메뉴 건너뛰기




Volumn 1, Issue 2 SUPPL, 2007, Pages

Current understanding of the molecular mechanisms of kidney cancer: A primer for urologists

Author keywords

[No Author keywords available]

Indexed keywords


EID: 70449406703     PISSN: 19116470     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review
Times cited : (11)

References (116)
  • 2
    • 0031255567 scopus 로고    scopus 로고
    • Heidelberg classification of renal cell tumours
    • Kovacs G, Akhtar M, Beckwith BJ, et al. Heidelberg classification of renal cell tumours. J Pathol 1997;183:131-3.
    • (1997) J Pathol , vol.183 , pp. 131-133
    • Kovacs, G.1    Akhtar, M.2    Beckwith, B.J.3
  • 3
    • 0000020119 scopus 로고
    • Intra-ocular growths (two cases, brother and sister, with peculiar vascular new growth, probably retinal, affecting both eyes)
    • Collins E. Intra-ocular growths (two cases, brother and sister, with peculiar vascular new growth, probably retinal, affecting both eyes). Trans Ophthalmol Soc U K 1894;14: 141-9.
    • (1894) Trans Ophthalmol Soc U K , vol.14 , pp. 141-149
    • Collins, E.1
  • 4
    • 0031445126 scopus 로고    scopus 로고
    • von Hippel-Lindau disease
    • Maher ER, Kaelin WG. von Hippel-Lindau disease. Medicine 1997;76:381-91.
    • (1997) Medicine , vol.76 , pp. 381-391
    • Maher, E.R.1    Kaelin, W.G.2
  • 5
    • 16644373473 scopus 로고    scopus 로고
    • Role of VHL gene mutation in human cancer
    • Kim WY, Kaelin WG. Role of VHL gene mutation in human cancer. J Clin Oncol 2004; 22:4991-5004.
    • (2004) J Clin Oncol , vol.22 , pp. 4991-5004
    • Kim, W.Y.1    Kaelin, W.G.2
  • 6
    • 0029090338 scopus 로고
    • Tumor suppression by the human von Hippel-Lindau gene product
    • Iliopoulos O, Kibel A, Gray S, et al. Tumor suppression by the human von Hippel-Lindau gene product. Nat Med 1995;1:822-6.
    • (1995) Nat Med , vol.1 , pp. 822-826
    • Iliopoulos, O.1    Kibel, A.2    Gray, S.3
  • 7
    • 0028805059 scopus 로고
    • Suppression of growth of renal carcinoma cells by the von Hippel-Lindau tumor suppressor gene
    • Chen F, Kishida T, Duh FM, et al. Suppression of growth of renal carcinoma cells by the von Hippel-Lindau tumor suppressor gene. Cancer Res 1995;55:4804-7.
    • (1995) Cancer Res , vol.55 , pp. 4804-4807
    • Chen, F.1    Kishida, T.2    Duh, F.M.3
  • 8
    • 0023865666 scopus 로고    scopus 로고
    • Von Hippel-Lindau disease maps to the region of chromosome 3 associated with renal cell carcinoma
    • Seizinger BR, Rouleau GA, Ozelius LJ, et al. Von Hippel-Lindau disease maps to the region of chromosome 3 associated with renal cell carcinoma. Nature1988;332:268-9.
    • Nature1988 , vol.332 , pp. 268-269
    • Seizinger, B.R.1    Rouleau, G.A.2    Ozelius, L.J.3
  • 9
    • 0027240519 scopus 로고
    • Identification of von Hippel-Lindau disease tumor sup-pressor gene
    • Latif F, Tory K, Gnarra J, et al. Identification of von Hippel-Lindau disease tumor sup-pressor gene. Science 1993;260:1317-20.
    • (1993) Science , vol.260 , pp. 1317-1320
    • Latif, F.1    Tory, K.2    Gnarra, J.3
  • 10
    • 0031869573 scopus 로고    scopus 로고
    • Subcellular localization of the von Hippel-Lindau dis-ease gene product is cell cycle-dependent
    • Ye Y, Vasavada S, Kuzmin I, et al. Subcellular localization of the von Hippel-Lindau dis-ease gene product is cell cycle-dependent. Int J Cancer 1998;78:62-9.
    • (1998) Int J Cancer , vol.78 , pp. 62-69
    • Ye, Y.1    Vasavada, S.2    Kuzmin, I.3
  • 11
    • 0029946004 scopus 로고    scopus 로고
    • Nuclear/cytoplasmic localization of the von Hippel-Lindau tumor suppressor gene product is determined by cell density
    • Lee S, Chen DY, Humphrey JS, et al. Nuclear/cytoplasmic localization of the von Hippel-Lindau tumor suppressor gene product is determined by cell density. Proc Natl Acad Sci U S A 1996;93:1770-5.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 1770-1775
    • Lee, S.1    Chen, D.Y.2    Humphrey, J.S.3
  • 12
    • 0344026345 scopus 로고    scopus 로고
    • Transcription-dependent nuclear-cytoplasmic trafficking is required for the function of the von Hippel-Lindau tumor suppressor pro-tein
    • Lee S, Neumann M, Stearman R, et al. Transcription-dependent nuclear-cytoplasmic trafficking is required for the function of the von Hippel-Lindau tumor suppressor pro-tein. Mol Cell Biol 1999;19:1486-97.
    • (1999) Mol Cell Biol , vol.19 , pp. 1486-1497
    • Lee, S.1    Neumann, M.2    Stearman, R.3
  • 13
    • 0029028652 scopus 로고
    • Characterization of the VHL tumor suppres-sor gene product: Localization, complex formation, and the effect of natural inactivat-ing mutations
    • Duan DR, Humphrey JS, Chen DY, et al. Characterization of the VHL tumor suppres-sor gene product: localization, complex formation, and the effect of natural inactivat-ing mutations. Proc Natl Acad Sci U S A 1995;92:6459-63.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 6459-6463
    • Duan, D.R.1    Humphrey, J.S.2    Chen, D.Y.3
  • 14
    • 0036314978 scopus 로고    scopus 로고
    • Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor sup-pressor protein
    • Groulx I, Lee S. Oxygen-dependent ubiquitination and degradation of hypoxia-inducible factor requires nuclear-cytoplasmic trafficking of the von Hippel-Lindau tumor sup-pressor protein. Mol Cell Biol 2002;22:5319-36.
    • (2002) Mol Cell Biol , vol.22 , pp. 5319-5336
    • Groulx, I.1    Lee, S.2
  • 15
    • 0029126892 scopus 로고
    • Inhibition of transcription elongation by the VHL tumor suppressor protein
    • Duan DR, Pause A, Burgess WH, et al. Inhibition of transcription elongation by the VHL tumor suppressor protein. Science 1995;269:1402-6.
    • (1995) Science , vol.269 , pp. 1402-1406
    • Duan, D.R.1    Pause, A.2    Burgess, W.H.3
  • 16
    • 0029147430 scopus 로고
    • Binding of the von Hippel-Lindau tumor sup-pressor protein to Elongin B and C
    • Kibel A, Iliopoulos O, DeCaprio JA, et al. Binding of the von Hippel-Lindau tumor sup-pressor protein to Elongin B and C. Science 1995;269:1444-6.
    • (1995) Science , vol.269 , pp. 1444-1446
    • Kibel, A.1    Iliopoulos, O.2    Decaprio, J.A.3
  • 17
    • 0030813061 scopus 로고    scopus 로고
    • Identification of Elongin C sequences required for interaction with the von Hippel-Lindau tumor suppressor protein
    • Takagi Y, Pause A, Conaway RC, et al. Identification of Elongin C sequences required for interaction with the von Hippel-Lindau tumor suppressor protein. J Biol Chem1997; 272:27444-9.
    • J Biol Chem1997 , vol.272 , pp. 27444-27449
    • Takagi, Y.1    Pause, A.2    Conaway, R.C.3
  • 18
    • 0030953635 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor-suppressor gene prod-uct forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins
    • Pause A, Lee S, Worrell RA, et al. The von Hippel-Lindau tumor-suppressor gene prod-uct forms a stable complex with human CUL-2, a member of the Cdc53 family of proteins. Proc Natl Acad Sci U S A 1997;94:2156-61.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 2156-2161
    • Pause, A.1    Lee, S.2    Worrell, R.A.3
  • 19
    • 0031907152 scopus 로고    scopus 로고
    • Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes con-taining elongins B/C and Cul2
    • Lonergan KM, Iliopoulos O, Ohh M, et al. Regulation of hypoxia-inducible mRNAs by the von Hippel-Lindau tumor suppressor protein requires binding to complexes con-taining elongins B/C and Cul2. Mol Cell Biol 1998;18:732-41.
    • (1998) Mol Cell Biol , vol.18 , pp. 732-741
    • Lonergan, K.M.1    Iliopoulos, O.2    Ohh, M.3
  • 20
    • 0033597443 scopus 로고    scopus 로고
    • Rbx1, a component of the VHL tumor sup-pressor complex and SCF ubiquitin ligase
    • Kamura T, Koepp DM, Conrad MN, et al. Rbx1, a component of the VHL tumor sup-pressor complex and SCF ubiquitin ligase. Science 1999;284:657-61.
    • (1999) Science , vol.284 , pp. 657-661
    • Kamura, T.1    Koepp, D.M.2    Conrad, M.N.3
  • 21
    • 0034641615 scopus 로고    scopus 로고
    • Activation of HIF1alpha ubiquitination by a reconsti-tuted von Hippel-Lindau (VHL) tumor suppressor complex
    • Kamura T, Sato S, Iwai K, et al. Activation of HIF1alpha ubiquitination by a reconsti-tuted von Hippel-Lindau (VHL) tumor suppressor complex. Proc Natl Acad Sci U S A 2000;97:10430-5.
    • (2000) Proc Natl Acad Sci U S A , vol.97 , pp. 10430-10435
    • Kamura, T.1    Sato, S.2    Iwai, K.3
  • 22
    • 0029051439 scopus 로고
    • Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2tension
    • Wang GL, Jiang B-H, Rue EA, et al. Hypoxia-inducible factor 1 is a basic-helix-loop-helix-PAS heterodimer regulated by cellular O2tension. Proc Natl Acad Sci U S A 1995;92:5510-4.
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 5510-5514
    • Wang, G.L.1    Jiang, B.-H.2    Rue, E.A.3
  • 23
    • 0033526781 scopus 로고    scopus 로고
    • Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor alpha (HIF-alpha) proteins
    • Srinivas V, Zhang LP, Zhu XH, et al. Characterization of an oxygen/redox-dependent degradation domain of hypoxia-inducible factor alpha (HIF-alpha) proteins. Biochem Biophys Res Commun 1999;260:557-61.
    • (1999) Biochem Biophys Res Commun , vol.260 , pp. 557-561
    • Srinivas, V.1    Zhang, L.P.2    Zhu, X.H.3
  • 24
    • 0035903468 scopus 로고    scopus 로고
    • Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation
    • Masson N, William C, Maxwell PH, et al. Independent function of two destruction domains in hypoxia-inducible factor-alpha chains activated by prolyl hydroxylation. EMBO J 2001;20:5197-206.
    • (2001) EMBO J , vol.20 , pp. 5197-5206
    • Masson, N.1    William, C.2    Maxwell, P.H.3
  • 25
    • 0036469038 scopus 로고    scopus 로고
    • Asparagine hydroxylation of the HIF transactiva-tion domain: A hypoxic switch
    • Lando D, Peet DJ, Whelan DA, et al. Asparagine hydroxylation of the HIF transactiva-tion domain: a hypoxic switch. Science 2002;295:858-61.
    • (2002) Science , vol.295 , pp. 858-861
    • Lando, D.1    Peet, D.J.2    Whelan, D.A.3
  • 26
    • 0026075610 scopus 로고
    • Hypoxia-inducible nuclear factors bind to an enhancer element located 3' to the human erythropoietin gene
    • Semenza GL, Nejfelt MK, Chi SM, et al. Hypoxia-inducible nuclear factors bind to an enhancer element located 3' to the human erythropoietin gene. Proc Natl Acad Sci U S A 1991;88:5680-4.
    • (1991) Proc Natl Acad Sci U S A , vol.88 , pp. 5680-5684
    • Semenza, G.L.1    Nejfelt, M.K.2    Chi, S.M.3
  • 27
    • 0035937715 scopus 로고    scopus 로고
    • Regulation of glut 1 mRNA by hypoxia-inducible factor-1.Interaction between H-ras and hypoxia
    • Chen C, Pore N, Behrooz A, et al. Regulation of glut 1 mRNA by hypoxia-inducible factor-1.Interaction between H-ras and hypoxia. J Biol Chem 2001;276:9519-25.
    • (2001) J Biol Chem , vol.276 , pp. 9519-9525
    • Chen, C.1    Pore, N.2    Behrooz, A.3
  • 28
    • 0032514685 scopus 로고    scopus 로고
    • Down-regulation of transmembrane carbonic anhy-drase in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgene
    • Ivanov SV, Kuzmin I, Wei MH, et al. Down-regulation of transmembrane carbonic anhy-drase in renal cell carcinoma cell lines by wild-type von Hippel-Lindau transgene. Proc Natl Acad Sci U S A 1998;95:12596-601.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 12596-12601
    • Ivanov, S.V.1    Kuzmin, I.2    Wei, M.H.3
  • 29
    • 0041062296 scopus 로고    scopus 로고
    • Human carbonic anhydrase XII: CDNA cloning expres-sion and chromosomal localization of a carbonic anhydrase gene that is overex-pressed in some renal cell cancers
    • Tureci O, Sahin U, Vollmar E, et al. Human carbonic anhydrase XII: cDNA cloning expres-sion and chromosomal localization of a carbonic anhydrase gene that is overex-pressed in some renal cell cancers. Proc Natl Acad Sci U S A 1998;95:7608-13.
    • (1998) Proc Natl Acad Sci U S A , vol.95 , pp. 7608-7613
    • Tureci, O.1    Sahin, U.2    Vollmar, E.3
  • 30
    • 0030834249 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor sup-pressor gene product interacts with Sp1 to repress vascular endothelial growth factor promoter activity
    • Mukhopadhyay D, Knebelmann B, Cohen HT, et al. The von Hippel-Lindau tumor sup-pressor gene product interacts with Sp1 to repress vascular endothelial growth factor promoter activity. Mol Cell Biol 1997;17:5629-39.
    • (1997) Mol Cell Biol , vol.17 , pp. 5629-5639
    • Mukhopadhyay, D.1    Knebelmann, B.2    Cohen, H.T.3
  • 31
    • 0029785838 scopus 로고    scopus 로고
    • Post-transcriptional regulation of vascular endothe-lial growth factor mRNA by the product of the VHL tumor suppressor gene
    • Gnarra JR, Zhou S, Merrill MJ, et al. Post-transcriptional regulation of vascular endothe-lial growth factor mRNA by the product of the VHL tumor suppressor gene. Proc Natl Acad Sci U S A 1996;93:10589-94.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 10589-10594
    • Gnarra, J.R.1    Zhou, S.2    Merrill, M.J.3
  • 32
    • 0031964099 scopus 로고    scopus 로고
    • Transforming growth factor α is a target for the von Hippel-Lindau tumor suppressor
    • Knebelmann B, Ananth S, Cohen HT, et al. Transforming growth factor α is a target for the von Hippel-Lindau tumor suppressor. Cancer Res 1998;58:226-31.
    • (1998) Cancer Res , vol.58 , pp. 226-231
    • Knebelmann, B.1    Ananth, S.2    Cohen, H.T.3
  • 33
    • 0038383678 scopus 로고    scopus 로고
    • Loss of pVHL is sufficient to cause HIF dys-regulation in primary cells but does not promote tumor growth
    • Mack FA, Rathmell WK, Arsham AM, et al. Loss of pVHL is sufficient to cause HIF dys-regulation in primary cells but does not promote tumor growth. Cancer Cell2003;3:75-88.
    • Cancer Cell2003 , vol.3 , pp. 75-88
    • Mack, F.A.1    Rathmell, W.K.2    Arsham, A.M.3
  • 34
    • 0036527785 scopus 로고    scopus 로고
    • The contribution of VHL substrate binding and HIF-1 alpha to the phenotype of VHL loss in renal cell carcinoma
    • Maranchie JK, Vasselli JR, Riss J, et al. The contribution of VHL substrate binding and HIF-1 alpha to the phenotype of VHL loss in renal cell carcinoma. Cancer Cell2002;1: 247-55.
    • Cancer Cell2002 , vol.1 , pp. 247-255
    • Maranchie, J.K.1    Vasselli, J.R.2    Riss, J.3
  • 35
    • 0037395395 scopus 로고    scopus 로고
    • Gene expression profiling in a renal cell carcinoma cell line: Dissecting VHL and hypoxia-dependent pathways
    • Jiang Y, Zhang W, Kondo K, et al. Gene expression profiling in a renal cell carcinoma cell line: dissecting VHL and hypoxia-dependent pathways. Mol Cancer Res 2003;1: 453-62.
    • (2003) Mol Cancer Res , vol.1 , pp. 453-462
    • Jiang, Y.1    Zhang, W.2    Kondo, K.3
  • 36
    • 0034649507 scopus 로고    scopus 로고
    • Identification of novel hypoxia dependent and independent target genes of the von Hippel-Lindau (VHL) tumour suppressor by mRNA differential expression profiling
    • Wykoff CC, Pugh CW, Maxwell PH, et al. Identification of novel hypoxia dependent and independent target genes of the von Hippel-Lindau (VHL) tumour suppressor by mRNA differential expression profiling. Oncogene 2000;19:6297-305.
    • (2000) Oncogene , vol.19 , pp. 6297-6305
    • Wykoff, C.C.1    Pugh, C.W.2    Maxwell, P.H.3
  • 37
    • 32944457801 scopus 로고    scopus 로고
    • von Hippel-Lindau tumor suppres-sor protein regulates the assembly of intercellular junctions in renal cancer cells through hypoxia-inducible factor-independent mechanisms
    • Calzada MJ, Esteban MA, Feijoo-Cuaresma M, et al. von Hippel-Lindau tumor suppres-sor protein regulates the assembly of intercellular junctions in renal cancer cells through hypoxia-inducible factor-independent mechanisms. Cancer Res 2006;66:1553-60.
    • (2006) Cancer Res , vol.66 , pp. 1553-1560
    • Calzada, M.J.1    Esteban, M.A.2    Feijoo-Cuaresma, M.3
  • 38
    • 0032085240 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor pro-tein is required for proper assembly of an extracellular fibronectin matrix
    • Ohh M, Yauch R, Lonergan M, et al. The von Hippel-Lindau tumor suppressor pro-tein is required for proper assembly of an extracellular fibronectin matrix. Mol Cell1998; 1:959-68.
    • Mol Cell1998 , vol.1 , pp. 959-968
    • Ohh, M.1    Yauch, R.2    Lonergan, M.3
  • 39
    • 0037093099 scopus 로고    scopus 로고
    • Role of the von Hippel-Lindau tumor suppressor gene in the formation of beta1-integrin fibrillar adhesions
    • Esteban-Barragan MA, Avila P, Alvarez-Tejado M, et al. Role of the von Hippel-Lindau tumor suppressor gene in the formation of beta1-integrin fibrillar adhesions. Cancer Res 2002;62:2929-36.
    • (2002) Cancer Res , vol.62 , pp. 2929-2936
    • Esteban-Barragan, M.A.1    Avila, P.2    Alvarez-Tejado, M.3
  • 40
    • 0032795938 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor gene inhibits hepatocyte growth factor/scatter factor-induced invasion and branching morphogenesis in renal carcinoma cells
    • Koochekpour S, Jeffers M, Wang PH, et al. The von Hippel-Lindau tumor suppressor gene inhibits hepatocyte growth factor/scatter factor-induced invasion and branching morphogenesis in renal carcinoma cells. Mol Cell Biol 1999;19:5902-12.
    • (1999) Mol Cell Biol , vol.19 , pp. 5902-5912
    • Koochekpour, S.1    Jeffers, M.2    Wang, P.H.3
  • 41
    • 0037131189 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1
    • Zhou MI, Wang H, Ross JJ, et al. The von Hippel-Lindau tumor suppressor stabilizes novel plant homeodomain protein Jade-1. J Biol Chem 2002;277:39887-98.
    • (2002) J Biol Chem , vol.277 , pp. 39887-39898
    • Zhou, M.I.1    Wang, H.2    Ross, J.J.3
  • 42
    • 0345708112 scopus 로고    scopus 로고
    • Tumorigenic mutations in VHL disrupt fold-ing in vivo by interfering with chaperonin binding
    • Feldman DE, Spiess C, Howard DE, et al. Tumorigenic mutations in VHL disrupt fold-ing in vivo by interfering with chaperonin binding. Mol Cell 2003;12:1213-24.
    • (2003) Mol Cell , vol.12 , pp. 1213-1224
    • Feldman, D.E.1    Spiess, C.2    Howard, D.E.3
  • 43
    • 0037446951 scopus 로고    scopus 로고
    • The VHL protein recruits a novel KRAB-A domain protein to repress HIF-1alpha transcriptional activity
    • Li Z, Wang D, Na X, et al. The VHL protein recruits a novel KRAB-A domain protein to repress HIF-1alpha transcriptional activity. EMBO J 2003;22:1857-67.
    • (2003) EMBO J , vol.22 , pp. 1857-1867
    • Li, Z.1    Wang, D.2    Na, X.3
  • 44
    • 0035941291 scopus 로고    scopus 로고
    • The von Hippel-Lindau tumor suppressor protein medi-ates ubiquitination of activated atypical protein kinase C
    • Okuda H, Saitoh K, Hirai S, et al. The von Hippel-Lindau tumor suppressor protein medi-ates ubiquitination of activated atypical protein kinase C. J Biol Chem 2001;276: 43611-7.
    • (2001) J Biol Chem , vol.276 , pp. 43611-43617
    • Okuda, H.1    Saitoh, K.2    Hirai, S.3
  • 45
    • 0033600881 scopus 로고    scopus 로고
    • Direct interaction of the beta-domain of VHL tumor suppressor protein with the regulatory domain of atypical PKC isotypes
    • Okuda H, Hirai S, Takaki Y, et al. Direct interaction of the beta-domain of VHL tumor suppressor protein with the regulatory domain of atypical PKC isotypes. Biochem Biophys Res Commun 1999;263:491-7.
    • (1999) Biochem Biophys Res Commun , vol.263 , pp. 491-497
    • Okuda, H.1    Hirai, S.2    Takaki, Y.3
  • 46
    • 0036290499 scopus 로고    scopus 로고
    • Identification of a deubiquitinating enzyme subfamily as sub-strates of the von Hippel-Lindau tumor suppressor
    • Li Z, Wang D, Na X, et al. Identification of a deubiquitinating enzyme subfamily as sub-strates of the von Hippel-Lindau tumor suppressor. Biochem Biophys Res Commun2002; 294:700-9.
    • Biochem Biophys Res Commun2002 , vol.294 , pp. 700-709
    • Li, Z.1    Wang, D.2    Na, X.3
  • 47
    • 0037085456 scopus 로고    scopus 로고
    • Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein
    • Li Z, Na X, Wang D, et al. Ubiquitination of a novel deubiquitinating enzyme requires direct binding to von Hippel-Lindau tumor suppressor protein. J Biol Chem 2002; 277:4656-62.
    • (2002) J Biol Chem , vol.277 , pp. 4656-4662
    • Li, Z.1    Na, X.2    Wang, D.3
  • 48
    • 0042466570 scopus 로고    scopus 로고
    • Identification of the RNA polymerase II subunit hsRPB7 as a novel target of the von Hippel-Lindau protein
    • Na X, Duan HO, Messing E, et al. Identification of the RNA polymerase II subunit hsRPB7 as a novel target of the von Hippel-Lindau protein. EMBO J 2003;22:4249-59.
    • (2003) EMBO J , vol.22 , pp. 4249-4259
    • Na, X.1    Duan, H.O.2    Messing, E.3
  • 49
    • 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
  • 50
    • 0036606006 scopus 로고    scopus 로고
    • VHL mediated hypoxia regulation of cyclin D1 in renal cancer cells
    • Bindra RS, Vasselli JR, Stearman R, et al. VHL mediated hypoxia regulation of cyclin D1 in renal cancer cells. Cancer Res 2002;62:3014-9.
    • (2002) Cancer Res , vol.62 , pp. 3014-3019
    • Bindra, R.S.1    Vasselli, J.R.2    Stearman, R.3
  • 52
    • 16144365122 scopus 로고    scopus 로고
    • Germline mutations in the von Hippel-Lindau disease (VHL) gene in families from North America, Europe, and Japan
    • Zbar B, Kishida T, Chen F, et al. Germline mutations in the von Hippel-Lindau disease (VHL) gene in families from North America, Europe, and Japan. Hum Mutat 1996;8: 348-57.
    • (1996) Hum Mutat , vol.8 , pp. 348-357
    • Zbar, B.1    Kishida, T.2    Chen, F.3
  • 53
    • 0028981766 scopus 로고
    • Germline mutations in the von Hippel-Lindau disease tumor suppressor gene: Correlations with phenotype
    • Chen F, Kishida T, Yao M, et al. Germline mutations in the von Hippel-Lindau disease tumor suppressor gene: correlations with phenotype. Hum Mutat 1995;5:66-75.
    • (1995) Hum Mutat , vol.5 , pp. 66-75
    • Chen, F.1    Kishida, T.2    Yao, M.3
  • 54
    • 0035336706 scopus 로고    scopus 로고
    • von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF
    • Hoffman MA, Ohh M, Yang H, et al. von Hippel-Lindau protein mutants linked to type 2C VHL disease preserve the ability to downregulate HIF. Hum Mol Genet2001; 10:1019-27.
    • Hum Mol Genet2001 , vol.10 , pp. 1019-1027
    • Hoffman, M.A.1    Ohh, M.2    Yang, H.3
  • 55
    • 0035339044 scopus 로고    scopus 로고
    • Contrasting effects on HIF1a regula-tion by disease-causing pVHL mutations correlate with patterns of tumorigenesis in von Hippel-Lindau disease
    • Clifford SC, Cockman ME, Smallwood A, et al. Contrasting effects on HIF1a regula-tion by disease-causing pVHL mutations correlate with patterns of tumorigenesis in von Hippel-Lindau disease. Hum Mol Genet 2001;10:1029-38.
    • (2001) Hum Mol Genet , vol.10 , pp. 1029-1038
    • Clifford, S.C.1    Cockman, M.E.2    Smallwood, A.3
  • 56
    • 0028157342 scopus 로고    scopus 로고
    • Hereditary papillary renal carcinoma
    • Zbar B, Tory K, Merino M, et al. Hereditary papillary renal carcinoma. J Urol1994;151: 561-6.
    • J Urol1994 , vol.151 , pp. 561-566
    • Zbar, B.1    Tory, K.2    Merino, M.3
  • 57
    • 0028897350 scopus 로고
    • Hereditary papillary renal carcinoma clinical studies in 10 families
    • Zbar B, Glenn G, Lubensky I, et al. Hereditary papillary renal carcinoma clinical studies in 10 families. J Urol 1995;153:907-12.
    • (1995) J Urol , vol.153 , pp. 907-912
    • Zbar, B.1    Glenn, G.2    Lubensky, I.3
  • 58
    • 17344381429 scopus 로고    scopus 로고
    • Germline and somatic mutations in the tyrosine kinase domain of the Met proto-oncogene in papillary renal carcinomas
    • Schmidt L, Duh FM, Chen F, et al. Germline and somatic mutations in the tyrosine kinase domain of the Met proto-oncogene in papillary renal carcinomas. Nat Genet 1997;16:68-73.
    • (1997) Nat Genet , vol.16 , pp. 68-73
    • Schmidt, L.1    Duh, F.M.2    Chen, F.3
  • 59
    • 0029564113 scopus 로고
    • Hepatocyte growth factor/scatter factor induces a variety of tissue-specific morphogenic programs in epithelial cells
    • Brinkmann V, Foroutan H, Sachs M, et al. Hepatocyte growth factor/scatter factor induces a variety of tissue-specific morphogenic programs in epithelial cells. J Cell Biol 1995;131:1573-86.
    • (1995) J Cell Biol , vol.131 , pp. 1573-1586
    • Brinkmann, V.1    Foroutan, H.2    Sachs, M.3
  • 60
    • 10544235690 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor-Met sig-naling induces proliferation, migration, and morphogenesis of pancreatic oval cells
    • Jeffers M, Rao MS, Rulong S, et al. Hepatocyte growth factor/scatter factor-Met sig-naling induces proliferation, migration, and morphogenesis of pancreatic oval cells. Cell Growth Differ 1996;7:1805-13.
    • (1996) Cell Growth Differ , vol.7 , pp. 1805-1813
    • Jeffers, M.1    Rao, M.S.2    Rulong, S.3
  • 61
    • 0029880298 scopus 로고    scopus 로고
    • The tyrosine kinase receptors Ron and Sea control "scattering" and morphogenesis of liver progenitor cells in vitro
    • Medico E, Mongiovi AM, Huff J, et al. The tyrosine kinase receptors Ron and Sea control "scattering" and morphogenesis of liver progenitor cells in vitro. Mol Biol Cell 1996;7:495-504.
    • (1996) Mol Biol Cell , vol.7 , pp. 495-504
    • Medico, E.1    Mongiovi, A.M.2    Huff, J.3
  • 62
    • 0025825990 scopus 로고
    • Induction of epithelial tubular morphogenesis in vitro by fibroblast-derived soluble factors
    • Montesano R, Schaller G, Orci L. Induction of epithelial tubular morphogenesis in vitro by fibroblast-derived soluble factors. Cell 1991;66:697-711.
    • (1991) Cell , vol.66 , pp. 697-711
    • Montesano, R.1    Schaller, G.2    Orci, L.3
  • 63
    • 0029997180 scopus 로고    scopus 로고
    • Constitutive activation of the RON gene promotes invasive growth but not transformation
    • Santoro MM, Collesi C, Grisendi S, et al. Constitutive activation of the RON gene promotes invasive growth but not transformation. Mol Cell Biol 1996;16:7072-83.
    • (1996) Mol Cell Biol , vol.16 , pp. 7072-7083
    • Santoro, M.M.1    Collesi, C.2    Grisendi, S.3
  • 64
    • 0022269174 scopus 로고
    • An epithelial scatter factor released by embryo fibroblasts
    • Stoker M, Perryman M. An epithelial scatter factor released by embryo fibroblasts. J Cell Sci 1985;77:209-23.
    • (1985) J Cell Sci , vol.77 , pp. 209-223
    • Stoker, M.1    Perryman, M.2
  • 65
    • 0025805633 scopus 로고
    • Identification of the hepatocyte growth factor receptor as the c-met proto-oncogene product
    • Bottaro DP, Rubin JS, Faletto DL, et al. Identification of the hepatocyte growth factor receptor as the c-met proto-oncogene product. Science 1991;251:802-4.
    • (1991) Science , vol.251 , pp. 802-804
    • Bottaro, D.P.1    Rubin, J.S.2    Faletto, D.L.3
  • 66
    • 0026607926 scopus 로고
    • Evidence for non-covalent clusters of the c-met proto-oncogene product
    • Faletto DL, Tsarfaty I, Kmiecik TE, et al. Evidence for non-covalent clusters of the c-met proto-oncogene product. Oncogene 1992;7:1149-57.
    • (1992) Oncogene , vol.7 , pp. 1149-1157
    • Faletto, D.L.1    Tsarfaty, I.2    Kmiecik, T.E.3
  • 67
    • 0025959661 scopus 로고
    • The tyrosine kinase encoded by the MET protooncogene is activated by autophosphorylation
    • Naldini L, Vigna E, Ferracini R, et al. The tyrosine kinase encoded by the MET protooncogene is activated by autophosphorylation. Mol Cell Biol 1991;11:1793-803.
    • (1991) Mol Cell Biol , vol.11 , pp. 1793-1803
    • Naldini, L.1    Vigna, E.2    Ferracini, R.3
  • 68
    • 0028301299 scopus 로고
    • Autophosphorylation modulates the kinase activity and onco-genic potential of the Met receptor tyrosine kinase
    • Rodrigues GA, Park M. Autophosphorylation modulates the kinase activity and onco-genic potential of the Met receptor tyrosine kinase. Oncogene 1994;9:2019-27.
    • (1994) Oncogene , vol.9 , pp. 2019-2027
    • Rodrigues, G.A.1    Park, M.2
  • 69
    • 0028351702 scopus 로고
    • A multifunctional docking site mediates signal-ing and transformation by the hepatocyte growth factor/scatter factor receptor family
    • Ponzetto C, Bardelli A, Zhen Z, et al. A multifunctional docking site mediates signal-ing and transformation by the hepatocyte growth factor/scatter factor receptor family. Cell 1994;77:261-71.
    • (1994) Cell , vol.77 , pp. 261-271
    • Ponzetto, C.1    Bardelli, A.2    Zhen, Z.3
  • 70
    • 0027264590 scopus 로고
    • The cell dissociation and motility triggered by scatter factor/hepa-tocyte growth factor are mediated through the cytoplasmic domain of the c-Met receptor
    • Komada M, Kitamura N. The cell dissociation and motility triggered by scatter factor/hepa-tocyte growth factor are mediated through the cytoplasmic domain of the c-Met receptor. Oncogene 1993;8:2381-90.
    • (1993) Oncogene , vol.8 , pp. 2381-2390
    • Komada, M.1    Kitamura, N.2
  • 71
    • 0027410889 scopus 로고
    • The met receptor tyrosine kinase transduces motility, proliferation and morphogenic signals of scatter factor/hepatocyte growth factor in epithelial cells
    • Weidner KM, Sachs M, Birchmeier W. The met receptor tyrosine kinase transduces motility, proliferation and morphogenic signals of scatter factor/hepatocyte growth factor in epithelial cells. J Cell Biol 1993;121:145-54.
    • (1993) J Cell Biol , vol.121 , pp. 145-154
    • Weidner, K.M.1    Sachs, M.2    Birchmeier, W.3
  • 72
    • 0028026665 scopus 로고
    • Receptor chimeras indicate that the met tyrosine kinase mediates the motility and morphogenic responses of hepatocyte growth/scatter factor
    • Zhu H, Naujokas MA, Park M. Receptor chimeras indicate that the met tyrosine kinase mediates the motility and morphogenic responses of hepatocyte growth/scatter factor. Cell Growth Differ 1994;5:359-66.
    • (1994) Cell Growth Differ , vol.5 , pp. 359-366
    • Zhu, H.1    Naujokas, M.A.2    Park, M.3
  • 73
    • 0029816082 scopus 로고    scopus 로고
    • Hepatocyte growth factor/scatter factor-Met signaling in tumorigenicity and invasion/metastasis
    • Jeffers M, Rong S, Vande Woude GF. Hepatocyte growth factor/scatter factor-Met signaling in tumorigenicity and invasion/metastasis. J Mol Med 1996;74:505-13.
    • (1996) J Mol Med , vol.74 , pp. 505-513
    • Jeffers, M.1    Rong, S.2    vande Woude, G.F.3
  • 74
    • 0026022284 scopus 로고    scopus 로고
    • Hepatocyte growth factor is a potent mitogen for cultured rabbit renal tubular epithelial cells
    • Igawa T, Kanda S, Kanetake H. Hepatocyte growth factor is a potent mitogen for cultured rabbit renal tubular epithelial cells. Biochem Biophys Res Commun1991;174: 831-8.
    • Biochem Biophys Res Commun1991 , vol.174 , pp. 831-838
    • Igawa, T.1    Kanda, S.2    Kanetake, H.3
  • 75
    • 0026010993 scopus 로고    scopus 로고
    • Hepatocyte growth factor/hepatopoietin A stim-ulates the growth of rat kidney proximal tubule epithelial cells (RPTE), rat nonparenchy-mal liver cells, human melanoma cells, mouse keratinocytes and stimulates anchorage-independent growth of SV-40 transformed RPTE
    • Kan M, Zhang G, Zarnegar R, et al. Hepatocyte growth factor/hepatopoietin A stim-ulates the growth of rat kidney proximal tubule epithelial cells (RPTE), rat nonparenchy-mal liver cells, human melanoma cells, mouse keratinocytes and stimulates anchorage-independent growth of SV-40 transformed RPTE. Biochem Biophys Res Commun1991; 174:331-7.
    • Biochem Biophys Res Commun1991 , vol.174 , pp. 331-337
    • Kan, M.1    Zhang, G.2    Zarnegar, R.3
  • 76
    • 0025824738 scopus 로고
    • Identification of a fibroblast-derived epithelial morphogen as hepatocyte growth factor
    • Montesano R, Matsumoto K, Nakamura T, et al. Identification of a fibroblast-derived epithelial morphogen as hepatocyte growth factor. Cell 1991;67:901-8.
    • (1991) Cell , vol.67 , pp. 901-908
    • Montesano, R.1    Matsumoto, K.2    Nakamura, T.3
  • 77
    • 17344373892 scopus 로고    scopus 로고
    • Trisomy 7-harbouring non-random duplication of the mutant met allele in hereditary papillary renal carcinomas
    • Zhuang Z, Park W, Pack S, et al. Trisomy 7-harbouring non-random duplication of the mutant met allele in hereditary papillary renal carcinomas. Nat Genet1998;20:66-9.
    • Nat Genet1998 , vol.20 , pp. 66-69
    • Zhuang, Z.1    Park, W.2    Pack, S.3
  • 78
    • 0032569883 scopus 로고    scopus 로고
    • Signaling requirements for oncogenic forms of the Met tyrosine kinase receptor
    • Jeffers M, Koochekpour S, Fiscella M, et al. Signaling requirements for oncogenic forms of the Met tyrosine kinase receptor. Oncogene 1998;17:2691-700.
    • (1998) Oncogene , vol.17 , pp. 2691-2700
    • Jeffers, M.1    Koochekpour, S.2    Fiscella, M.3
  • 79
    • 0030799090 scopus 로고    scopus 로고
    • Activating mutations for the Met tyrosine receptor in human cancer
    • Jeffers M, Schmidt L, Nakaigawa N, et al. Activating mutations for the Met tyrosine receptor in human cancer. Proc Natl Acad Sci U S A 1997;94:11445-50.
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 11445-11450
    • Jeffers, M.1    Schmidt, L.2    Nakaigawa, N.3
  • 80
    • 0036711644 scopus 로고    scopus 로고
    • The semaphorin 4D receptor controls invasive growth by coupling with Met
    • Giordano S, Corso S, Conrotto P, et al. The semaphorin 4D receptor controls invasive growth by coupling with Met. Nat Cell Biol 2002;4:720-4.
    • (2002) Nat Cell Biol , vol.4 , pp. 720-724
    • Giordano, S.1    Corso, S.2    Conrotto, P.3
  • 81
    • 0037478437 scopus 로고    scopus 로고
    • Hypoxia promotes invasive growth by transcriptional activation of met protooncogene
    • Pennacchietti S, Michieli P, Galluzzo M, et al. Hypoxia promotes invasive growth by transcriptional activation of met protooncogene. Cancer Cell 2003;3:347-61.
    • (2003) Cancer Cell , vol.3 , pp. 347-361
    • Pennacchietti, S.1    Michieli, P.2    Galluzzo, M.3
  • 82
    • 0035853166 scopus 로고    scopus 로고
    • Inherited susceptibility to uterine leiomy-omas and renal cell cancer
    • Launonen V, Vierimaa O, Kiuru M, et al. Inherited susceptibility to uterine leiomy-omas and renal cell cancer. Proc Natl Acad Sci U S A 2001;98:3387-92.
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 3387-3392
    • Launonen, V.1    Vierimaa, O.2    Kiuru, M.3
  • 83
    • 18544365990 scopus 로고    scopus 로고
    • Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell can-cer
    • Tomlinson IP, Alam NA, Rowan AJ, et al. Germline mutations in FH predispose to dominantly inherited uterine fibroids, skin leiomyomata and papillary renal cell can-cer. Nat Genet 2002;30:406-10.
    • (2002) Nat Genet , vol.30 , pp. 406-410
    • Tomlinson, I.P.1    Alam, N.A.2    Rowan, A.J.3
  • 84
    • 12444259659 scopus 로고    scopus 로고
    • Genetic and functional analyses of FH mutations in multiple cutaneous and uterine leiomyomatosis, hereditary leiomyomatosis and renal cancer, and fumarate hydratase deficiency
    • Alam NA, Rowan AJ, Wortham NC, et al. Genetic and functional analyses of FH mutations in multiple cutaneous and uterine leiomyomatosis, hereditary leiomyomatosis and renal cancer, and fumarate hydratase deficiency. Hum Mol Genet2003;12:1241-52.
    • Hum Mol Genet2003 , vol.12 , pp. 1241-1252
    • Alam, N.A.1    Rowan, A.J.2    Wortham, N.C.3
  • 85
    • 0037713729 scopus 로고    scopus 로고
    • Mutations in the fumarate hydratase gene cause hereditary leiomyomatosis and renal cell cancer in families in North America
    • Toro JR, Nickerson ML, Wei MH, et al. Mutations in the fumarate hydratase gene cause hereditary leiomyomatosis and renal cell cancer in families in North America. Am J Hum Genet 2003;73:95-106.
    • (2003) Am J Hum Genet , vol.73 , pp. 95-106
    • Toro, J.R.1    Nickerson, M.L.2    Wei, M.H.3
  • 86
    • 30744457565 scopus 로고    scopus 로고
    • Novel mutation in FH and expansion of the spec-trum of phenotypes expressed in families with hereditary leiomyomatosis and renal cell cancer
    • Wei MH, Toure O, Glenn GM, et al. Novel mutation in FH and expansion of the spec-trum of phenotypes expressed in families with hereditary leiomyomatosis and renal cell cancer. J Med Genet 2006;43:18-27.
    • (2006) J Med Genet , vol.43 , pp. 18-27
    • Wei, M.H.1    Toure, O.2    Glenn, G.M.3
  • 87
    • 22944469759 scopus 로고    scopus 로고
    • Fumarate hydratase mutations and predisposition to cutaneous leiomyomas, uterine leiomyomas and renal cancer
    • Alam NA, Olpin S, Leigh IM. Fumarate hydratase mutations and predisposition to cutaneous leiomyomas, uterine leiomyomas and renal cancer. Br J Dermatol 2005; 153:11-7.
    • (2005) Br J Dermatol , vol.153 , pp. 11-17
    • Alam, N.A.1    Olpin, S.2    Leigh, I.M.3
  • 88
    • 0034849758 scopus 로고    scopus 로고
    • Familial cutaneous leiomyomatosis is a two hit condition associated with renal cell cancer of characteristic histopathology
    • Kiuru M, Launonen V, Hietala M, et al. Familial cutaneous leiomyomatosis is a two hit condition associated with renal cell cancer of characteristic histopathology. Am J Pathol 2001;159:825-9.
    • (2001) Am J Pathol , vol.159 , pp. 825-829
    • Kiuru, M.1    Launonen, V.2    Hietala, M.3
  • 89
    • 0017760671 scopus 로고
    • Hereditary multiple fibrofolliculomas with trichodiscomas and acrochordons
    • Birt AR, Hogg GR, Dubé J. Hereditary multiple fibrofolliculomas with trichodiscomas and acrochordons. Arch Dermatol 1977;113:1674-7.
    • (1977) Arch Dermatol , vol.113 , pp. 1674-1677
    • Birt, A.R.1    Hogg, G.R.2    Dubé, J.3
  • 90
    • 0000939691 scopus 로고    scopus 로고
    • Mutations in a novel gene lead to kidney tumors, lung wall defects, and benign tumors of the hair follicle in patients with the Birt-Hogg-Dubé syndrome
    • Nickerson ML, Warren MB, Toro J, et al. Mutations in a novel gene lead to kidney tumors, lung wall defects, and benign tumors of the hair follicle in patients with the Birt-Hogg-Dubé syndrome. Cancer Cell 2002;2:157-64.
    • (2002) Cancer Cell , vol.2 , pp. 157-164
    • Nickerson, M.L.1    Warren, M.B.2    Toro, J.3
  • 91
    • 0034821623 scopus 로고    scopus 로고
    • Birt-Hogg-Dubé syndrome, a genoder-matosis associated with spontaneous pneumothorax and kidney neoplasia, maps to chromosome 17p11.2
    • Schmidt LS, Warren MB, Nickerson ML, et al. Birt-Hogg-Dubé syndrome, a genoder-matosis associated with spontaneous pneumothorax and kidney neoplasia, maps to chromosome 17p11.2. Am J Hum Genet 2001;69:876-82.
    • (2001) Am J Hum Genet , vol.69 , pp. 876-882
    • Schmidt, L.S.1    Warren, M.B.2    Nickerson, M.L.3
  • 92
    • 0035939821 scopus 로고    scopus 로고
    • Birt-Hogg-Dubé syndrome: Mapping of a novel hereditary neoplasia gene to chromosome 17p12-q11.2
    • Khoo SK, Bradley M, Wong FK, et al. Birt-Hogg-Dubé syndrome: mapping of a novel hereditary neoplasia gene to chromosome 17p12-q11.2. Oncogene2001;20:5239-42.
    • Oncogene2001 , vol.20 , pp. 5239-5242
    • Khoo, S.K.1    Bradley, M.2    Wong, F.K.3
  • 93
    • 33750293584 scopus 로고    scopus 로고
    • Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signal-ing
    • Baba M, Hong SB, Sharma N, et al. Folliculin encoded by the BHD gene interacts with a binding protein, FNIP1, and AMPK, and is involved in AMPK and mTOR signal-ing. Proc Natl Acad Sci U S A 2006;103:15552-7.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 15552-15557
    • Baba, M.1    Hong, S.B.2    Sharma, N.3
  • 94
    • 0242608613 scopus 로고    scopus 로고
    • The genetic basis of cancer of the kidney
    • Linehan WM, Walther MM, Zbar B, et al. The genetic basis of cancer of the kidney. J Urol 2003;170:2163-72.
    • (2003) J Urol , vol.170 , pp. 2163-2172
    • Linehan, W.M.1    Walther, M.M.2    Zbar, B.3
  • 95
    • 0027380152 scopus 로고
    • Bilateral renal cell carcinoma in the Birt-Hogg-Dubé syndrome
    • Roth JS, Rabinowitz AD, Benson M, et al. Bilateral renal cell carcinoma in the Birt-Hogg-Dubé syndrome. J Am Acad Dermatol 1993;29:1055-6.
    • (1993) J Am Acad Dermatol , vol.29 , pp. 1055-1056
    • Roth, J.S.1    Rabinowitz, A.D.2    Benson, M.3
  • 97
    • 21044457377 scopus 로고    scopus 로고
    • Germline BHD-mutation spectrum and phenotype analysis of a large cohort of families with Birt-Hogg-Dubé syndrome
    • Schmidt LS, Nickerson ML, Warren MB, et al. Germline BHD-mutation spectrum and phenotype analysis of a large cohort of families with Birt-Hogg-Dubé syndrome. Am J Hum Genet 2005;76:1023-33.
    • (2005) Am J Hum Genet , vol.76 , pp. 1023-1033
    • Schmidt, L.S.1    Nickerson, M.L.2    Warren, M.B.3
  • 98
    • 21444432561 scopus 로고    scopus 로고
    • High frequency of somatic frameshift BHD gene mutations in Birt-Hogg-Dubé-associated renal tumors
    • Vocke CD, Yang Y, Pavlovich CP, et al. High frequency of somatic frameshift BHD gene mutations in Birt-Hogg-Dubé-associated renal tumors. J Natl Cancer Inst 2005; 97:931-5.
    • (2005) J Natl Cancer Inst , vol.97 , pp. 931-935
    • Vocke, C.D.1    Yang, Y.2    Pavlovich, C.P.3
  • 99
    • 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;91:9700-4.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 9700-9704
    • Herman, J.G.1    Latif, F.2    Weng, Y.3
  • 100
    • 34247385849 scopus 로고    scopus 로고
    • Molecular biology of renal cell cancer and the identification of therapeutic targets
    • Iliopoulos O. Molecular biology of renal cell cancer and the identification of therapeutic targets. J Clin Oncol 2006;24:5593-600.
    • (2006) J Clin Oncol , vol.24 , pp. 5593-5600
    • Iliopoulos, O.1
  • 101
    • 2942689618 scopus 로고    scopus 로고
    • The role of von Hippel-Lindau tumor suppressor protein and hypoxia in renal clear cell carcinoma
    • Sufan RI, Jewett MA, Ohh M. The role of von Hippel-Lindau tumor suppressor protein and hypoxia in renal clear cell carcinoma. Am J Physiol Renal Physiol2004;287:F1-6.
    • Am J Physiol Renal Physiol2004 , vol.287 , pp. 1-6
    • Sufan, R.I.1    Jewett, M.A.2    Ohh, M.3
  • 102
    • 0027954044 scopus 로고
    • Mutations of the VHL tumour suppressor gene in renal carcinoma
    • Gnarra JR, Tory K, Weng Y, et al. Mutations of the VHL tumour suppressor gene in renal carcinoma. Nat Genet 1994;7:85-90.
    • (1994) Nat Genet , vol.7 , pp. 85-90
    • Gnarra, J.R.1    Tory, K.2    Weng, Y.3
  • 103
    • 0036190056 scopus 로고    scopus 로고
    • Prognostic impact of histologic subtyping of adult renal epithelial neoplasms: An experience of 405 cases
    • Amin MB, Tamboli J, Javidan H, et al. Prognostic impact of histologic subtyping of adult renal epithelial neoplasms: an experience of 405 cases. Am J Surg Pathol 2002;26: 281-91.
    • (2002) Am J Surg Pathol , vol.26 , pp. 281-291
    • Amin, M.B.1    Tamboli, J.2    Javidan, H.3
  • 104
    • 0030788677 scopus 로고    scopus 로고
    • Papillary renal cell carcinoma: A clinicopathologic and immuno-histochemical study of 105 tumors
    • Delahunt B, Eble JN. Papillary renal cell carcinoma: a clinicopathologic and immuno-histochemical study of 105 tumors. Mod Pathol 1997;10:537-44.
    • (1997) Mod Pathol , vol.10 , pp. 537-544
    • Delahunt, B.1    Eble, J.N.2
  • 105
    • 0032813906 scopus 로고    scopus 로고
    • Hereditary and sporadic papillary renal car-cinomas with c-MET mutations share a distinct morphological phenotype
    • Lubensky IA., Schmidt L, Zhuang Z, et al. Hereditary and sporadic papillary renal car-cinomas with c-MET mutations share a distinct morphological phenotype. Am J Pathol 1999;155:517-26.
    • (1999) Am J Pathol , vol.155 , pp. 517-526
    • Lubensky, I.A.1    Schmidt, L.2    Zhuang, Z.3
  • 106
    • 0028253335 scopus 로고
    • The value of molecular genetic analysis in the diagnosis and prognosis of renal cell tumours
    • Kovacs G. The value of molecular genetic analysis in the diagnosis and prognosis of renal cell tumours. World J Urol 1994;12:64-8.
    • (1994) World J Urol , vol.12 , pp. 64-68
    • Kovacs, G.1
  • 107
    • 0034866962 scopus 로고    scopus 로고
    • The genetic basis of renal epithelial tumors: Advances in research and its impact on prognosis and therapy
    • Phillips JL, Pavlovich CP, Walther M, et al. The genetic basis of renal epithelial tumors: advances in research and its impact on prognosis and therapy. Curr Opin Urol 2001; 11:463-9.
    • (2001) Curr Opin Urol , vol.11 , pp. 463-469
    • Phillips, J.L.1    Pavlovich, C.P.2    Walther, M.3
  • 108
    • 0033535530 scopus 로고    scopus 로고
    • Novel mutations of the MET proto-onco-gene in papillary renal carcinomas
    • Schmidt L, Junker K, Nakaigawa N, et al. Novel mutations of the MET proto-onco-gene in papillary renal carcinomas. Oncogene 1999;18:2343-50.
    • (1999) Oncogene , vol.18 , pp. 2343-2350
    • Schmidt, L.1    Junker, K.2    Nakaigawa, N.3
  • 109
    • 0034628444 scopus 로고    scopus 로고
    • Mapping of the 7q31 subregion common to the small chromosome 7 derivatives from two sporadic papillary renal cell carcino-mas: Increased copy number and overexpression of the MET proto-oncogene
    • Glukhova L, Lavialle C, Fauvet D, et al. Mapping of the 7q31 subregion common to the small chromosome 7 derivatives from two sporadic papillary renal cell carcino-mas: increased copy number and overexpression of the MET proto-oncogene. Oncogene 2000;19:754-61.
    • (2000) Oncogene , vol.19 , pp. 754-761
    • Glukhova, L.1    Lavialle, C.2    Fauvet, D.3
  • 110
    • 0032869860 scopus 로고    scopus 로고
    • Histopathology and molecular genetics of renal tumors toward unification of a classification system
    • Zambrano NR, Lubensky IA, Merino MJ, et al. Histopathology and molecular genetics of renal tumors toward unification of a classification system. J Urol1999;162:1246-58.
    • J Urol1999 , vol.162 , pp. 1246-1258
    • Zambrano, N.R.1    Lubensky, I.A.2    Merino, M.J.3
  • 111
    • 0028832733 scopus 로고
    • Mapping the X chromosome breakpoint in two papillary renal cell carcinoma cell lines with a t(X;1)(p11.2;q21.2) and the first report of a female case
    • Shipley JM, Birdsall S, Clark J, et al. Mapping the X chromosome breakpoint in two papillary renal cell carcinoma cell lines with a t(X;1)(p11.2;q21.2) and the first report of a female case. Cytogenet Cell Genet 1995;71:280-4.
    • (1995) Cytogenet Cell Genet , vol.71 , pp. 280-284
    • Shipley, J.M.1    Birdsall, S.2    Clark, J.3
  • 113
    • 4544299668 scopus 로고    scopus 로고
    • Focus on kidney cancer
    • Linehan WM, Zbar B. Focus on kidney cancer. Cancer Cell 2004;6:223-8.
    • (2004) Cancer Cell , vol.6 , pp. 223-228
    • Linehan, W.M.1    Zbar, B.2
  • 114
    • 0344010917 scopus 로고    scopus 로고
    • Analysis of the Birt-Hogg-Dubé (BHD) tumour suppressor gene in sporadic renal cell carcinoma and colorectal cancer
    • Da Silva NF, Gentle D, Hesson LB, et al. Analysis of the Birt-Hogg-Dubé (BHD) tumour suppressor gene in sporadic renal cell carcinoma and colorectal cancer. J Med Genet 2003;40:820-4.
    • (2003) J Med Genet , vol.40 , pp. 820-824
    • da Silva, N.F.1    Gentle, D.2    Hesson, L.B.3
  • 115
    • 0041633905 scopus 로고    scopus 로고
    • Inactivation of BHD in sporadic renal tumors
    • Khoo SK., Kahnoski K, Sugimura J, et al. Inactivation of BHD in sporadic renal tumors. Cancer Res 2003;63:4583-7.
    • (2003) Cancer Res , vol.63 , pp. 4583-4587
    • Khoo, S.K.1    Kahnoski, K.2    Sugimura, J.3
  • 116
    • 25144442538 scopus 로고    scopus 로고
    • Role of molecular markers in the diagnosis and therapy of renal cell carcinoma
    • Lam JS, Leppert JT, Figlin RA, et al. Role of molecular markers in the diagnosis and therapy of renal cell carcinoma. Urology 2005;66:1-9.
    • (2005) Urology , vol.66 , pp. 1-9
    • Lam, J.S.1    Leppert, J.T.2    Figlin, R.A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.