메뉴 건너뛰기




Volumn 8, Issue 8, 2006, Pages 630-644

Balance of yin and yang: Ubiquitylation-mediated regulation of p53 and c-Myc

Author keywords

c Myc; Oncogenesis; p53; Ubiquitylation; Yin and yang

Indexed keywords

ARF PROTEIN; MYC PROTEIN; NUCLEAR PROTEIN; ONCOPROTEIN; PROTEIN MDM2; PROTEIN P53; S PHASE KINASE ASSOCIATED PROTEIN 2; TUMOR SUPPRESSOR PROTEIN; UBIQUITIN PROTEIN LIGASE; UBIQUITIN PROTEIN LIGASE E3; UBIQUITIN;

EID: 33748522684     PISSN: 15228002     EISSN: 14765586     Source Type: Journal    
DOI: 10.1593/neo.06334     Document Type: Review
Times cited : (69)

References (245)
  • 1
    • 0036561908 scopus 로고    scopus 로고
    • Modelling the molecular circuitry of cancer
    • Hahn WC and Weinberg RA (2002). Modelling the molecular circuitry of cancer. Nat Rev Cancer 2, 331-341.
    • (2002) Nat Rev Cancer , vol.2 , pp. 331-341
    • Hahn, W.C.1    Weinberg, R.A.2
  • 4
    • 0025648762 scopus 로고
    • Germ-line transmission of a mutated p53 gene in a cancer-prone family with Li-Fraumeni syndrome
    • Srivastava S, Zou ZQ, Pirollo K, Blattner W, and Chang EH (1990). Germ-line transmission of a mutated p53 gene in a cancer-prone family with Li-Fraumeni syndrome. Nature 348, 747-749.
    • (1990) Nature , vol.348 , pp. 747-749
    • Srivastava, S.1    Zou, Z.Q.2    Pirollo, K.3    Blattner, W.4    Chang, E.H.5
  • 7
    • 0033986412 scopus 로고    scopus 로고
    • p53 website and analysis of p53 gene mutations in human cancer: Forging a link between epidemiology and carcinogenesis
    • Soussi T, Dehouche K, and Beroud C (2000). p53 website and analysis of p53 gene mutations in human cancer: forging a link between epidemiology and carcinogenesis. Hum Mutat 15, 105-113.
    • (2000) Hum Mutat , vol.15 , pp. 105-113
    • Soussi, T.1    Dehouche, K.2    Beroud, C.3
  • 9
    • 0037075898 scopus 로고    scopus 로고
    • Activation of the p53 tumor suppressor protein
    • Vousden KH (2002). Activation of the p53 tumor suppressor protein. Biochim Biophys Acta 1602, 47-59.
    • (2002) Biochim Biophys Acta , vol.1602 , pp. 47-59
    • Vousden, K.H.1
  • 10
    • 0038075338 scopus 로고    scopus 로고
    • Decision making by p53: Life, death and cancer
    • Oren M (2003). Decision making by p53: life, death and cancer. Cell Death Differ 10, 431-442.
    • (2003) Cell Death Differ , vol.10 , pp. 431-442
    • Oren, M.1
  • 11
    • 0032475878 scopus 로고    scopus 로고
    • Signaling to p53: Breaking the MDM2-p53 circuit
    • Prives C (1998). Signaling to p53: breaking the MDM2-p53 circuit. Cell 95, 5-8.
    • (1998) Cell , vol.95 , pp. 5-8
    • Prives, C.1
  • 12
    • 0037372005 scopus 로고    scopus 로고
    • The codon 72 polymorphic variants of p53 have markedly different apoptotic potential
    • Dumont P, Leu JI, Della Pietra AC III, George DL, and Murphy M (2003). The codon 72 polymorphic variants of p53 have markedly different apoptotic potential. Nat Genet 33, 357-365.
    • (2003) Nat Genet , vol.33 , pp. 357-365
    • Dumont, P.1    Leu, J.I.2    Della Pietra III, A.C.3    George, D.L.4    Murphy, M.5
  • 15
    • 24044506283 scopus 로고    scopus 로고
    • Regulation of DNA damage recognition and nucleotide excision repair: Another role for p53
    • Ford JM (2005). Regulation of DNA damage recognition and nucleotide excision repair: another role for p53. Mutat Res 577, 195-202.
    • (2005) Mutat Res , vol.577 , pp. 195-202
    • Ford, J.M.1
  • 16
    • 0034327504 scopus 로고    scopus 로고
    • Ubiquitin in chains
    • Pickart CM (2000). Ubiquitin in chains. Trends Biochem Sci 25, 544-548.
    • (2000) Trends Biochem Sci , vol.25 , pp. 544-548
    • Pickart, C.M.1
  • 17
    • 3242696232 scopus 로고    scopus 로고
    • Proteolysis-independent regulation of the transcription factor Met4 by a single Lys 48-linked ubiquitin chain
    • Flick K, Ouni I, Wohlschlegel JA, Capati C, McDonald WH, Yates JR, and Kaiser P (2004). Proteolysis-independent regulation of the transcription factor Met4 by a single Lys 48-linked ubiquitin chain. Nat Cell Biol 6, 634-641.
    • (2004) Nat Cell Biol , vol.6 , pp. 634-641
    • Flick, K.1    Ouni, I.2    Wohlschlegel, J.A.3    Capati, C.4    McDonald, W.H.5    Yates, J.R.6    Kaiser, P.7
  • 18
    • 0023339504 scopus 로고
    • Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line
    • Cahilly-Snyder L, Yang-Feng T, Francke U, and George DL (1987). Molecular analysis and chromosomal mapping of amplified genes isolated from a transformed mouse 3T3 cell line. Somat Cell Mol Genet 13, 235-244.
    • (1987) Somat Cell Mol Genet , vol.13 , pp. 235-244
    • Cahilly-Snyder, L.1    Yang-Feng, T.2    Francke, U.3    George, D.L.4
  • 19
    • 0347716455 scopus 로고    scopus 로고
    • MDM2, an introduction
    • Iwakuma T and Lozano G (2003). MDM2, an introduction. Mol Cancer Res 1, 993-1000.
    • (2003) Mol Cancer Res , vol.1 , pp. 993-1000
    • Iwakuma, T.1    Lozano, G.2
  • 20
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J, Marechal V, and Levine AJ (1993). Mapping of the p53 and mdm-2 interaction domains. Mol Cell Biol 13, 4107-4114.
    • (1993) Mol Cell Biol , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 22
    • 0038788827 scopus 로고    scopus 로고
    • Critical contribution of the MDM2 acidic domain to p53 ubiquitination
    • Kawai H, Wiederschain D, and Yuan ZM (2003). Critical contribution of the MDM2 acidic domain to p53 ubiquitination. Mol Cell Biol 23, 4939-4947.
    • (2003) Mol Cell Biol , vol.23 , pp. 4939-4947
    • Kawai, H.1    Wiederschain, D.2    Yuan, Z.M.3
  • 24
    • 0035868386 scopus 로고    scopus 로고
    • The contribution of the acidic domain of MDM2 to p53 and MDM2 stability
    • Argentini M, Barboule N, and Wasylyk B (2001). The contribution of the acidic domain of MDM2 to p53 and MDM2 stability. Oncogene 20, 1267-1275.
    • (2001) Oncogene , vol.20 , pp. 1267-1275
    • Argentini, M.1    Barboule, N.2    Wasylyk, B.3
  • 25
    • 0035839451 scopus 로고    scopus 로고
    • Mdm2 mutant defective in binding p300 promotes ubiquitination but not degradation of p53: Evidence for the role of p300 in integrating ubiquitination and proteolysis
    • Zhu Q, Yao J, Wani G, Wani MA, and Wani AA (2001). Mdm2 mutant defective in binding p300 promotes ubiquitination but not degradation of p53: evidence for the role of p300 in integrating ubiquitination and proteolysis. J Biol Chem 276, 29695-29701.
    • (2001) J Biol Chem , vol.276 , pp. 29695-29701
    • Zhu, Q.1    Yao, J.2    Wani, G.3    Wani, M.A.4    Wani, A.A.5
  • 26
    • 0034708458 scopus 로고    scopus 로고
    • Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53
    • Fang S, Jensen JP, Ludwig RL, Vousden KH, and Weissman AM (2000). Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53. J Biol Chem 275, 8945-8951.
    • (2000) J Biol Chem , vol.275 , pp. 8945-8951
    • Fang, S.1    Jensen, J.P.2    Ludwig, R.L.3    Vousden, K.H.4    Weissman, A.M.5
  • 27
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6
    • Freedman DA and Levine AJ (1998). Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol Cell Biol 18, 7288-7293.
    • (1998) Mol Cell Biol , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 28
    • 0032518917 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein
    • Roth J, Dobbelstein M, Freedman DA, Shenk T, and Levine AJ (1998). Nucleocytoplasmic shuttling of the hdm2 oncoprotein regulates the levels of the p53 protein via a pathway used by the human immunodeficiency virus rev protein. EMBO J 17, 554-564.
    • (1998) EMBO J , vol.17 , pp. 554-564
    • Roth, J.1    Dobbelstein, M.2    Freedman, D.A.3    Shenk, T.4    Levine, A.J.5
  • 29
    • 0034193492 scopus 로고    scopus 로고
    • Contribution of two independent MDM2-binding domains in p14(ARF) to p53 stabilization
    • Lohrum MA, Ashcroft M, Kubbutat MH, and Vousden KH (2000). Contribution of two independent MDM2-binding domains in p14(ARF) to p53 stabilization. Curr Biol 10, 539-542.
    • (2000) Curr Biol , vol.10 , pp. 539-542
    • Lohrum, M.A.1    Ashcroft, M.2    Kubbutat, M.H.3    Vousden, K.H.4
  • 30
    • 0026649648 scopus 로고
    • The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation
    • Momand J, Zambetti GP, Olson DC, George D, and Levine AJ (1992). The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 69, 1237-1245.
    • (1992) Cell , vol.69 , pp. 1237-1245
    • Momand, J.1    Zambetti, G.P.2    Olson, D.C.3    George, D.4    Levine, A.J.5
  • 31
    • 0028678543 scopus 로고
    • The regulation of p53-mediated transcription and the roles of hTAFII31 and mdm-2
    • Lu H, Lin J, Chen J, and Levine AJ (1994). The regulation of p53-mediated transcription and the roles of hTAFII31 and mdm-2. Harvey Lect 90, 81-93.
    • (1994) Harvey Lect , vol.90 , pp. 81-93
    • Lu, H.1    Lin, J.2    Chen, J.3    Levine, A.J.4
  • 32
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R, Tanaka H, and Yasuda H (1997). Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 420, 25-27.
    • (1997) FEBS Lett , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 33
    • 0034282102 scopus 로고    scopus 로고
    • An intact HDM2 RING-finger domain is required for nuclear exclusion of p53
    • Boyd SD, Tsai KY, and Jacks T (2000). An intact HDM2 RING-finger domain is required for nuclear exclusion of p53. Nat Cell Biol 2, 563-568.
    • (2000) Nat Cell Biol , vol.2 , pp. 563-568
    • Boyd, S.D.1    Tsai, K.Y.2    Jacks, T.3
  • 34
    • 0034282220 scopus 로고    scopus 로고
    • The MDM2 RING-finger domain is required to promote p53 nuclear export
    • Geyer RK, Yu ZK, and Maki CG (2000). The MDM2 RING-finger domain is required to promote p53 nuclear export. Nat Cell Biol 2, 569-573.
    • (2000) Nat Cell Biol , vol.2 , pp. 569-573
    • Geyer, R.K.1    Yu, Z.K.2    Maki, C.G.3
  • 36
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao W and Levine AJ (1999). Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc Natl Acad Sci USA 96, 3077-3080.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 37
    • 8844232663 scopus 로고    scopus 로고
    • The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression
    • Minsky N and Oren M (2004). The RING domain of Mdm2 mediates histone ubiquitylation and transcriptional repression. Mol Cell 16, 631-639.
    • (2004) Mol Cell , vol.16 , pp. 631-639
    • Minsky, N.1    Oren, M.2
  • 38
    • 0037163085 scopus 로고    scopus 로고
    • MDM2 inhibits PCAF (p300/CREB-binding protein-associated factor)-mediated p53 acetylation
    • Jin Y, Zeng SX, Dai MS, Yang XJ, and Lu H (2002). MDM2 inhibits PCAF (p300/CREB-binding protein-associated factor)-mediated p53 acetylation. J Biol Chem 277, 30838-30843.
    • (2002) J Biol Chem , vol.277 , pp. 30838-30843
    • Jin, Y.1    Zeng, S.X.2    Dai, M.S.3    Yang, X.J.4    Lu, H.5
  • 40
    • 0027459198 scopus 로고
    • mdm2 expression is induced by wild type p53 activity
    • Barak Y, Juven T, Haffner R, and Oren M (1993). mdm2 expression is induced by wild type p53 activity. EMBO J 12, 461-468.
    • (1993) EMBO J , vol.12 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 41
    • 0027673764 scopus 로고
    • The p53-mdm2 autoregulatory feedback loop: A paradigm for the regulation of growth control by p53?
    • Picksley SM and Lane DP (1993). The p53-mdm2 autoregulatory feedback loop: a paradigm for the regulation of growth control by p53? Bioessays 15, 689-690.
    • (1993) Bioessays , vol.15 , pp. 689-690
    • Picksley, S.M.1    Lane, D.P.2
  • 42
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu X, Bayle JH, Olson D, and Levine AJ (1993). The p53-mdm-2 autoregulatory feedback loop. Genes Dev 7, 1126-1132.
    • (1993) Genes Dev , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 43
    • 0028834902 scopus 로고
    • Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53
    • Jones SN, Roe AE, Donehower LA, and Bradley A (1995). Rescue of embryonic lethality in Mdm2-deficient mice by absence of p53. Nature 378, 206-208.
    • (1995) Nature , vol.378 , pp. 206-208
    • Jones, S.N.1    Roe, A.E.2    Donehower, L.A.3    Bradley, A.4
  • 44
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R, Wagner DS, and Lozano G (1995). Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378, 203-206.
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes De Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 45
    • 2342567852 scopus 로고    scopus 로고
    • Accelerated MDM2 auto-degradation induced by DNA-damage kinases is required for p53 activation
    • Stommel JM and Wahl GM (2004). Accelerated MDM2 auto-degradation induced by DNA-damage kinases is required for p53 activation. EMBO J 23, 1547-1556.
    • (2004) EMBO J , vol.23 , pp. 1547-1556
    • Stommel, J.M.1    Wahl, G.M.2
  • 46
    • 0036517104 scopus 로고    scopus 로고
    • Nuclear degradation of p53 occurs during down-regulation of the p53 response after DNA damage
    • Shirangi TR, Zaika A, and Moll UM (2002). Nuclear degradation of p53 occurs during down-regulation of the p53 response after DNA damage. FASEB J 16, 420-422.
    • (2002) FASEB J , vol.16 , pp. 420-422
    • Shirangi, T.R.1    Zaika, A.2    Moll, U.M.3
  • 47
    • 0042415612 scopus 로고    scopus 로고
    • Nuclear and cytoplasmic degradation of endogenous p53 and HDM2 occurs during downregulation of the p53 response after multiple types of DNA damage
    • Joseph TW, Zaika A, and Moll UM (2003). Nuclear and cytoplasmic degradation of endogenous p53 and HDM2 occurs during downregulation of the p53 response after multiple types of DNA damage. FASEB J 17, 1622-1630.
    • (2003) FASEB J , vol.17 , pp. 1622-1630
    • Joseph, T.W.1    Zaika, A.2    Moll, U.M.3
  • 48
    • 0033767235 scopus 로고    scopus 로고
    • Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome- mediated degradation
    • Rodriguez MS, Desterro JM, Lain S, Lane DP, and Hay RT (2000). Multiple C-terminal lysine residues target p53 for ubiquitin-proteasome-mediated degradation. Mol Cell Biol 20, 8458-8467.
    • (2000) Mol Cell Biol , vol.20 , pp. 8458-8467
    • Rodriguez, M.S.1    Desterro, J.M.2    Lain, S.3    Lane, D.P.4    Hay, R.T.5
  • 54
    • 0034863683 scopus 로고    scopus 로고
    • Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53
    • Parant J, Chavez-Reyes A, Little NA, Yan W, Reinke V, Jochemsen AG, and Lozano G (2001). Rescue of embryonic lethality in Mdm4-null mice by loss of Trp53 suggests a nonoverlapping pathway with MDM2 to regulate p53. Nat Genet 29, 92-95.
    • (2001) Nat Genet , vol.29 , pp. 92-95
    • Parant, J.1    Chavez-Reyes, A.2    Little, N.A.3    Yan, W.4    Reinke, V.5    Jochemsen, A.G.6    Lozano, G.7
  • 55
    • 0042592947 scopus 로고    scopus 로고
    • MDM2 promotes ubiquitination and degradation of MDMX
    • Pan Y and Chen J (2003). MDM2 promotes ubiquitination and degradation of MDMX. Mol Cell Biol 23, 5113-5121.
    • (2003) Mol Cell Biol , vol.23 , pp. 5113-5121
    • Pan, Y.1    Chen, J.2
  • 57
    • 2942558344 scopus 로고    scopus 로고
    • A postubiquitination role for MDM2 and hHR23A in the p53 degradation pathway
    • Brignone C, Bradley KE, Kisselev AF, and Grossman SR (2004). A postubiquitination role for MDM2 and hHR23A in the p53 degradation pathway. Oncogene 23, 4121-4129.
    • (2004) Oncogene , vol.23 , pp. 4121-4129
    • Brignone, C.1    Bradley, K.E.2    Kisselev, A.F.3    Grossman, S.R.4
  • 60
    • 0027358723 scopus 로고
    • The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53
    • Scheffner M, Huibregtse JM, Vierstra RD, and Howley PM (1993). The HPV-16 E6 and E6-AP complex functions as a ubiquitin-protein ligase in the ubiquitination of p53. Cell 75, 495-505.
    • (1993) Cell , vol.75 , pp. 495-505
    • Scheffner, M.1    Huibregtse, J.M.2    Vierstra, R.D.3    Howley, P.M.4
  • 61
    • 0024535228 scopus 로고
    • The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product
    • Dyson N, Howley PM, Munger K, and Harlow E (1989). The human papilloma virus-16 E7 oncoprotein is able to bind to the retinoblastoma gene product. Science 243, 934-937.
    • (1989) Science , vol.243 , pp. 934-937
    • Dyson, N.1    Howley, P.M.2    Munger, K.3    Harlow, E.4
  • 62
    • 0025271203 scopus 로고
    • Association of human papillomavirus types 16 and 18 E6 proteins with p53
    • Werness BA, Levine AJ, and Howley PM (1990). Association of human papillomavirus types 16 and 18 E6 proteins with p53. Science 248, 76-79.
    • (1990) Science , vol.248 , pp. 76-79
    • Werness, B.A.1    Levine, A.J.2    Howley, P.M.3
  • 63
    • 0028939392 scopus 로고
    • Reconstitution of p53-ubiquitinylation reactions from purified components: The role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP)
    • Rolfe M, Beer-Romero P, Glass S, Eckstein J, Berdo I, Theodoras A, Pagano M, and Draetta G (1995). Reconstitution of p53-ubiquitinylation reactions from purified components: the role of human ubiquitin-conjugating enzyme UBC4 and E6-associated protein (E6AP). Proc Natl Acad Sci USA 92, 3264-3268.
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 3264-3268
    • Rolfe, M.1    Beer-Romero, P.2    Glass, S.3    Eckstein, J.4    Berdo, I.5    Theodoras, A.6    Pagano, M.7    Draetta, G.8
  • 64
    • 21244451434 scopus 로고    scopus 로고
    • ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor
    • Chen D, Kon N, Li M, Zhang W, Qin J, and Gu W (2005). ARF-BP1/Mule is a critical mediator of the ARF tumor suppressor. Cell 121, 1071-1083.
    • (2005) Cell , vol.121 , pp. 1071-1083
    • Chen, D.1    Kon, N.2    Li, M.3    Zhang, W.4    Qin, J.5    Gu, W.6
  • 65
    • 22844447871 scopus 로고    scopus 로고
    • The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation
    • Esser C, Scheffner M, and Hohfeld J (2005). The chaperone-associated ubiquitin ligase CHIP is able to target p53 for proteasomal degradation. J Biol Chem 280, 27443-27448.
    • (2005) J Biol Chem , vol.280 , pp. 27443-27448
    • Esser, C.1    Scheffner, M.2    Hohfeld, J.3
  • 66
    • 0027749169 scopus 로고
    • A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein
    • Bargonetti J, Manfredi JJ, Chen X, Marshak DR, and Prives C (1993). A proteolytic fragment from the central region of p53 has marked sequence-specific DNA-binding activity when generated from wild-type but not from oncogenic mutant p53 protein. Genes Dev 7, 2565-2574.
    • (1993) Genes Dev , vol.7 , pp. 2565-2574
    • Bargonetti, J.1    Manfredi, J.J.2    Chen, X.3    Marshak, D.R.4    Prives, C.5
  • 67
    • 0025618980 scopus 로고
    • Mutant p53 DNA clones from human colon carcinomas cooperate with ras in transforming primary rat cells: A comparison nomas of the "hot spot" mutant phenotypes
    • Hinds PW, Finlay CA, Quartin RS, Baker SJ, Fearon ER, Vogelstein B, and Levine AJ (1990). Mutant p53 DNA clones from human colon carcinomas cooperate with ras in transforming primary rat cells: a comparison nomas of the "hot spot" mutant phenotypes. Cell Growth Differ 1, 571-580.
    • (1990) Cell Growth Differ , vol.1 , pp. 571-580
    • Hinds, P.W.1    Finlay, C.A.2    Quartin, R.S.3    Baker, S.J.4    Fearon, E.R.5    Vogelstein, B.6    Levine, A.J.7
  • 68
    • 0025248598 scopus 로고
    • Activating mutations in p53 produce a common conformational effect. A monoclonal antibody specific for the mutant form
    • Gannon JV, Greaves R, Iggo R, and Lane DP (1990). Activating mutations in p53 produce a common conformational effect. A monoclonal antibody specific for the mutant form. EMBO J 9, 1595-1602.
    • (1990) EMBO J , vol.9 , pp. 1595-1602
    • Gannon, J.V.1    Greaves, R.2    Iggo, R.3    Lane, D.P.4
  • 70
    • 0026708148 scopus 로고
    • Mutant conformation of p53. Precise epitope mapping using a filamentous phage epitope library
    • Stephen CW and Lane DP (1992). Mutant conformation of p53. Precise epitope mapping using a filamentous phage epitope library. J Mol Biol 225, 577-583.
    • (1992) J Mol Biol , vol.225 , pp. 577-583
    • Stephen, C.W.1    Lane, D.P.2
  • 71
    • 0033279836 scopus 로고    scopus 로고
    • SCF and Cullin/Ring H2- based ubiquitin ligases
    • Deshaies RJ (1999). SCF and Cullin/Ring H2- based ubiquitin ligases. Annu Rev Cell Dev Biol 15, 435-467.
    • (1999) Annu Rev Cell Dev Biol , vol.15 , pp. 435-467
    • Deshaies, R.J.1
  • 74
    • 0035158586 scopus 로고    scopus 로고
    • Identification of three functions of the adenovirus e4orf6 protein that mediate p53 degradation by the E4orf6-E1B55K complex
    • Querido E, Morrison MR, Chu-Pham-Dang H, Thirlwell SW, Boivin D, and Branton PE (2001). Identification of three functions of the adenovirus e4orf6 protein that mediate p53 degradation by the E4orf6-E1B55K complex. J Virol 75, 699-709.
    • (2001) J Virol , vol.75 , pp. 699-709
    • Querido, E.1    Morrison, M.R.2    Chu-Pham-Dang, H.3    Thirlwell, S.W.4    Boivin, D.5    Branton, P.E.6
  • 75
    • 33746676801 scopus 로고    scopus 로고
    • Cytoplasmic localized ubiquitin ligase cullin 7 binds to p53 and promotes cell growth by antagonizing p53 function
    • March 20 [Epub ahead of print]
    • Andrews P, He YJ, and Xiong Y (2006). Cytoplasmic localized ubiquitin ligase cullin 7 binds to p53 and promotes cell growth by antagonizing p53 function. Oncogene 25, March 20 [Epub ahead of print].
    • (2006) Oncogene , vol.25
    • Andrews, P.1    He, Y.J.2    Xiong, Y.3
  • 76
    • 0037061508 scopus 로고    scopus 로고
    • Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization
    • Li M, Chen D, Shiloh A, Luo J, Nikolaev AY, Qin J, and Gu W (2002). Deubiquitination of p53 by HAUSP is an important pathway for p53 stabilization. Nature 416, 648-653.
    • (2002) Nature , vol.416 , pp. 648-653
    • Li, M.1    Chen, D.2    Shiloh, A.3    Luo, J.4    Nikolaev, A.Y.5    Qin, J.6    Gu, W.7
  • 79
    • 1842421376 scopus 로고    scopus 로고
    • A dynamic role of HAUSP in the p53-Mdm2 pathway
    • Li M, Brooks CL, Kon N, and Gu W (2004). A dynamic role of HAUSP in the p53-Mdm2 pathway. Mol Cell 13, 879-886.
    • (2004) Mol Cell , vol.13 , pp. 879-886
    • Li, M.1    Brooks, C.L.2    Kon, N.3    Gu, W.4
  • 80
    • 0034818446 scopus 로고    scopus 로고
    • Post-translational modifications and activation of p53 by genotoxic stresses
    • Appella E and Anderson CW (2001). Post-translational modifications and activation of p53 by genotoxic stresses. Eur J Biochem 268, 2764-2772.
    • (2001) Eur J Biochem , vol.268 , pp. 2764-2772
    • Appella, E.1    Anderson, C.W.2
  • 81
    • 0346455772 scopus 로고    scopus 로고
    • Posttranslational modification of MDM2
    • Meek DW and Knippschild U (2003). Posttranslational modification of MDM2. Mol Cancer Res 1, 1017-1026.
    • (2003) Mol Cancer Res , vol.1 , pp. 1017-1026
    • Meek, D.W.1    Knippschild, U.2
  • 82
    • 33645293151 scopus 로고    scopus 로고
    • 14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation
    • Jin Y, Dai MS, Lu SZ, Xu Y, Luo Z, Zhao Y, and Lu H (2006). 14-3-3gamma binds to MDMX that is phosphorylated by UV-activated Chk1, resulting in p53 activation. EMBO J 25, 1207-1218.
    • (2006) EMBO J , vol.25 , pp. 1207-1218
    • Jin, Y.1    Dai, M.S.2    Lu, S.Z.3    Xu, Y.4    Luo, Z.5    Zhao, Y.6    Lu, H.7
  • 83
    • 33645290219 scopus 로고    scopus 로고
    • Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3
    • LeBron C, Chen L, Gilkes DM, and Chen J (2006). Regulation of MDMX nuclear import and degradation by Chk2 and 14-3-3. EMBO J 25, 1196-1206.
    • (2006) EMBO J , vol.25 , pp. 1196-1206
    • LeBron, C.1    Chen, L.2    Gilkes, D.M.3    Chen, J.4
  • 85
    • 0035882058 scopus 로고    scopus 로고
    • Deconstructing myc
    • Eisenman RN (2001). Deconstructing myc. Genes Dev 15, 2023-2030.
    • (2001) Genes Dev , vol.15 , pp. 2023-2030
    • Eisenman, R.N.1
  • 86
    • 0036781812 scopus 로고    scopus 로고
    • c-MYC: More than just a matter of life and death
    • Pelengaris S, Khan M, and Evan G (2002). c-MYC: more than just a matter of life and death. Nat Rev Cancer 2, 764-776.
    • (2002) Nat Rev Cancer , vol.2 , pp. 764-776
    • Pelengaris, S.1    Khan, M.2    Evan, G.3
  • 87
    • 0033551388 scopus 로고    scopus 로고
    • New Myc-interacting proteins: A second Myc network emerges
    • Sakamuro D and Prendergast GC (1999). New Myc-interacting proteins: a second Myc network emerges. Oncogene 18, 2942-2954.
    • (1999) Oncogene , vol.18 , pp. 2942-2954
    • Sakamuro, D.1    Prendergast, G.C.2
  • 88
    • 0026665523 scopus 로고
    • Transcriptional activation by the human c-Myc oncoprotein in yeast requires interaction with Max
    • Amati B, Dalton S, Brooks MW, Littlewood TD, Evan GI, and Land H (1992). Transcriptional activation by the human c-Myc oncoprotein in yeast requires interaction with Max. Nature 359, 423-426.
    • (1992) Nature , vol.359 , pp. 423-426
    • Amati, B.1    Dalton, S.2    Brooks, M.W.3    Littlewood, T.D.4    Evan, G.I.5    Land, H.6
  • 89
    • 23144464363 scopus 로고    scopus 로고
    • Transcriptional regulation and transformation by Myc proteins
    • Adhikary S and Eilers M (2005). Transcriptional regulation and transformation by Myc proteins. Nat Rev Mol Cell Biol 6, 635-645.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 635-645
    • Adhikary, S.1    Eilers, M.2
  • 90
    • 0033551393 scopus 로고    scopus 로고
    • The basic region/helix-loop-helix/leucine zipper domain of Myc proto-oncoproteins: Function and regulation
    • Luscher B and Larsson LG (1999). The basic region/helix-loop-helix/ leucine zipper domain of Myc proto-oncoproteins: function and regulation. Oncogene 18, 2955-2966.
    • (1999) Oncogene , vol.18 , pp. 2955-2966
    • Luscher, B.1    Larsson, L.G.2
  • 91
    • 0027408096 scopus 로고
    • Mad: A heterodimeric partner for Max that antagonizes Myc transcriptional activity
    • Ayer DE, Kretzner L, and Eisenman RN (1993). Mad: a heterodimeric partner for Max that antagonizes Myc transcriptional activity. Cell 72, 211-222.
    • (1993) Cell , vol.72 , pp. 211-222
    • Ayer, D.E.1    Kretzner, L.2    Eisenman, R.N.3
  • 92
    • 0027431276 scopus 로고
    • A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation
    • Ayer DE and Eisenman RN (1993). A switch from Myc:Max to Mad:Max heterocomplexes accompanies monocyte/macrophage differentiation. Genes Dev 7, 2110-2119.
    • (1993) Genes Dev , vol.7 , pp. 2110-2119
    • Ayer, D.E.1    Eisenman, R.N.2
  • 96
    • 0037126303 scopus 로고    scopus 로고
    • Myc suppression of the p21(Cip1) Cdk inhibitor influences the outcome of the p53 response to DNA damage
    • Seoane J, Le HV, and Massague J (2002). Myc suppression of the p21(Cip1) Cdk inhibitor influences the outcome of the p53 response to DNA damage. Nature 419, 729-734.
    • (2002) Nature , vol.419 , pp. 729-734
    • Seoane, J.1    Le, H.V.2    Massague, J.3
  • 99
    • 14744297005 scopus 로고    scopus 로고
    • Myc-dependent regulation of ribosomal RNA synthesis during dependent Drosophila development
    • Grewal SS, Li L, Orian A, Eisenman RN, and Edgar BA (2005). Myc-dependent regulation of ribosomal RNA synthesis during dependent Drosophila development. Nat Cell Biol 7, 295-302.
    • (2005) Nat Cell Biol , vol.7 , pp. 295-302
    • Grewal, S.S.1    Li, L.2    Orian, A.3    Eisenman, R.N.4    Edgar, B.A.5
  • 101
    • 0027315650 scopus 로고
    • A null c-myc mutation causes lethality before 10.5 days of gestation in homozygotes and reduced fertility in heterozygous female mice
    • Davis AC, Wims M, Spotts GD, Hann SR, and Bradley A (1993). A null c-myc mutation causes lethality before 10.5 days of gestation in homozygotes and reduced fertility in heterozygous female mice. Genes Dev 7, 671-682.
    • (1993) Genes Dev , vol.7 , pp. 671-682
    • Davis, A.C.1    Wims, M.2    Spotts, G.D.3    Hann, S.R.4    Bradley, A.5
  • 104
    • 0030860849 scopus 로고    scopus 로고
    • Cell-cycle progression is not essential for c-Myc to block differentiation
    • Ryan KM and Birnie GD (1997). Cell-cycle progression is not essential for c-Myc to block differentiation. Oncogene 14, 2835-2843.
    • (1997) Oncogene , vol.14 , pp. 2835-2843
    • Ryan, K.M.1    Birnie, G.D.2
  • 105
    • 0028037187 scopus 로고
    • C-Myc inhibits myogenic differentiation and myoD expression by a mechanism which can be dissociated from cell transformation
    • La Rocca SA, Crouch DH, and Gillespie DA (1994). c-Myc inhibits myogenic differentiation and myoD expression by a mechanism which can be dissociated from cell transformation. Oncogene 9, 3499-3508.
    • (1994) Oncogene , vol.9 , pp. 3499-3508
    • La Rocca, S.A.1    Crouch, D.H.2    Gillespie, D.A.3
  • 106
    • 1642430733 scopus 로고    scopus 로고
    • Myc pathways provoking cell suicide and cancer
    • Nilsson JA and Cleveland JL (2003). Myc pathways provoking cell suicide and cancer. Oncogene 22, 9007-9021.
    • (2003) Oncogene , vol.22 , pp. 9007-9021
    • Nilsson, J.A.1    Cleveland, J.L.2
  • 108
    • 0023020262 scopus 로고
    • The myc oncogene: Its role in transformation and differentiation
    • Cole MD (1986). The myc oncogene: its role in transformation and differentiation. Annu Rev Genet 20, 361-384.
    • (1986) Annu Rev Genet , vol.20 , pp. 361-384
    • Cole, M.D.1
  • 109
    • 0033551374 scopus 로고    scopus 로고
    • MYC oncogenes and human neoplastic disease
    • Nesbit CE, Tersak JM, and Prochownik EV (1999). MYC oncogenes and human neoplastic disease. Oncogene 18, 3004-3016.
    • (1999) Oncogene , vol.18 , pp. 3004-3016
    • Nesbit, C.E.1    Tersak, J.M.2    Prochownik, E.V.3
  • 110
    • 0026096540 scopus 로고
    • Control of c-myc regulation in normal and neoplastic cells
    • Spencer CA and Groudine M (1991). Control of c-myc regulation in normal and neoplastic cells. Adv Cancer Res 56, 1-48.
    • (1991) Adv Cancer Res , vol.56 , pp. 1-48
    • Spencer, C.A.1    Groudine, M.2
  • 111
    • 0021178906 scopus 로고
    • Biological activities of logical v-myc and rearranged c-myc oncogenes in rat fibroblast cells in culture
    • Mougneau E, Lemieux L, Rassoulzadegan M, and Cuzin F (1984). Biological activities of logical v-myc and rearranged c-myc oncogenes in rat fibroblast cells in culture. Proc Natl Acad Sci USA 81, 5758-5762.
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 5758-5762
    • Mougneau, E.1    Lemieux, L.2    Rassoulzadegan, M.3    Cuzin, F.4
  • 112
    • 0023629979 scopus 로고
    • Role of c-myc in the transformation of REF52 cells by viral and cellular oncogenes
    • Kohl NE and Ruley HE (1987). Role of c-myc in the transformation of REF52 cells by viral and cellular oncogenes. Oncogene 2, 41-48.
    • (1987) Oncogene , vol.2 , pp. 41-48
    • Kohl, N.E.1    Ruley, H.E.2
  • 114
    • 0033001621 scopus 로고    scopus 로고
    • Reversible activation of c-Myc in skin: Induction of a complex neoplastic versible phenotype by a single oncogenic lesion
    • Pelengaris S, Littlewood T, Khan M, Elia G, and Evan G (1999). Reversible activation of c-Myc in skin: induction of a complex neoplastic versible phenotype by a single oncogenic lesion. Mol Cell 3, 565-577.
    • (1999) Mol Cell , vol.3 , pp. 565-577
    • Pelengaris, S.1    Littlewood, T.2    Khan, M.3    Elia, G.4    Evan, G.5
  • 115
    • 0033180211 scopus 로고    scopus 로고
    • Reversible tumorigenesis by MYC in hematopoietic lineages
    • Felsher DW and Bishop JM (1999). Reversible tumorigenesis by MYC in hematopoietic lineages. Mol Cell 4, 199-207.
    • (1999) Mol Cell , vol.4 , pp. 199-207
    • Felsher, D.W.1    Bishop, J.M.2
  • 116
    • 0037013147 scopus 로고    scopus 로고
    • Suppression of Myc-induced apoptosis in beta cells exposes multiple oncogenic properties induced of Myc and triggers carcinogenic progression
    • Pelengaris S, Khan M, and Evan GI (2002). Suppression of Myc-induced apoptosis in beta cells exposes multiple oncogenic properties induced of Myc and triggers carcinogenic progression. Cell 109, 321-334.
    • (2002) Cell , vol.109 , pp. 321-334
    • Pelengaris, S.1    Khan, M.2    Evan, G.I.3
  • 117
    • 0030965946 scopus 로고    scopus 로고
    • Regulation of p53 stability by Mdm2
    • Kubbutat MH, Jones SN, and Vousden KH (1997). Regulation of p53 stability by Mdm2. Nature 387, 299-303.
    • (1997) Nature , vol.387 , pp. 299-303
    • Kubbutat, M.H.1    Jones, S.N.2    Vousden, K.H.3
  • 118
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, and Oren M (1997). Mdm2 promotes the rapid degradation of p53. Nature 387, 296-299.
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 119
    • 0021688655 scopus 로고
    • Proteins encoded by the human c-myc oncogene: Differential expression in neoplastic cells
    • Hann SR and Eisenman RN (1984). Proteins encoded by the human c-myc oncogene: differential expression in neoplastic cells. Mol Cell Biol 4, 2486-2497.
    • (1984) Mol Cell Biol , vol.4 , pp. 2486-2497
    • Hann, S.R.1    Eisenman, R.N.2
  • 121
    • 3543060464 scopus 로고    scopus 로고
    • myc boxes, which are conserved in myc family proteins, are signals for protein degradation via the proteasome
    • Flinn EM, Busch CM, and Wright AP (1998). myc boxes, which are conserved in myc family proteins, are signals for protein degradation via the proteasome. Mol Cell Biol 18, 5961-5969.
    • (1998) Mol Cell Biol , vol.18 , pp. 5961-5969
    • Flinn, E.M.1    Busch, C.M.2    Wright, A.P.3
  • 123
    • 0034724166 scopus 로고    scopus 로고
    • Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis
    • Salghetti SE, Muratani M, Wijnen H, Futcher B, and Tansey WP (2000). Functional overlap of sequences that activate transcription and signal ubiquitin-mediated proteolysis. Proc Natl Acad Sci USA 97, 3118-3123.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3118-3123
    • Salghetti, S.E.1    Muratani, M.2    Wijnen, H.3    Futcher, B.4    Tansey, W.P.5
  • 124
    • 0037335034 scopus 로고    scopus 로고
    • How the ubiquitin-proteasome system controls transcription
    • Muratani M and Tansey WP (2003). How the ubiquitin-proteasome system controls transcription. Nat Rev Mol Cell Biol 4, 192-201.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , pp. 192-201
    • Muratani, M.1    Tansey, W.P.2
  • 125
    • 0033081027 scopus 로고    scopus 로고
    • Destruction of Myc by ubiquitin-mediated proteolysis: Cancer-associated and transforming mutations stabilize Myc
    • Salghetti SE, Kim SY, and Tansey WP (1999). Destruction of Myc by ubiquitin-mediated proteolysis: cancer-associated and transforming mutations stabilize Myc. EMBO J 18, 717-726.
    • (1999) EMBO J , vol.18 , pp. 717-726
    • Salghetti, S.E.1    Kim, S.Y.2    Tansey, W.P.3
  • 126
    • 0034059667 scopus 로고    scopus 로고
    • c-Myc proteolysis by the ubiquitin-proteasome pathway: Stabilization of c-Myc in Burkitt's lymphoma cells
    • Gregory MA and Hann SR (2000). c-Myc proteolysis by the ubiquitin-proteasome pathway: stabilization of c-Myc in Burkitt's lymphoma cells. Mol Cell Biol 20, 2423-2435.
    • (2000) Mol Cell Biol , vol.20 , pp. 2423-2435
    • Gregory, M.A.1    Hann, S.R.2
  • 127
    • 0031037987 scopus 로고    scopus 로고
    • Identification of downstream-initiated c-Myc proteins which are dominant-negative inhibitors of transactivation by full-length c-Myc proteins
    • Spotts GD, Patel SV, Xiao Q, and Hann SR (1997). Identification of downstream-initiated c-Myc proteins which are dominant-negative inhibitors of transactivation by full-length c-Myc proteins. Mol Cell Biol 17, 1459-1468.
    • (1997) Mol Cell Biol , vol.17 , pp. 1459-1468
    • Spotts, G.D.1    Patel, S.V.2    Xiao, Q.3    Hann, S.R.4
  • 129
    • 2342513572 scopus 로고    scopus 로고
    • Implication of the ubiquitin/proteasome system in Myc-regulated transcription
    • von der Lehr N, Johansson S, and Larsson LG (2003). Implication of the ubiquitin/proteasome system in Myc-regulated transcription. Cell Cycle 2, 403-407.
    • (2003) Cell Cycle , vol.2 , pp. 403-407
    • Von Der Lehr, N.1    Johansson, S.2    Larsson, L.G.3
  • 133
    • 2942650133 scopus 로고    scopus 로고
    • The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation
    • Welcker M, Orian A, Jin J, Grim JE, Harper JW, Eisenman RN, and Clurman BE (2004). The Fbw7 tumor suppressor regulates glycogen synthase kinase 3 phosphorylation-dependent c-Myc protein degradation. Proc Natl Acad Sci USA 101, 9085-9090.
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 9085-9090
    • Welcker, M.1    Orian, A.2    Jin, J.3    Grim, J.E.4    Harper, J.W.5    Eisenman, R.N.6    Clurman, B.E.7
  • 134
    • 6944227551 scopus 로고    scopus 로고
    • A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size
    • Welcker M, Orian A, Grim JE, Eisenman RN, and Clurman BE (2004). A nucleolar isoform of the Fbw7 ubiquitin ligase regulates c-Myc and cell size. Curr Biol 14, 1852-1857.
    • (2004) Curr Biol , vol.14 , pp. 1852-1857
    • Welcker, M.1    Orian, A.2    Grim, J.E.3    Eisenman, R.N.4    Clurman, B.E.5
  • 135
  • 136
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh SY, Ikeda M, Taya Y, and Prives C (1997). DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91, 325-334.
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 137
    • 0034688263 scopus 로고    scopus 로고
    • Cooperative phosphorylation at multiple sites is required to activate p53 in response to UV radiation
    • Kapoor M, Hamm R, Yan W, Taya Y, and Lozano G (2000). Cooperative phosphorylation at multiple sites is required to activate p53 in response to UV radiation. Oncogene 19, 358-364.
    • (2000) Oncogene , vol.19 , pp. 358-364
    • Kapoor, M.1    Hamm, R.2    Yan, W.3    Taya, Y.4    Lozano, G.5
  • 139
    • 0034142325 scopus 로고    scopus 로고
    • Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53
    • Chehab NH, Malikzay A, Appel M, and Halazonetis TD (2000). Chk2/hCds1 functions as a DNA damage checkpoint in G(1) by stabilizing p53. Genes Dev 14, 278-288.
    • (2000) Genes Dev , vol.14 , pp. 278-288
    • Chehab, N.H.1    Malikzay, A.2    Appel, M.3    Halazonetis, T.D.4
  • 140
    • 0347695988 scopus 로고    scopus 로고
    • Phosphorylation by glycogen synthase kinase-3 controls c-myc proteolysis and subnuclear localization
    • Gregory MA, Qi Y, and Hann SR (2003). Phosphorylation by glycogen synthase kinase-3 controls c-myc proteolysis and subnuclear localization. J Biol Chem 278, 51606-51612.
    • (2003) J Biol Chem , vol.278 , pp. 51606-51612
    • Gregory, M.A.1    Qi, Y.2    Hann, S.R.3
  • 141
    • 0034037132 scopus 로고    scopus 로고
    • The c-Myc transactivation domain is a direct modulator of apoptotic versus proliferative signals
    • Chang DW, Claassen GF, Hann SR, and Cole MD (2000). The c-Myc transactivation domain is a direct modulator of apoptotic versus proliferative signals. Mol Cell Biol 20, 4309-4319.
    • (2000) Mol Cell Biol , vol.20 , pp. 4309-4319
    • Chang, D.W.1    Claassen, G.F.2    Hann, S.R.3    Cole, M.D.4
  • 142
    • 0028023421 scopus 로고
    • Hierarchical phosphorylation at N-terminal transformation-sensitive sites in c-Myc protein is regulated by mitogens and in mitosis
    • Lutterbach B and Hann SR (1994). Hierarchical phosphorylation at N-terminal transformation-sensitive sites in c-Myc protein is regulated by mitogens and in mitosis. Mol Cell Biol 14, 5510-5522.
    • (1994) Mol Cell Biol , vol.14 , pp. 5510-5522
    • Lutterbach, B.1    Hann, S.R.2
  • 143
    • 0034306997 scopus 로고    scopus 로고
    • Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability
    • Sears R, Nuckolls F, Haura E, Taya Y, Tamai K, and Nevins JR (2000). Multiple Ras-dependent phosphorylation pathways regulate Myc protein stability. Genes Dev 14, 2501-2514.
    • (2000) Genes Dev , vol.14 , pp. 2501-2514
    • Sears, R.1    Nuckolls, F.2    Haura, E.3    Taya, Y.4    Tamai, K.5    Nevins, J.R.6
  • 147
    • 0029176520 scopus 로고
    • The amino-terminal phosphorylation sites of C-MYC are frequently mutated in Burkitt's lymphoma lines but not in mouse plasmacytomas and rat immunocytomas
    • Axelson H, Henriksson M, Wang Y, Magnusson KP, and Klein G (1995). The amino-terminal phosphorylation sites of C-MYC are frequently mutated in Burkitt's lymphoma lines but not in mouse plasmacytomas and rat immunocytomas. Eur J Cancer 31A, 2099-2104.
    • (1995) Eur J Cancer , vol.31 A , pp. 2099-2104
    • Axelson, H.1    Henriksson, M.2    Wang, Y.3    Magnusson, K.P.4    Klein, G.5
  • 148
    • 0028055178 scopus 로고
    • Ongoing mutations in the N-terminal domain of c-Myc affect transactivation in Burkitt's lymphoma cell lines
    • Albert T, Urlbauer B, Kohlhuber F, Hammersen B, and Eick D (1994). Ongoing mutations in the N-terminal domain of c-Myc affect transactivation in Burkitt's lymphoma cell lines. Oncogene 9, 759-763.
    • (1994) Oncogene , vol.9 , pp. 759-763
    • Albert, T.1    Urlbauer, B.2    Kohlhuber, F.3    Hammersen, B.4    Eick, D.5
  • 149
    • 0027275755 scopus 로고
    • Point mutations in the c-Myc transactivation domain are common in Burkitt's lymphoma and mouse plasmacytomas
    • Bhatia K, Huppi K, Spangler G, Siwarski D, Iyer R, and Magrath I (1993). Point mutations in the c-Myc transactivation domain are common in Burkitt's lymphoma and mouse plasmacytomas. Nat Genet 5, 56-61.
    • (1993) Nat Genet , vol.5 , pp. 56-61
    • Bhatia, K.1    Huppi, K.2    Spangler, G.3    Siwarski, D.4    Iyer, R.5    Magrath, I.6
  • 150
    • 0034653998 scopus 로고    scopus 로고
    • c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover
    • Bahram F, von der Lehr N, Cetinkaya C, and Larsson LG (2000). c-Myc hot spot mutations in lymphomas result in inefficient ubiquitination and decreased proteasome-mediated turnover. Blood 95, 2104-2110.
    • (2000) Blood , vol.95 , pp. 2104-2110
    • Bahram, F.1    Von Der Lehr, N.2    Cetinkaya, C.3    Larsson, L.G.4
  • 152
    • 26444480631 scopus 로고    scopus 로고
    • Mechanisms of tumor suppression by the SCF(Fbw7)
    • Minella AC and Clurman BE (2005). Mechanisms of tumor suppression by the SCF(Fbw7). Cell Cycle 4, 1356-1359.
    • (2005) Cell Cycle , vol.4 , pp. 1356-1359
    • Minella, A.C.1    Clurman, B.E.2
  • 153
    • 0035395872 scopus 로고    scopus 로고
    • The ATM-related domain of TRRAP is required for histone acetyltransferase recruitment and Myc-dependent oncogenesis
    • Park J, Kunjibettu S, McMahon SB, and Cole MD (2001). The ATM-related domain of TRRAP is required for histone acetyltransferase recruitment and Myc-dependent oncogenesis. Genes Dev 15, 1619-1624.
    • (2001) Genes Dev , vol.15 , pp. 1619-1624
    • Park, J.1    Kunjibettu, S.2    McMahon, S.B.3    Cole, M.D.4
  • 154
    • 0033970431 scopus 로고    scopus 로고
    • The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc
    • McMahon SB, Wood MA, and Cole MD (2000). The essential cofactor TRRAP recruits the histone acetyltransferase hGCN5 to c-Myc. Mol Cell Biol 20, 556-562.
    • (2000) Mol Cell Biol , vol.20 , pp. 556-562
    • McMahon, S.B.1    Wood, M.A.2    Cole, M.D.3
  • 155
    • 0035881472 scopus 로고    scopus 로고
    • Binding of c-Myc to chromatin mediates mitogen-induced acetylation of histone H4 and gene activation
    • Frank SR, Schroeder M, Fernandez P, Taubert S, and Amati B (2001). Binding of c-Myc to chromatin mediates mitogen-induced acetylation of histone H4 and gene activation. Genes Dev 15, 2069-2082.
    • (2001) Genes Dev , vol.15 , pp. 2069-2082
    • Frank, S.R.1    Schroeder, M.2    Fernandez, P.3    Taubert, S.4    Amati, B.5
  • 156
    • 0035881691 scopus 로고    scopus 로고
    • Regulation of cyclin D2 gene expression by the Myc/Max/Mad network: Myc-dependent TRRAP recruitment and histone acetylation at the cyclin D2 promoter
    • Bouchard C, Dittrich O, Kiermaier A, Dohmann K, Menkel A, Eilers M, and Luscher B (2001). Regulation of cyclin D2 gene expression by the Myc/Max/Mad network: Myc-dependent TRRAP recruitment and histone acetylation at the cyclin D2 promoter. Genes Dev 15, 2042-2047.
    • (2001) Genes Dev , vol.15 , pp. 2042-2047
    • Bouchard, C.1    Dittrich, O.2    Kiermaier, A.3    Dohmann, K.4    Menkel, A.5    Eilers, M.6    Luscher, B.7
  • 157
    • 0033859666 scopus 로고    scopus 로고
    • An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc
    • Wood MA, McMahon SB, and Cole MD (2000). An ATPase/helicase complex is an essential cofactor for oncogenic transformation by c-Myc. Mol Cell 5, 321-330.
    • (2000) Mol Cell , vol.5 , pp. 321-330
    • Wood, M.A.1    McMahon, S.B.2    Cole, M.D.3
  • 158
  • 159
    • 0035979738 scopus 로고    scopus 로고
    • Regulation of transcriptional activation domain function by ubiquitin
    • Salghetti SE, Caudy AA, Chenoweth JG, and Tansey WP (2001). Regulation of transcriptional activation domain function by ubiquitin. Science 293, 1651-1653.
    • (2001) Science , vol.293 , pp. 1651-1653
    • Salghetti, S.E.1    Caudy, A.A.2    Chenoweth, J.G.3    Tansey, W.P.4
  • 160
    • 0035947238 scopus 로고    scopus 로고
    • The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II
    • Ferdous A, Gonzalez F, Sun L, Kodadek T, and Johnston SA (2001). The 19S regulatory particle of the proteasome is required for efficient transcription elongation by RNA polymerase II. Mol Cell 7, 981-991.
    • (2001) Mol Cell , vol.7 , pp. 981-991
    • Ferdous, A.1    Gonzalez, F.2    Sun, L.3    Kodadek, T.4    Johnston, S.A.5
  • 161
    • 0037134015 scopus 로고    scopus 로고
    • Recruitment of a 19S proteasome subcomplex to an activated promoter
    • Gonzalez F, Delahodde A, Kodadek T, and Johnston SA (2002). Recruitment of a 19S proteasome subcomplex to an activated promoter. Science 296, 548-550.
    • (2002) Science , vol.296 , pp. 548-550
    • Gonzalez, F.1    Delahodde, A.2    Kodadek, T.3    Johnston, S.A.4
  • 162
    • 0345276485 scopus 로고    scopus 로고
    • Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation
    • Itahana K, Bhat KP, Jin A, Itahana Y, Hawke D, Kobayashi R, and Zhang Y (2003). Tumor suppressor ARF degrades B23, a nucleolar protein involved in ribosome biogenesis and cell proliferation. Mol Cell 12, 1151-1164.
    • (2003) Mol Cell , vol.12 , pp. 1151-1164
    • Itahana, K.1    Bhat, K.P.2    Jin, A.3    Itahana, Y.4    Hawke, D.5    Kobayashi, R.6    Zhang, Y.7
  • 163
    • 0037291204 scopus 로고    scopus 로고
    • Nucleolar Arf tumor suppressor inhibits ribosomal RNA processing
    • Sugimoto M, Kuo ML, Roussel MF, and Sherr CJ (2003). Nucleolar Arf tumor suppressor inhibits ribosomal RNA processing. Mol Cell 11, 415-424.
    • (2003) Mol Cell , vol.11 , pp. 415-424
    • Sugimoto, M.1    Kuo, M.L.2    Roussel, M.F.3    Sherr, C.J.4
  • 165
    • 0034915032 scopus 로고    scopus 로고
    • Control of p53 ubiquitination and nuclear export by MDM2 and ARF
    • Zhang Y and Xiong Y (2001). Control of p53 ubiquitination and nuclear export by MDM2 and ARF. Cell Growth Differ 12, 175-186.
    • (2001) Cell Growth Differ , vol.12 , pp. 175-186
    • Zhang, Y.1    Xiong, Y.2
  • 166
    • 0032549711 scopus 로고    scopus 로고
    • ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways
    • Zhang Y, Xiong Y, and Yarbrough WG (1998). ARF promotes MDM2 degradation and stabilizes p53: ARF-INK4a locus deletion impairs both the Rb and p53 tumor suppression pathways. Cell 92, 725-734.
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 167
    • 0032504784 scopus 로고    scopus 로고
    • p19 ARF links the tumour suppressor p53 to Ras
    • Palmero I, Pantoja C, and Serrano M (1998). p19 ARF links the tumour suppressor p53 to Ras. Nature 395, 125-126.
    • (1998) Nature , vol.395 , pp. 125-126
    • Palmero, I.1    Pantoja, C.2    Serrano, M.3
  • 169
    • 0033536063 scopus 로고    scopus 로고
    • P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2
    • Tao W and Levine AJ (1999). P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2. Proc Natl Acad Sci USA 96, 6937-6941.
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6937-6941
    • Tao, W.1    Levine, A.J.2
  • 170
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • Honda R and Yasuda H (1999). Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. EMBO J 18, 22-27.
    • (1999) EMBO J , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 175
    • 21244472965 scopus 로고    scopus 로고
    • Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis
    • Zhong Q, Gao W, Du F, and Wang X (2005). Mule/ARF-BP1, a BH3-only E3 ubiquitin ligase, catalyzes the polyubiquitination of Mcl-1 and regulates apoptosis. Cell 121, 1085-1095.
    • (2005) Cell , vol.121 , pp. 1085-1095
    • Zhong, Q.1    Gao, W.2    Du, F.3    Wang, X.4
  • 176
    • 0028225081 scopus 로고
    • Cloning of a DNA binding protein that is a tyrosine kinase substrate and recognizes an upstream initiator-like sequence in the promoter of the preprodynorphin gene
    • Gu J, Ren K, Dubner R, and Iadarola MJ (1994). Cloning of a DNA binding protein that is a tyrosine kinase substrate and recognizes an upstream initiator-like sequence in the promoter of the preprodynorphin gene. Brain Res Mol Brain Res 24, 77-88.
    • (1994) Brain Res Mol Brain Res , vol.24 , pp. 77-88
    • Gu, J.1    Ren, K.2    Dubner, R.3    Iadarola, M.J.4
  • 177
    • 31544457877 scopus 로고    scopus 로고
    • p53 ubiquitination: Mdm2 and beyond
    • Brooks CL and Gu W (2006). p53 ubiquitination: Mdm2 and beyond. Mol Cell 21, 307-315.
    • (2006) Mol Cell , vol.21 , pp. 307-315
    • Brooks, C.L.1    Gu, W.2
  • 180
    • 0033912841 scopus 로고    scopus 로고
    • Bop1 is a mouse WD40 repeat nucleolar protein involved in 28S and 5.8S RRNA processing and 60S ribosome biogenesis
    • Strezoska Z, Pestov DG, and Lau LF (2000). Bop1 is a mouse WD40 repeat nucleolar protein involved in 28S and 5.8S RRNA processing and 60S ribosome biogenesis. Mol Cell Biol 20, 5516-5528.
    • (2000) Mol Cell Biol , vol.20 , pp. 5516-5528
    • Strezoska, Z.1    Pestov, D.G.2    Lau, L.F.3
  • 181
    • 0037119468 scopus 로고    scopus 로고
    • Functional inactivation of the mouse nucleolar protein Bop1 inhibits multiple steps in pre-rRNA processing and blocks cell cycle progression
    • Strezoska Z, Pestov DG, and Lau LF (2002). Functional inactivation of the mouse nucleolar protein Bop1 inhibits multiple steps in pre-rRNA processing and blocks cell cycle progression. J Biol Chem 277, 29617-29625.
    • (2002) J Biol Chem , vol.277 , pp. 29617-29625
    • Strezoska, Z.1    Pestov, D.G.2    Lau, L.F.3
  • 182
    • 0034977001 scopus 로고    scopus 로고
    • Evidence of p53-dependent cross-talk between ribosome biogenesis and the cell cycle: Effects of nucleolar protein Bop1 on G(1)/S transition
    • Pestov DG, Strezoska Z, and Lau LF (2001). Evidence of p53-dependent cross-talk between ribosome biogenesis and the cell cycle: effects of nucleolar protein Bop1 on G(1)/S transition. Mol Cell Biol 21, 4246-4255.
    • (2001) Mol Cell Biol , vol.21 , pp. 4246-4255
    • Pestov, D.G.1    Strezoska, Z.2    Lau, L.F.3
  • 183
    • 0034003005 scopus 로고    scopus 로고
    • Stress signals utilize multiple pathways to stabilize p53
    • Ashcroft M, Taya Y, and Vousden KH (2000). Stress signals utilize multiple pathways to stabilize p53. Mol Cell Biol 20, 3224-3233.
    • (2000) Mol Cell Biol , vol.20 , pp. 3224-3233
    • Ashcroft, M.1    Taya, Y.2    Vousden, K.H.3
  • 184
    • 29144438951 scopus 로고    scopus 로고
    • Inactivation of S6 ribosomal protein gene in T lymphocytes activates a p53-dependent checkpoint response
    • Sulic S, Panic L, Barkic M, Mercep M, Uzelac M, and Volarevic S (2005). Inactivation of S6 ribosomal protein gene in T lymphocytes activates a
    • (2005) Genes Dev , vol.19 , pp. 3070-3082
    • Sulic, S.1    Panic, L.2    Barkic, M.3    Mercep, M.4    Uzelac, M.5    Volarevic, S.6
  • 186
    • 0033020147 scopus 로고    scopus 로고
    • Regulation of p53 function and stability by phosphorylation
    • Ashcroft M, Kubbutat MH, and Vousden KH (1999). Regulation of p53 function and stability by phosphorylation. Mol Cell Biol 19, 1751-1758.
    • (1999) Mol Cell Biol , vol.19 , pp. 1751-1758
    • Ashcroft, M.1    Kubbutat, M.H.2    Vousden, K.H.3
  • 187
    • 7244238177 scopus 로고    scopus 로고
    • Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5
    • Dai MS and Lu H (2004). Inhibition of MDM2-mediated p53 ubiquitination and degradation by ribosomal protein L5. J Biol Chem 279, 44475-44482.
    • (2004) J Biol Chem , vol.279 , pp. 44475-44482
    • Dai, M.S.1    Lu, H.2
  • 188
    • 4344685939 scopus 로고    scopus 로고
    • Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition
    • Dai MS, Zeng SX, Jin Y, Sun XX, David L, and Lu H (2004). Ribosomal protein L23 activates p53 by inhibiting MDM2 function in response to ribosomal perturbation but not to translation inhibition. Mol Cell Biol 24, 7654-7668.
    • (2004) Mol Cell Biol , vol.24 , pp. 7654-7668
    • Dai, M.S.1    Zeng, S.X.2    Jin, Y.3    Sun, X.X.4    David, L.5    Lu, H.6
  • 189
    • 0242721592 scopus 로고    scopus 로고
    • Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway
    • Zhang Y, Wolf GW, Bhat K, Jin A, Allio T, Burkhart WA, and Xiong Y (2003). Ribosomal protein L11 negatively regulates oncoprotein MDM2 and mediates a p53-dependent ribosomal-stress checkpoint pathway. Mol Cell Biol 23, 8902-8912.
    • (2003) Mol Cell Biol , vol.23 , pp. 8902-8912
    • Zhang, Y.1    Wolf, G.W.2    Bhat, K.3    Jin, A.4    Allio, T.5    Burkhart, W.A.6    Xiong, Y.7
  • 191
    • 4344660471 scopus 로고    scopus 로고
    • Inhibition of HDM2 and activation of p53 by ribosomal protein L23
    • Jin A, Itahana K, O'Keefe K, and Zhang Y (2004). Inhibition of HDM2 and activation of p53 by ribosomal protein L23. Mol Cell Biol 24, 7669-7680.
    • (2004) Mol Cell Biol , vol.24 , pp. 7669-7680
    • Jin, A.1    Itahana, K.2    O'Keefe, K.3    Zhang, Y.4
  • 192
    • 3242715867 scopus 로고    scopus 로고
    • Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation
    • Bhat KP, Itahana K, Jin A, and Zhang Y (2004). Essential role of ribosomal protein L11 in mediating growth inhibition-induced p53 activation. EMBO J 23, 2402-2412.
    • (2004) EMBO J , vol.23 , pp. 2402-2412
    • Bhat, K.P.1    Itahana, K.2    Jin, A.3    Zhang, Y.4
  • 194
    • 0032917157 scopus 로고    scopus 로고
    • Nucleolar protein B23 has molecular chaperone activities
    • Szebeni A and Olson MO (1999). Nucleolar protein B23 has molecular chaperone activities. Protein Sci 8, 905-912.
    • (1999) Protein Sci , vol.8 , pp. 905-912
    • Szebeni, A.1    Olson, M.O.2
  • 195
    • 0032189707 scopus 로고    scopus 로고
    • Preferential cleavage in pre-ribosomal RNA byprotein B23 endoribonuclease
    • Savkur RS and Olson MO (1998). Preferential cleavage in pre-ribosomal RNA byprotein B23 endoribonuclease. Nucleic Acids Res 26, 4508-4515.
    • (1998) Nucleic Acids Res , vol.26 , pp. 4508-4515
    • Savkur, R.S.1    Olson, M.O.2
  • 196
    • 2342491487 scopus 로고    scopus 로고
    • Nucleolar protein NPM interacts with HDM2 and protects tumor suppressor protein p53 from HDM2-mediated degradation
    • Kurki S, Peltonen K, Latonen L, Kiviharju TM, Ojala PM, Meek D, and Laiho M (2004). Nucleolar protein NPM interacts with HDM2 and protects tumor suppressor protein p53 from HDM2-mediated degradation. Cancer Cell 5, 465-475.
    • (2004) Cancer Cell , vol.5 , pp. 465-475
    • Kurki, S.1    Peltonen, K.2    Latonen, L.3    Kiviharju, T.M.4    Ojala, P.M.5    Meek, D.6    Laiho, M.7
  • 197
    • 0036302062 scopus 로고    scopus 로고
    • Nucleophosmin regulates the stability and transcriptional activity of p53
    • Colombo E, Marine JC, Danovi D, Falini B, and Pelicci PG (2002). Nucleophosmin regulates the stability and transcriptional activity of p53. Nat Cell Biol 4, 529-533.
    • (2002) Nat Cell Biol , vol.4 , pp. 529-533
    • Colombo, E.1    Marine, J.C.2    Danovi, D.3    Falini, B.4    Pelicci, P.G.5
  • 198
    • 0344011603 scopus 로고    scopus 로고
    • Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses
    • Rubbi CP and Milner J (2003). Disruption of the nucleolus mediates stabilization of p53 in response to DNA damage and other stresses. EMBO J 22, 6068-6077.
    • (2003) EMBO J , vol.22 , pp. 6068-6077
    • Rubbi, C.P.1    Milner, J.2
  • 199
    • 0030063697 scopus 로고    scopus 로고
    • Quantitation of the nucleophosmin/B23-translocation using imaging analysis
    • Chan PK, Qi Y, Amley J, and Koller CA (1996). Quantitation of the nucleophosmin/B23-translocation using imaging analysis. Cancer Lett 100, 191-197.
    • (1996) Cancer Lett , vol.100 , pp. 191-197
    • Chan, P.K.1    Qi, Y.2    Amley, J.3    Koller, C.A.4
  • 200
    • 1942471135 scopus 로고    scopus 로고
    • At the crossroads of growth control; making ribosomal RNA
    • Moss T (2004). At the crossroads of growth control; making ribosomal RNA. Curr Opin Genet Dev 14, 210-217.
    • (2004) Curr Opin Genet Dev , vol.14 , pp. 210-217
    • Moss, T.1
  • 201
    • 5444237797 scopus 로고    scopus 로고
    • What better measure than ribosome synthesis?
    • Rudra D and Warner JR (2004). What better measure than ribosome synthesis? Genes Dev 18, 2431-2436.
    • (2004) Genes Dev , vol.18 , pp. 2431-2436
    • Rudra, D.1    Warner, J.R.2
  • 204
    • 11244281646 scopus 로고    scopus 로고
    • RNA polymerases I and III, growth control and cancer
    • White RJ (2005). RNA polymerases I and III, growth control and cancer. Nat Rev Mol Cell Biol 6, 69-78.
    • (2005) Nat Rev Mol Cell Biol , vol.6 , pp. 69-78
    • White, R.J.1
  • 205
    • 0037363075 scopus 로고    scopus 로고
    • Does the ribosome translate cancer?
    • Ruggero D and Pandolfi PP (2003). Does the ribosome translate cancer? Nat Rev Cancer 3, 179-192.
    • (2003) Nat Rev Cancer , vol.3 , pp. 179-192
    • Ruggero, D.1    Pandolfi, P.P.2
  • 206
    • 0037197962 scopus 로고    scopus 로고
    • Characterization of the c-MYC-regulated transcriptome by SAGE: Identification and analysis of c-MYC target genes
    • Menssen A and Hermeking H (2002). Characterization of the c-MYC-regulated transcriptome by SAGE: identification and analysis of c-MYC target genes. Proc Natl Acad Sci USA 99, 6274-6279.
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6274-6279
    • Menssen, A.1    Hermeking, H.2
  • 207
    • 0034724389 scopus 로고    scopus 로고
    • Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, arrays signaling, and adhesion
    • Coller HA, Grandori C, Tamayo P, Colbert T, Lander ES, Eisenman RN, and Golub TR (2000). Expression analysis with oligonucleotide microarrays reveals that MYC regulates genes involved in growth, cell cycle, arrays signaling, and adhesion. Proc Natl Acad Sci USA 97, 3260-3265.
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3260-3265
    • Coller, H.A.1    Grandori, C.2    Tamayo, P.3    Colbert, T.4    Lander, E.S.5    Eisenman, R.N.6    Golub, T.R.7
  • 210
    • 0347721764 scopus 로고    scopus 로고
    • Direct activation of RNA polymerase III transcription by c-Myc
    • Gomez-Roman N, Grandori C, Eisenman RN, and White RJ (2003). Direct activation of RNA polymerase III transcription by c-Myc. Nature 421, 290-294.
    • (2003) Nature , vol.421 , pp. 290-294
    • Gomez-Roman, N.1    Grandori, C.2    Eisenman, R.N.3    White, R.J.4
  • 212
    • 0027498314 scopus 로고
    • The mdm-2 oncogene can overcome wild-type p53 suppression of transformed cell growth
    • Finlay CA (1993). The mdm-2 oncogene can overcome wild-type p53 suppression of transformed cell growth. Mol Cell Biol 13, 301-306.
    • (1993) Mol Cell Biol , vol.13 , pp. 301-306
    • Finlay, C.A.1
  • 213
    • 0025853776 scopus 로고
    • Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line
    • Fakharzadeh SS, Trusko SP, and George DL (1991). Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line. EMBO J 10, 1565-1569.
    • (1991) EMBO J , vol.10 , pp. 1565-1569
    • Fakharzadeh, S.S.1    Trusko, S.P.2    George, D.L.3
  • 217
    • 0345824732 scopus 로고    scopus 로고
    • Cell cycle regulatory functions of the human oncoprotein MDM2
    • Deb SP (2003). Cell cycle regulatory functions of the human oncoprotein MDM2. Mol Cancer Res 1, 1009-1016.
    • (2003) Mol Cancer Res , vol.1 , pp. 1009-1016
    • Deb, S.P.1
  • 219
    • 0029914660 scopus 로고    scopus 로고
    • Overexpression of the MDM2 oncogene in leukemia and lymphoma
    • color plate XVI following 5
    • Watanabe T, Ichikawa A, Saito H, and Hotta T (1996). Overexpression of the MDM2 oncogene in leukemia and lymphoma. Leuk Lymphoma 21, 391-397 (color plate XVI following 5).
    • (1996) Leuk Lymphoma , vol.21 , pp. 391-397
    • Watanabe, T.1    Ichikawa, A.2    Saito, H.3    Hotta, T.4
  • 221
    • 0035921928 scopus 로고    scopus 로고
    • Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines
    • Moberg KH, Bell DW, Wahrer DC, Haber DA, and Hariharan IK (2001). Archipelago regulates Cyclin E levels in Drosophila and is mutated in human cancer cell lines. Nature 413, 311-316.
    • (2001) Nature , vol.413 , pp. 311-316
    • Moberg, K.H.1    Bell, D.W.2    Wahrer, D.C.3    Haber, D.A.4    Hariharan, I.K.5
  • 222
    • 0035921849 scopus 로고    scopus 로고
    • Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line
    • Strohmaier H, Spruck CH, Kaiser P, Won KA, Sangfelt O, and Reed SI (2001). Human F-box protein hCdc4 targets cyclin E for proteolysis and is mutated in a breast cancer cell line. Nature 413, 316-322.
    • (2001) Nature , vol.413 , pp. 316-322
    • Strohmaier, H.1    Spruck, C.H.2    Kaiser, P.3    Won, K.A.4    Sangfelt, O.5    Reed, S.I.6
  • 224
    • 22244476115 scopus 로고    scopus 로고
    • The v-Jun point mutation allows c-Jun to escape GSK3-dependent recognition and destruction by the Fbw7 ubiquitin ligase
    • Wei W, Jin J, Schlisio S, Harper JW, and Kaelin WG Jr (2005). The v-Jun point mutation allows c-Jun to escape GSK3-dependent recognition and destruction by the Fbw7 ubiquitin ligase. Cancer Cell 8, 25-33.
    • (2005) Cancer Cell , vol.8 , pp. 25-33
    • Wei, W.1    Jin, J.2    Schlisio, S.3    Harper, J.W.4    Kaelin Jr., W.G.5
  • 226
    • 0035929669 scopus 로고    scopus 로고
    • The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog
    • Oberg C, Li J, Pauley A, Wolf E, Gurney M, and Lendahl U (2001). The Notch intracellular domain is ubiquitinated and negatively regulated by the mammalian Sel-10 homolog. J Biol Chem 276, 35847-35853.
    • (2001) J Biol Chem , vol.276 , pp. 35847-35853
    • Oberg, C.1    Li, J.2    Pauley, A.3    Wolf, E.4    Gurney, M.5    Lendahl, U.6
  • 231
    • 0033575920 scopus 로고    scopus 로고
    • Deregulated cyclin E induces chromosome instability
    • Spruck CH, Won KA, and Reed SI (1999). Deregulated cyclin E induces chromosome instability. Nature 401, 297-300.
    • (1999) Nature , vol.401 , pp. 297-300
    • Spruck, C.H.1    Won, K.A.2    Reed, S.I.3
  • 232
    • 0032923368 scopus 로고    scopus 로고
    • Cyclin E in human cancers
    • Donnellan R and Chetty R (1999). Cyclin E in human cancers. FASEB J 13, 773-780.
    • (1999) FASEB J , vol.13 , pp. 773-780
    • Donnellan, R.1    Chetty, R.2
  • 233
    • 0035048540 scopus 로고    scopus 로고
    • Prognostic implications of p27 and cyclin E protein contents in malignant lymphomas
    • Erlanson M and Landberg G (2001). Prognostic implications of p27 and cyclin E protein contents in malignant lymphomas. Leuk Lymphoma 40, 461-470.
    • (2001) Leuk Lymphoma , vol.40 , pp. 461-470
    • Erlanson, M.1    Landberg, G.2
  • 234
    • 0031048716 scopus 로고    scopus 로고
    • Expression of cell-cycle regulators p27Kip1 and cyclin E, alone and in combination, correlate with survival in young breast cancer patients
    • Porter PL, Malone KE, Heagerty PJ, Alexander GM, Gatti LA, Firpo EJ, Daling JR, and Roberts JM (1997). Expression of cell-cycle regulators p27Kip1 and cyclin E, alone and in combination, correlate with survival in young breast cancer patients. Nat Med 3, 222-225.
    • (1997) Nat Med , vol.3 , pp. 222-225
    • Porter, P.L.1    Malone, K.E.2    Heagerty, P.J.3    Alexander, G.M.4    Gatti, L.A.5    Firpo, E.J.6    Daling, J.R.7    Roberts, J.M.8
  • 235
    • 0031028246 scopus 로고    scopus 로고
    • Induction of mammary gland hyperplasia and carcinomas in transgenic mice expressing human cyclin E
    • Bortner DM and Rosenberg MP (1997). Induction of mammary gland hyperplasia and carcinomas in transgenic mice expressing human cyclin E. Mol Cell Biol 17, 453-459.
    • (1997) Mol Cell Biol , vol.17 , pp. 453-459
    • Bortner, D.M.1    Rosenberg, M.P.2
  • 237
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27
    • Carrano AC, Eytan E, Hershko A, and Pagano M (1999). SKP2 is required for ubiquitin-mediated degradation of the CDK inhibitor p27. Nat Cell Biol 1, 193-199.
    • (1999) Nat Cell Biol , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 240
    • 0037379776 scopus 로고    scopus 로고
    • Expression of the F-box protein SKP2 induces hyperplasia, dysplasia, and low-grade carcinoma in the mouse prostate
    • Shim EH, Johnson L, Noh HL, Kim YJ, Sun H, Zeiss C, and Zhang H (2003). Expression of the F-box protein SKP2 induces hyperplasia, dysplasia, and low-grade carcinoma in the mouse prostate. Cancer Res 63, 1583-1588.
    • (2003) Cancer Res , vol.63 , pp. 1583-1588
    • Shim, E.H.1    Johnson, L.2    Noh, H.L.3    Kim, Y.J.4    Sun, H.5    Zeiss, C.6    Zhang, H.7
  • 241
    • 17144410731 scopus 로고    scopus 로고
    • Small molecule inhibitors of p53/MDM2 interaction
    • Fotouhi N and Graves B (2005). Small molecule inhibitors of p53/MDM2 interaction. Curr Top Med Chem 5, 159-165.
    • (2005) Curr Top Med Chem , vol.5 , pp. 159-165
    • Fotouhi, N.1    Graves, B.2
  • 242
    • 3042523534 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the p53 suppressor HDM2: Have protein-protein interactions come of age as drug targets?
    • Fischer PM and Lane DP (2004). Small-molecule inhibitors of the p53 suppressor HDM2: have protein-protein interactions come of age as drug targets? Trends Pharmacol Sci 25, 343-346.
    • (2004) Trends Pharmacol Sci , vol.25 , pp. 343-346
    • Fischer, P.M.1    Lane, D.P.2
  • 245
    • 33747654496 scopus 로고    scopus 로고
    • Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism
    • Jun 27, [Epub ahead of print]
    • Dai MS, Shi D, Jin Y, Sun XX, Zhang Y, Grossman SR, and Lu H. (2006) Regulation of the MDM2-p53 pathway by ribosomal protein L11 involves a post-ubiquitination mechanism. J Biol Chem 281, Jun 27, [Epub ahead of print].
    • (2006) J Biol Chem , vol.281
    • Dai, M.S.1    Shi, D.2    Jin, Y.3    Sun, X.X.4    Zhang, Y.5    Grossman, S.R.6    Lu, H.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.