메뉴 건너뛰기




Volumn 694, Issue , 2010, Pages 160-171

Roles for SUMO modification during senescence

Author keywords

[No Author keywords available]

Indexed keywords

PROTEIN INHIBITOR OF ACTIVATED STAT; PROTEIN P53; SUMO 1 PROTEIN; SUMO 2 PROTEIN; SUMO 3 PROTEIN; SUMO PROTEIN; UBIQUITIN PROTEIN LIGASE E3; PROTEIN;

EID: 78049368535     PISSN: 00652598     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-1-4419-7002-2_12     Document Type: Article
Times cited : (14)

References (119)
  • 2
    • 0035852990 scopus 로고    scopus 로고
    • Heteronuclear nuclear magnetic resonance assignments, structure and dynamics of SUMO-1, a human ubiquitin-like protein
    • DOI 10.1016/S0141-8130(00)00169-0, PII S0141813000001690
    • Jin C, Shiyanova T, Shen Z et al. Heteronuclear nuclear magnetic resonance assignments, structure and dynamics of SUMO-1, a human ubiquitin-like protein. Int J Biol Macromol 2001; 28(3):227-234. (Pubitemid 32197458)
    • (2001) International Journal of Biological Macromolecules , vol.28 , Issue.3 , pp. 227-234
    • Jin, C.1    Shiyanova, T.2    Shen, Z.3    Liao, X.4
  • 3
    • 3943099375 scopus 로고    scopus 로고
    • Protein modification by SUMO
    • DOI 10.1146/annurev.biochem.73.011303.074118
    • Johnson ES. Protein modification by SUMO. Annu Rev Biochem 2004; 73:355-382. (Pubitemid 39050373)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 355-382
    • Johnson, E.S.1
  • 4
    • 3042644131 scopus 로고    scopus 로고
    • A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus
    • DOI 10.1074/jbc.M402273200
    • Bohren KM, Nadkarni V, Song JH et al. A M55V polymorphism in a novel SUMO gene (SUMO-4) differentially activates heat shock transcription factors and is associated with susceptibility to type I diabetes mellitus. J Biol Chem 2004; 279(26):27233-27238. (Pubitemid 38812561)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.26 , pp. 27233-27238
    • Bohren, K.M.1    Nadkarni, V.2    Song, J.H.3    Gabbay, K.H.4    Owerbach, D.5
  • 5
    • 0034054669 scopus 로고    scopus 로고
    • Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3
    • DOI 10.1074/jbc.275.9.6252
    • Saitoh H, Hinchey J. Functional heterogeneity of small ubiquitin-related protein modifiers SUMO-1 versus SUMO-2/3. J Biol Chem 2000; 275(9):6252-6258. (Pubitemid 30129915)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.9 , pp. 6252-6258
    • Saitoh, H.1    Hinchey, J.2
  • 6
    • 15944406765 scopus 로고    scopus 로고
    • SUMO: A history of modification
    • DOI 10.1016/j.molcel.2005.03.012
    • Hay RT. SUMO: a history of modification. Mol Cell 2005; 18(1):1-12. (Pubitemid 40444643)
    • (2005) Molecular Cell , vol.18 , Issue.1 , pp. 1-12
    • Hay, R.T.1
  • 7
    • 24344445216 scopus 로고    scopus 로고
    • Something about SUMO inhibits transcription
    • DOI 10.1016/j.gde.2005.07.004, PII S0959437X05001309
    • Gill G. Something about SUMO inhibits transcription. Curr Opin Genet Dev 2005; 15(5):536-541. (Pubitemid 41262410)
    • (2005) Current Opinion in Genetics and Development , vol.15 , Issue.5 SPEC. ISSUE , pp. 536-541
    • Gill, G.1
  • 8
    • 0035877693 scopus 로고    scopus 로고
    • The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification
    • Sampson DA, Wang M, Matunis MJ. The small ubiquitin-like modifier-1 (SUMO-1) consensus sequence mediates Ubc9 binding and is essential for SUMO-1 modification. J Biol Chem 2001; 276(24):21664-21669.
    • (2001) J Biol Chem , vol.276 , Issue.24 , pp. 21664-21669
    • Sampson, D.A.1    Wang, M.2    Matunis, M.J.3
  • 9
    • 1542501958 scopus 로고    scopus 로고
    • SUMO: Ligases, isopeptidases and nuclear pores
    • DOI 10.1016/j.tibs.2003.09.002, PII S0968000403002263
    • Melchior F, Schergaut M, Pichler A. SUMO: ligases, isopeptidases and nuclear pores. Trends Biochem Sci 2003; 28(11):612-618. (Pubitemid 38352808)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.11 , pp. 612-618
    • Melchior, F.1    Schergaut, M.2    Pichler, A.3
  • 10
    • 0034680441 scopus 로고    scopus 로고
    • Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif
    • Minty A, Dumont X, Kaghad M et al. Covalent modification of p73alpha by SUMO-1. Two-hybrid screening with p73 identifies novel SUMO-1-interacting proteins and a SUMO-1 interaction motif. J Biol Chem 2000; 275(46):36316-36323.
    • (2000) J Biol Chem , vol.275 , Issue.46 , pp. 36316-36323
    • Minty, A.1    Dumont, X.2    Kaghad, M.3
  • 11
    • 0035918226 scopus 로고    scopus 로고
    • SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting
    • Rodriguez MS, Dargemont C, Hay RT. SUMO-1 conjugation in vivo requires both a consensus modification motif and nuclear targeting. J Biol Chem 2001; 276(16):12654-12659.
    • (2001) J Biol Chem , vol.276 , Issue.16 , pp. 12654-12659
    • Rodriguez, M.S.1    Dargemont, C.2    Hay, R.T.3
  • 13
    • 33750439105 scopus 로고    scopus 로고
    • An extended consensus motif enhances the specificity of substrate modification by SUMO
    • DOI 10.1038/sj.emboj.7601383, PII 7601383
    • Yang SH, Galanis A, Witty J et al. An extended consensus motif enhances the specificity of substrate modification by SUMO. EMBO J 2006; 25(21):5083-5093. (Pubitemid 44658526)
    • (2006) EMBO Journal , vol.25 , Issue.21 , pp. 5083-5093
    • Yang, S.-H.1    Galanis, A.2    Witty, J.3    Sharrocks, A.D.4
  • 14
    • 0032135131 scopus 로고    scopus 로고
    • SUMO-1 modification of IκBα inhibits NF-κB activation
    • Desterro JM, Rodriguez MS, Hay RT. SUMO-1 modification of IkappaBalpha inhibits NF-kappaB activation. Mol Cell 1998; 2(2):233-239. (Pubitemid 128373648)
    • (1998) Molecular Cell , vol.2 , Issue.2 , pp. 233-239
    • Desterro, J.M.P.1    Rodriguez, M.S.2    Hay, R.T.3
  • 15
    • 0037068455 scopus 로고    scopus 로고
    • RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO
    • DOI 10.1038/nature00991
    • Hoege C, Pfander B, Moldovan GL et al. RAD6-dependent DNA repair is linked to modification of PCNA by ubiquitin and SUMO. Nature 2002; 419(6903):135-141. (Pubitemid 35025438)
    • (2002) Nature , vol.419 , Issue.6903 , pp. 135-141
    • Hoege, C.1    Pfander, B.2    Moldovan, G.-L.3    Pyrowolakis, G.4    Jentsch, S.5
  • 18
    • 4344685954 scopus 로고    scopus 로고
    • Association of Ubc9, an E2 ligase for SUMO conjugation, with p53 is regulated by phosphorylation of p53
    • DOI 10.1016/j.febslet.2004.07.059, PII S0014579304009238
    • Lin JY, Ohshima T, Shimotohno K. Association of Ubc9, an E2 ligase for SUMO conjugation, with p53 is regulated by phosphorylation of p53. FEBS Lett 2004; 573(1-3):15-18. (Pubitemid 39141028)
    • (2004) FEBS Letters , vol.573 , Issue.1-3 , pp. 15-18
    • Lin, J.-Y.1    Ohshima, T.2    Shimotohno, K.3
  • 21
    • 1542285164 scopus 로고    scopus 로고
    • SUMO promotes HDAC-mediated transcriptional repression
    • DOI 10.1016/S1097-2765(04)00060-7, PII S1097276504000607
    • Yang SH, Sharrocks AD. SUMO promotes HDAC-mediated transcriptional repression. Mol Cell 2004; 13(4):611-617. (Pubitemid 38299387)
    • (2004) Molecular Cell , vol.13 , Issue.4 , pp. 611-617
    • Yang, S.-H.1    Sharrocks, A.D.2
  • 22
    • 34147208064 scopus 로고    scopus 로고
    • An acetylation/deacetylation-SUMOylation switch through a phylogenetically conserved ψKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity
    • DOI 10.1128/MCB.01098-06
    • Stankovic-Valentin N, Deltour S, Seeler J et al. An acetylation/ deacetylation-SUMOylation switch through a phylogenetically conserved psiKXEP motif in the tumor suppressor HIC1 regulates transcriptional repression activity. Mol Cell Biol 2007; 27(7):2661-2675. (Pubitemid 46581356)
    • (2007) Molecular and Cellular Biology , vol.27 , Issue.7 , pp. 2661-2675
    • Stankovic-Valentin, N.1    Deltour, S.2    Seeler, J.3    Pinte, S.4    Vergoten, G.5    Guerardel, C.6    Dejean, A.7    Leprince, D.8
  • 24
    • 0033580444 scopus 로고    scopus 로고
    • A new protease required for cell-cycle progression in yeast
    • Li SJ, Hochstrasser M. A new protease required for cell-cycle progression in yeast. Nature 1999; 398(6724):246-251.
    • (1999) Nature , vol.398 , Issue.6724 , pp. 246-251
    • Li, S.J.1    Hochstrasser, M.2
  • 25
    • 0034018312 scopus 로고    scopus 로고
    • The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein
    • DOI 10.1128/MCB.20.7.2367-2377.2000
    • Li SJ, Hochstrasser M. The yeast ULP2 (SMT4) gene encodes a novel protease specific for the ubiquitin-like Smt3 protein. Mol Cell Biol 2000; 20(7):2367-2377. (Pubitemid 30152045)
    • (2000) Molecular and Cellular Biology , vol.20 , Issue.7 , pp. 2367-2377
    • Li, S.-J.1    Hochstrasser, M.2
  • 26
    • 0035433114 scopus 로고    scopus 로고
    • Expression and regulation of the mammalian SUMO-1 E1 enzyme
    • Azuma Y, Tan SH, Cavenagh MM et al. Expression and regulation of the mammalian SUMO-1 E1 enzyme. FASEB J 2001; 15(10):1825-1827.
    • (2001) FASEB J , vol.15 , Issue.10 , pp. 1825-1827
    • Azuma, Y.1    Tan, S.H.2    Cavenagh, M.M.3
  • 27
    • 0346422441 scopus 로고    scopus 로고
    • Characterization of the Localization and Proteolytic Activity of the SUMO-specific Protease, SENP1
    • DOI 10.1074/jbc.M306195200
    • Bailey D, O'Hare P. Characterization of the localization and proteolytic activity of the SUMO-specific protease, SENP1. J Biol Chem 2004; 279(1):692-703. (Pubitemid 38044874)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.1 , pp. 692-703
    • Bailey, D.1    O'Hare, P.2
  • 28
    • 34249880519 scopus 로고    scopus 로고
    • Modification in reverse: The SUMO proteases
    • DOI 10.1016/j.tibs.2007.05.002, PII S0968000407001223
    • Mukhopadhyay D, Dasso M. Modification in reverse: the SUMO proteases. Trends Biochem Sci 2007; 32(6):286-295. (Pubitemid 46874931)
    • (2007) Trends in Biochemical Sciences , vol.32 , Issue.6 , pp. 286-295
    • Mukhopadhyay, D.1    Dasso, M.2
  • 29
    • 0036939820 scopus 로고    scopus 로고
    • Herpes simplex virus 1 ICPO co-localizes with a SUMO-specific protease
    • Bailey D, O'Hare P. Herpes simplex virus 1 ICP0 colocalizes with a SUMO-specific protease. J Gen Virol 2002; 83(Pt 12):2951-2964. (Pubitemid 36054340)
    • (2002) Journal of General Virology , vol.83 , Issue.12 , pp. 2951-2964
    • Bailey, D.1    O'Hare, P.2
  • 30
    • 0034603179 scopus 로고    scopus 로고
    • Differential regulation of sentrinized proteins by a novel sentrin- specific protease
    • DOI 10.1074/jbc.275.5.3355
    • Gong L, Millas S, Maul GG et al. Differential regulation of sentrinized proteins by a novel sentrin-specific protease. J Biol Chem 2000; 275(5):3355-3359. (Pubitemid 30083039)
    • (2000) Journal of Biological Chemistry , vol.275 , Issue.5 , pp. 3355-3359
    • Gong, L.1    Millas, S.2    Maul, G.G.3    Yeh, E.T.H.4
  • 31
    • 0037205460 scopus 로고    scopus 로고
    • Association of the human SUMO-1 protease SENP2 with the nuclear pore
    • DOI 10.1074/jbc.M201799200
    • Hang J, Dasso M. Association of the human SUMO-1 protease SENP2 with the nuclear pore. J Biol Chem 2002; 277(22):19961-19966. (Pubitemid 34967518)
    • (2002) Journal of Biological Chemistry , vol.277 , Issue.22 , pp. 19961-19966
    • Hang, J.1    Dasso, M.2
  • 32
    • 0037417333 scopus 로고    scopus 로고
    • The Ulp1 SUMO isopeptidase: Distinct domains required for viability, nuclear envelope localization, and substrate specificity
    • DOI 10.1083/jcb.200212052
    • Li SJ, Hochstrasser M. The Ulp1 SUMO isopeptidase: distinct domains required for viability, nuclear envelope localization and substrate specificity. J Cell Biol 2003; 160(7):1069-1081. (Pubitemid 36443875)
    • (2003) Journal of Cell Biology , vol.160 , Issue.7 , pp. 1069-1081
    • Li, S.-J.1    Hochstrasser, M.2
  • 33
    • 33744917849 scopus 로고    scopus 로고
    • Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3
    • DOI 10.1074/jbc.M511658200
    • Gong L, Yeh ET. Characterization of a family of nucleolar SUMO-specific proteases with preference for SUMO-2 or SUMO-3. J Biol Chem 2006; 281(23):15869-15877. (Pubitemid 43848478)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.23 , pp. 15869-15877
    • Gong, L.1    Yeh, E.T.H.2
  • 36
    • 9444260454 scopus 로고    scopus 로고
    • Distinct in vivo dynamics of vertebrate SUMO paralogues
    • DOI 10.1091/mbc.E04-07-0589
    • Ayaydin F, Dasso M. Distinct in vivo dynamics of vertebrate SUMO paralogues. Mol Biol Cell 2004; 15(12):5208-5218. (Pubitemid 39564718)
    • (2004) Molecular Biology of the Cell , vol.15 , Issue.12 , pp. 5208-5218
    • Ayaydin, F.1    Dasso, M.2
  • 38
    • 21244449061 scopus 로고    scopus 로고
    • Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p
    • DOI 10.1016/j.molcel.2005.06.001, PII S1097276505013766
    • Papouli E, Chen S, Davies AA et al. Crosstalk between SUMO and ubiquitin on PCNA is mediated by recruitment of the helicase Srs2p. Mol Cell 2005; 19(1):123-133. (Pubitemid 40884663)
    • (2005) Molecular Cell , vol.19 , Issue.1 , pp. 123-133
    • Papouli, E.1    Chen, S.2    Davies, A.A.3    Huttner, D.4    Krejci, L.5    Sung, P.6    Ulrich, H.D.7
  • 39
    • 22944474665 scopus 로고    scopus 로고
    • SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase
    • DOI 10.1038/nature03665
    • Pfander B, Moldovan GL, Sacher M et al. SUMO-modified PCNA recruits Srs2 to prevent recombination during S phase. Nature 2005; 436(7049):428-433. (Pubitemid 41059056)
    • (2005) Nature , vol.436 , Issue.7049 , pp. 428-433
    • Pfander, B.1    Moldovan, G.-L.2    Sacher, M.3    Hoege, C.4    Jentsch, S.5
  • 42
    • 0037086643 scopus 로고    scopus 로고
    • Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover
    • DOI 10.1093/emboj/21.6.1456
    • Hardeland U, Steinacher R, Jiricny J et al. Modification of the human thymine-DNA glycosylase by ubiquitin-like proteins facilitates enzymatic turnover. EMBO J 2002; 21(6):1456-1464. (Pubitemid 34246524)
    • (2002) EMBO Journal , vol.21 , Issue.6 , pp. 1456-1464
    • Hardeland, U.1    Steinacher, R.2    Jiricny, J.3    Schar, P.4
  • 43
    • 0344622606 scopus 로고
    • The serial cultivation of human diploid cell strains
    • Hayflick L, Moorhead PS. The serial cultivation of human diploid cell strains. Exp Cell Res 1961; 25:585-621.
    • (1961) Exp Cell Res , vol.25 , pp. 585-621
    • Hayflick, L.1    Moorhead, P.S.2
  • 44
    • 0035500487 scopus 로고    scopus 로고
    • Cellular senescence as a tumor-suppressor mechanism
    • Campisi J. Cellular senescence as a tumor-suppressor mechanism. Trends Cell Biol 2001; 11(11): S27-31.
    • (2001) Trends Cell Biol , vol.11 , Issue.11
    • Campisi, J.1
  • 45
    • 0036463405 scopus 로고    scopus 로고
    • A matter of life and death
    • DOI 10.1016/S1535-6108(02)00024-7
    • Green DR, Evan GI. A matter of life and death. Cancer Cell 2002; 1(1):19-30. (Pubitemid 41039172)
    • (2002) Cancer Cell , vol.1 , Issue.1 , pp. 19-30
    • Green, D.R.1    Evan, G.I.2
  • 46
    • 45449084795 scopus 로고    scopus 로고
    • Cellular senescence and organismal aging
    • Jeyapalan JC, Sedivy JM. Cellular senescence and organismal aging. Mech Ageing Dev 2008; 129(7-8):467-474.
    • (2008) Mech Ageing Dev , vol.129 , Issue.7-8 , pp. 467-474
    • Jeyapalan, J.C.1    Sedivy, J.M.2
  • 47
    • 24344447780 scopus 로고    scopus 로고
    • P63 deficiency activates a program of cellular senescence and leads to accelerated aging
    • DOI 10.1101/gad.342305
    • Keyes WM, Wu Y, Vogel H et al. p63 deficiency activates a program of cellular senescence and leads to accelerated aging. Genes Dev 2005; 19(17):1986-1999. (Pubitemid 41247957)
    • (2005) Genes and Development , vol.19 , Issue.17 , pp. 1986-1999
    • Keyes, W.M.1    Wu, Y.2    Vogel, H.3    Guo, X.4    Lowe, S.W.5    Mills, A.A.6
  • 48
    • 38049059966 scopus 로고    scopus 로고
    • DNA damage, cellular senescence and organismal ageing: Causal or correlative?
    • Chen JH, Hales CN, Ozanne SE. DNA damage, cellular senescence and organismal ageing: causal or correlative? Nucleic Acids Res 2007; 35(22):7417-7428.
    • (2007) Nucleic Acids Res , vol.35 , Issue.22 , pp. 7417-7428
    • Chen, J.H.1    Hales, C.N.2    Ozanne, S.E.3
  • 49
    • 20444370974 scopus 로고    scopus 로고
    • What has senescence got to do with cancer?
    • DOI 10.1016/j.ccr.2005.05.025, PII S1535610805001662
    • Dimri GP. What has senescence got to do with cancer? Cancer Cell 2005; 7(6):505-512. (Pubitemid 40799244)
    • (2005) Cancer Cell , vol.7 , Issue.6 , pp. 505-512
    • Dimri, G.P.1
  • 50
    • 0029047362 scopus 로고
    • A biomarker that identifies senescent human cells in culture and in aging skin in vivo
    • Dimri GP, Lee X, Basile G et al. A biomarker that identifies senescent human cells in culture and in aging skin in vivo. Proc Natl Acad Sci USA 1995; 92(20):9363-9367.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.20 , pp. 9363-9367
    • Dimri, G.P.1    Lee, X.2    Basile, G.3
  • 51
    • 0025145238 scopus 로고
    • Replicative senescence: The human fibroblast comes of age
    • Goldstein S. Replicative senescence: the human fibroblast comes of age. Science 1990; 249(4973):1129-1133.
    • (1990) Science , vol.249 , Issue.4973 , pp. 1129-1133
    • Goldstein, S.1
  • 52
    • 0035219092 scopus 로고    scopus 로고
    • Telomeres and telomerase: Implications for cancer and aging
    • Shay JW, Wright WE. Telomeres and telomerase: implications for cancer and aging. Radiat Res 2001; 155(1 Pt 2):188-193. (Pubitemid 33723537)
    • (2001) Radiation Research , vol.155 , Issue.1 , pp. 188-193
    • Shay, J.W.1    Wright, W.E.2
  • 53
    • 0034472472 scopus 로고    scopus 로고
    • Telomerase and human tumorigenesis
    • DOI 10.1006/scbi.2000.0339
    • Stewart SA, Weinberg RA. Telomerase and human tumorigenesis. Semin Cancer Biol 2000; 10(6):399-406. (Pubitemid 32181910)
    • (2000) Seminars in Cancer Biology , vol.10 , Issue.6 , pp. 399-406
    • Stewart, S.A.1    Weinberg, R.A.2
  • 55
    • 0033834247 scopus 로고    scopus 로고
    • Telomere dynamics in cancer progression and prevention: Fundamental differences in human and mouse telomere biology
    • DOI 10.1038/78592
    • Wright WE, Shay JW. Telomere dynamics in cancer progression and prevention: fundamental differences in human and mouse telomere biology. Nat Med 2000; 6(8):849-851. (Pubitemid 30644735)
    • (2000) Nature Medicine , vol.6 , Issue.8 , pp. 849-851
    • Wright, W.E.1    Shay, J.W.2
  • 58
    • 0035545802 scopus 로고    scopus 로고
    • Putting the stress on senescence
    • DOI 10.1016/S0955-0674(00)00278-7
    • Serrano M, Blasco MA. Putting the stress on senescence. Curr Opin Cell Biol 2001; 13(6):748-753. (Pubitemid 33042736)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.6 , pp. 748-753
    • Serrano, M.1    Blasco, M.A.2
  • 59
    • 65349126392 scopus 로고    scopus 로고
    • Cellular senescence: Its role in tumor suppression and aging
    • Ohtani N, Mann DJ, Hara E. Cellular senescence: its role in tumor suppression and aging. Cancer Sci2009; 100(5):792-797.
    • (2009) Cancer Sci , vol.100 , Issue.5 , pp. 792-797
    • Ohtani, N.1    Mann, D.J.2    Hara, E.3
  • 61
    • 33847184227 scopus 로고    scopus 로고
    • Human papillomavirus E7 repression in cervical carcinoma cells initiates a transcriptional cascade driven by the retinoblastoma family, resulting in senescence
    • Johung K, Goodwin EC, DiMaio D. Human papillomavirus E7 repression in cervical carcinoma cells initiates a transcriptional cascade driven by the retinoblastoma family, resulting in senescence. J Virol 2007; 81(5):2102-2116.
    • (2007) J Virol , vol.81 , Issue.5 , pp. 2102-2116
    • Johung, K.1    Goodwin, E.C.2    Dimaio, D.3
  • 62
    • 13944270339 scopus 로고    scopus 로고
    • Senescent cells, tumor suppression, and organismal aging: Good citizens, bad neighbors
    • DOI 10.1016/j.cell.2005.02.003
    • Campisi J. Senescent cells, tumor supression and organismal aging: good citizens, bad neighbors. Cell 2005; 120:513-522. (Pubitemid 40269765)
    • (2005) Cell , vol.120 , Issue.4 , pp. 513-522
    • Campisi, J.1
  • 63
    • 3543092021 scopus 로고    scopus 로고
    • Pathways of apoptotic and non-apoptotic death in tumour cells
    • Okada H, Mak TW. Pathways of apoptotic and non-apoptotic death in tumour cells. Nat Rev Cancer 2004; 4(8):592-603. (Pubitemid 39025054)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.8 , pp. 592-603
    • Okada, H.1    Mak, T.W.2
  • 64
    • 1542781659 scopus 로고    scopus 로고
    • When cells get stressed: An integrative view of cellular senescence
    • Ben-Porath IaW RA. When cells get stressed: an integrative view of cellular senescence. J Clin Invest 2004; 113:8-13.
    • (2004) J Clin Invest , vol.113 , pp. 8-13
    • Ben-Porath Iaw, R.A.1
  • 68
    • 34047205692 scopus 로고    scopus 로고
    • SUMO is growing senescent
    • Bischof O, DEjean A. SUMO is growing senescent. Cell Cycle 2007; 6:677-681. (Pubitemid 46535679)
    • (2007) Cell Cycle , vol.6 , Issue.6 , pp. 677-681
    • Bischof, O.1    Dejean, A.2
  • 69
    • 65349111974 scopus 로고    scopus 로고
    • Modulation of inducible nitric oxide synthase expression by sumoylation
    • Akar CA, Feinstein DL. Modulation of inducible nitric oxide synthase expression by sumoylation. J Neuroinflammation 2009; 6:12.
    • (2009) J Neuroinflammation , vol.6 , pp. 12
    • Akar, C.A.1    Feinstein, D.L.2
  • 72
    • 19844383887 scopus 로고    scopus 로고
    • Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor suppressor
    • DOI 10.1038/sj.onc.1208539
    • Ledl A, Schmidt D, Muller S. Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor supressor. Oncogene 2005; 24:3810-3818. (Pubitemid 40826879)
    • (2005) Oncogene , vol.24 , Issue.23 , pp. 3810-3818
    • Ledl, A.1    Schmidt, D.2    Muller, S.3
  • 74
    • 33745210316 scopus 로고    scopus 로고
    • The E3 SUMO ligase PIASy is a regulator of cellular senescence and apoptosis
    • Bischof O, Schwamborn K, Martin N et al. The E3 SUMO ligase PIASy is a regulator of cellular senescence and apoptosis. Mol Cell 2006; 22(6):783-794.
    • (2006) Mol Cell , vol.22 , Issue.6 , pp. 783-794
    • Bischof, O.1    Schwamborn, K.2    Martin, N.3
  • 76
    • 0346100493 scopus 로고    scopus 로고
    • PIAS/SUMO: New partners in transcriptional regulation
    • Schmidt DaM S. PIAS/SUMO: new partners in transcriptional regulation. Cell Mol Life Sci 2003; 60:2561-2574.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2561-2574
    • Schmidt Dam, S.1
  • 77
    • 33747373841 scopus 로고    scopus 로고
    • Involvement of SUMO modification in MBD1- and MCAF1- mediated heterochromatin formation
    • Uchimura Y, Ichimura T, Uwada J et al. Involvement of SUMO modification in MBD1- and MCAF1- mediated heterochromatin formation. J Biol Chem 2006; 281:23180-23190.
    • (2006) J Biol Chem , vol.281 , pp. 23180-23190
    • Uchimura, Y.1    Ichimura, T.2    Uwada, J.3
  • 78
    • 20444370974 scopus 로고    scopus 로고
    • What has senescence got to do with cancer?
    • DOI 10.1016/j.ccr.2005.05.025, PII S1535610805001662
    • Dimri GP. What has senescence got to do with cancer? Cancer Cell 2005; 7(6):505-512. (Pubitemid 40799244)
    • (2005) Cancer Cell , vol.7 , Issue.6 , pp. 505-512
    • Dimri, G.P.1
  • 79
    • 0029047362 scopus 로고
    • A biomarker that identifies senescent human cells in culture and in aging skin in vivo
    • Dimri GP, Lee X, Basile G et al. A biomarker that identifies senescent human cells in culture and in aging skin in vivo. Proc Natl Acad Sci USA 1995; 92(20):9363-9367.
    • (1995) Proc Natl Acad Sci USA , vol.92 , Issue.20 , pp. 9363-9367
    • Dimri, G.P.1    Lee, X.2    Basile, G.3
  • 80
    • 0025145238 scopus 로고
    • Replicative senescence: The human fibroblast comes of age
    • Goldstein S. Replicative senescence: the human fibroblast comes of age. Science 1990; 249(4973):1129-1133.
    • (1990) Science , vol.249 , Issue.4973 , pp. 1129-1133
    • Goldstein, S.1
  • 81
    • 0035219092 scopus 로고    scopus 로고
    • Telomeres and telomerase: Implications for cancer and aging
    • Shay JW, Wright WE. Telomeres and telomerase: implications for cancer and aging. Radiat Res 2001; 155(1 Pt 2):188-193. (Pubitemid 33723537)
    • (2001) Radiation Research , vol.155 , Issue.1 , pp. 188-193
    • Shay, J.W.1    Wright, W.E.2
  • 82
    • 0034472472 scopus 로고    scopus 로고
    • Telomerase and human tumorigenesis
    • DOI 10.1006/scbi.2000.0339
    • Stewart SA, Weinberg RA. Telomerase and human tumorigenesis. Semin Cancer Biol 2000; 10(6):399-406. (Pubitemid 32181910)
    • (2000) Seminars in Cancer Biology , vol.10 , Issue.6 , pp. 399-406
    • Stewart, S.A.1    Weinberg, R.A.2
  • 84
    • 0033834247 scopus 로고    scopus 로고
    • Telomere dynamics in cancer progression and prevention: Fundamental differences in human and mouse telomere biology
    • DOI 10.1038/78592
    • Wright WE, Shay JW. Telomere dynamics in cancer progression and prevention: fundamental differences in human and mouse telomere biology. Nat Med 2000; 6(8):849-851. (Pubitemid 30644735)
    • (2000) Nature Medicine , vol.6 , Issue.8 , pp. 849-851
    • Wright, W.E.1    Shay, J.W.2
  • 87
    • 0035545802 scopus 로고    scopus 로고
    • Putting the stress on senescence
    • DOI 10.1016/S0955-0674(00)00278-7
    • Serrano M, Blasco MA. Putting the stress on senescence. Curr Opin Cell Biol 2001; 13(6):748-753. (Pubitemid 33042736)
    • (2001) Current Opinion in Cell Biology , vol.13 , Issue.6 , pp. 748-753
    • Serrano, M.1    Blasco, M.A.2
  • 88
    • 65349126392 scopus 로고    scopus 로고
    • Cellular senescence: Its role in tumor suppression and aging
    • Ohtani N, Mann DJ, Hara E. Cellular senescence: its role in tumor suppression and aging. Cancer Sci2009; 100(5):792-797.
    • (2009) Cancer Sci , vol.100 , Issue.5 , pp. 792-797
    • Ohtani, N.1    Mann, D.J.2    Hara, E.3
  • 90
    • 33847184227 scopus 로고    scopus 로고
    • Human papillomavirus E7 repression in cervical carcinoma cells initiates a transcriptional cascade driven by the retinoblastoma family, resulting in senescence
    • Johung K, Goodwin EC, DiMaio D. Human papillomavirus E7 repression in cervical carcinoma cells initiates a transcriptional cascade driven by the retinoblastoma family, resulting in senescence. J Virol 2007; 81(5):2102-2116.
    • (2007) J Virol , vol.81 , Issue.5 , pp. 2102-2116
    • Johung, K.1    Goodwin, E.C.2    Dimaio, D.3
  • 91
    • 13944270339 scopus 로고    scopus 로고
    • Senescent cells, tumor suppression, and organismal aging: Good citizens, bad neighbors
    • DOI 10.1016/j.cell.2005.02.003
    • Campisi J. Senescent cells, tumor supression and organismal aging: good citizens, bad neighbors. Cell 2005; 120:513-522. (Pubitemid 40269765)
    • (2005) Cell , vol.120 , Issue.4 , pp. 513-522
    • Campisi, J.1
  • 92
    • 3543092021 scopus 로고    scopus 로고
    • Pathways of apoptotic and non-apoptotic death in tumour cells
    • Okada H, Mak TW. Pathways of apoptotic and non-apoptotic death in tumour cells. Nat Rev Cancer 2004; 4(8):592-603. (Pubitemid 39025054)
    • (2004) Nature Reviews Cancer , vol.4 , Issue.8 , pp. 592-603
    • Okada, H.1    Mak, T.W.2
  • 93
    • 1542781659 scopus 로고    scopus 로고
    • When cells get stressed: An integrative view of cellular senescence
    • Ben-Porath IaW RA. When cells get stressed: an integrative view of cellular senescence. J Clin Invest 2004; 113:8-13.
    • (2004) J Clin Invest , vol.113 , pp. 8-13
    • Ben-Porath Iaw, R.A.1
  • 97
    • 34047205692 scopus 로고    scopus 로고
    • SUMO is growing senescent
    • Bischof O, DEjean A. SUMO is growing senescent. Cell Cycle 2007; 6:677-681. (Pubitemid 46535679)
    • (2007) Cell Cycle , vol.6 , Issue.6 , pp. 677-681
    • Bischof, O.1    Dejean, A.2
  • 98
    • 65349111974 scopus 로고    scopus 로고
    • Modulation of inducible nitric oxide synthase expression by sumoylation
    • Akar CA, Feinstein DL. Modulation of inducible nitric oxide synthase expression by sumoylation. J Neuroinflammation 2009; 6:12.
    • (2009) J Neuroinflammation , vol.6 , pp. 12
    • Akar, C.A.1    Feinstein, D.L.2
  • 101
    • 19844383887 scopus 로고    scopus 로고
    • Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor suppressor
    • DOI 10.1038/sj.onc.1208539
    • Ledl A, Schmidt D, Muller S. Viral oncoproteins E1A and E7 and cellular LxCxE proteins repress SUMO modification of the retinoblastoma tumor supressor. Oncogene 2005; 24:3810-3818. (Pubitemid 40826879)
    • (2005) Oncogene , vol.24 , Issue.23 , pp. 3810-3818
    • Ledl, A.1    Schmidt, D.2    Muller, S.3
  • 103
    • 33745210316 scopus 로고    scopus 로고
    • The E3 SUMO ligase PIASy is a regulator of cellular senescence and apoptosis
    • Bischof O, Schwamborn K, Martin N et al. The E3 SUMO ligase PIASy is a regulator of cellular senescence and apoptosis. Mol Cell 2006; 22(6):783-794.
    • (2006) Mol Cell , vol.22 , Issue.6 , pp. 783-794
    • Bischof, O.1    Schwamborn, K.2    Martin, N.3
  • 105
    • 0346100493 scopus 로고    scopus 로고
    • PIAS/SUMO: New partners in transcriptional regulation
    • Schmidt DaM S. PIAS/SUMO: new partners in transcriptional regulation. Cell Mol Life Sci 2003; 60:2561-2574.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 2561-2574
    • Schmidt Dam, S.1
  • 106
    • 33747373841 scopus 로고    scopus 로고
    • Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation
    • Uchimura Y, Ichimura T, Uwada J et al. Involvement of SUMO modification in MBD1- and MCAF1-mediated heterochromatin formation. J Biol Chem 2006; 281:23180-23190.
    • (2006) J Biol Chem , vol.281 , pp. 23180-23190
    • Uchimura, Y.1    Ichimura, T.2    Uwada, J.3
  • 107
    • 33645879818 scopus 로고    scopus 로고
    • Histone sumoylation is a negative regulator in Saccharomycesserevisiae and shown dynamic interplay with positive-acting histone modifications
    • Nathan D, Ingvarsdottir K, Sterner DE et al. Histone sumoylation is a negative regulator in Saccharomycesserevisiae and shown dynamic interplay with positive-acting histone modifications. Genes Dev 2006; 20:966-76.
    • (2006) Genes Dev , vol.20 , pp. 966-976
    • Nathan, D.1    Ingvarsdottir, K.2    Sterner, D.E.3
  • 108
    • 52449102121 scopus 로고    scopus 로고
    • Repression of the SUMO-specific protease Senp1 induces p53-dependent premature senescence in normal human fibroblasts
    • Yates KE, Korbel GA, Shtutman M et al. Repression of the SUMO-specific protease Senp1 induces p53-dependent premature senescence in normal human fibroblasts. Aging Cell 2008; 7(5):609-621.
    • (2008) Aging Cell , vol.7 , Issue.5 , pp. 609-621
    • Yates, K.E.1    Korbel, G.A.2    Shtutman, M.3
  • 109
    • 24944460598 scopus 로고    scopus 로고
    • Shelterin: The protein complex that shapes and safeguards human telomeres
    • DOI 10.1101/gad.1346005
    • de Lange T. Shelterin: The protein complex that shapes and safeguards human telomeres. Genes Dev 2005; 19:2100-2110. (Pubitemid 41330312)
    • (2005) Genes and Development , vol.19 , Issue.18 , pp. 2100-2110
    • De Lange, T.1
  • 112
    • 6344254386 scopus 로고    scopus 로고
    • Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance
    • DOI 10.1038/sj.emboj.7600394
    • Xhemalce B, Seeler JS, Thon G et al. Role of the fission yeast SUMO E3 ligase Pli1p in centromere and telomere maintenance. EMBO J 2004; 23:3844-3853. (Pubitemid 39389715)
    • (2004) EMBO Journal , vol.23 , Issue.19 , pp. 3844-3853
    • Xhemalce, B.1    Seeler, J.-S.2    Thon, G.3    Dejean, A.4    Arcangioli, B.5
  • 113
    • 36149000190 scopus 로고    scopus 로고
    • Effects of aging and dietary restriction on ubiquitination, sumoylation, and the proteasome in the spleen
    • DOI 10.1016/j.febslet.2007.10.054, PII S0014579307011222
    • Zhang L, Li F, Dimayuga E et al. Effects of aging and dietary restriction on ubiquitination, sumoylation and the proteasome in the spleen. FEBS Lett 2007; 581:5543-5547. (Pubitemid 350110436)
    • (2007) FEBS Letters , vol.581 , Issue.28 , pp. 5543-5547
    • Zhang, L.1    Li, F.2    Dimayuga, E.3    Craddock, J.4    Keller, J.N.5
  • 114
    • 34547113757 scopus 로고    scopus 로고
    • Sumoylation of Oct4 enhances its stability, DNA binding, and transactivation
    • DOI 10.1074/jbc.M611041200
    • Wei F, Scholer HR, Atchison ML. Sumoylation od Oct4 enhances its stability, DNA binding and transactivation. J Biol Chem 2007; 282:21551-21560. (Pubitemid 47099909)
    • (2007) Journal of Biological Chemistry , vol.282 , Issue.29 , pp. 21551-21560
    • Wei, F.1    Scholer, H.R.2    Atchison, M.L.3
  • 115
  • 117
    • 0036837660 scopus 로고    scopus 로고
    • Induction of extracellular matrix-remodelling genes by the senescence-associated protein APA-1
    • Benanti J, Williams DK, Robinson KL et al. Induction of extracellular matrix-remodelling genes by the senescence-associated protein APA-1. Mol Cell Biol 2002; 22:7385-7397.
    • (2002) Mol Cell Biol , vol.22 , pp. 7385-7397
    • Benanti, J.1    Williams, D.K.2    Robinson, K.L.3
  • 118
    • 35548935098 scopus 로고    scopus 로고
    • SUMO-Specific Protease 1 Is Essential for Stabilization of HIF1α during Hypoxia
    • DOI 10.1016/j.cell.2007.08.045, PII S0092867407011439
    • Cheng J, Kang X, Zhang S et al. SUMO-specific protease 1 is essential for stabilization of hypoxia-inducible factor-1a during hypoxia. Cell 2007; 131:584-595. (Pubitemid 350007694)
    • (2007) Cell , vol.131 , Issue.3 , pp. 584-595
    • Cheng, J.1    Kang, X.2    Zhang, S.3    Yeh, E.T.H.4
  • 119
    • 45849120181 scopus 로고    scopus 로고
    • Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process
    • Wang YT, Chuang JY, Shen MR et al. Sumoylation of specificity protein 1 augments its degradation by changing the localization and increasing the specificity protein 1 proteolytic process. J Mol Biol 2008; 380:869-885.
    • (2008) J Mol Biol , vol.380 , pp. 869-885
    • Wang, Y.T.1    Chuang, J.Y.2    Shen, M.R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.