    • Lauriol, J.1    Kontaridis, M.I.2
  • 93
    • 79955631529 scopus 로고    scopus 로고
    • Loss-of-function mutations in PTPN11 cause metachondromatosis, but not Ollier disease or Maffucci syndrome
    • Bowen ME, Boyden ED, Holm IA, Campos-Xavier B, Bonafe L, Superti-Furga A et al. Loss-of-function mutations in PTPN11 cause metachondromatosis, but not Ollier disease or Maffucci syndrome. PLoS Genet 2011; 7: e1002050.
    • (2011) PLoS Genet , vol.7 , pp. e1002050
    • Bowen, M.E.1    Boyden, E.D.2    Holm, I.A.3    Campos-Xavier, B.4    Bonafe, L.5    Superti-Furga, A.6
  • 94
    • 84881119110 scopus 로고    scopus 로고
    • Ptpn11 deletion in a novel progenitor causes metachondromatosis by inducing hedgehog signalling
    • Yang W, Wang J, Moore DC, Liang H, Dooner M, Wu Q et al. Ptpn11 deletion in a novel progenitor causes metachondromatosis by inducing hedgehog signalling. Nature 2013; 499: 491-495.
    • (2013) Nature , vol.499 , pp. 491-495
    • Yang, W.1    Wang, J.2    Moore, D.C.3    Liang, H.4    Dooner, M.5    Wu, Q.6
  • 95
    • 0037064549 scopus 로고    scopus 로고
    • Role of the SHP-2 tyrosine phosphatase in cytokine-induced signaling and cellular response
    • Qu CK. Role of the SHP-2 tyrosine phosphatase in cytokine-induced signaling and cellular response. Biochim Biophys Acta 2002; 1592: 297-301.
    • (2002) Biochim Biophys Acta , vol.1592 , pp. 297-301
    • Qu, C.K.1
  • 96
    • 84883710048 scopus 로고    scopus 로고
    • 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 CK. Induction of a tumor-associated activating mutation in protein tyrosine phosphatase Ptpn11 (Shp2) enhances mitochondrial metabolism, leading to oxidative stress and senescence. J Biol Chem 2013; 288: 25727-25738.
    • (2013) J Biol Chem , vol.288 , pp. 25727-25738
    • Zheng, H.1    Li, S.2    Hsu, P.3    Qu, C.K.4
  • 97
    • 84867565732 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase Shp2 (Ptpn11) plays an important role in maintenance of chromosome stability
    • Liu X, Zheng H, Qu CK. Protein tyrosine phosphatase Shp2 (Ptpn11) plays an important role in maintenance of chromosome stability. Cancer Res 2012; 72: 5296-5306.
    • (2012) Cancer Res , vol.72 , pp. 5296-5306
    • Liu, X.1    Zheng, H.2    Qu, C.K.3
  • 98
    • 84898058507 scopus 로고    scopus 로고
    • Recurrent somatic mutations of PTPN1 in primary mediastinal B cell lymphoma and Hodgkin lymphoma
    • Gunawardana J, Chan FC, Telenius A, Woolcock B, Kridel R, Tan KL et al. Recurrent somatic mutations of PTPN1 in primary mediastinal B cell lymphoma and Hodgkin lymphoma. Nat Genet 2014; 46: 329-335.
    • (2014) Nat Genet , vol.46 , pp. 329-335
    • Gunawardana, J.1    Chan, F.C.2    Telenius, A.3    Woolcock, B.4    Kridel, R.5    Tan, K.L.6
  • 99
    • 77955279589 scopus 로고    scopus 로고
    • PTP1B: A double agent in metabolism and oncogenesis
    • Yip SC, Saha S, Chernoff J. PTP1B: A double agent in metabolism and oncogenesis. Trends BiochemSci 2010; 35: 442-449.
    • (2010) Trends BiochemSci , vol.35 , pp. 442-449
    • Yip, S.C.1    Saha, S.2    Chernoff, J.3
  • 100
    • 33847375227 scopus 로고    scopus 로고
    • Protein-tyrosine phosphatase 1B is required for HER2/Neu-induced breast cancer
    • Bentires-Alj M, Neel BG. Protein-tyrosine phosphatase 1B is required for HER2/Neu-induced breast cancer. Cancer Res 2007; 67: 2420-2424.
    • (2007) Cancer Res , vol.67 , pp. 2420-2424
    • Bentires-Alj, M.1    Neel, B.G.2
  • 101
    • 79952996490 scopus 로고    scopus 로고
    • PTPN13/PTPL1: An important regulator of tumor aggressiveness
    • Freiss G, Chalbos D. PTPN13/PTPL1: An important regulator of tumor aggressiveness. Anticancer Agents Med Chem 2011; 11: 78-88.
    • (2011) Anticancer Agents Med Chem , vol.11 , pp. 78-88
    • Freiss, G.1    Chalbos, D.2
  • 102
    • 33744494280 scopus 로고    scopus 로고
    • Epigenetic disruption of two proapoptotic genes MAPK10/JNK3 and PTPN13/FAP-1 in multiple lymphomas and carcinomas through hypermethylation of a common bidirectional promoter
    • Ying J, Li H, Cui Y, Wong AH, Langford C, Tao Q. Epigenetic disruption of two proapoptotic genes MAPK10/JNK3 and PTPN13/FAP-1 in multiple lymphomas and carcinomas through hypermethylation of a common bidirectional promoter. Leukemia 2006; 20: 1173-1175.
    • (2006) Leukemia , vol.20 , pp. 1173-1175
    • Ying, J.1    Li, H.2    Cui, Y.3    Wong, A.H.4    Langford, C.5    Tao, Q.6
  • 103
    • 84857220124 scopus 로고    scopus 로고
    • The nonreceptor-type tyrosine phosphatase PTPN13 is a tumor suppressor gene in non-small cell lung cancer
    • Scrima M, De Marco C, De Vita F, Fabiani F, Franco R, Pirozzi G et al. The nonreceptor-type tyrosine phosphatase PTPN13 is a tumor suppressor gene in non-small cell lung cancer. Am J Pathol 2012; 180: 1202-1214.
    • (2012) Am J Pathol , vol.180 , pp. 1202-1214
    • Scrima, M.1    De Marco, C.2    De Vita, F.3    Fabiani, F.4    Franco, R.5    Pirozzi, G.6
  • 104
    • 33845608666 scopus 로고    scopus 로고
    • FAP-1-mediated activation of NF-kappaB induces resistance of head and neck cancer to Fasinduced apoptosis
    • Wieckowski E, Atarashi Y, Stanson J, Sato TA, Whiteside TL. FAP-1-mediated activation of NF-kappaB induces resistance of head and neck cancer to Fasinduced apoptosis. J Cell Biochem 2007; 100: 16-28.
    • (2007) J Cell Biochem , vol.100 , pp. 16-28
    • Wieckowski, E.1    Atarashi, Y.2    Stanson, J.3    Sato, T.A.4    Whiteside, T.L.5
  • 105
    • 79954418848 scopus 로고    scopus 로고
    • FAP-1 and NF-kappaB expressions in oral squamous cell carcinoma as potential markers for chemo-radio sensitivity and prognosis
    • Nariai Y, Mishima K, Yoshimura Y, Sekine J. FAP-1 and NF-kappaB expressions in oral squamous cell carcinoma as potential markers for chemo-radio sensitivity and prognosis. Int J Oral Maxillofac Surg 2011; 40: 419-426.
    • (2011) Int J Oral Maxillofac Surg , vol.40 , pp. 419-426
    • Nariai, Y.1    Mishima, K.2    Yoshimura, Y.3    Sekine, J.4
  • 106
    • 75449095661 scopus 로고    scopus 로고
    • Silencing Fas-associated phosphatase 1 expression enhances efficiency of chemotherapy for colon carcinoma with oxaliplatin
    • Xiao ZY, Wu W, Eagleton N, Chen HQ, Shao J, Teng H et al. Silencing Fas-associated phosphatase 1 expression enhances efficiency of chemotherapy for colon carcinoma with oxaliplatin. World J Gastroenterol 2010; 16: 112-118.
    • (2010) World J Gastroenterol , vol.16 , pp. 112-118
    • Xiao, Z.Y.1    Wu, W.2    Eagleton, N.3    Chen, H.Q.4    Shao, J.5    Teng, H.6
  • 107
    • 58149279840 scopus 로고    scopus 로고
    • Expression of the putative tumor suppressor gene PTPN13/PTPL1 is an independent prognostic marker for overall survival in breast cancer
    • Revillion F, Puech C, Rabenoelina F, Chalbos D, Peyrat JP, Freiss G. Expression of the putative tumor suppressor gene PTPN13/PTPL1 is an independent prognostic marker for overall survival in breast cancer. Int J Cancer 2009; 124: 638-643.
    • (2009) Int J Cancer , vol.124 , pp. 638-643
    • Revillion, F.1    Puech, C.2    Rabenoelina, F.3    Chalbos, D.4    Peyrat, J.P.5    Freiss, G.6
  • 108
    • 42249109536 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase PTPN13 negatively regulates Her2/ErbB2 malignant signaling
    • Zhu JH, Chen R, Yi W, Cantin GT, Fearns C, Yang Y et al. Protein tyrosine phosphatase PTPN13 negatively regulates Her2/ErbB2 malignant signaling. Oncogene 2008; 27: 2525-2531.
    • (2008) Oncogene , vol.27 , pp. 2525-2531
    • Zhu, J.H.1    Chen, R.2    Yi, W.3    Cantin, G.T.4    Fearns, C.5    Yang, Y.6
  • 109
    • 84862907930 scopus 로고    scopus 로고
    • ErbB2, EphrinB1, Src kinase and PTPN13 signaling complex regulates MAP kinase signaling in human cancers
    • Vermeer PD, Bell M, Lee K, Vermeer DW, Wieking BG, Bilal E et al. ErbB2, EphrinB1, Src kinase and PTPN13 signaling complex regulates MAP kinase signaling in human cancers. PLoS One 2012; 7: e30447.
    • (2012) PLoS One , vol.7 , pp. e30447
    • Vermeer, P.D.1    Bell, M.2    Lee, K.3    Vermeer, D.W.4    Wieking, B.G.5    Bilal, E.6
  • 110
    • 84877577024 scopus 로고    scopus 로고
    • FBXL2-and PTPL1-mediated degradation of p110-free p85beta regulatory subunit controls the PI(3)K signalling cascade
    • Kuchay S, Duan S, Schenkein E, Peschiaroli A, Saraf A, Florens L et al. FBXL2-and PTPL1-mediated degradation of p110-free p85beta regulatory subunit controls the PI(3)K signalling cascade. Nat Cell Biol 2013; 15: 472-480.
    • (2013) Nat Cell Biol , vol.15 , pp. 472-480
    • Kuchay, S.1    Duan, S.2    Schenkein, E.3    Peschiaroli, A.4    Saraf, A.5    Florens, L.6
  • 111
    • 84877139731 scopus 로고    scopus 로고
    • Fas-associated phosphatase 1 (Fap1) influences betacatenin activity in myeloid progenitor cells expressing the Bcr-abl oncogene
    • Huang W, Bei L, Eklund EA. Fas-associated phosphatase 1 (Fap1) influences betacatenin activity in myeloid progenitor cells expressing the Bcr-abl oncogene. J Biol Chem 2013; 288: 12766-12776.
    • (2013) J Biol Chem , vol.288 , pp. 12766-12776
    • Huang, W.1    Bei, L.2    Eklund, E.A.3
  • 112
    • 70449651958 scopus 로고    scopus 로고
    • Impaired PTPN13 phosphatase activity in spontaneous or HPV-induced squamous cell carcinomas potentiates oncogene signaling through the MAP kinase pathway
    • Hoover AC, Strand GL, Nowicki PN, Anderson ME, Vermeer PD, Klingelhutz AJ et al. Impaired PTPN13 phosphatase activity in spontaneous or HPV-induced squamous cell carcinomas potentiates oncogene signaling through the MAP kinase pathway. Oncogene 2009; 28: 3960-3970.
    • (2009) Oncogene , vol.28 , pp. 3960-3970
    • Hoover, A.C.1    Strand, G.L.2    Nowicki, P.N.3    Anderson, M.E.4    Vermeer, P.D.5    Klingelhutz, A.J.6
  • 113
    • 84884902313 scopus 로고    scopus 로고
    • The serologically defined colon cancer antigen-3 interacts with the protein tyrosine phosphatase PTPN13 and is involved in the regulation of cytokinesis
    • Hagemann N, Ackermann N, Christmann J, Brier S, Yu F, Erdmann KS. The serologically defined colon cancer antigen-3 interacts with the protein tyrosine phosphatase PTPN13 and is involved in the regulation of cytokinesis. Oncogene 2013; 32: 4602-4613.
    • (2013) Oncogene , vol.32 , pp. 4602-4613
    • Hagemann, N.1    Ackermann, N.2    Christmann, J.3    Brier, S.4    Yu, F.5    Erdmann, K.S.6
  • 114
    • 84869091005 scopus 로고    scopus 로고
    • Valosin containing protein (VCP/p97) is a novel substrate for the protein tyrosine phosphatase PTPL1
    • Abaan OD, Hendriks W, Uren A, Toretsky JA, Erkizan HV. Valosin containing protein (VCP/p97) is a novel substrate for the protein tyrosine phosphatase PTPL1. Exp Cell Res 2013; 319: 1-11.
    • (2013) Exp Cell Res , vol.319 , pp. 1-11
    • Abaan, O.D.1    Hendriks, W.2    Uren, A.3    Toretsky, J.A.4    Erkizan, H.V.5
  • 115
    • 39749192555 scopus 로고    scopus 로고
    • The PDZ binding motif of human papillomavirus type 16 E6 induces PTPN13 loss, which allows anchorage-independent growth and synergizes with ras for invasive growth
    • Spanos WC, Hoover A, Harris GF, Wu S, Strand GL, Anderson ME et al. The PDZ binding motif of human papillomavirus type 16 E6 induces PTPN13 loss, which allows anchorage-independent growth and synergizes with ras for invasive growth. J Virol 2008; 82: 2493-2500.
    • (2008) J Virol , vol.82 , pp. 2493-2500
    • Spanos, W.C.1    Hoover, A.2    Harris, G.F.3    Wu, S.4    Strand, G.L.5    Anderson, M.E.6
  • 116
    • 77955507555 scopus 로고    scopus 로고
    • MIR-200c regulates induction of apoptosis through CD95 by targeting FAP-1
    • Schickel R, Park SM, Murmann AE, Peter ME. miR-200c regulates induction of apoptosis through CD95 by targeting FAP-1. Mol Cell 2010; 38: 908-915.
    • (2010) Mol Cell , vol.38 , pp. 908-915
    • Schickel, R.1    Park, S.M.2    Murmann, A.E.3    Peter, M.E.4
  • 117
    • 84873356810 scopus 로고    scopus 로고
    • Fas-associated phosphatase 1 mediates Fas resistance in myeloid progenitor cells expressing the Bcr-abl oncogene
    • Huang W, Bei L, Eklund EA. Fas-associated phosphatase 1 mediates Fas resistance in myeloid progenitor cells expressing the Bcr-abl oncogene. Leuk Lymphoma 2013; 54: 619-630.
    • (2013) Leuk Lymphoma , vol.54 , pp. 619-630
    • Huang, W.1    Bei, L.2    Eklund, E.A.3
  • 118
    • 48849087797 scopus 로고    scopus 로고
    • PTP-Pez: A novel regulator of TGFbeta signaling
    • Wyatt L, Khew-Goodall Y. PTP-Pez: A novel regulator of TGFbeta signaling. Cell Cycle 2008; 7: 2290-2295.
    • (2008) Cell Cycle , vol.7 , pp. 2290-2295
    • Wyatt, L.1    Khew-Goodall, Y.2
  • 119
    • 77956385127 scopus 로고    scopus 로고
    • Protein tyrosine phosphatase PTPN14 is a regulator of lymphatic function and choanal development in humans
    • Au AC, Hernandez PA, Lieber E, Nadroo AM, Shen YM, Kelley KA et al. Protein tyrosine phosphatase PTPN14 is a regulator of lymphatic function and choanal development in humans. Am J Hum Genet 2010; 87: 436-444.
    • (2010) Am J Hum Genet , vol.87 , pp. 436-444
    • Au, A.C.1    Hernandez, P.A.2    Lieber, E.3    Nadroo, A.M.4    Shen, Y.M.5    Kelley, K.A.6
  • 120
    • 84865840957 scopus 로고    scopus 로고
    • PTPN14 is required for the density-dependent control of YAP1
    • Wang W, Huang J, Wang X, Yuan J, Li X, Feng L et al. PTPN14 is required for the density-dependent control of YAP1. Genes Dev 2012; 26: 1959-1971.
    • (2012) Genes Dev , vol.26 , pp. 1959-1971
    • Wang, W.1    Huang, J.2    Wang, X.3    Yuan, J.4    Li, X.5    Feng, L.6
  • 121
    • 0038308412 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin
    • Wadham C, Gamble JR, Vadas MA, Khew-Goodall Y. The protein tyrosine phosphatase Pez is a major phosphatase of adherens junctions and dephosphorylates beta-catenin. Mol Biol Cell 2003; 14: 2520-2529.
    • (2003) Mol Biol Cell , vol.14 , pp. 2520-2529
    • Wadham, C.1    Gamble, J.R.2    Vadas, M.A.3    Khew-Goodall, Y.4
  • 122
    • 84876694091 scopus 로고    scopus 로고
    • Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14
    • Zhang P, Guo A, Possemato A, Wang C, Beard L, Carlin C et al. Identification and functional characterization of p130Cas as a substrate of protein tyrosine phosphatase nonreceptor 14. Oncogene 2013; 32: 2087-2095.
    • (2013) Oncogene , vol.32 , pp. 2087-2095
    • Zhang, P.1    Guo, A.2    Possemato, A.3    Wang, C.4    Beard, L.5    Carlin, C.6
  • 124
    • 84876943442 scopus 로고    scopus 로고
    • YAP modifies cancer cell sensitivity to EGFR and survivin inhibitors and is negatively regulated by the non-receptor type protein tyrosine phosphatase 14
    • Huang JM, Nagatomo I, Suzuki E, Mizuno T, Kumagai T, Berezov A et al. YAP modifies cancer cell sensitivity to EGFR and survivin inhibitors and is negatively regulated by the non-receptor type protein tyrosine phosphatase 14. Oncogene 2013; 32: 2220-2229.
    • (2013) Oncogene , vol.32 , pp. 2220-2229
    • Huang, J.M.1    Nagatomo, I.2    Suzuki, E.3    Mizuno, T.4    Kumagai, T.5    Berezov, A.6
  • 125
    • 84874767303 scopus 로고    scopus 로고
    • PTPN14 interacts with and negatively regulates the oncogenic function of YAP
    • Liu X, Yang N, Figel SA, Wilson KE, Morrison CD, Gelman IH et al. PTPN14 interacts with and negatively regulates the oncogenic function of YAP. Oncogene 2013; 32: 1266-1273.
    • (2013) Oncogene , vol.32 , pp. 1266-1273
    • Liu, X.1    Yang, N.2    Figel, S.A.3    Wilson, K.E.4    Morrison, C.D.5    Gelman, I.H.6
  • 126
    • 0031055324 scopus 로고    scopus 로고
    • Development of 'substrate-trapping' mutants to identify physiological substrates of protein tyrosine phosphatases
    • Flint AJ, Tiganis T, Barford D, Tonks NK. Development of 'substrate-trapping' mutants to identify physiological substrates of protein tyrosine phosphatases. Proc Natl Acad Sci USA 1997; 94: 1680-1685.
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1680-1685
    • Flint, A.J.1    Tiganis, T.2    Barford, D.3    Tonks, N.K.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.