메뉴 건너뛰기




Volumn 229, Issue 4, 2013, Pages 525-534

The protein tyrosine phosphatase receptor type J is regulated by the pVHL-HIF axis in clear cell renal cell carcinoma

Author keywords

PTPRJ; RCC; VHL HIF pathway

Indexed keywords

HYPOXIA INDUCIBLE FACTOR 2ALPHA; MESSENGER RNA; PROTEIN TYROSINE PHOSPHATASE RECEPTOR TYPE J; RNA; TYROSINE KINASE RECEPTOR; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN;

EID: 84874101235     PISSN: 00223417     EISSN: 10969896     Source Type: Journal    
DOI: 10.1002/path.4107     Document Type: Article
Times cited : (10)

References (46)
  • 1
    • 33644510421 scopus 로고    scopus 로고
    • Genetic and epigenetic analysis of von Hippel-Lindau (VHL) gene alterations and relationship with clinical variables in sporadic renal cancer
    • Banks RE, Tirukonda P, Taylor C, et al,. Genetic and epigenetic analysis of von Hippel-Lindau (VHL) gene alterations and relationship with clinical variables in sporadic renal cancer. Cancer Res 2006; 66: 2000-2011.
    • (2006) Cancer Res , vol.66 , pp. 2000-2011
    • Banks, R.E.1    Tirukonda, P.2    Taylor, C.3
  • 2
    • 36749102487 scopus 로고    scopus 로고
    • Multitasking by pVHL in tumour suppression
    • Frew IJ, Krek W,. Multitasking by pVHL in tumour suppression. Curr Opin Cell Biol 2007; 19: 685-690.
    • (2007) Curr Opin Cell Biol , vol.19 , pp. 685-690
    • Frew, I.J.1    Krek, W.2
  • 3
    • 77951877765 scopus 로고    scopus 로고
    • Alterations in VHL as potential biomarkers in renal-cell carcinoma
    • Gossage L, Eisen T,. Alterations in VHL as potential biomarkers in renal-cell carcinoma. Nature Rev Clin Oncol 2010; 7: 277-288.
    • (2010) Nature Rev Clin Oncol , vol.7 , pp. 277-288
    • Gossage, L.1    Eisen, T.2
  • 4
    • 9144232529 scopus 로고    scopus 로고
    • Fibronectin is a hypoxia-independent target of the tumor suppressor VHL
    • Bluyssen HA, Lolkema MP, van Beest M, et al,. Fibronectin is a hypoxia-independent target of the tumor suppressor VHL. FEBS Lett 2004; 556: 137-142.
    • (2004) FEBS Lett , vol.556 , pp. 137-142
    • Bluyssen, H.A.1    Lolkema, M.P.2    Van Beest, M.3
  • 5
    • 33645748171 scopus 로고    scopus 로고
    • Regulation of E-cadherin expression by VHL and hypoxia-inducible factor
    • Esteban MA, Tran MG, Harten SK, et al,. Regulation of E-cadherin expression by VHL and hypoxia-inducible factor. Cancer Res 2006; 66: 3567-3575.
    • (2006) Cancer Res , vol.66 , pp. 3567-3575
    • Esteban, M.A.1    Tran, M.G.2    Harten, S.K.3
  • 6
    • 66149190688 scopus 로고    scopus 로고
    • Loss of VHL and hypoxia provokes PAX2 up-regulation in clear cell renal cell carcinoma
    • Luu VD, Boysen G, Struckmann K, et al,. Loss of VHL and hypoxia provokes PAX2 up-regulation in clear cell renal cell carcinoma. Clin Cancer Res 2009; 15: 3297-3304.
    • (2009) Clin Cancer Res , vol.15 , pp. 3297-3304
    • Luu, V.D.1    Boysen, G.2    Struckmann, K.3
  • 7
    • 33646140913 scopus 로고    scopus 로고
    • P53 stabilization and transactivation by a von Hippel-Lindau protein
    • Roe JS, Kim H, Lee SM, et al,. p53 stabilization and transactivation by a von Hippel-Lindau protein. Mol Cell 2006; 22: 395-405.
    • (2006) Mol Cell , vol.22 , pp. 395-405
    • Roe, J.S.1    Kim, H.2    Lee, S.M.3
  • 8
    • 84865652325 scopus 로고    scopus 로고
    • Identification and functional characterization of pVHL-dependent cell surface proteins in renal cell carcinoma
    • Boysen G, Bausch-Fluck D, Thoma CR, et al,. Identification and functional characterization of pVHL-dependent cell surface proteins in renal cell carcinoma. Neoplasia 2012; 14: 535-546.
    • (2012) Neoplasia , vol.14 , pp. 535-546
    • Boysen, G.1    Bausch-Fluck, D.2    Thoma, C.R.3
  • 9
    • 0027971245 scopus 로고
    • Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta
    • Honda H, Inazawa J, Nishida J, et al,. Molecular cloning, characterization, and chromosomal localization of a novel protein-tyrosine phosphatase, HPTP eta. Blood 1994; 84: 4186-4194.
    • (1994) Blood , vol.84 , pp. 4186-4194
    • Honda, H.1    Inazawa, J.2    Nishida, J.3
  • 10
    • 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, 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
  • 11
    • 0037699447 scopus 로고    scopus 로고
    • The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell-matrix adhesion
    • Jandt E, Denner K, Kovalenko M, et al,. The protein-tyrosine phosphatase DEP-1 modulates growth factor-stimulated cell migration and cell-matrix adhesion. Oncogene 2003; 22: 4175-4185.
    • (2003) Oncogene , vol.22 , pp. 4175-4185
    • Jandt, E.1    Denner, K.2    Kovalenko, M.3
  • 12
    • 1242329400 scopus 로고    scopus 로고
    • The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation
    • Kellie S, Craggs G, Bird IN, et al,. The tyrosine phosphatase DEP-1 induces cytoskeletal rearrangements, aberrant cell-substratum interactions and a reduction in cell proliferation. J Cell Sci 2004; 117: 609-618.
    • (2004) J Cell Sci , vol.117 , pp. 609-618
    • Kellie, S.1    Craggs, G.2    Bird, I.N.3
  • 13
    • 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, 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
  • 14
    • 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, 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
  • 15
    • 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, 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
  • 16
    • 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, et al,. Ptprj is a candidate for the mouse colon-cancer susceptibility locus Scc1 and is frequently deleted in human cancers. Nature Genet 2002; 31: 295-300.
    • (2002) Nature Genet , vol.31 , pp. 295-300
    • Ruivenkamp, C.A.1    Van Wezel, T.2    Zanon, C.3
  • 17
    • 71849092111 scopus 로고    scopus 로고
    • An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis
    • Tarcic G, Boguslavsky SK, Wakim J, et al,. An unbiased screen identifies DEP-1 tumor suppressor as a phosphatase controlling EGFR endocytosis. Curr Biol 2009; 19: 1788-1798.
    • (2009) Curr Biol , vol.19 , pp. 1788-1798
    • Tarcic, G.1    Boguslavsky, S.K.2    Wakim, J.3
  • 18
    • 0034717163 scopus 로고    scopus 로고
    • Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1
    • Kovalenko M, Denner K, Sandstrom J, et al,. Site-selective dephosphorylation of the platelet-derived growth factor beta-receptor by the receptor-like protein-tyrosine phosphatase DEP-1. J Biol Chem 2000; 275: 16219-16226.
    • (2000) J Biol Chem , vol.275 , pp. 16219-16226
    • Kovalenko, M.1    Denner, K.2    Sandstrom, J.3
  • 19
    • 0038699077 scopus 로고    scopus 로고
    • Contact inhibition of VEGF-induced proliferation requires vascular endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148
    • Grazia Lampugnani M, Zanetti A, Corada M, et al,. Contact inhibition of VEGF-induced proliferation requires vascular endothelial cadherin, beta-catenin, and the phosphatase DEP-1/CD148. J Cell Biol 2003; 161: 793-804.
    • (2003) J Cell Biol , vol.161 , pp. 793-804
    • Grazia Lampugnani, M.1    Zanetti, A.2    Corada, M.3
  • 20
    • 0037458646 scopus 로고    scopus 로고
    • Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1
    • Palka HL, Park M, Tonks NK,. Hepatocyte growth factor receptor tyrosine kinase met is a substrate of the receptor protein-tyrosine phosphatase DEP-1. J Biol Chem 2003; 278: 5728-5735.
    • (2003) J Biol Chem , vol.278 , pp. 5728-5735
    • Palka, H.L.1    Park, M.2    Tonks, N.K.3
  • 21
    • 34548666626 scopus 로고    scopus 로고
    • Automated immunofluorescence analysis defines microvessel area as a prognostic parameter in clear cell renal cell cancer
    • Mertz KD, Demichelis F, Kim R, et al,. Automated immunofluorescence analysis defines microvessel area as a prognostic parameter in clear cell renal cell cancer. Hum Pathol 2007; 38: 1454-1462.
    • (2007) Hum Pathol , vol.38 , pp. 1454-1462
    • Mertz, K.D.1    Demichelis, F.2    Kim, R.3
  • 22
    • 34447300959 scopus 로고    scopus 로고
    • In search of suitable reference genes for gene expression studies of human renal cell carcinoma by real-time PCR
    • Jung M, Ramankulov A, Roigas J, et al,. In search of suitable reference genes for gene expression studies of human renal cell carcinoma by real-time PCR. BMC Mol Biol 2007; 8: 47.
    • (2007) BMC Mol Biol , vol.8 , pp. 47
    • Jung, M.1    Ramankulov, A.2    Roigas, J.3
  • 23
    • 39649108663 scopus 로고    scopus 로고
    • Distinct expression patterns of the immunogenic differentiation antigen NY-BR-1 in normal breast, testis and their malignant counterparts
    • Theurillat JP, Zurrer-Hardi U, Varga Z, et al,. Distinct expression patterns of the immunogenic differentiation antigen NY-BR-1 in normal breast, testis and their malignant counterparts. Int J Cancer 2008; 122: 1585-1591.
    • (2008) Int J Cancer , vol.122 , pp. 1585-1591
    • Theurillat, J.P.1    Zurrer-Hardi, U.2    Varga, Z.3
  • 24
    • 58149159900 scopus 로고    scopus 로고
    • Sporadic clear cell renal cell carcinoma but not the papillary type is characterized by severely reduced frequency of primary cilia
    • Schraml P, Frew IJ, Thoma CR, et al,. Sporadic clear cell renal cell carcinoma but not the papillary type is characterized by severely reduced frequency of primary cilia. Mod Pathol 2009; 22: 31-36.
    • (2009) Mod Pathol , vol.22 , pp. 31-36
    • Schraml, P.1    Frew, I.J.2    Thoma, C.R.3
  • 25
    • 18844408840 scopus 로고    scopus 로고
    • Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: Identification of a functional hypoxia-responsive element
    • Metzen E, Stiehl DP, Doege K, et al,. Regulation of the prolyl hydroxylase domain protein 2 (phd2/egln-1) gene: identification of a functional hypoxia-responsive element. Biochem J 2005; 387: 711-717.
    • (2005) Biochem J , vol.387 , pp. 711-717
    • Metzen, E.1    Stiehl, D.P.2    Doege, K.3
  • 26
    • 34247863920 scopus 로고    scopus 로고
    • PVHL and GSK3beta are components of a primary cilium-maintenance signalling network
    • Thoma CR, Frew IJ, Hoerner CR, et al,. pVHL and GSK3beta are components of a primary cilium-maintenance signalling network. Nature Cell Biol 2007; 9: 588-595.
    • (2007) Nature Cell Biol , vol.9 , pp. 588-595
    • Thoma, C.R.1    Frew, I.J.2    Hoerner, C.R.3
  • 27
    • 80051697173 scopus 로고    scopus 로고
    • VHL gene mutations and their effects on hypoxia inducible factor HIFα: Identification of potential driver and passenger mutations
    • Rechsteiner MP, von Teichman A, Nowicka A, et al,. VHL gene mutations and their effects on hypoxia inducible factor HIFα: identification of potential driver and passenger mutations. Cancer Res 2011; 71: 5500-5511.
    • (2011) Cancer Res , vol.71 , pp. 5500-5511
    • Rechsteiner, M.P.1    Von Teichman, A.2    Nowicka, A.3
  • 28
    • 51049084870 scopus 로고    scopus 로고
    • Improved identification of von Hippel-Lindau gene alterations in clear cell renal tumors
    • Nickerson ML, Jaeger E, Shi Y, et al,. Improved identification of von Hippel-Lindau gene alterations in clear cell renal tumors. Clin Cancer Res 2008; 14: 4726-4734.
    • (2008) Clin Cancer Res , vol.14 , pp. 4726-4734
    • Nickerson, M.L.1    Jaeger, E.2    Shi, Y.3
  • 29
    • 16744366213 scopus 로고    scopus 로고
    • VHL alterations in human clear cell renal cell carcinoma: Association with advanced tumor stage and a novel hot spot mutation
    • Brauch H, Weirich G, Brieger J, et al,. VHL alterations in human clear cell renal cell carcinoma: association with advanced tumor stage and a novel hot spot mutation. Cancer Res 2000; 60: 1942-1948.
    • (2000) Cancer Res , vol.60 , pp. 1942-1948
    • Brauch, H.1    Weirich, G.2    Brieger, J.3
  • 30
    • 0028072991 scopus 로고
    • Silencing of the VHL tumor-suppressor gene by DNA methylation in renal carcinoma
    • Herman JG, Latif F, Weng Y, et al,. Silencing of the VHL tumor-suppressor gene by DNA methylation in renal carcinoma. Proc Natl Acad Sci U S A 1994; 91: 9700-9704.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9700-9704
    • Herman, J.G.1    Latif, F.2    Weng, Y.3
  • 31
    • 0345491599 scopus 로고    scopus 로고
    • Differential roles of hypoxia-inducible factor 1α (HIF-1α) and HIF-2α in hypoxic gene regulation
    • Hu CJ, Wang LY, Chodosh LA, et al,. Differential roles of hypoxia-inducible factor 1α (HIF-1α) and HIF-2α in hypoxic gene regulation. Mol Cell Biol 2003; 23: 9361-9374.
    • (2003) Mol Cell Biol , vol.23 , pp. 9361-9374
    • Hu, C.J.1    Wang, L.Y.2    Chodosh, L.A.3
  • 32
    • 20744445650 scopus 로고    scopus 로고
    • Contrasting properties of hypoxia-inducible factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-associated renal cell carcinoma
    • Raval RR, Lau KW, Tran MG, et al,. Contrasting properties of hypoxia-inducible factor 1 (HIF-1) and HIF-2 in von Hippel-Lindau-associated renal cell carcinoma. Mol Cell Biol 2005; 25: 5675-5686.
    • (2005) Mol Cell Biol , vol.25 , pp. 5675-5686
    • Raval, R.R.1    Lau, K.W.2    Tran, M.G.3
  • 33
    • 0036174191 scopus 로고    scopus 로고
    • Repression of α-fetoprotein gene expression under hypoxic conditions in human hepatoma cells: Characterization of a negative hypoxia response element that mediates opposite effects of hypoxia inducible factor-1 and c-Myc
    • Mazure NM, Chauvet C, Bois-Joyeux B, et al,. Repression of α-fetoprotein gene expression under hypoxic conditions in human hepatoma cells: characterization of a negative hypoxia response element that mediates opposite effects of hypoxia inducible factor-1 and c-Myc. Cancer Res 2002; 62: 1158-1165.
    • (2002) Cancer Res , vol.62 , pp. 1158-1165
    • Mazure, N.M.1    Chauvet, C.2    Bois-Joyeux, B.3
  • 34
    • 0035877163 scopus 로고    scopus 로고
    • Hypoxia-inducible factor 1-mediated inhibition of peroxisome proliferator-activated receptor alpha expression during hypoxia
    • Narravula S, Colgan SP,. Hypoxia-inducible factor 1-mediated inhibition of peroxisome proliferator-activated receptor alpha expression during hypoxia. J Immunol 2001; 166: 7543-7548.
    • (2001) J Immunol , vol.166 , pp. 7543-7548
    • Narravula, S.1    Colgan, S.P.2
  • 35
    • 77951938407 scopus 로고    scopus 로고
    • Downregulation of a tumor suppressor RECK by hypoxia through recruitment of HDAC1 and HIF-1α to reverse HRE site in the promoter
    • Lee KJ, Lee KY, Lee YM,. Downregulation of a tumor suppressor RECK by hypoxia through recruitment of HDAC1 and HIF-1α to reverse HRE site in the promoter. Biochim Biophys Acta 2010; 1803: 608-616.
    • (2010) Biochim Biophys Acta , vol.1803 , pp. 608-616
    • Lee, K.J.1    Lee, K.Y.2    Lee, Y.M.3
  • 36
    • 9144262524 scopus 로고    scopus 로고
    • The tyrosine phosphatase PTPRJ/DEP-1 genotype affects thyroid carcinogenesis
    • Iuliano R, Le Pera I, Cristofaro C, 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
  • 37
    • 78649834975 scopus 로고    scopus 로고
    • Role of PTPRJ genotype in papillary thyroid carcinoma risk
    • Iuliano R, Palmieri D, He H, et al,. Role of PTPRJ genotype in papillary thyroid carcinoma risk. Endocr Relat Cancer 2010; 17: 1001-1006.
    • (2010) Endocr Relat Cancer , vol.17 , pp. 1001-1006
    • Iuliano, R.1    Palmieri, D.2    He, H.3
  • 38
    • 74049111302 scopus 로고    scopus 로고
    • Missense polymorphisms of PTPRJ and PTPN13 genes affect susceptibility to a variety of human cancers
    • Mita Y, Yasuda Y, Sakai A, et al,. Missense polymorphisms of PTPRJ and PTPN13 genes affect susceptibility to a variety of human cancers. J Cancer Res Clin Oncol 2010; 136: 249-259.
    • (2010) J Cancer Res Clin Oncol , vol.136 , pp. 249-259
    • Mita, Y.1    Yasuda, Y.2    Sakai, A.3
  • 39
    • 0037442696 scopus 로고    scopus 로고
    • An adenovirus carrying the rat protein tyrosine phosphatase eta suppresses the growth of human thyroid carcinoma cell lines in vitro and in vivo
    • Iuliano R, Trapasso F, Le Pera I, et al,. An adenovirus carrying the rat protein tyrosine phosphatase eta suppresses the growth of human thyroid carcinoma cell lines in vitro and in vivo. Cancer Res 2003; 63: 882-886.
    • (2003) Cancer Res , vol.63 , pp. 882-886
    • Iuliano, R.1    Trapasso, F.2    Le Pera, I.3
  • 40
    • 0029789246 scopus 로고    scopus 로고
    • The protein tyrosine phosphatase DEP-1 is induced during differentiation and inhibits growth of breast cancer cells
    • Keane MM, Lowrey GA, Ettenberg SA, et al,. The protein tyrosine phosphatase DEP-1 is induced during differentiation and inhibits growth of breast cancer cells. Cancer Res 1996; 56: 4236-4243.
    • (1996) Cancer Res , vol.56 , pp. 4236-4243
    • Keane, M.M.1    Lowrey, G.A.2    Ettenberg, S.A.3
  • 41
    • 84857358303 scopus 로고    scopus 로고
    • Epidermal growth factor receptor protein expression and genomic alterations in renal cell carcinoma
    • Minner S, Rump D, Tennstedt P, et al,. Epidermal growth factor receptor protein expression and genomic alterations in renal cell carcinoma. Cancer 2012; 118: 1268-1275.
    • (2012) Cancer , vol.118 , pp. 1268-1275
    • Minner, S.1    Rump, D.2    Tennstedt, P.3
  • 42
    • 0030786030 scopus 로고    scopus 로고
    • Epidermal growth factor receptor expression is associated with rapid tumor cell proliferation in renal cell carcinoma
    • Moch H, Sauter G, Buchholz N, et al,. Epidermal growth factor receptor expression is associated with rapid tumor cell proliferation in renal cell carcinoma. Hum Pathol 1997; 28: 1255-1259.
    • (1997) Hum Pathol , vol.28 , pp. 1255-1259
    • Moch, H.1    Sauter, G.2    Buchholz, N.3
  • 43
    • 0345714775 scopus 로고    scopus 로고
    • Phase II trial of ZD1839 (IRESSA) in patients with advanced renal cell carcinoma
    • Drucker B, Bacik J, Ginsberg M, et al,. Phase II trial of ZD1839 (IRESSA) in patients with advanced renal cell carcinoma. Invest New Drugs 2003; 21: 341-345.
    • (2003) Invest New Drugs , vol.21 , pp. 341-345
    • Drucker, B.1    Bacik, J.2    Ginsberg, M.3
  • 44
    • 4143050397 scopus 로고    scopus 로고
    • Safety, pharmacokinetics, and activity of ABX-EGF, a fully human anti-epidermal growth factor receptor monoclonal antibody in patients with metastatic renal cell cancer
    • Rowinsky EK, Schwartz GH, Gollob JA, et al,. Safety, pharmacokinetics, and activity of ABX-EGF, a fully human anti-epidermal growth factor receptor monoclonal antibody in patients with metastatic renal cell cancer. J Clin Oncol 2004; 22: 3003-3015.
    • (2004) J Clin Oncol , vol.22 , pp. 3003-3015
    • Rowinsky, E.K.1    Schwartz, G.H.2    Gollob, J.A.3
  • 45
    • 2342471392 scopus 로고    scopus 로고
    • Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib
    • Lynch TJ, Bell DW, Sordella R, et al,. Activating mutations in the epidermal growth factor receptor underlying responsiveness of non-small-cell lung cancer to gefitinib. N Engl J Med 2004; 350: 2129-2139.
    • (2004) N Engl J Med , vol.350 , pp. 2129-2139
    • Lynch, T.J.1    Bell, D.W.2    Sordella, R.3
  • 46
    • 71049185867 scopus 로고    scopus 로고
    • Extraction of phosphorylated proteins from formalin-fixed cancer cells and tissues
    • Becker KF, Mack H, Schott C, et al,. Extraction of phosphorylated proteins from formalin-fixed cancer cells and tissues. Open Pathol J 2008; 2: 46-52.
    • (2008) Open Pathol J , vol.2 , pp. 46-52
    • Becker, K.F.1    MacK, H.2    Schott, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.