메뉴 건너뛰기




Volumn 67, Issue 24, 2007, Pages 11798-11810

Inhibition of RAS-mediated transformation and tumorigenesis by targeting the downstream E3 ubiquitin ligase seven in absentia homologue

Author keywords

[No Author keywords available]

Indexed keywords

AGAR; E3 UBIQUITIN LIGASE SEVEN IN ABSENTIA; GLYCERALDEHYDE 3 PHOSPHATE DEHYDROGENASE; K RAS PROTEIN; MITOGEN ACTIVATED PROTEIN KINASE; RAS PROTEIN; UBIQUITIN PROTEIN LIGASE E3; UNCLASSIFIED DRUG;

EID: 37549018162     PISSN: 00085472     EISSN: None     Source Type: Journal    
DOI: 10.1158/0008-5472.CAN-06-4471     Document Type: Article
Times cited : (60)

References (48)
  • 1
    • 0023068346 scopus 로고    scopus 로고
    • Barbacid M. ras genes. Annu Rev Biochem 1987;56:779-827.
    • Barbacid M. ras genes. Annu Rev Biochem 1987;56:779-827.
  • 3
    • 0025838675 scopus 로고
    • Regulators and effectors of ras proteins
    • Bollag G, McCormick F. Regulators and effectors of ras proteins. Annu Rev Cell Biol 1991;7:601-32.
    • (1991) Annu Rev Cell Biol , vol.7 , pp. 601-632
    • Bollag, G.1    McCormick, F.2
  • 5
    • 0032750043 scopus 로고    scopus 로고
    • How do small GTPase signal transduction pathways regulate cell cycle entry?
    • Marshall C. How do small GTPase signal transduction pathways regulate cell cycle entry? Curr Opin Cell Biol 1999;11:732-6.
    • (1999) Curr Opin Cell Biol , vol.11 , pp. 732-736
    • Marshall, C.1
  • 7
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • Hanahan D, Weinberg RA. The hallmarks of cancer. Cell 2000;100:57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 8
    • 0037264633 scopus 로고    scopus 로고
    • Targeting RAS signalling pathways in cancer therapy
    • Downward J. Targeting RAS signalling pathways in cancer therapy. Nat Rev Cancer 2003;3:11-22.
    • (2003) Nat Rev Cancer , vol.3 , pp. 11-22
    • Downward, J.1
  • 9
    • 33947594129 scopus 로고    scopus 로고
    • Hyperactive Ras in developmental disorders and cancer
    • Schubbert S, Shannon K, Bollag G. Hyperactive Ras in developmental disorders and cancer. Nat Rev Cancer 2007;7:295-308.
    • (2007) Nat Rev Cancer , vol.7 , pp. 295-308
    • Schubbert, S.1    Shannon, K.2    Bollag, G.3
  • 10
    • 0024376173 scopus 로고    scopus 로고
    • Bos JL. ras oncogenes in human cancer: a review. Cancer Res 1989;49:4682-9.
    • Bos JL. ras oncogenes in human cancer: a review. Cancer Res 1989;49:4682-9.
  • 11
    • 31144438305 scopus 로고    scopus 로고
    • Cancer biology: Signatures guide drug choice
    • Downward J. Cancer biology: signatures guide drug choice. Nature 2006;439:274-5.
    • (2006) Nature , vol.439 , pp. 274-275
    • Downward, J.1
  • 13
    • 0036883940 scopus 로고    scopus 로고
    • Pancreatic cancer biology and genetics
    • Bardeesy N, DePinho RA. Pancreatic cancer biology and genetics. Nat Rev Cancer 2002;2:897-909.
    • (2002) Nat Rev Cancer , vol.2 , pp. 897-909
    • Bardeesy, N.1    DePinho, R.A.2
  • 15
    • 10344258041 scopus 로고    scopus 로고
    • Targeting the mitogen-activated protein kinase cascade to treat cancer
    • Sebolt-Leopold JS, Herrera R. Targeting the mitogen-activated protein kinase cascade to treat cancer. Nat Rev Cancer 2004;4:937-47.
    • (2004) Nat Rev Cancer , vol.4 , pp. 937-947
    • Sebolt-Leopold, J.S.1    Herrera, R.2
  • 16
    • 0037941536 scopus 로고    scopus 로고
    • Gene expression phenotypic models that predict the activity of oncogenic pathways
    • Huang E, Ishida S, Pittman J, et al. Gene expression phenotypic models that predict the activity of oncogenic pathways. Nat Genet 2003;34:226-30.
    • (2003) Nat Genet , vol.34 , pp. 226-230
    • Huang, E.1    Ishida, S.2    Pittman, J.3
  • 17
    • 31144459985 scopus 로고    scopus 로고
    • Oncogenic pathway signatures in human cancers as a guide to targeted therapies
    • Bild AH, Yao G, Chang JT, et al. Oncogenic pathway signatures in human cancers as a guide to targeted therapies. Nature 2006;439:353-7.
    • (2006) Nature , vol.439 , pp. 353-357
    • Bild, A.H.1    Yao, G.2    Chang, J.T.3
  • 18
    • 0033029811 scopus 로고    scopus 로고
    • Ras caught in another affair: The exchange factors for Ral
    • Wolthuis RM, Bos JL. Ras caught in another affair: the exchange factors for Ral. Curr Opin Genet Dev 1999;9:112-7.
    • (1999) Curr Opin Genet Dev , vol.9 , pp. 112-117
    • Wolthuis, R.M.1    Bos, J.L.2
  • 19
    • 0038335337 scopus 로고    scopus 로고
    • Ras signaling, deregulation of gene expression and oncogenesis
    • Ulku AS, Der CJ. Ras signaling, deregulation of gene expression and oncogenesis. Cancer Treat Res 2003;115:189-208.
    • (2003) Cancer Treat Res , vol.115 , pp. 189-208
    • Ulku, A.S.1    Der, C.J.2
  • 20
    • 7444245100 scopus 로고    scopus 로고
    • Renewing the conspiracy theory debate: Does Raf function alone to mediate Ras oncogenesis?
    • Repasky GA, Chenette EJ, Der CJ. Renewing the conspiracy theory debate: does Raf function alone to mediate Ras oncogenesis? Trends Cell Biol 2004;14:639-47.
    • (2004) Trends Cell Biol , vol.14 , pp. 639-647
    • Repasky, G.A.1    Chenette, E.J.2    Der, C.J.3
  • 21
    • 0033981639 scopus 로고    scopus 로고
    • A genome-wide survey of RAS transformation targets
    • Zuber J, Tchernitsa OI, Hinzmann B, et al. A genome-wide survey of RAS transformation targets. Nat Genet 2000;24:144-52.
    • (2000) Nat Genet , vol.24 , pp. 144-152
    • Zuber, J.1    Tchernitsa, O.I.2    Hinzmann, B.3
  • 22
    • 2942534604 scopus 로고    scopus 로고
    • Gene expression profiling by DNA microarray analysis in mouse embryonic fibroblasts transformed by rasV12 mutated protein and the E1A oncogene
    • Vasseur S, Malicet C, Calvo EL, et al. Gene expression profiling by DNA microarray analysis in mouse embryonic fibroblasts transformed by rasV12 mutated protein and the E1A oncogene. Mol Cancer 2003;2:19.
    • (2003) Mol Cancer , vol.2 , pp. 19
    • Vasseur, S.1    Malicet, C.2    Calvo, E.L.3
  • 23
    • 0028353694 scopus 로고
    • Determination of neuronal cell fate: Lessons from the R7 neuron of Drosophila
    • Zipursky SL, Rubin GM. Determination of neuronal cell fate: lessons from the R7 neuron of Drosophila. Annu Rev Neurosci 1994;17:373-97.
    • (1994) Annu Rev Neurosci , vol.17 , pp. 373-397
    • Zipursky, S.L.1    Rubin, G.M.2
  • 24
    • 0025029382 scopus 로고    scopus 로고
    • Carthew RW, Rubin GM. Seven in absentia, a gene required for specification of R7 cell fate in the Drosophila eye. Cell 1990;63:561-77.
    • Carthew RW, Rubin GM. Seven in absentia, a gene required for specification of R7 cell fate in the Drosophila eye. Cell 1990;63:561-77.
  • 25
    • 0030849728 scopus 로고    scopus 로고
    • PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism
    • Tang AH, Neufeld TP, Kwan E, Rubin GM. PHYL acts to down-regulate TTK88, a transcriptional repressor of neuronal cell fates, by a SINA-dependent mechanism. Cell 1997;90:459-67.
    • (1997) Cell , vol.90 , pp. 459-467
    • Tang, A.H.1    Neufeld, T.P.2    Kwan, E.3    Rubin, G.M.4
  • 26
    • 0031573441 scopus 로고    scopus 로고
    • Characterization of human homologs of the Drosophila seven in absentia (sina) gene
    • Hu G, Chung YL, Glover T, Valentine V, Look AT, Fearon ER. Characterization of human homologs of the Drosophila seven in absentia (sina) gene. Genomics 1997;46:103-11.
    • (1997) Genomics , vol.46 , pp. 103-111
    • Hu, G.1    Chung, Y.L.2    Glover, T.3    Valentine, V.4    Look, A.T.5    Fearon, E.R.6
  • 27
    • 33645958587 scopus 로고    scopus 로고
    • Elucidation of the substrate binding site of Siah ubiquitin ligase
    • House CM, Hancock NC, Moller A, et al. Elucidation of the substrate binding site of Siah ubiquitin ligase. Structure 2006;14:695-701.
    • (2006) Structure , vol.14 , pp. 695-701
    • House, C.M.1    Hancock, N.C.2    Moller, A.3
  • 28
    • 26644464383 scopus 로고    scopus 로고
    • Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex
    • Santelli E, Leone M, Li C, et al. Structural analysis of Siah1-Siah-interacting protein interactions and insights into the assembly of an E3 ligase multiprotein complex. J Biol Chem 2005;280:34278-87.
    • (2005) J Biol Chem , vol.280 , pp. 34278-34287
    • Santelli, E.1    Leone, M.2    Li, C.3
  • 29
    • 0036143826 scopus 로고    scopus 로고
    • Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-α signaling
    • Polekhina G, House CM, Traficante N, et al. Siah ubiquitin ligase is structurally related to TRAF and modulates TNF-α signaling. Nat Struct Biol 2002;9:68-75.
    • (2002) Nat Struct Biol , vol.9 , pp. 68-75
    • Polekhina, G.1    House, C.M.2    Traficante, N.3
  • 30
    • 9244251506 scopus 로고    scopus 로고
    • Isolation of 10 differentially expressed cDNAs in p53-induced apoptosis: Activation of the vertebrate homologue of the drosophila seven in absentia gene
    • Amson RB, Nemani M, Roperch JP, et al. Isolation of 10 differentially expressed cDNAs in p53-induced apoptosis: activation of the vertebrate homologue of the drosophila seven in absentia gene. Proc Natl Acad Sci U S A 1996;93:3953-7.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 3953-3957
    • Amson, R.B.1    Nemani, M.2    Roperch, J.P.3
  • 31
    • 9444262440 scopus 로고    scopus 로고
    • Activation of the human homologue of the Drosophila sina gene in apoptosis and tumor suppression
    • Nemani M, Linares-Cruz G, Bruzzoni-Giovanelli H, et al. Activation of the human homologue of the Drosophila sina gene in apoptosis and tumor suppression. Proc Natl Acad Sci U S A 1996;93:9039-42.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 9039-9042
    • Nemani, M.1    Linares-Cruz, G.2    Bruzzoni-Giovanelli, H.3
  • 32
    • 0033529217 scopus 로고    scopus 로고
    • SIAH-1 promotes apoptosis and tumor suppression through a network involving the regulation of protein folding, unfolding, and trafficking: Identification of common effectors with p53 and p21(Waf1)
    • Roperch JP, Lethrone F, Prieur S, et al. SIAH-1 promotes apoptosis and tumor suppression through a network involving the regulation of protein folding, unfolding, and trafficking: identification of common effectors with p53 and p21(Waf1). Proc Natl Acad Sci U S A 1999;96:8070-3.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 8070-8073
    • Roperch, J.P.1    Lethrone, F.2    Prieur, S.3
  • 33
    • 0028673845 scopus 로고
    • Biological assays for cellular transformation
    • Cox AD, Der CJ. Biological assays for cellular transformation. Methods Enzymol 1994;238:277-94.
    • (1994) Methods Enzymol , vol.238 , pp. 277-294
    • Cox, A.D.1    Der, C.J.2
  • 34
    • 0030819379 scopus 로고    scopus 로고
    • Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo
    • Zufferey R, Nagy D, Mandel RJ, Naldini L, Trono D. Multiply attenuated lentiviral vector achieves efficient gene delivery in vivo. Nat Biotechnol 1997;15:871-5.
    • (1997) Nat Biotechnol , vol.15 , pp. 871-875
    • Zufferey, R.1    Nagy, D.2    Mandel, R.J.3    Naldini, L.4    Trono, D.5
  • 35
    • 0035182556 scopus 로고    scopus 로고
    • In vivo gene transfer to the mouse eye using an HIV-based lentiviral vector; efficient long-term transduction of corneal endothelium and retinal pigment epithelium
    • Bainbridge JW, Stephens C, Parsley K, et al. In vivo gene transfer to the mouse eye using an HIV-based lentiviral vector; efficient long-term transduction of corneal endothelium and retinal pigment epithelium. Gene Ther 2001;8:1665-8.
    • (2001) Gene Ther , vol.8 , pp. 1665-1668
    • Bainbridge, J.W.1    Stephens, C.2    Parsley, K.3
  • 36
    • 0029996147 scopus 로고    scopus 로고
    • In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector
    • Naldini L, Blomer U, Gallay P, et al. In vivo gene delivery and stable transduction of nondividing cells by a lentiviral vector. Science 1996;272:263-7.
    • (1996) Science , vol.272 , pp. 263-267
    • Naldini, L.1    Blomer, U.2    Gallay, P.3
  • 37
    • 33646033137 scopus 로고    scopus 로고
    • A lentiviral RNAi library for human and mouse genes applied to an arrayed viral high-content screen
    • Moffat J, Grueneberg DA, Yang X, et al. A lentiviral RNAi library for human and mouse genes applied to an arrayed viral high-content screen. Cell 2006;124:1283-98.
    • (2006) Cell , vol.124 , pp. 1283-1298
    • Moffat, J.1    Grueneberg, D.A.2    Yang, X.3
  • 38
    • 0034050073 scopus 로고    scopus 로고
    • Heparanase expression in invasive trophoblasts and acute vascular damage
    • Dempsey LA, Plummer TB, Coombes SL, Platt JL. Heparanase expression in invasive trophoblasts and acute vascular damage. Glycobiology 2000;10:467-75.
    • (2000) Glycobiology , vol.10 , pp. 467-475
    • Dempsey, L.A.1    Plummer, T.B.2    Coombes, S.L.3    Platt, J.L.4
  • 41
    • 0023239517 scopus 로고
    • Functional inactivation of genes by dominant negative mutations
    • Herskowitz I. Functional inactivation of genes by dominant negative mutations. Nature 1987;329:219-22.
    • (1987) Nature , vol.329 , pp. 219-222
    • Herskowitz, I.1
  • 42
    • 2942731503 scopus 로고    scopus 로고
    • Siah2 regulates stability of prolyl-hydroxylases, controls HIF1α abundance, and modulates physiological responses to hypoxia
    • Nakayama K, Frew IJ, Hagensen M, et al. Siah2 regulates stability of prolyl-hydroxylases, controls HIF1α abundance, and modulates physiological responses to hypoxia. Cell 2004;117:941-52.
    • (2004) Cell , vol.117 , pp. 941-952
    • Nakayama, K.1    Frew, I.J.2    Hagensen, M.3
  • 43
    • 2342613652 scopus 로고    scopus 로고
    • The proteasome: A suitable antineoplastic target
    • Adams J. The proteasome: a suitable antineoplastic target. Nat Rev Cancer 2004;4:349-60.
    • (2004) Nat Rev Cancer , vol.4 , pp. 349-360
    • Adams, J.1
  • 44
    • 33748991453 scopus 로고    scopus 로고
    • Ubiquitin and ubiquitin-like proteins in cancer pathogenesis
    • Hoeller D, Hecker CM, Dikic I. Ubiquitin and ubiquitin-like proteins in cancer pathogenesis. Nat Rev Cancer 2006;6:776-88.
    • (2006) Nat Rev Cancer , vol.6 , pp. 776-788
    • Hoeller, D.1    Hecker, C.M.2    Dikic, I.3
  • 45
    • 33646345376 scopus 로고    scopus 로고
    • Ubiquitin ligases: Cellcycle control and cancer
    • Nakayama KI, Nakayama K. Ubiquitin ligases: cellcycle control and cancer. Nat Rev Cancer 2006;6:369-81.
    • (2006) Nat Rev Cancer , vol.6 , pp. 369-381
    • Nakayama, K.I.1    Nakayama, K.2
  • 46
    • 13844320703 scopus 로고    scopus 로고
    • Proteasome inhibition in multiple myeloma: Therapeutic implication
    • Chauhan D, Hideshima T, Anderson KC. Proteasome inhibition in multiple myeloma: therapeutic implication. Annu Rev Pharmacol Toxicol 2005;45:465-76.
    • (2005) Annu Rev Pharmacol Toxicol , vol.45 , pp. 465-476
    • Chauhan, D.1    Hideshima, T.2    Anderson, K.C.3
  • 47
    • 33144469102 scopus 로고    scopus 로고
    • The proteasome and proteasome inhibitors in cancer therapy
    • Voorhees PM, Orlowski RZ. The proteasome and proteasome inhibitors in cancer therapy. Annu Rev Pharmacol Toxicol 2006;46:189-213.
    • (2006) Annu Rev Pharmacol Toxicol , vol.46 , pp. 189-213
    • Voorhees, P.M.1    Orlowski, R.Z.2
  • 48
    • 10744221485 scopus 로고    scopus 로고
    • In vivo activation of the p53 pathway by small-molecule antagonists of MDM2
    • Vassilev LT, Vu BT, Graves B, et al. In vivo activation of the p53 pathway by small-molecule antagonists of MDM2. Science 2004;303:844-8.
    • (2004) Science , vol.303 , pp. 844-848
    • Vassilev, L.T.1    Vu, B.T.2    Graves, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.