메뉴 건너뛰기




Volumn 1210, Issue 1, 2010, Pages 1-7

New cancer targets emerging from studies of the Von Hippel-Lindau tumor suppressor protein

Author keywords

Cancer; Transcription factor; Tumor suppressor protein

Indexed keywords

2 OXOGLUTARATE MIMETIC; 2 OXOGLUTARIC ACID; ANTINEOPLASTIC AGENT; BEVACIZUMAB; CYCLIN D1; EGLN2 INHIBITOR; EVEROLIMUS; FUMARATE HYDRATASE; HYPOXIA INDUCIBLE FACTOR 1ALPHA; HYPOXIA INDUCIBLE FACTOR 2ALPHA; ISOCITRATE DEHYDROGENASE; ISOCITRATE DEHYDROGENASE 1; ISOCITRATE DEHYDROGENASE ISOENZYME; JARID1B PROTEIN; MYC PROTEIN; OXYGEN; PAZOPANIB; PROCOLLAGEN PROLINE 2 OXOGLUTARATE 4 DIOXYGENASE; PROLYL HYDROXYLASE EGLN1; PROLYL HYDROXYLASE EGLN2; PROLYL HYDROXYLASE EGLN3; RETINOBLASTOMA BINDING PROTEIN 2; RETINOBLASTOMA PROTEIN; SORAFENIB; SUCCINATE DEHYDROGENASE; SUCCINIC ACID; SUNITINIB; TEMSIROLIMUS; TUMOR MARKER; UNCLASSIFIED DRUG; VON HIPPEL LINDAU PROTEIN; PROLINE;

EID: 78349292235     PISSN: 00778923     EISSN: 17496632     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2010.05781.x     Document Type: Article
Times cited : (10)

References (86)
  • 1
    • 0036718539 scopus 로고    scopus 로고
    • Molecular basis of the VHL hereditary cancer syndrome
    • Kaelin, W.G. 2002. Molecular basis of the VHL hereditary cancer syndrome. Nat Rev Cancer. 2: 673-682.
    • (2002) Nat Rev Cancer. , vol.2 , pp. 673-682
    • Kaelin, W.G.1
  • 2
    • 43649093915 scopus 로고    scopus 로고
    • Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway
    • Kaelin, W.G. Jr. & P.J. Ratcliffe 2008. Oxygen sensing by metazoans: the central role of the HIF hydroxylase pathway. Mol. Cell. 30: 393-402.
    • (2008) Mol. Cell. , vol.30 , pp. 393-402
    • Kaelin Jr., W.G.1    Ratcliffe, P.J.2
  • 3
    • 0043234538 scopus 로고    scopus 로고
    • Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor
    • Hirsila, M. et al 2003. Characterization of the human prolyl 4-hydroxylases that modify the hypoxia-inducible factor. J. Biol. Chem. 278: 30772-30780.
    • (2003) J. Biol. Chem. , vol.278 , pp. 30772-30780
    • Hirsila, M.1
  • 4
    • 0037124173 scopus 로고    scopus 로고
    • The use of dioxygen by HIF prolyl hydroxylase (PHD1)
    • McNeill, L.A. et al 2002. The use of dioxygen by HIF prolyl hydroxylase (PHD1). Bioorg. Med. Chem. Lett. 12: 1547-1550.
    • (2002) Bioorg. Med. Chem. Lett. , vol.12 , pp. 1547-1550
    • McNeill, L.A.1
  • 5
    • 0041465022 scopus 로고    scopus 로고
    • HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia
    • Berra, E. et al 2003. HIF prolyl-hydroxylase 2 is the key oxygen sensor setting low steady-state levels of HIF-1alpha in normoxia. Embo. J. 22: 4082-4090.
    • (2003) Embo. J. , vol.22 , pp. 4082-4090
    • Berra, E.1
  • 6
    • 4644318828 scopus 로고    scopus 로고
    • Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor
    • Appelhoff, R.J. et al 2004. Differential function of the prolyl hydroxylases PHD1, PHD2, and PHD3 in the regulation of hypoxia-inducible factor. J. Biol. Chem. 279: 38458-38465.
    • (2004) J. Biol. Chem. , vol.279 , pp. 38458-38465
    • Appelhoff, R.J.1
  • 7
    • 70350456693 scopus 로고    scopus 로고
    • A feedback loop involving the Phd3 prolyl hydroxylase tunes the mammalian hypoxic response in vivo
    • Minamishima, Y.A. et al 2009. A feedback loop involving the Phd3 prolyl hydroxylase tunes the mammalian hypoxic response in vivo. Mol. Cell. Biol. 29: 5729-5741.
    • (2009) Mol. Cell. Biol. , vol.29 , pp. 5729-5741
    • Minamishima, Y.A.1
  • 8
    • 42449163874 scopus 로고    scopus 로고
    • Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure
    • Minamishima, Y.A. et al 2008. Somatic inactivation of the PHD2 prolyl hydroxylase causes polycythemia and congestive heart failure. Blood 111: 3236-3244.
    • (2008) Blood , vol.111 , pp. 3236-3244
    • Minamishima, Y.A.1
  • 9
    • 40949090791 scopus 로고    scopus 로고
    • Regulation of adult erythropoiesis by prolyl hydroxylase domain proteins
    • Takeda, K. et al 2008. Regulation of adult erythropoiesis by prolyl hydroxylase domain proteins. Blood 111: 3229-3235.
    • (2008) Blood , vol.111 , pp. 3229-3235
    • Takeda, K.1
  • 10
    • 31444436640 scopus 로고    scopus 로고
    • A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis
    • Percy, M.J. et al 2006. A family with erythrocytosis establishes a role for prolyl hydroxylase domain protein 2 in oxygen homeostasis. Proc. Natl. Acad. Sci. USA 103: 654-659.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 654-659
    • Percy, M.J.1
  • 11
    • 34548848799 scopus 로고    scopus 로고
    • A novel erythrocytosis-associated PHD2 mutation suggests the location of a HIF binding groove
    • Percy, M.J. et al 2007. A novel erythrocytosis-associated PHD2 mutation suggests the location of a HIF binding groove. Blood 110: 2193-2196.
    • (2007) Blood , vol.110 , pp. 2193-2196
    • Percy, M.J.1
  • 12
    • 34347378904 scopus 로고    scopus 로고
    • Prevalence, etiology, and consequences of anemia and clinical and economic benefits of anemia correction in patients with chronic kidney disease: an overview
    • S3-7; quiz S23-25
    • Dowling, T.C. 2007. Prevalence, etiology, and consequences of anemia and clinical and economic benefits of anemia correction in patients with chronic kidney disease: an overview. Am. J. Health Syst. Pharm. 64: S3-7; quiz S23-25.
    • (2007) Am. J. Health Syst. Pharm. , vol.64
    • Dowling, T.C.1
  • 13
    • 77954837178 scopus 로고    scopus 로고
    • Reactivation of hepatic EPO synthesis in mice after PHD loss
    • Minamishima, Y.A. & W.G. Kaelin Jr. Reactivation of hepatic EPO synthesis in mice after PHD loss. Science 329: 407.
    • Science , vol.329 , pp. 407
    • Minamishima, Y.A.1    Kaelin Jr., W.G.2
  • 14
    • 30444445382 scopus 로고    scopus 로고
    • Mouse model for noninvasive imaging of HIF prolyl hydroxylase activity: assessment of an oral agent that stimulates erythropoietin production
    • Safran, M. et al 2006. Mouse model for noninvasive imaging of HIF prolyl hydroxylase activity: assessment of an oral agent that stimulates erythropoietin production. Proc. Natl. Acad. Sci. USA 103: 105-110.
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 105-110
    • Safran, M.1
  • 16
    • 39749132878 scopus 로고    scopus 로고
    • The von hippel-lindau tumor suppressor protein: an update
    • Kaelin, W.G., Jr. 2007. The von hippel-lindau tumor suppressor protein: an update. Methods Enzymol. 435: 371-383.
    • (2007) Methods Enzymol. , vol.435 , pp. 371-383
    • Kaelin Jr., W.G.1
  • 17
    • 34047156190 scopus 로고    scopus 로고
    • HIF-2alpha promotes hypoxic cell proliferation by enhancing c-myc transcriptional activity
    • Gordan, J.D. et al 2007. HIF-2alpha promotes hypoxic cell proliferation by enhancing c-myc transcriptional activity. Cancer Cell. 11: 335-347.
    • (2007) Cancer Cell. , vol.11 , pp. 335-347
    • Gordan, J.D.1
  • 18
    • 56849096837 scopus 로고    scopus 로고
    • HIF-alpha effects on c-Myc distinguish two subtypes of sporadic VHL-deficient clear cell renal carcinoma
    • Gordan, J.D. et al 2008. HIF-alpha effects on c-Myc distinguish two subtypes of sporadic VHL-deficient clear cell renal carcinoma. Cancer Cell. 14: 435-446.
    • (2008) Cancer Cell. , vol.14 , pp. 435-446
    • Gordan, J.D.1
  • 19
    • 0033587146 scopus 로고    scopus 로고
    • The von Hippel-Lindau gene product is necessary for oxgyen-dependent proteolysis of hypoxia-inducible factor a subunits
    • Maxwell, P. et al 1999. The von Hippel-Lindau gene product is necessary for oxgyen-dependent proteolysis of hypoxia-inducible factor a subunits. Nature 399: 271-275.
    • (1999) Nature , vol.399 , pp. 271-275
    • Maxwell, P.1
  • 20
    • 0036528246 scopus 로고    scopus 로고
    • Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein
    • Kondo, K. et al 2002. Inhibition of HIF is necessary for tumor suppression by the von Hippel-Lindau protein. Cancer Cell. 1: 237-246.
    • (2002) Cancer Cell. , vol.1 , pp. 237-246
    • Kondo, K.1
  • 21
    • 0036527785 scopus 로고    scopus 로고
    • The contribution of VHL substrate binding and HIF1-alpha to the phenotype of VHL loss in renal cell carcinoma
    • Maranchie, J.K. et al 2002. The contribution of VHL substrate binding and HIF1-alpha to the phenotype of VHL loss in renal cell carcinoma. Cancer Cell. 1: 247-255.
    • (2002) Cancer Cell. , vol.1 , pp. 247-255
    • Maranchie, J.K.1
  • 22
    • 85027722628 scopus 로고    scopus 로고
    • Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth
    • Kondo, K. et al 2003. Inhibition of HIF2alpha is sufficient to suppress pVHL-defective tumor growth. PLos Biol. 1: 439-444.
    • (2003) PLos Biol , vol.1 , pp. 439-444
    • Kondo, K.1
  • 23
    • 1342280515 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor is sufficient for growth suppression of VHL-/- tumors
    • Zimmer, M. et al 2004. Inhibition of hypoxia-inducible factor is sufficient for growth suppression of VHL-/- tumors. Mol. Cancer Res. 2: 89-95.
    • (2004) Mol. Cancer Res. , vol.2 , pp. 89-95
    • Zimmer, M.1
  • 24
    • 33749344471 scopus 로고    scopus 로고
    • Failure to prolyl hydroxylate hypoxia-inducible factor alpha phenocopies VHL inactivation in vivo
    • Kim, W.Y. et al 2006. Failure to prolyl hydroxylate hypoxia-inducible factor alpha phenocopies VHL inactivation in vivo. Embo J. 25: 4650-4662.
    • (2006) Embo J. , vol.25 , pp. 4650-4662
    • Kim, W.Y.1
  • 25
    • 34147124264 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo
    • Rankin, E.B. et al 2007. Hypoxia-inducible factor-2 (HIF-2) regulates hepatic erythropoietin in vivo. J. Clin. Invest. 117: 1068-1077.
    • (2007) J. Clin. Invest. , vol.117 , pp. 1068-1077
    • Rankin, E.B.1
  • 26
    • 51649090078 scopus 로고    scopus 로고
    • Hypoxia-inducible factor-2 regulates vascular tumorigenesis in mice
    • Rankin, E.B. et al 2008. Hypoxia-inducible factor-2 regulates vascular tumorigenesis in mice. Oncogene 27: 5354-5358.
    • (2008) Oncogene , vol.27 , pp. 5354-5358
    • Rankin, E.B.1
  • 27
    • 68949098346 scopus 로고    scopus 로고
    • HIF-2 regulates hepatic lipid metabolism
    • Rankin, E.B. et al 2009. HIF-2 regulates hepatic lipid metabolism. Mol. Cel. Biol. 29: 4527-4538.
    • (2009) Mol. Cel. Biol. , vol.29 , pp. 4527-4538
    • Rankin, E.B.1
  • 28
    • 17044452288 scopus 로고    scopus 로고
    • HIF activation identifies early lesions in VHL kidneys: evidence for site-specific tumor suppressor function in the nephron
    • Mandriota, S.J. et al 2002. HIF activation identifies early lesions in VHL kidneys: evidence for site-specific tumor suppressor function in the nephron. Cancer Cell. 1: 459-468.
    • (2002) Cancer Cell. , vol.1 , pp. 459-468
    • Mandriota, S.J.1
  • 29
    • 37349080670 scopus 로고    scopus 로고
    • Bevacizumab plus interferon alfa-2a for treatment of metastatic renal cell carcinoma: a randomised, double-blind phase III trial
    • Escudier, B. et al 2007. Bevacizumab plus interferon alfa-2a for treatment of metastatic renal cell carcinoma: a randomised, double-blind phase III trial. Lancet 370: 2103-2111.
    • (2007) Lancet , vol.370 , pp. 2103-2111
    • Escudier, B.1
  • 30
    • 33846148701 scopus 로고    scopus 로고
    • Sorafenib in advanced clear-cell renal-cell carcinoma
    • Escudier, B. et al 2007. Sorafenib in advanced clear-cell renal-cell carcinoma. N. Engl. J. Med. 356: 125-134.
    • (2007) N. Engl. J. Med. , vol.356 , pp. 125-134
    • Escudier, B.1
  • 31
    • 33846181370 scopus 로고    scopus 로고
    • Sunitinib versus interferon alfa in metastatic renal-cell carcinoma
    • Motzer, R.J. et al 2007. Sunitinib versus interferon alfa in metastatic renal-cell carcinoma. N. Engl. J. Med. 356: 115-124.
    • (2007) N. Engl. J. Med. , vol.356 , pp. 115-124
    • Motzer, R.J.1
  • 32
    • 77949890945 scopus 로고    scopus 로고
    • Pazopanib in locally advanced or metastatic renal cell carcinoma: results of a randomized phase III trial
    • Sternberg, C.N. et al Pazopanib in locally advanced or metastatic renal cell carcinoma: results of a randomized phase III trial. J. Clin. Oncol. 28: 1061-1068.
    • J. Clin. Oncol. , vol.28 , pp. 1061-1068
    • Sternberg, C.N.1
  • 33
    • 84859920853 scopus 로고    scopus 로고
    • A phase 3, randomized, 3-arm study of temsirolimus (TEMSR) or interferon-alpha (IFN) or the combination of TEMSR + IFN in the treatment of first-line, poor-risk patients with advanced renal cell carcinoma (adv RCC). In JCO, 2006 ASCO Annual Meetings Proceedings Part I. 24: LBA4.
    • Hudes, G. et al 2006. A phase 3, randomized, 3-arm study of temsirolimus (TEMSR) or interferon-alpha (IFN) or the combination of TEMSR + IFN in the treatment of first-line, poor-risk patients with advanced renal cell carcinoma (adv RCC). In JCO, 2006 ASCO Annual Meetings Proceedings Part I. 24: LBA4.
    • (2006)
    • Hudes, G.1
  • 34
    • 48649107474 scopus 로고    scopus 로고
    • Efficacy of everolimus in advanced renal cell carcinoma: a double-blind, randomised, placebo-controlled phase III trial
    • Motzer, R.J. et al 2008. Efficacy of everolimus in advanced renal cell carcinoma: a double-blind, randomised, placebo-controlled phase III trial. Lancet 372: 449-456.
    • (2008) Lancet , vol.372 , pp. 449-456
    • Motzer, R.J.1
  • 35
    • 34347220473 scopus 로고    scopus 로고
    • Defining the role of mTOR in cancer
    • Guertin, D.A. & D.M. Sabatini 2007. Defining the role of mTOR in cancer. Cancer Cell. 12: 9-22.
    • (2007) Cancer Cell. , vol.12 , pp. 9-22
    • Guertin, D.A.1    Sabatini, D.M.2
  • 36
    • 58049216350 scopus 로고    scopus 로고
    • Differential dependence of HIF1alpha and HIF2alpha on mTORC1 and mTORC2
    • Toschi, A. et al 2008. Differential dependence of HIF1alpha and HIF2alpha on mTORC1 and mTORC2. J. Biol. Chem. 283: 34495-34499.
    • (2008) J. Biol. Chem. , vol.283 , pp. 34495-34499
    • Toschi, A.1
  • 37
    • 75149188170 scopus 로고    scopus 로고
    • Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes
    • Dalgliesh, G.L. et al 2010. Systematic sequencing of renal carcinoma reveals inactivation of histone modifying genes. Nature 463: 360-363.
    • (2010) Nature , vol.463 , pp. 360-363
    • Dalgliesh, G.L.1
  • 38
    • 66349100709 scopus 로고    scopus 로고
    • Patterns of gene expression and copy-number alterations in von-hippel lindau disease-associated and sporadic clear cell carcinoma of the kidney
    • Beroukhim, R. et al 2009. Patterns of gene expression and copy-number alterations in von-hippel lindau disease-associated and sporadic clear cell carcinoma of the kidney. Cancer Res. 69: 4674-4681.
    • (2009) Cancer Res. , vol.69 , pp. 4674-4681
    • Beroukhim, R.1
  • 39
    • 70349880529 scopus 로고    scopus 로고
    • Genome-wide profiling of chromosomal alterations in renal cell carcinoma using high-density single nucleotide polymorphism arrays
    • Chen, M. et al 2009. Genome-wide profiling of chromosomal alterations in renal cell carcinoma using high-density single nucleotide polymorphism arrays. Int. J. Cancer 125: 2342-2348.
    • (2009) Int. J. Cancer , vol.125 , pp. 2342-2348
    • Chen, M.1
  • 40
    • 36749049879 scopus 로고    scopus 로고
    • High-resolution analysis of DNA copy number alterations and gene expression in renal clear cell carcinoma
    • Yoshimoto, T. et al 2007. High-resolution analysis of DNA copy number alterations and gene expression in renal clear cell carcinoma. J. Pathol. 213: 392-401.
    • (2007) J. Pathol. , vol.213 , pp. 392-401
    • Yoshimoto, T.1
  • 41
    • 39749116278 scopus 로고    scopus 로고
    • Genome-wide screening of copy number alterations and LOH events in renal cell carcinomas and integration with gene expression profile
    • Cifola, I. et al 2008. Genome-wide screening of copy number alterations and LOH events in renal cell carcinomas and integration with gene expression profile. Mol. Cancer 7: 6.
    • (2008) Mol. Cancer , vol.7 , pp. 6
    • Cifola, I.1
  • 42
    • 55949101858 scopus 로고    scopus 로고
    • Kinase requirements in human cells: III. Altered kinase requirements in VHL-/- cancer cells detected in a pilot synthetic lethal screen
    • Bommi-Reddy, A. et al 2008. Kinase requirements in human cells: III. Altered kinase requirements in VHL-/- cancer cells detected in a pilot synthetic lethal screen. Proc. Natl Acad. Sci. USA 105: 16484-16489.
    • (2008) Proc. Natl Acad. Sci. USA , vol.105 , pp. 16484-16489
    • Bommi-Reddy, A.1
  • 43
    • 45849147350 scopus 로고    scopus 로고
    • A molecule targeting VHL-deficient renal cell carcinoma that induces autophagy
    • Turcotte, S. et al 2008. A molecule targeting VHL-deficient renal cell carcinoma that induces autophagy. Cancer Cell. 14: 90-102.
    • (2008) Cancer Cell. , vol.14 , pp. 90-102
    • Turcotte, S.1
  • 44
    • 69249247037 scopus 로고    scopus 로고
    • SDH5 mutations and familial paraganglioma: somewhere Warburg is smiling
    • Kaelin, W.G., Jr. 2009. SDH5 mutations and familial paraganglioma: somewhere Warburg is smiling. Cancer Cell. 16: 180-182.
    • (2009) Cancer Cell. , vol.16 , pp. 180-182
    • Kaelin Jr., W.G.1
  • 45
    • 33947520506 scopus 로고    scopus 로고
    • Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF
    • Koivunen, P. et al 2007. Inhibition of hypoxia-inducible factor (HIF) hydroxylases by citric acid cycle intermediates: possible links between cell metabolism and stabilization of HIF. J. Biol. Chem. 282: 4524-4532.
    • (2007) J. Biol. Chem. , vol.282 , pp. 4524-4532
    • Koivunen, P.1
  • 46
    • 26444570010 scopus 로고    scopus 로고
    • Accumulation of Krebs cycle intermediates and over-expression of HIF1alpha in tumours which result from germline FH and SDH mutations
    • Pollard, P.J. et al 2005. Accumulation of Krebs cycle intermediates and over-expression of HIF1alpha in tumours which result from germline FH and SDH mutations. Hum. Mol. Genet. 14: 2231-2239.
    • (2005) Hum. Mol. Genet. , vol.14 , pp. 2231-2239
    • Pollard, P.J.1
  • 47
    • 19944433653 scopus 로고    scopus 로고
    • Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase
    • Selak, M.A. et al 2005. Succinate links TCA cycle dysfunction to oncogenesis by inhibiting HIF-alpha prolyl hydroxylase. Cancer Cell. 7: 77-85.
    • (2005) Cancer Cell. , vol.7 , pp. 77-85
    • Selak, M.A.1
  • 48
    • 34047167041 scopus 로고    scopus 로고
    • Targeted inactivation of fh1 causes proliferative renal cyst development and activation of the hypoxia pathway
    • Pollard, P.J. et al 2007. Targeted inactivation of fh1 causes proliferative renal cyst development and activation of the hypoxia pathway. Cancer Cell. 11: 311-319.
    • (2007) Cancer Cell. , vol.11 , pp. 311-319
    • Pollard, P.J.1
  • 49
    • 77955594623 scopus 로고    scopus 로고
    • A HIF1alpha regulatory loop links hypoxia and mitochondrial signals in pheochromocytomas
    • Dahia, P.L. et al 2005. A HIF1alpha regulatory loop links hypoxia and mitochondrial signals in pheochromocytomas. PLoS Genet 1: 72-80.
    • (2005) PLoS Genet , vol.1 , pp. 72-80
    • Dahia, P.L.1
  • 50
    • 56749156414 scopus 로고    scopus 로고
    • Analysis of the IDH1 codon 132 mutation in brain tumors
    • Balss, J. et al 2008. Analysis of the IDH1 codon 132 mutation in brain tumors. Acta Neuropathol. 116: 597-602.
    • (2008) Acta Neuropathol. , vol.116 , pp. 597-602
    • Balss, J.1
  • 51
    • 52949127312 scopus 로고    scopus 로고
    • An integrated genomic analysis of human glioblastoma multiforme
    • Parsons, D.W. et al 2008. An integrated genomic analysis of human glioblastoma multiforme. Science 321: 1807-1812.
    • (2008) Science , vol.321 , pp. 1807-1812
    • Parsons, D.W.1
  • 52
    • 65349150503 scopus 로고    scopus 로고
    • IDH1 mutations are early events in the development of astrocytomas and oligodendrogliomas
    • Watanabe, T. et al 2009. IDH1 mutations are early events in the development of astrocytomas and oligodendrogliomas. Am. J. Pathol. 174: 1149-1153.
    • (2009) Am. J. Pathol. , vol.174 , pp. 1149-1153
    • Watanabe, T.1
  • 53
    • 60849115270 scopus 로고    scopus 로고
    • IDH1 and IDH2 mutations in gliomas
    • Yan, H. et al 2009. IDH1 and IDH2 mutations in gliomas. N. Engl. J. Med. 360: 765-773.
    • (2009) N. Engl. J. Med. , vol.360 , pp. 765-773
    • Yan, H.1
  • 54
    • 77952536841 scopus 로고    scopus 로고
    • IDH1 and IDH2 gene mutations identify novel molecular subsets within de novo cytogenetically normal acute myeloid leukemia: a Cancer and Leukemia Group B study
    • Marcucci, G. et al IDH1 and IDH2 gene mutations identify novel molecular subsets within de novo cytogenetically normal acute myeloid leukemia: a Cancer and Leukemia Group B study. J. Clin. Oncol. 28: 2348-2355.
    • J. Clin. Oncol. , vol.28 , pp. 2348-2355
    • Marcucci, G.1
  • 55
    • 77649305610 scopus 로고    scopus 로고
    • The common feature of leukemia-associated IDH1 and IDH2 mutations is a neomorphic enzyme activity converting alpha-ketoglutarate to 2-hydroxyglutarate
    • Ward, P.S. et al 2010. The common feature of leukemia-associated IDH1 and IDH2 mutations is a neomorphic enzyme activity converting alpha-ketoglutarate to 2-hydroxyglutarate. Cancer Cell. 17: 225-234.
    • (2010) Cancer Cell. , vol.17 , pp. 225-234
    • Ward, P.S.1
  • 56
    • 72049125350 scopus 로고    scopus 로고
    • Cancer-associated IDH1 mutations produce 2-hydroxyglutarate
    • Dang, L. et al 2009. Cancer-associated IDH1 mutations produce 2-hydroxyglutarate. Nature 462: 739-744.
    • (2009) Nature , vol.462 , pp. 739-744
    • Dang, L.1
  • 57
    • 77149134353 scopus 로고    scopus 로고
    • Cancer-associated metabolite 2-hydroxyglutarate accumulates in acute myelogenous leukemia with isocitrate dehydrogenase 1 and 2 mutations
    • Gross, S. et al 2010. Cancer-associated metabolite 2-hydroxyglutarate accumulates in acute myelogenous leukemia with isocitrate dehydrogenase 1 and 2 mutations. J. Exp. Med. 207: 339-344.
    • (2010) J. Exp. Med. , vol.207 , pp. 339-344
    • Gross, S.1
  • 58
    • 0035221419 scopus 로고    scopus 로고
    • The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases
    • Aravind, L. & E.V. Koonin 2001. The DNA-repair protein AlkB, EGL-9, and leprecan define new families of 2-oxoglutarate- and iron-dependent dioxygenases. Genome Bio. 2: research0007.1-0007.8.
    • (2001) Genome Bio. , vol.2
    • Aravind, L.1    Koonin, E.V.2
  • 59
    • 59649117924 scopus 로고    scopus 로고
    • Heterozygous deficiency of PHD2 restores tumor oxygenation and inhibits metastasis via endothelial normalization
    • Mazzone, M. et al 2009. Heterozygous deficiency of PHD2 restores tumor oxygenation and inhibits metastasis via endothelial normalization. Cell 136: 839-851.
    • (2009) Cell , vol.136 , pp. 839-851
    • Mazzone, M.1
  • 60
    • 0037165244 scopus 로고    scopus 로고
    • Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression)
    • Seth, P. et al 2002. Novel estrogen and tamoxifen induced genes identified by SAGE (Serial Analysis of Gene Expression). Oncogene 21: 836-843.
    • (2002) Oncogene , vol.21 , pp. 836-843
    • Seth, P.1
  • 61
    • 70350507985 scopus 로고    scopus 로고
    • Control of cyclin D1 and breast tumorigenesis by the EglN2 prolyl hydroxylase
    • Zhang, Q. et al 2009. Control of cyclin D1 and breast tumorigenesis by the EglN2 prolyl hydroxylase. Cancer Cell. 16: 413-424.
    • (2009) Cancer Cell. , vol.16 , pp. 413-424
    • Zhang, Q.1
  • 62
    • 0029111934 scopus 로고
    • Cyclin D1 provides a link between development and oncogenesis in the retina and breast
    • Sicinski, P. et al 1995. Cyclin D1 provides a link between development and oncogenesis in the retina and breast. Cell 82: 621-630.
    • (1995) Cell , vol.82 , pp. 621-630
    • Sicinski, P.1
  • 63
    • 23644436667 scopus 로고    scopus 로고
    • Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer
    • Lee, S. et al 2005. Neuronal apoptosis linked to EglN3 prolyl hydroxylase and familial pheochromocytoma genes: developmental culling and cancer. Cancer Cell. 8: 155-167.
    • (2005) Cancer Cell. , vol.8 , pp. 155-167
    • Lee, S.1
  • 64
    • 0033066605 scopus 로고    scopus 로고
    • Expression of the SM-20 gene promotes death in nerve growth factor-dependent sympathetic neurons
    • Lipscomb, E. et al 1999. Expression of the SM-20 gene promotes death in nerve growth factor-dependent sympathetic neurons. J. Neurochem. 73: 429-432.
    • (1999) J. Neurochem. , vol.73 , pp. 429-432
    • Lipscomb, E.1
  • 65
    • 0035895928 scopus 로고    scopus 로고
    • SM-20 is a novel mitochondrial protein that causes caspase-dependent cell death in nerve growth factor-dependent neurons
    • Lipscomb, E. P. Sarmiere & R. Freeman 2001. SM-20 is a novel mitochondrial protein that causes caspase-dependent cell death in nerve growth factor-dependent neurons. J. Biol. Chem. 276: 11775-11782.
    • (2001) J. Biol. Chem. , vol.276 , pp. 11775-11782
    • Lipscomb, E.1    Sarmiere, P.2    Freeman, R.3
  • 66
    • 43249108443 scopus 로고    scopus 로고
    • Abnormal sympathoadrenal development and systemic hypotension in PHD3-/- mice
    • Bishop, T. et al 2008. Abnormal sympathoadrenal development and systemic hypotension in PHD3-/- mice. Mol. Cell. Biol. 28: 3386-3400.
    • (2008) Mol. Cell. Biol. , vol.28 , pp. 3386-3400
    • Bishop, T.1
  • 67
    • 41649116940 scopus 로고    scopus 로고
    • The kinesin KIF1Bbeta acts downstream from EglN3 to induce apoptosis and is a potential 1p36 tumor suppressor
    • Schlisio, S. et al 2008. The kinesin KIF1Bbeta acts downstream from EglN3 to induce apoptosis and is a potential 1p36 tumor suppressor. Genes Dev. 22: 884-893.
    • (2008) Genes Dev. , vol.22 , pp. 884-893
    • Schlisio, S.1
  • 68
    • 48249154559 scopus 로고    scopus 로고
    • Prolyl hydroxylase PHD3 activates oxygen-dependent protein aggregation
    • Rantanen, K. et al 2008. Prolyl hydroxylase PHD3 activates oxygen-dependent protein aggregation. Mol. Biol. Cell. 19: 2231-2240.
    • (2008) Mol. Biol. Cell. , vol.19 , pp. 2231-2240
    • Rantanen, K.1
  • 69
    • 53749107898 scopus 로고    scopus 로고
    • A germline mutation of the KIF1B beta gene on 1p36 in a family with neural and nonneural tumors
    • Yeh, I.T. et al 2008. A germline mutation of the KIF1B beta gene on 1p36 in a family with neural and nonneural tumors. Hum Genet. 124: 279-285.
    • (2008) Hum Genet. , vol.124 , pp. 279-285
    • Yeh, I.T.1
  • 70
    • 54049148638 scopus 로고    scopus 로고
    • KIF1Bbeta functions as a haploinsufficient tumor suppressor gene mapped to chromosome 1p36.2 by inducing apoptotic cell death
    • Munirajan, A.K. et al 2008. KIF1Bbeta functions as a haploinsufficient tumor suppressor gene mapped to chromosome 1p36.2 by inducing apoptotic cell death. J. Biol. Chem. 283: 24426-24434.
    • (2008) J. Biol. Chem. , vol.283 , pp. 24426-24434
    • Munirajan, A.K.1
  • 71
    • 34247553146 scopus 로고    scopus 로고
    • Cell-permeating alpha-ketoglutarate derivatives alleviate pseudohypoxia in succinate dehydrogenase-deficient cells
    • MacKenzie, E.D. et al 2007. Cell-permeating alpha-ketoglutarate derivatives alleviate pseudohypoxia in succinate dehydrogenase-deficient cells. Mol. Cell Biol. 27: 3282-3289.
    • (2007) Mol. Cell Biol. , vol.27 , pp. 3282-3289
    • MacKenzie, E.D.1
  • 72
    • 70449624093 scopus 로고    scopus 로고
    • Reactivating HIF prolyl hydroxylases under hypoxia results in metabolic catastrophe and cell death
    • Tennant, D.A. et al 2009. Reactivating HIF prolyl hydroxylases under hypoxia results in metabolic catastrophe and cell death. Oncogene 28: 4009-4021.
    • (2009) Oncogene , vol.28 , pp. 4009-4021
    • Tennant, D.A.1
  • 73
    • 33747455678 scopus 로고    scopus 로고
    • JmjC-domain-containing proteins and histone demethylation
    • Klose, R.J. E.M. Kallin & Y. Zhang 2006. JmjC-domain-containing proteins and histone demethylation. Nat. Rev. Genet. 7: 715-727.
    • (2006) Nat. Rev. Genet. , vol.7 , pp. 715-727
    • Klose, R.J.1    Kallin, E.M.2    Zhang, Y.3
  • 74
    • 33748291758 scopus 로고    scopus 로고
    • Roles of jumonji and jumonji family genes in chromatin regulation and development
    • Takeuchi, T. et al 2006. Roles of jumonji and jumonji family genes in chromatin regulation and development. Dev Dyn. 235: 2449-2459.
    • (2006) Dev Dyn. , vol.235 , pp. 2449-2459
    • Takeuchi, T.1
  • 75
    • 33746332412 scopus 로고    scopus 로고
    • The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3
    • Cloos, P.A. et al 2006. The putative oncogene GASC1 demethylates tri- and dimethylated lysine 9 on histone H3. Nature 442: 307-311.
    • (2006) Nature , vol.442 , pp. 307-311
    • Cloos, P.A.1
  • 76
    • 63449115501 scopus 로고    scopus 로고
    • Multiple recurrent genetic events converge on control of histone lysine methylation in medulloblastoma
    • Northcott, P.A. et al 2009. Multiple recurrent genetic events converge on control of histone lysine methylation in medulloblastoma. Nat. Genet. 41: 465-472.
    • (2009) Nat. Genet. , vol.41 , pp. 465-472
    • Northcott, P.A.1
  • 77
    • 67349203626 scopus 로고    scopus 로고
    • Somatic mutations of the histone H3K27 demethylase gene UTX in human cancer
    • van Haaften, G. et al 2009. Somatic mutations of the histone H3K27 demethylase gene UTX in human cancer. Nat. Genet. 41: 521-523.
    • (2009) Nat. Genet. , vol.41 , pp. 521-523
    • van Haaften, G.1
  • 78
    • 67349266612 scopus 로고    scopus 로고
    • Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger
    • Wang, G.G. et al 2009. Haematopoietic malignancies caused by dysregulation of a chromatin-binding PHD finger. Nature 459: 847-851.
    • (2009) Nature , vol.459 , pp. 847-851
    • Wang, G.G.1
  • 79
    • 0037145309 scopus 로고    scopus 로고
    • PLU-1 nuclear protein, which is upregulated in breast cancer, shows restricted expression in normal human adult tissues: a new cancer/testis antigen?
    • Barrett, A. et al 2002. PLU-1 nuclear protein, which is upregulated in breast cancer, shows restricted expression in normal human adult tissues: a new cancer/testis antigen? Int. J. Cancer 101: 581-588.
    • (2002) Int. J. Cancer , vol.101 , pp. 581-588
    • Barrett, A.1
  • 80
    • 33645826250 scopus 로고    scopus 로고
    • Identification of NUP98 abnormalities in acute leukemia: JARID1A (12p13) as a new partner gene
    • van Zutven, L.J. et al 2006. Identification of NUP98 abnormalities in acute leukemia: JARID1A (12p13) as a new partner gene. Genes Chromosomes Cancer 45: 437-446.
    • (2006) Genes Chromosomes Cancer , vol.45 , pp. 437-446
    • van Zutven, L.J.1
  • 81
    • 0025808021 scopus 로고
    • Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product
    • Defeo-Jones, D. et al 1991. Cloning of cDNAs for cellular proteins that bind to the retinoblastoma gene product. Nature 352: 251-254.
    • (1991) Nature , vol.352 , pp. 251-254
    • Defeo-Jones, D.1
  • 82
    • 0031930466 scopus 로고    scopus 로고
    • Stable binding to E2F is not required for the retinoblastoma protein to activate transcription, promote differentiation, and suppress tumor cell growth
    • Sellers, W.R. et al 1998. Stable binding to E2F is not required for the retinoblastoma protein to activate transcription, promote differentiation, and suppress tumor cell growth. Genes Dev. 12: 95-106.
    • (1998) Genes Dev. , vol.12 , pp. 95-106
    • Sellers, W.R.1
  • 83
    • 20444429760 scopus 로고    scopus 로고
    • Binding of pRB to the PHD protein RBP2 promotes cellular differentiation
    • Benevolenskaya, E.V. et al 2005. Binding of pRB to the PHD protein RBP2 promotes cellular differentiation. Mol. Cell 18: 623-635.
    • (2005) Mol. Cell , vol.18 , pp. 623-635
    • Benevolenskaya, E.V.1
  • 84
    • 77950809059 scopus 로고    scopus 로고
    • A chromatin-mediated reversible drug-tolerant state in cancer cell subpopulations
    • Sharma, S.V. et al 2010. A chromatin-mediated reversible drug-tolerant state in cancer cell subpopulations. Cell 141: 69-80.
    • (2010) Cell , vol.141 , pp. 69-80
    • Sharma, S.V.1
  • 85
    • 33947244845 scopus 로고    scopus 로고
    • PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation
    • Yamane, K. et al 2007. PLU-1 is an H3K4 demethylase involved in transcriptional repression and breast cancer cell proliferation. Mol. Cell 25: 801-812.
    • (2007) Mol. Cell , vol.25 , pp. 801-812
    • Yamane, K.1
  • 86
    • 77952502408 scopus 로고    scopus 로고
    • A temporarily distinct subpopulation of slow-cycling melanoma cells is required for continuous tumor growth
    • Roesch, A. et al 2010. A temporarily distinct subpopulation of slow-cycling melanoma cells is required for continuous tumor growth. Cell 141: 583-594.
    • (2010) Cell , vol.141 , pp. 583-594
    • Roesch, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.