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Volumn 51, Issue 3, 2001, Pages 183-204

Integration of the pRB and p53 cell cycle control pathways

Author keywords

Cell cycle; Cell death; Cell growth; P53; PRB; Tumor suppressor gene

Indexed keywords

CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE INHIBITOR; CYCLINE; DNA; PROTEIN MDM2; PROTEIN P21; PROTEIN P27; PROTEIN P53; PROTEIN P57; RETINOBLASTOMA PROTEIN; TRANSCRIPTION FACTOR E2F;

EID: 0035020051     PISSN: 0167594X     EISSN: None     Source Type: Journal    
DOI: 10.1023/A:1010615822317     Document Type: Review
Times cited : (17)

References (270)
  • 1
    • 0025246110 scopus 로고
    • Universal control mechanism regulating onset of M-phase
    • Nurse P: Universal control mechanism regulating onset of M-phase. Nature 344: 503-508, 1990
    • (1990) Nature , vol.344 , pp. 503-508
    • Nurse, P.1
  • 2
    • 0003418645 scopus 로고
    • A restriction point for control of normal animal proliferation
    • Pardee AB: A restriction point for control of normal animal proliferation. Proc Natl Acad Sci USA 71: 1286-1290, 1974
    • (1974) Proc Natl Acad Sci USA , vol.71 , pp. 1286-1290
    • Pardee, A.B.1
  • 3
    • 0028169237 scopus 로고
    • Collaboration of G1 cyclins in the functional inactivation of the retinoblastoma protein
    • Hatakeyama M, Brill JA, Fink GR, Weinberg RA: Collaboration of G1 cyclins in the functional inactivation of the retinoblastoma protein. Genes Dev 8: 1759-1771, 1994
    • (1994) Genes Dev , vol.8 , pp. 1759-1771
    • Hatakeyama, M.1    Brill, J.A.2    Fink, G.R.3    Weinberg, R.A.4
  • 4
    • 0028935698 scopus 로고
    • G1 cyclins control the retinoblastoma gene product growth regulation activity via upstream mechanisms
    • Horton LE, Qian Y, Templeton DJ: G1 cyclins control the retinoblastoma gene product growth regulation activity via upstream mechanisms. Cell Growth Differ 6: 395-407, 1995
    • (1995) Cell Growth Differ , vol.6 , pp. 395-407
    • Horton, L.E.1    Qian, Y.2    Templeton, D.J.3
  • 5
    • 0027336491 scopus 로고
    • Mammalian G1 cyclins
    • Sherr CJ: Mammalian G1 cyclins. Cell 73: 1059-1065, 1993
    • (1993) Cell , vol.73 , pp. 1059-1065
    • Sherr, C.J.1
  • 7
    • 0027154638 scopus 로고
    • Cyclin D1 is a nuclear protein required for cell cycle progression in G1
    • Baldin V, Lukas J, Marcote MJ, Pagano M, Draetta G: Cyclin D1 is a nuclear protein required for cell cycle progression in G1. Genes Dev 7: 812-821, 1993
    • (1993) Genes Dev , vol.7 , pp. 812-821
    • Baldin, V.1    Lukas, J.2    Marcote, M.J.3    Pagano, M.4    Draetta, G.5
  • 8
    • 0028980858 scopus 로고
    • Developmental control of the G1 to S transition in Drosophila: Cyclin e is a limiting downstream target of E2F
    • Duronio RJ, O'Farrell PH: Developmental control of the G1 to S transition in Drosophila: cyclin E is a limiting downstream target of E2F. Genes Dev 9: 1456-1468, 1995
    • (1995) Genes Dev , vol.9 , pp. 1456-1468
    • Duronio, R.J.1    O'Farrell, P.H.2
  • 12
    • 0028999777 scopus 로고
    • Cyclin D2 is a moderately oscillating nucleoprotein required for G1 phase progression in specific cell types
    • Lukas J, Bartkova J, Welcker M, Peterson OW, Peters G, Strauss M, Bartek J: Cyclin D2 is a moderately oscillating nucleoprotein required for G1 phase progression in specific cell types. Oncogene 10: 2125-2134, 1995
    • (1995) Oncogene , vol.10 , pp. 2125-2134
    • Lukas, J.1    Bartkova, J.2    Welcker, M.3    Peterson, O.W.4    Peters, G.5    Strauss, M.6    Bartek, J.7
  • 13
    • 0025850767 scopus 로고
    • Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast
    • Lew DJ, Dulic V, Reed SI: Isolation of three novel human cyclins by rescue of G1 cyclin (Cln) function in yeast. Cell 66: 1197-1206, 1991
    • (1991) Cell , vol.66 , pp. 1197-1206
    • Lew, D.J.1    Dulic, V.2    Reed, S.I.3
  • 14
    • 0028980858 scopus 로고
    • Developmental control of the G1 to S transition in Drosophila: Cyclin e is a limiting downstream target of E2F
    • Duronio RJ, O'Farrell PH: Developmental control of the G1 to S transition in Drosophila: cyclin E is a limiting downstream target of E2F. Genes Dev 9: 1456-1468, 1995
    • (1995) Genes Dev , vol.9 , pp. 1456-1468
    • Duronio, R.J.1    O'Farrell, P.H.2
  • 17
    • 0028039027 scopus 로고
    • CDK6 (PLSTIRE) and CDK4 (PSK-J3) are a distinct subset of the cyclin-dependent kinases that associate with cyclin D1
    • Bates S, Bonetta L, MacAllan D, Parry D, Holder A, Dickson C, Peters G: CDK6 (PLSTIRE) and CDK4 (PSK-J3) are a distinct subset of the cyclin-dependent kinases that associate with cyclin D1. Oncogene 9: 71-79, 1994
    • (1994) Oncogene , vol.9 , pp. 71-79
    • Bates, S.1    Bonetta, L.2    MacAllan, D.3    Parry, D.4    Holder, A.5    Dickson, C.6    Peters, G.7
  • 18
    • 0026778547 scopus 로고
    • Identification and properties of an atypical catalytic subunit (p34PSK-J3/cdk4) for mammalian D type G1 cyclins
    • Matsushime H, Ewen ME, Strom DK, Kato JY, Hanks SK, Roussel MF, Sherr CJ: Identification and properties of an atypical catalytic subunit (p34PSK-J3/cdk4) for mammalian D type G1 cyclins. Cell 71: 323-334, 1992
    • (1992) Cell , vol.71 , pp. 323-334
    • Matsushime, H.1    Ewen, M.E.2    Strom, D.K.3    Kato, J.Y.4    Hanks, S.K.5    Roussel, M.F.6    Sherr, C.J.7
  • 19
    • 0028181760 scopus 로고
    • Identification of G1 kinase activity for cdk6, a novel cyclin D partner
    • Meyerson M, Harlow E: Identification of G1 kinase activity for cdk6, a novel cyclin D partner. Mol Cell Biol 14: 2077-2086, 1994
    • (1994) Mol Cell Biol , vol.14 , pp. 2077-2086
    • Meyerson, M.1    Harlow, E.2
  • 20
    • 0026698263 scopus 로고
    • Association of human cyclin e with a periodic G1-S phase protein kinase
    • Dulic V, Lees E, Reed SI: Association of human cyclin E with a periodic G1-S phase protein kinase. Science 257: 1958-1961, 1992
    • (1992) Science , vol.257 , pp. 1958-1961
    • Dulic, V.1    Lees, E.2    Reed, S.I.3
  • 24
    • 0030012440 scopus 로고    scopus 로고
    • Cyclins D1, D2 and D3 are expressed in distinct tissues during mouse embryogenesis
    • Aguzzi A, Kiess M, Rüedi D, Hamel PA: Cyclins D1, D2 and D3 are expressed in distinct tissues during mouse embryogenesis. Transgenics 2: 29-39, 1996
    • (1996) Transgenics , vol.2 , pp. 29-39
    • Aguzzi, A.1    Kiess, M.2    Rüedi, D.3    Hamel, P.A.4
  • 27
    • 0028987932 scopus 로고
    • Expression of RB, E2F1, cdc2, and D-cyclins, and B-cyclins in developing spinal-cord
    • Zhao JZ, Nornes HO, Neuman T: Expression of RB, E2F1, cdc2, and D-cyclins, and B-cyclins in developing spinal-cord. Neuroscience letters 191: 49-52, 1995
    • (1995) Neuroscience Letters , vol.191 , pp. 49-52
    • Zhao, J.Z.1    Nornes, H.O.2    Neuman, T.3
  • 28
    • 0028869492 scopus 로고
    • Expression of the positive regulator of cell cycle progression, cyclin D3, is induced during differentiation of myoblasts into quiescent myotubes
    • Kiess M, Gill RM, Hamel PA: Expression of the positive regulator of cell cycle progression, cyclin D3, is induced during differentiation of myoblasts into quiescent myotubes. Oncogene 10: 159-166, 1995
    • (1995) Oncogene , vol.10 , pp. 159-166
    • Kiess, M.1    Gill, R.M.2    Hamel, P.A.3
  • 32
    • 0028145332 scopus 로고
    • Ectopic expression of cyclin D1 prevents activation of gene transcription by myogenic basic helix-loop-helix regulators
    • Rao SS, Chu C, Kohtz DS: Ectopic expression of cyclin D1 prevents activation of gene transcription by myogenic basic helix-loop-helix regulators. Mol Cell Biol 14: 5259-5267, 1994
    • (1994) Mol Cell Biol , vol.14 , pp. 5259-5267
    • Rao, S.S.1    Chu, C.2    Kohtz, D.S.3
  • 33
    • 0027133239 scopus 로고
    • Inhibition of granulocyte differentiation by G1 cyclins D2 and D3 but not D1
    • Kato J-Y, Sherr CJ: Inhibition of granulocyte differentiation by G1 cyclins D2 and D3 but not D1. Proc Natl Acad Sci USA 90: 11513-11517, 1993
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 11513-11517
    • Kato, J.-Y.1    Sherr, C.J.2
  • 34
    • 0028926433 scopus 로고
    • Positive and negative regulation of D-type cyclin expression in skeletal myoblasts by basic fibroblast growth factor and transforming growth factor b. a role for cyclin D1 in control of myoblast differentiation
    • Rao SS, Kohtz DS: Positive and negative regulation of D-type cyclin expression in skeletal myoblasts by basic fibroblast growth factor and transforming growth factor b. A role for cyclin D1 in control of myoblast differentiation. J Biol Chem 270: 4093-4100, 1995
    • (1995) J Biol Chem , vol.270 , pp. 4093-4100
    • Rao, S.S.1    Kohtz, D.S.2
  • 35
    • 0033066683 scopus 로고    scopus 로고
    • Critical role played by cyclin D3 in the MyoD-mediated arrest of cell cycle during myoblast differentiation
    • Cenciarelli C, De Santa F, Puri PL, Mattei E, Ricci L, Bucci F, Felsani A, Caruso M: Critical role played by cyclin D3 in the MyoD-mediated arrest of cell cycle during myoblast differentiation (in process citation). Mol Cell Biol 19: 5203-5217, 1999
    • (1999) Mol Cell Biol , vol.19 , pp. 5203-5217
    • Cenciarelli, C.1    De Santa, F.2    Puri, P.L.3    Mattei, E.4    Ricci, L.5    Bucci, F.6    Felsani, A.7    Caruso, M.8
  • 37
    • 0024439444 scopus 로고
    • The retinoblastoma protein is phosphorylated during specific phases of the cell cycle
    • Buchkovich K, Duffy LA, Harlow E: The retinoblastoma protein is phosphorylated during specific phases of the cell cycle. Cell 58: 1097-1105, 1989
    • (1989) Cell , vol.58 , pp. 1097-1105
    • Buchkovich, K.1    Duffy, L.A.2    Harlow, E.3
  • 38
    • 0024429019 scopus 로고
    • Phosphorylation of the retinoblastoma gene product is modulated during the cell cycle and cellular differentiation
    • Chen PL, Scully P, Shew JY, Wang JY, Lee WH: Phosphorylation of the retinoblastoma gene product is modulated during the cell cycle and cellular differentiation. Cell 58: 1193-1198, 1989
    • (1989) Cell , vol.58 , pp. 1193-1198
    • Chen, P.L.1    Scully, P.2    Shew, J.Y.3    Wang, J.Y.4    Lee, W.H.5
  • 41
    • 0027288908 scopus 로고
    • Direct binding of cyclin D to the retinoblastoma gene product (pRB) and pRB phosphorylation by the cyclin D-dependent kinase CDK4
    • Kato J, Matsushime H, Hiebert SW, Ewen ME, Sherr CJ: Direct binding of cyclin D to the retinoblastoma gene product (pRB) and pRB phosphorylation by the cyclin D-dependent kinase CDK4. Genes Dev 7: 331-342, 1993
    • (1993) Genes Dev , vol.7 , pp. 331-342
    • Kato, J.1    Matsushime, H.2    Hiebert, S.W.3    Ewen, M.E.4    Sherr, C.J.5
  • 42
    • 0027229136 scopus 로고
    • Functional interactions of the retinoblastoma protein with mammalian D-type cyclins
    • Ewen ME, Sluss HK, Sherr CJ, Matsushime H, Kato J, Livingston DM: Functional interactions of the retinoblastoma protein with mammalian D-type cyclins. Cell 73: 487-497, 1993
    • (1993) Cell , vol.73 , pp. 487-497
    • Ewen, M.E.1    Sluss, H.K.2    Sherr, C.J.3    Matsushime, H.4    Kato, J.5    Livingston, D.M.6
  • 43
    • 0030015264 scopus 로고    scopus 로고
    • Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases
    • Xiao Z-X, Ginsberg D, Ewen M, Livingston D: Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-associated kinases. Proc Natl Acad Sci USA 93: 4633-4637, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 4633-4637
    • Xiao, Z.-X.1    Ginsberg, D.2    Ewen, M.3    Livingston, D.4
  • 44
    • 0026802989 scopus 로고
    • Regulation of retinoblastoma functions by ectopic expression of human cyclins
    • Hinds PW, Mittnacht S, Dulic V, Arnold A, Reed SI, Weinberg RA: Regulation of retinoblastoma functions by ectopic expression of human cyclins. Cell 70: 993-1006, 1992
    • (1992) Cell , vol.70 , pp. 993-1006
    • Hinds, P.W.1    Mittnacht, S.2    Dulic, V.3    Arnold, A.4    Reed, S.I.5    Weinberg, R.A.6
  • 45
  • 46
    • 0025810049 scopus 로고
    • G1/S phosphorylation of the retinoblastoma protein is associated with an altered affinity for the nuclear compartment
    • Mittnacht S, Weinberg RA: G1/S phosphorylation of the retinoblastoma protein is associated with an altered affinity for the nuclear compartment. Cell 65: 381-393, 1991
    • (1991) Cell , vol.65 , pp. 381-393
    • Mittnacht, S.1    Weinberg, R.A.2
  • 47
    • 0026569054 scopus 로고
    • Regions controlling hyper-phosphorylation and conformation of the retinoblastoma gene product are independent of domains required for transcriptional repression
    • Hamel PA, Gill M, Phillips RA, Gallie BL: Regions controlling hyper-phosphorylation and conformation of the retinoblastoma gene product are independent of domains required for transcriptional repression. Oncogene 7: 693-701, 1992
    • (1992) Oncogene , vol.7 , pp. 693-701
    • Hamel, P.A.1    Gill, M.2    Phillips, R.A.3    Gallie, B.L.4
  • 48
    • 0026769912 scopus 로고
    • Transcriptional repression of the E2-containing promoters EIIaE, c-myc and RB1 by the product of the RB1 gene
    • Hamel PA, Gill RM, Phillips RA, Gallie BL: Transcriptional repression of the E2-containing promoters EIIaE, c-myc and RB1 by the product of the RB1 gene. Mol Cell Biol 12: 3431-3438, 1992
    • (1992) Mol Cell Biol , vol.12 , pp. 3431-3438
    • Hamel, P.A.1    Gill, R.M.2    Phillips, R.A.3    Gallie, B.L.4
  • 49
    • 0028902753 scopus 로고
    • Cytostatic gene therapy for vascular proliferative disorders with a constitutively active form of the retinoblastoma gene product
    • Chang MW, Barr E, Seltzer J, Jiang Y-Q, Nabel GJ, Nabel E, Parmacek MS and Leiden JM: Cytostatic gene therapy for vascular proliferative disorders with a constitutively active form of the retinoblastoma gene product. Science 267: 518-522, 1995
    • (1995) Science , vol.267 , pp. 518-522
    • Chang, M.W.1    Barr, E.2    Seltzer, J.3    Jiang, Y.-Q.4    Nabel, G.J.5    Nabel, E.6    And, P.M.S.7    Leiden, J.M.8
  • 51
    • 0029050533 scopus 로고
    • Deficiency of retinoblastoma protein leads to inappropriate S-phase entry, activation of E2F-responsive genes, and apoptosis
    • Almasan A, Yin YX, Kelly RE, Lee E, Bradley A, Li WW, Bertino JR, Wahl GM: Deficiency of retinoblastoma protein leads to inappropriate S-phase entry, activation of E2F-responsive genes, and apoptosis. Proc Natl Acad Sci USA 92: 5436-5440, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5436-5440
    • Almasan, A.1    Yin, Y.X.2    Kelly, R.E.3    Lee, E.4    Bradley, A.5    Li, W.W.6    Bertino, J.R.7    Wahl, G.M.8
  • 52
    • 0030069682 scopus 로고    scopus 로고
    • Disruption of RB/E2F-1 interaction by single point mutations in E2F-1 enhances S-phase entry and apoptosis
    • Shan B, Durfee T, Lee W-H: Disruption of RB/E2F-1 interaction by single point mutations in E2F-1 enhances S-phase entry and apoptosis. Proc Natl Acad Sci USA 93: 679-684, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 679-684
    • Shan, B.1    Durfee, T.2    Lee, W.-H.3
  • 54
    • 0028914946 scopus 로고
    • Cells differentiating into neuralectoderm undergo apoptosis in the absence of functional retinoblastoma family proteins
    • Slack RS, Skerjanc IS, Lach B, Craig J, Jardine K, McBurney MW: Cells differentiating into neuralectoderm undergo apoptosis in the absence of functional retinoblastoma family proteins. J Cell Biol 129: 779-788, 1995
    • (1995) J Cell Biol , vol.129 , pp. 779-788
    • Slack, R.S.1    Skerjanc, I.S.2    Lach, B.3    Craig, J.4    Jardine, K.5    McBurney, M.W.6
  • 55
    • 0028339957 scopus 로고
    • Reversal of terminal differentiation mediated by p107 in Rb-/- Muscle cells
    • Schneider JW, Gu W, Zhu L, Mahdavi V, Nadal-Ginard B: Reversal of terminal differentiation mediated by p107 in Rb-/- muscle cells. Science 264: 1467-1471, 1994
    • (1994) Science , vol.264 , pp. 1467-1471
    • Schneider, J.W.1    Gu, W.2    Zhu, L.3    Mahdavi, V.4    Nadal-Ginard, B.5
  • 56
    • 0031983190 scopus 로고    scopus 로고
    • p130 is dispensable in peripheral T lymphocytes: Evidence for functional compensation by p107 and pRB
    • Mulligan GJ, Wong J, Jacks T: p130 is dispensable in peripheral T lymphocytes: evidence for functional compensation by p107 and pRB. Mol Cell Biol 18: 206-220, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 206-220
    • Mulligan, G.J.1    Wong, J.2    Jacks, T.3
  • 61
    • 0025785484 scopus 로고
    • Molecular cloning, chromosomal mapping, and expression of the cDNa for p107, a retinoblastoma gene product-related protein
    • Ewen ME, Xing YG, Lawrence JB, Livingston DM: Molecular cloning, chromosomal mapping, and expression of the cDNA for p107, a retinoblastoma gene product-related protein. Cell 66: 1155-1164, 1991
    • (1991) Cell , vol.66 , pp. 1155-1164
    • Ewen, M.E.1    Xing, Y.G.2    Lawrence, J.B.3    Livingston, D.M.4
  • 62
    • 0032437776 scopus 로고    scopus 로고
    • Role of the retinoblastoma protein family, pRB, p107 and p130 in the negative control of cell growth
    • Grana X, Garriga J, Mayol X: Role of the retinoblastoma protein family, pRB, p107 and p130 in the negative control of cell growth. Oncogene 17: 3365-3383, 1998
    • (1998) Oncogene , vol.17 , pp. 3365-3383
    • Grana, X.1    Garriga, J.2    Mayol, X.3
  • 63
    • 0029031349 scopus 로고
    • Regulation of the retinoblastoma protein-related p107 by G1 cyclin complexes
    • Beijersbergen RL, Carlee L, Kerkhoven RM, Bernards R: Regulation of the retinoblastoma protein-related p107 by G1 cyclin complexes. Genes Dev 9: 1340-1353, 1995
    • (1995) Genes Dev , vol.9 , pp. 1340-1353
    • Beijersbergen, R.L.1    Carlee, L.2    Kerkhoven, R.M.3    Bernards, R.4
  • 64
    • 0032473605 scopus 로고    scopus 로고
    • Hyperphosphorylated p107 and p130 bind to T-antigen: Identification of a critical regulatory sequence present in RB but not in p107/p130
    • Knudsen ES, Wang JY: Hyperphosphorylated p107 and p130 bind to T-antigen: identification of a critical regulatory sequence present in RB but not in p107/p130. Oncogene 16: 1655-1663, 1998
    • (1998) Oncogene , vol.16 , pp. 1655-1663
    • Knudsen, E.S.1    Wang, J.Y.2
  • 65
    • 0029026176 scopus 로고
    • The pRB-related protein p107 contains two growth suppression domains: Independent interactions with E2F and cyclin/cdk complexes
    • Zhu L, Enders G, Lees JA, Beijersbergen RL, Bernards R, Harlow E: The pRB-related protein p107 contains two growth suppression domains: independent interactions with E2F and cyclin/cdk complexes. Embo J 14: 1904-1913, 1995
    • (1995) Embo J , vol.14 , pp. 1904-1913
    • Zhu, L.1    Enders, G.2    Lees, J.A.3    Beijersbergen, R.L.4    Bernards, R.5    Harlow, E.6
  • 66
    • 0027415429 scopus 로고
    • Transcriptional repression by the Rb related protein p107
    • Zamanian M, La Thangue NB: Transcriptional repression by the Rb related protein p107. Mol Biol Cell 4: 389-396, 1993
    • (1993) Mol Biol Cell , vol.4 , pp. 389-396
    • Zamanian, M.1    La Thangue, N.B.2
  • 68
    • 0027135209 scopus 로고
    • The adenovirus Ela-associated 130-kDa protein is encoded by a member of the retinoblastoma gene family and physically interacts with cyclins a and E
    • Li Y, Graham C, Lacy S, Duncan AMV, Whyte P: The adenovirus Ela-associated 130-kDa protein is encoded by a member of the retinoblastoma gene family and physically interacts with cyclins A and E. Genes Dev 7: 2366-2377, 1993
    • (1993) Genes Dev , vol.7 , pp. 2366-2377
    • Li, Y.1    Graham, C.2    Lacy, S.3    Duncan, A.M.V.4    Whyte, P.5
  • 70
    • 12044258811 scopus 로고
    • Cloning of a new member of the retinoblastoma gene family (pRb2) which binds to the E1a transforming domain
    • Mayol X, Grana X, Baldi A, Sang N, Hu Q, Giordano A: Cloning of a new member of the retinoblastoma gene family (pRb2) which binds to the E1A transforming domain. Oncogene 8: 2561-2566, 1993
    • (1993) Oncogene , vol.8 , pp. 2561-2566
    • Mayol, X.1    Grana, X.2    Baldi, A.3    Sang, N.4    Hu, Q.5    Giordano, A.6
  • 71
    • 0031782695 scopus 로고    scopus 로고
    • Strain-dependent myeloid hyperplasia, growth deficiency, and accelerated cell cycle in mice lacking the Rb-related p107 gene
    • LeCouter JE, Kablar B, Hardy WR, Ying C, Megeney LA, May LL, Rudnicki MA: Strain-dependent myeloid hyperplasia, growth deficiency, and accelerated cell cycle in mice lacking the Rb-related p107 gene. Mol Cell Biol 18: 7455-7465, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 7455-7465
    • LeCouter, J.E.1    Kablar, B.2    Hardy, W.R.3    Ying, C.4    Megeney, L.A.5    May, L.L.6    Rudnicki, M.A.7
  • 73
    • 0032518906 scopus 로고    scopus 로고
    • Interaction of the pRB-family proteins with paired-like homeodomains
    • Wiggan O, Taniguchi-Sidle A, Hamel PA: Interaction of the pRB-family proteins with paired-like homeodomains. Oncogene 16: 227-236, 1998
    • (1998) Oncogene , vol.16 , pp. 227-236
    • Wiggan, O.1    Taniguchi-Sidle, A.2    Hamel, P.A.3
  • 74
    • 0027499060 scopus 로고
    • Interaction of myogenic factors and the retinblastoma protein mediates muscle cell commitment and differentiation
    • Gu W, Schneider JW, Condorelli G, Kaushai S, Mahdavi V, Nadal-Ginard B: Interaction of myogenic factors and the retinblastoma protein mediates muscle cell commitment and differentiation. Cell 72: 309-324, 1993
    • (1993) Cell , vol.72 , pp. 309-324
    • Gu, W.1    Schneider, J.W.2    Condorelli, G.3    Kaushai, S.4    Mahdavi, V.5    Nadal-Ginard, B.6
  • 75
    • 0029086190 scopus 로고
    • Association of p107 with Sp1: Genetically separable regions of p107 are involved in regulation of E2F- And Sp1-dependent transcription
    • Datta PK, Raychaudhuri P, Bagchi S: Association of p107 with Sp1: genetically separable regions of p107 are involved in regulation of E2F- and Sp1-dependent transcription. Mol Cell Biol 15: 5444-5452, 1995
    • (1995) Mol Cell Biol , vol.15 , pp. 5444-5452
    • Datta, P.K.1    Raychaudhuri, P.2    Bagchi, S.3
  • 78
    • 0029020759 scopus 로고
    • The retinoblastoma protein binds to RIZ, a zinc-finger protein that shares an epitope with the adenovirus E1a protein
    • Buyse IM, Shao G, Huang S: The retinoblastoma protein binds to RIZ, a zinc-finger protein that shares an epitope with the adenovirus E1A protein. Proc Natl Acad Sci USA 92: 4467-4471, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4467-4471
    • Buyse, I.M.1    Shao, G.2    Huang, S.3
  • 79
    • 0030031409 scopus 로고    scopus 로고
    • Retinoblastoma protein directly interacts with and activates the transcription factor NF-IL6
    • Chen P-L, Riley DJ, Chen-Kiang S, Lee W-H: Retinoblastoma protein directly interacts with and activates the transcription factor NF-IL6. Proc Natl Acad Sci USA 93: 465-469, 1996
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 465-469
    • Chen, P.-L.1    Riley, D.J.2    Chen-Kiang, S.3    Lee, W.-H.4
  • 80
    • 0029830342 scopus 로고    scopus 로고
    • Retinoblastoma protein positively regulates terminal adipocyte differentiation through direct interaction with C/EBPs
    • Chen PL, Riley DJ, Chen Y, Lee WH: Retinoblastoma protein positively regulates terminal adipocyte differentiation through direct interaction with C/EBPs. Genes Dev 10: 2794-2804, 1996
    • (1996) Genes Dev , vol.10 , pp. 2794-2804
    • Chen, P.L.1    Riley, D.J.2    Chen, Y.3    Lee, W.H.4
  • 81
  • 83
    • 0026582927 scopus 로고
    • The retinoblastoma protein physically associates with the human cdc2 kinase
    • Hu Q, Lees JA, Buchkovich KJ, Harlow E: The retinoblastoma protein physically associates with the human cdc2 kinase. Mol Cell Biol 12: 971-980, 1992
    • (1992) Mol Cell Biol , vol.12 , pp. 971-980
    • Hu, Q.1    Lees, J.A.2    Buchkovich, K.J.3    Harlow, E.4
  • 84
    • 0028303223 scopus 로고
    • The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein
    • Iavarone A, Garg P, Lasorella A, Hsu J, Israel MA: The helix-loop-helix protein Id-2 enhances cell proliferation and binds to the retinoblastoma protein. Genes Dev 8: 1270-1284, 1994
    • (1994) Genes Dev , vol.8 , pp. 1270-1284
    • Iavarone, A.1    Garg, P.2    Lasorella, A.3    Hsu, J.4    Israel, M.A.5
  • 85
    • 0029115796 scopus 로고
    • 70-kDa heat shock cognate protein interacts directly with the N-terminal region of the retinoblastoma gene product pRb. Identification of a novel region of pRb-mediating protein interaction
    • Inoue A, Torigoe T, Sogahata K, Kamiguchi K, Takahashi S, Sawada Y, Saijo M, Taya Y, Ishii S, Sato N et al.: 70-kDa heat shock cognate protein interacts directly with the N-terminal region of the retinoblastoma gene product pRb. Identification of a novel region of pRb-mediating protein interaction. J Biol Chem 270: 22571-22576, 1995
    • (1995) J Biol Chem , vol.270 , pp. 22571-22576
    • Inoue, A.1    Torigoe, T.2    Sogahata, K.3    Kamiguchi, K.4    Takahashi, S.5    Sawada, Y.6    Saijo, M.7    Taya, Y.8    Ishii, S.9    Sato, N.10
  • 86
    • 0026484975 scopus 로고
    • Molecular cloning of cellular genes encoding retinoblastoma-associated proteins: Identification of a gene with properties of the transcription factor E2F
    • Shan B, Zhu X, Chen PL, Durfee T, Yang Y, Sharp D, Lee WH: Molecular cloning of cellular genes encoding retinoblastoma-associated proteins: identification of a gene with properties of the transcription factor E2F. Mol Cell Biol 12: 5620-5631, 1992
    • (1992) Mol Cell Biol , vol.12 , pp. 5620-5631
    • Shan, B.1    Zhu, X.2    Chen, P.L.3    Durfee, T.4    Yang, Y.5    Sharp, D.6    Lee, W.H.7
  • 88
    • 0027250809 scopus 로고
    • Regulation of the Ets-related transcription factor Elf-1 by binding the retinoblastoma protein
    • Wang C, Petryniak B, Thompson CB, Kaelin WG, Leiden JM: Regulation of the Ets-related transcription factor Elf-1 by binding the retinoblastoma protein. Science 260: 1330-1335, 1993
    • (1993) Science , vol.260 , pp. 1330-1335
    • Wang, C.1    Petryniak, B.2    Thompson, C.B.3    Kaelin, W.G.4    Leiden, J.M.5
  • 89
    • 0030970016 scopus 로고    scopus 로고
    • Functional roles of E2F in cell cycle regulation
    • Fan J, Bertino JR: Functional roles of E2F in cell cycle regulation. Oncogene 14: 1191-1200, 1997
    • (1997) Oncogene , vol.14 , pp. 1191-1200
    • Fan, J.1    Bertino, J.R.2
  • 90
    • 0032146274 scopus 로고    scopus 로고
    • The regulation of E2F by pRB-family proteins
    • Dyson N: The regulation of E2F by pRB-family proteins. Genes Dev 12: 2245-2262, 1998
    • (1998) Genes Dev , vol.12 , pp. 2245-2262
    • Dyson, N.1
  • 91
    • 0031815596 scopus 로고    scopus 로고
    • Toward an understanding of the functional complexity of the E2F and retinoblastoma families
    • Nevins JR: Toward an understanding of the functional complexity of the E2F and retinoblastoma families. Cell Growth Differ 9: 585-593, 1998
    • (1998) Cell Growth Differ , vol.9 , pp. 585-593
    • Nevins, J.R.1
  • 92
    • 0022633668 scopus 로고
    • E1a transcription induction: Enhanced binding of a factor to upstream promoter sequences
    • Kovesdi I, Reichel R, Nevins JR: E1A transcription induction: enhanced binding of a factor to upstream promoter sequences. Science 231: 719-722, 1986
    • (1986) Science , vol.231 , pp. 719-722
    • Kovesdi, I.1    Reichel, R.2    Nevins, J.R.3
  • 93
    • 0029583648 scopus 로고
    • Regulation of the cyclin e gene by transcription factor E2F1
    • Ohtani K, DeGregori J, Nevins JR: Regulation of the cyclin E gene by transcription factor E2F1. Proc Natl Acad Sci USA 92: 12146-12150, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12146-12150
    • Ohtani, K.1    DeGregori, J.2    Nevins, J.R.3
  • 94
    • 0021812170 scopus 로고
    • Transcriptional regulation of mouse dihydrofolate reductase in the cell cycle
    • Farnham PJ, Schimke RT: Transcriptional regulation of mouse dihydrofolate reductase in the cell cycle. J Biol Chem 260: 7675-7680, 1985
    • (1985) J Biol Chem , vol.260 , pp. 7675-7680
    • Farnham, P.J.1    Schimke, R.T.2
  • 95
    • 0028960161 scopus 로고
    • An inverted repeat motif stabilizes binding of E2F and enhances transcription of the dihydrofolate reductase gene
    • Wade M, Blake MC, Jambou RC, Helin K, Harlow E, Azizkhan JC: An inverted repeat motif stabilizes binding of E2F and enhances transcription of the dihydrofolate reductase gene. J Biol Chem 270: 9783-9791, 1995
    • (1995) J Biol Chem , vol.270 , pp. 9783-9791
    • Wade, M.1    Blake, M.C.2    Jambou, R.C.3    Helin, K.4    Harlow, E.5    Azizkhan, J.C.6
  • 96
    • 0027403342 scopus 로고
    • A protein synthesis-dependent increase in E2F1 mRNA correlates with growth regulation of the dihydrofulate reductase promoter
    • Slansky JE, Li Y, Kaelin WG, Farnham PJ: A protein synthesis-dependent increase in E2F1 mRNA correlates with growth regulation of the dihydrofulate reductase promoter. Mol Cell Biol 12: 5620-5631, 1993
    • (1993) Mol Cell Biol , vol.12 , pp. 5620-5631
    • Slansky, J.E.1    Li, Y.2    Kaelin, W.G.3    Farnham, P.J.4
  • 97
    • 0029049577 scopus 로고
    • Cellular targets for activation by the E2F1 transcription factor include DNA synthesis and G1/S regulatory genes
    • DeGregori J, Kowalik T, Nevins JR: Cellular targets for activation by the E2F1 transcription factor include DNA synthesis and G1/S regulatory genes. Mol Cell Biol 15: 4215-4224, 1995
    • (1995) Mol Cell Biol , vol.15 , pp. 4215-4224
    • DeGregori, J.1    Kowalik, T.2    Nevins, J.R.3
  • 98
    • 0032933352 scopus 로고    scopus 로고
    • E2F and histone deacetylase mediate transforming growth factor beta repression of cdc25 a during keratinocyte cell cycle arrest
    • Iavarone A, Massague J: E2F and histone deacetylase mediate transforming growth factor beta repression of cdc25 A during keratinocyte cell cycle arrest. Mol Cell Biol 19: 916-922, 1999
    • (1999) Mol Cell Biol , vol.19 , pp. 916-922
    • Iavarone, A.1    Massague, J.2
  • 99
    • 0027988521 scopus 로고
    • The role of cellular transcription factor E2F in the regulation of cdc2 messenger-RNA expression and cell-cycle control of human hematopoietic-cells
    • Furukawa Y, Terui Y, Sakoe K, Ohta M, Saito M: The role of cellular transcription factor E2F in the regulation of cdc2 messenger-RNA expression and cell-cycle control of human hematopoietic-cells. J Biol Chem 269: 26249-26258, 1994
    • (1994) J Biol Chem , vol.269 , pp. 26249-26258
    • Furukawa, Y.1    Terui, Y.2    Sakoe, K.3    Ohta, M.4    Saito, M.5
  • 100
    • 0028364529 scopus 로고
    • Autoregulatory control of E2F1 expression in response to positive and negative regulators of cell cycle progression
    • Johnson DG, Ohtani K, Nevins JR: Autoregulatory control of E2F1 expression in response to positive and negative regulators of cell cycle progression. Genes Dev 8: 1514-1525, 1994
    • (1994) Genes Dev , vol.8 , pp. 1514-1525
    • Johnson, D.G.1    Ohtani, K.2    Nevins, J.R.3
  • 101
    • 0028276864 scopus 로고
    • Multiple DNA elements are required for the growth regulation of the mouse E2F1 promoter
    • Hsiao KM, McMahon SL, Farnham PJ: Multiple DNA elements are required for the growth regulation of the mouse E2F1 promoter. Genes Dev 8: 1526-1537, 1994
    • (1994) Genes Dev , vol.8 , pp. 1526-1537
    • Hsiao, K.M.1    McMahon, S.L.2    Farnham, P.J.3
  • 103
    • 0027186225 scopus 로고
    • Molecular cloning and characterization of the mouse RB1 promoter
    • Zacksenhaus E, Gill RM, Phillips RA, Gallie BL: Molecular cloning and characterization of the mouse RB1 promoter. Oncogene 8: 2343-2351, 1993
    • (1993) Oncogene , vol.8 , pp. 2343-2351
    • Zacksenhaus, E.1    Gill, R.M.2    Phillips, R.A.3    Gallie, B.L.4
  • 104
    • 0028144410 scopus 로고
    • The transcription factor E2F-1 mediates the autoregulation of RB gene expression
    • Shan B, Chang CY, Jones D, Lee WH: The transcription factor E2F-1 mediates the autoregulation of RB gene expression. Mol Cell Biol 14: 299-309, 1994
    • (1994) Mol Cell Biol , vol.14 , pp. 299-309
    • Shan, B.1    Chang, C.Y.2    Jones, D.3    Lee, W.H.4
  • 105
    • 0029054133 scopus 로고
    • Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins
    • Zhu L, Zhu L, Xie E, Chang LS: Differential roles of two tandem E2F sites in repression of the human p107 promoter by retinoblastoma and p107 proteins. Mol Cell Biol 15: 3552-3562, 1995
    • (1995) Mol Cell Biol , vol.15 , pp. 3552-3562
    • Zhu, L.1    Xie, E.2    Chang, L.S.3
  • 106
    • 0026636908 scopus 로고
    • Retinolastoma protein switches the E2F site from a positive to a negative element
    • Weintraub SJ, Prater CA, Dean DC: Retinolastoma protein switches the E2F site from a positive to a negative element. Nature 358: 259-261, 1992
    • (1992) Nature , vol.358 , pp. 259-261
    • Weintraub, S.J.1    Prater, C.A.2    Dean, D.C.3
  • 109
    • 0032549001 scopus 로고    scopus 로고
    • Rb interacts with histone deacetylase to repress transcription
    • Luo RX, Postigo AA, Dean DC: Rb interacts with histone deacetylase to repress transcription. Cell 92: 463-473, 1998
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 110
    • 0030959767 scopus 로고    scopus 로고
    • Expression patterns of the E2F family of transcription factors during mouse nervous system development
    • Dagnino L, Fry CJ, Bartley SM, Farnham P, Gallie BL, Phillips RA: Expression patterns of the E2F family of transcription factors during mouse nervous system development. Mech Dev 66: 13-25, 1997
    • (1997) Mech Dev , vol.66 , pp. 13-25
    • Dagnino, L.1    Fry, C.J.2    Bartley, S.M.3    Farnham, P.4    Gallie, B.L.5    Phillips, R.A.6
  • 111
  • 115
    • 0032528027 scopus 로고    scopus 로고
    • E2F3 activity is regulated during the cell cycle and is required for the induction of S phase
    • Leone G, DeGregori J, Yan Z, Jakoi L, Ishida S, Williams RS, Nevins JR: E2F3 activity is regulated during the cell cycle and is required for the induction of S phase. Genes Dev 12: 2120-2130, 1998
    • (1998) Genes Dev , vol.12 , pp. 2120-2130
    • Leone, G.1    DeGregori, J.2    Yan, Z.3    Jakoi, L.4    Ishida, S.5    Williams, R.S.6    Nevins, J.R.7
  • 117
    • 0034011378 scopus 로고    scopus 로고
    • Identification of a Novel E2F3 Product Suggests a Mechanism for Determining Specificity of Repression by Rb
    • Leone G, Nuckolls F, Ishida S, Adams M, Sears R, Jakoi L, Miron A, Nevins JR: Identification of a Novel E2F3 Product Suggests a Mechanism for Determining Specificity of Repression by Rb. Mol Cell Biol 20: 3626-3632, 2000
    • (2000) Mol Cell Biol , vol.20 , pp. 3626-3632
    • Leone, G.1    Nuckolls, F.2    Ishida, S.3    Adams, M.4    Sears, R.5    Jakoi, L.6    Miron, A.7    Nevins, J.R.8
  • 118
    • 0029008686 scopus 로고
    • Expression of a deletion mutant of the E2F1 transcription factor in fibroblasts lengthens S phase and increases sensitivity to S phase-specific toxins
    • Logan TJ, Evans DL, Mercer WE, Bjornsti MA, Hall DJ: Expression of a deletion mutant of the E2F1 transcription factor in fibroblasts lengthens S phase and increases sensitivity to S phase-specific toxins. Cancer Res 55: 2883-2891, 1995
    • (1995) Cancer Res , vol.55 , pp. 2883-2891
    • Logan, T.J.1    Evans, D.L.2    Mercer, W.E.3    Bjornsti, M.A.4    Hall, D.J.5
  • 119
    • 0032160407 scopus 로고    scopus 로고
    • Key Roles for E2F1 in Signaling p53-Dependent Apoptosis, in Cell Division within Developing Tumors
    • Pan H, Yin C, Dyson NJ, Harlow E, Yamasaki L, Van Dyke T: Key Roles for E2F1 in Signaling p53-Dependent Apoptosis, in Cell Division within Developing Tumors. Mol Cell 2: 283-292, 1998
    • (1998) Mol Cell , vol.2 , pp. 283-292
    • Pan, H.1    Yin, C.2    Dyson, N.J.3    Harlow, E.4    Yamasaki, L.5    Van Dyke, T.6
  • 120
    • 0031992159 scopus 로고    scopus 로고
    • E2F1-specific induction of apoptosis and p53 accumulation, which is blocked by Mdm2
    • Kowalik TF, DeGregori J, Leone G, Jakoi L, Nevins JR: E2F1-specific induction of apoptosis and p53 accumulation, which is blocked by Mdm2. Cell Growth Differ 9: 113-118, 1998
    • (1998) Cell Growth Differ , vol.9 , pp. 113-118
    • Kowalik, T.F.1    DeGregori, J.2    Leone, G.3    Jakoi, L.4    Nevins, J.R.5
  • 121
    • 0029819994 scopus 로고    scopus 로고
    • pRb controls proliferation, differentiation, and death of skeletal muscle cells and other lineages during embryogenesis
    • Zacksenhaus E, Jiang Z, Chung D, Marth JD, Phillips RA, Gallie BL: pRb controls proliferation, differentiation, and death of skeletal muscle cells and other lineages during embryogenesis. Genes Dev 10: 3051-3064, 1996
    • (1996) Genes Dev , vol.10 , pp. 3051-3064
    • Zacksenhaus, E.1    Jiang, Z.2    Chung, D.3    Marth, J.D.4    Phillips, R.A.5    Gallie, B.L.6
  • 122
    • 0032551995 scopus 로고    scopus 로고
    • The E2F-family proteins induce distinct cell cycle regulatory factors in p16-arrested, U343 astrocytoma cells
    • Dirks PB, Rutka JT, Hubbard SL, Mondal S, Hamel PA: The E2F-family proteins induce distinct cell cycle regulatory factors in p16-arrested, U343 astrocytoma cells. Oncogene 17: 867-876, 1998
    • (1998) Oncogene , vol.17 , pp. 867-876
    • Dirks, P.B.1    Rutka, J.T.2    Hubbard, S.L.3    Mondal, S.4    Hamel, P.A.5
  • 123
    • 15444353328 scopus 로고    scopus 로고
    • pRB and p107/p130 are required for the regulated expression of different sets of E2F responsive genes
    • Hurford RK Jr, Cobrinik D, Lee MH, Dyson N: pRB and p107/p130 are required for the regulated expression of different sets of E2F responsive genes. Genes Dev 11: 1447-1463, 1997
    • (1997) Genes Dev , vol.11 , pp. 1447-1463
    • Hurford R.K., Jr.1    Cobrinik, D.2    Lee, M.H.3    Dyson, N.4
  • 125
    • 0028819819 scopus 로고
    • Expression and activity of the retinoblastoma protein (pRB)-family proteins, p107 and p130, during L6 myoblast differentiation
    • Kiess M, Gill RM, Hamel PA: Expression and activity of the retinoblastoma protein (pRB)-family proteins, p107 and p130, during L6 myoblast differentiation. Cell Growth Differ 6: 1287-1298, 1995
    • (1995) Cell Growth Differ , vol.6 , pp. 1287-1298
    • Kiess, M.1    Gill, R.M.2    Hamel, P.A.3
  • 126
    • 0034175616 scopus 로고    scopus 로고
    • Analysis of promoter binding by the E2F and pRB families in vivo: Distinct E2F proteins mediate activation and repression
    • Takahashi Y, Rayman JB, Dynlacht BD: Analysis of promoter binding by the E2F and pRB families in vivo: distinct E2F proteins mediate activation and repression. Genes Dev 14: 804-816, 2000
    • (2000) Genes Dev , vol.14 , pp. 804-816
    • Takahashi, Y.1    Rayman, J.B.2    Dynlacht, B.D.3
  • 127
    • 0034689001 scopus 로고    scopus 로고
    • Subcellular compartmentalization of E2F family members is required for maintenance of the post-mitotic state in terminally differentiated muscle
    • Gill RM, Hamel PA: Subcellular compartmentalization of E2F family members is required for maintenance of the post-mitotic state in terminally differentiated muscle. J Cell Biol 148: 1187-1201, 2000
    • (2000) J Cell Biol , vol.148 , pp. 1187-1201
    • Gill, R.M.1    Hamel, P.A.2
  • 128
    • 0030667320 scopus 로고    scopus 로고
    • E2F activity is regulated by cell cycle-dependent changes in subcellular localization
    • Verona R, Moberg K, Estes S, Starz M, Vernon JP, Lees JA: E2F activity is regulated by cell cycle-dependent changes in subcellular localization. Mol Cell Biol 17: 7268-7282, 1997
    • (1997) Mol Cell Biol , vol.17 , pp. 7268-7282
    • Verona, R.1    Moberg, K.2    Estes, S.3    Starz, M.4    Vernon, J.P.5    Lees, J.A.6
  • 129
    • 0031051261 scopus 로고    scopus 로고
    • Concentration of RB protein in nucleus vs. cytoplasm is stable as phosphorylation of RB changes during the cell cycle and differentiation
    • Yen A, Coder D, Varvayanis S: Concentration of RB protein in nucleus vs. cytoplasm is stable as phosphorylation of RB changes during the cell cycle and differentiation. Eur J Cell Biol 72: 159-165, 1997
    • (1997) Eur J Cell Biol , vol.72 , pp. 159-165
    • Yen, A.1    Coder, D.2    Varvayanis, S.3
  • 130
    • 0029978325 scopus 로고    scopus 로고
    • E2F-4 switches from p130 to p107 and pRB in response to cell cycle reentry
    • Moberg K, Starz MA, Lees JA: E2F-4 switches from p130 to p107 and pRB in response to cell cycle reentry. Mol Cell Biol 16: 1436-1449, 1996
    • (1996) Mol Cell Biol , vol.16 , pp. 1436-1449
    • Moberg, K.1    Starz, M.A.2    Lees, J.A.3
  • 131
    • 0028362359 scopus 로고
    • Negative regulation of the growth-promoting transcription factor E2F-1 by a stably bound cyclin A-dependent protein kinase
    • Krek W, Ewen ME, Shirodkar S, Arany Z, Kaelin WG Jr, Livingston DM: Negative regulation of the growth-promoting transcription factor E2F-1 by a stably bound cyclin A-dependent protein kinase. Cell 78: 161-172, 1994
    • (1994) Cell , vol.78 , pp. 161-172
    • Krek, W.1    Ewen, M.E.2    Shirodkar, S.3    Arany, Z.4    Kaelin W.G., Jr.5    Livingston, D.M.6
  • 132
    • 0029559027 scopus 로고
    • Cyclin A-kinase regulation of E2F-1 DNA binding function underlies suppression of an S phase checkpoint
    • Krek W, Xu G, Livingston DM: Cyclin A-kinase regulation of E2F-1 DNA binding function underlies suppression of an S phase checkpoint. Cell 83: 1149-1158, 1995
    • (1995) Cell , vol.83 , pp. 1149-1158
    • Krek, W.1    Xu, G.2    Livingston, D.M.3
  • 133
    • 0030941458 scopus 로고    scopus 로고
    • p53, the cellular gatekeeper for growth and division
    • Levine AJ: p53, the cellular gatekeeper for growth and division. Cell 88: 323-331, 1997
    • (1997) Cell , vol.88 , pp. 323-331
    • Levine, A.J.1
  • 134
    • 0032192140 scopus 로고    scopus 로고
    • The complexity of p53 modulation: Emerging patterns from divergent signals
    • Giaccia AJ, Kastan MB: The complexity of p53 modulation: emerging patterns from divergent signals. Genes Dev 12: 2973-2983, 1998
    • (1998) Genes Dev , vol.12 , pp. 2973-2983
    • Giaccia, A.J.1    Kastan, M.B.2
  • 136
    • 0027459198 scopus 로고
    • mdm2 expression is induced by wild type p53 activity
    • Barak Y, Juven T, Haffner R, Oren M: mdm2 expression is induced by wild type p53 activity. Embo J 12: 461-468, 1993
    • (1993) Embo J , vol.12 , pp. 461-468
    • Barak, Y.1    Juven, T.2    Haffner, R.3    Oren, M.4
  • 138
    • 0027944251 scopus 로고
    • Cyclin G is a transcriptional target of the p53 tumor suppressor protein
    • Okamoto K, Beach D: Cyclin G is a transcriptional target of the p53 tumor suppressor protein. Embo J 13: 4816-4822, 1994
    • (1994) Embo J , vol.13 , pp. 4816-4822
    • Okamoto, K.1    Beach, D.2
  • 139
    • 0028883179 scopus 로고
    • Tumor suppressor p53 is a direct transcriptional activator of the human bax gene
    • Miyashita T, Reed JC: Tumor suppressor p53 is a direct transcriptional activator of the human bax gene. Cell 80: 293-299, 1995
    • (1995) Cell , vol.80 , pp. 293-299
    • Miyashita, T.1    Reed, J.C.2
  • 141
    • 0029972806 scopus 로고    scopus 로고
    • p53: Puzzle and paradigm
    • Ko LJ, Prives C: p53: puzzle and paradigm. Genes Dev 10: 1054-1072, 1996
    • (1996) Genes Dev , vol.10 , pp. 1054-1072
    • Ko, L.J.1    Prives, C.2
  • 142
    • 0025887476 scopus 로고
    • Wild-type p53 can down- Modulate the activity of various promoters
    • Ginsberg D, Mechta F, Yaniv M, Oren M: Wild-type p53 can down- modulate the activity of various promoters. Proc Natl Acad Sci USA 88: 9979-9983, 1991
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 9979-9983
    • Ginsberg, D.1    Mechta, F.2    Yaniv, M.3    Oren, M.4
  • 143
    • 0027318117 scopus 로고
    • Specific repression of TATA-mediated but not initiator-mediated transcription by wild-type p53
    • Mack DH, Vartikar J, Pipas JM, Laimins LA: Specific repression of TATA-mediated but not initiator-mediated transcription by wild-type p53. Nature 363: 281-283, 1993
    • (1993) Nature , vol.363 , pp. 281-283
    • Mack, D.H.1    Vartikar, J.2    Pipas, J.M.3    Laimins, L.A.4
  • 144
    • 0026642078 scopus 로고
    • Inhibition of viral and cellular promoters by human wild-type p53
    • Subler MA, Martin DW, Deb S: Inhibition of viral and cellular promoters by human wild-type p53. J Virol 66: 4757-4762, 1992
    • (1992) J Virol , vol.66 , pp. 4757-4762
    • Subler, M.A.1    Martin, D.W.2    Deb, S.3
  • 145
    • 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, George DL: Tumorigenic potential associated with enhanced expression of a gene that is amplified in a mouse tumor cell line. Embo J 10: 1565-1569, 1991
    • (1991) Embo J , vol.10 , pp. 1565-1569
    • Fakharzadeh, S.S.1    Trusko, S.P.2    George, D.L.3
  • 146
    • 0027222956 scopus 로고
    • Mapping of the p53 and mdm-2 interaction domains
    • Chen J, Marechal V, Levine AJ: Mapping of the p53 and mdm-2 interaction domains. Mol Cell Biol 13: 4107-4114, 1993
    • (1993) Mol Cell Biol , vol.13 , pp. 4107-4114
    • Chen, J.1    Marechal, V.2    Levine, A.J.3
  • 148
    • 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, Levine AJ: The mdm-2 oncogene product forms a complex with the p53 protein and inhibits p53-mediated transactivation. Cell 69: 1237-1245, 1992
    • (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
  • 150
    • 0030860911 scopus 로고    scopus 로고
    • Repression of p53-mediated transcription by MDM2: A dual mechanism
    • Thut CJ, Goodrich JA, Tjian R: Repression of p53-mediated transcription by MDM2: a dual mechanism. Genes Dev 11: 1974-1986, 1997
    • (1997) Genes Dev , vol.11 , pp. 1974-1986
    • Thut, C.J.1    Goodrich, J.A.2    Tjian, R.3
  • 151
    • 0029171789 scopus 로고
    • Regulation of transcription functions of the p53 tumor suppressor by the mdm-2 oncogene
    • Chen J, Lin J, Levine AJ: Regulation of transcription functions of the p53 tumor suppressor by the mdm-2 oncogene. Mol Med 1: 142-152, 1995
    • (1995) Mol Med , vol.1 , pp. 142-152
    • Chen, J.1    Lin, J.2    Levine, A.J.3
  • 152
    • 0028823020 scopus 로고
    • Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53
    • Montes de Oca Luna R, Wagner DS, Lozano, G: Rescue of early embryonic lethality in mdm2-deficient mice by deletion of p53. Nature 378: 203-206, 1995
    • (1995) Nature , vol.378 , pp. 203-206
    • Montes De Oca Luna, R.1    Wagner, D.S.2    Lozano, G.3
  • 153
    • 0030905284 scopus 로고    scopus 로고
    • Mdm2 promotes the rapid degradation of p53
    • Haupt Y, Maya R, Kazaz A, Oren M: Mdm2 promotes the rapid degradation of p53. Nature 387: 296-299, 1997
    • (1997) Nature , vol.387 , pp. 296-299
    • Haupt, Y.1    Maya, R.2    Kazaz, A.3    Oren, M.4
  • 154
  • 155
    • 0031702817 scopus 로고    scopus 로고
    • Regulation of Mdm2- Directed degradation by the C terminus of p53
    • Kubbutat MH, Ludwig RL, Ashcroft M, Vousden KH: Regulation of Mdm2- directed degradation by the C terminus of p53. Mol Cell Biol 18: 5690-5698, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 5690-5698
    • Kubbutat, M.H.1    Ludwig, R.L.2    Ashcroft, M.3    Vousden, K.H.4
  • 156
    • 0032980646 scopus 로고    scopus 로고
    • Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53
    • Tao W, Levine AJ: Nucleocytoplasmic shuttling of oncoprotein Hdm2 is required for Hdm2-mediated degradation of p53. Proc Natl Acad Sci USA 96: 3077-3080, 1999
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 3077-3080
    • Tao, W.1    Levine, A.J.2
  • 157
    • 0031724593 scopus 로고    scopus 로고
    • Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6
    • Freedman DA, Levine AJ: Nuclear export is required for degradation of endogenous p53 by MDM2 and human papillomavirus E6. Mol Cell Biol 18: 7288-7293, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 7288-7293
    • Freedman, D.A.1    Levine, A.J.2
  • 158
    • 0032518917 scopus 로고    scopus 로고
    • Nucleo-cytoplasmic 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, Levine AJ: Nucleo-cytoplasmic 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
    • (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
  • 159
    • 0031583962 scopus 로고    scopus 로고
    • Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53
    • Honda R, Tanaka H, Yasuda H: Oncoprotein MDM2 is a ubiquitin ligase E3 for tumor suppressor p53. FEBS Lett 420: 25-27, 1997
    • (1997) FEBS Lett , vol.420 , pp. 25-27
    • Honda, R.1    Tanaka, H.2    Yasuda, H.3
  • 160
    • 0034624678 scopus 로고    scopus 로고
    • Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase
    • Honda R, Yasuda H: Activity of MDM2, a ubiquitin ligase, toward p53 or itself is dependent on the RING finger domain of the ligase. Oncogene 19: 1473-1476, 2000
    • (2000) Oncogene , vol.19 , pp. 1473-1476
    • Honda, R.1    Yasuda, H.2
  • 161
    • 0032512057 scopus 로고    scopus 로고
    • Mdm2 association with p53 targets its ubiquitination
    • Fuchs SY, Adler V, Buschmann T, Wu X, Ronai Z: Mdm2 association with p53 targets its ubiquitination. Oncogene 17: 2543-2547, 1998
    • (1998) Oncogene , vol.17 , pp. 2543-2547
    • Fuchs, S.Y.1    Adler, V.2    Buschmann, T.3    Wu, X.4    Ronai, Z.5
  • 162
    • 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, Weissman AM: Mdm2 is a RING finger-dependent ubiquitin protein ligase for itself and p53 (in process itation). J Biol Chem 275: 8945-8951, 2000
    • (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
  • 163
    • 0027244853 scopus 로고
    • The p53-mdm-2 autoregulatory feedback loop
    • Wu X, Bayle JH, Olson D, Levine AJ: The p53-mdm-2 autoregulatory feedback loop. Genes Dev 7: 1126-1132, 1993
    • (1993) Genes Dev , vol.7 , pp. 1126-1132
    • Wu, X.1    Bayle, J.H.2    Olson, D.3    Levine, A.J.4
  • 164
    • 0030667702 scopus 로고    scopus 로고
    • DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2
    • Shieh SY, Ikeda M, Taya Y, Prives C: DNA damage-induced phosphorylation of p53 alleviates inhibition by MDM2. Cell 91: 325-334, 1997
    • (1997) Cell , vol.91 , pp. 325-334
    • Shieh, S.Y.1    Ikeda, M.2    Taya, Y.3    Prives, C.4
  • 166
    • 0029315510 scopus 로고
    • Tumour suppressors, kinases and clamps: How p53 regulates the cell cycle in response to DNA damage
    • Cox LS, Lane, DP: Tumour suppressors, kinases and clamps: how p53 regulates the cell cycle in response to DNA damage. Bioessays 17: 501-508, 1995
    • (1995) Bioessays , vol.17 , pp. 501-508
    • Cox, L.S.1    Lane, D.P.2
  • 167
    • 0033598754 scopus 로고    scopus 로고
    • Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage
    • Chehab NH, Malikzay A, Stavridi ES, Halazonetis TD: Phosphorylation of Ser-20 mediates stabilization of human p53 in response to DNA damage. Proc Natl Acad Sci USA 96: 13777-13782, 1999
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 13777-13782
    • Chehab, N.H.1    Malikzay, A.2    Stavridi, E.S.3    Halazonetis, T.D.4
  • 168
    • 0030665146 scopus 로고    scopus 로고
    • Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53
    • Mayo LD, Turchi JJ, Berberich SJ: Mdm-2 phosphorylation by DNA-dependent protein kinase prevents interaction with p53. Cancer Res 57: 5013-5016, 1997
    • (1997) Cancer Res , vol.57 , pp. 5013-5016
    • Mayo, L.D.1    Turchi, J.J.2    Berberich, S.J.3
  • 169
    • 0027496935 scopus 로고
    • The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases
    • Harper JW, Adami GR, Wei N, Keyomarsi K, Elledge SJ: The p21 Cdk-interacting protein Cip1 is a potent inhibitor of G1 cyclin-dependent kinases. Cell 75: 805-816, 1993
    • (1993) Cell , vol.75 , pp. 805-816
    • Harper, J.W.1    Adami, G.R.2    Wei, N.3    Keyomarsi, K.4    Elledge, S.J.5
  • 170
    • 0027437850 scopus 로고
    • Cdi1, a human G1 and S phase protein phosphatase that associates with cdk2
    • Gyuris J, Golemis E, Chertkov H, Brent R: Cdi1, a human G1 and S phase protein phosphatase that associates with cdk2. Cell 75: 791-803, 1993
    • (1993) Cell , vol.75 , pp. 791-803
    • Gyuris, J.1    Golemis, E.2    Chertkov, H.3    Brent, R.4
  • 171
    • 0028895385 scopus 로고
    • Identification of the active region of the DNA synthesis inhibitory gene p21Sdi1/CIP1/WAF1
    • Nakanishi M, Robetorye RS, Adami GR, Pereira-Smith OM, Smith JR: Identification of the active region of the DNA synthesis inhibitory gene p21Sdi1/CIP1/WAF1. Embo J 14: 555-563, 1995
    • (1995) Embo J , vol.14 , pp. 555-563
    • Nakanishi, M.1    Robetorye, R.S.2    Adami, G.R.3    Pereira-Smith, O.M.4    Smith, J.R.5
  • 174
  • 175
    • 0029670838 scopus 로고    scopus 로고
    • Inhibition of G1 cyclin-dependent kinase activity during growth arrest of human breast carcinoma cells
    • Gorospe M, Liu Y, Xu Q, Chrest FJ, Holbrook NJ: Inhibition of G1 cyclin-dependent kinase activity during growth arrest of human breast carcinoma cells. Mol Cell Biol 16: 762-770, 1996
    • (1996) Mol Cell Biol , vol.16 , pp. 762-770
    • Gorospe, M.1    Liu, Y.2    Xu, Q.3    Chrest, F.J.4    Holbrook, N.J.5
  • 178
    • 0030044395 scopus 로고    scopus 로고
    • p53-independent increase in p21WAF1 and reciprocal down-regulation of cyclin a and proliferating cell nuclear antigen in bromodeoxyuridine-mediated growth arrest of human melanoma cells
    • Strasberg Rieber M, Welch DR, Miele ME, Rieber M: p53-independent increase in p21WAF1 and reciprocal down-regulation of cyclin A and proliferating cell nuclear antigen in bromodeoxyuridine-mediated growth arrest of human melanoma cells. Cell Growth Differ 7: 197-202, 1996
    • (1996) Cell Growth Differ , vol.7 , pp. 197-202
    • Strasberg Rieber, M.1    Welch, D.R.2    Miele, M.E.3    Rieber, M.4
  • 179
    • 0030761736 scopus 로고    scopus 로고
    • A p53-independent pathway for induction of p21waf1cip1 and concomitant G1 arrest in UV-irradiated human skin fibroblasts
    • Loignon M, Fetni R, Gordon AJ, Drobetsky EA: A p53-independent pathway for induction of p21waf1cip1 and concomitant G1 arrest in UV-irradiated human skin fibroblasts. Cancer Res 57: 3390-3394, 1997
    • (1997) Cancer Res , vol.57 , pp. 3390-3394
    • Loignon, M.1    Fetni, R.2    Gordon, A.J.3    Drobetsky, E.A.4
  • 180
    • 0029073142 scopus 로고
    • Transforming growth factor beta induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism
    • Datto MB, Li Y, Panus JF, Howe DJ, Xiong Y, Wang XF: Transforming growth factor beta induces the cyclin-dependent kinase inhibitor p21 through a p53-independent mechanism. Proc Natl Acad Sci USA 92: 5545-5549, 1995
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 5545-5549
    • Datto, M.B.1    Li, Y.2    Panus, J.F.3    Howe, D.J.4    Xiong, Y.5    Wang, X.F.6
  • 181
    • 0028352434 scopus 로고
    • The p21 inhibitor of cyclin-dependent kinases controls DNA replication by interaction with PCNA
    • Waga S, Hannon GJ, Beach D, Stillman B: The p21 inhibitor of cyclin-dependent kinases controls DNA replication by interaction with PCNA. Nature 369: 574-578, 1994
    • (1994) Nature , vol.369 , pp. 574-578
    • Waga, S.1    Hannon, G.J.2    Beach, D.3    Stillman, B.4
  • 182
    • 0023091938 scopus 로고
    • Functional identity of proliferating cell nuclear antigen and a DNa polymerase-delta auxiliary protein
    • Prelich G, Tan CK, Kostura M, Mathews MB, So AG, Downey KM, Stillman B: Functional identity of proliferating cell nuclear antigen and a DNA polymerase-delta auxiliary protein. Nature 326: 517-520, 1987
    • (1987) Nature , vol.326 , pp. 517-520
    • Prelich, G.1    Tan, C.K.2    Kostura, M.3    Mathews, M.B.4    So, A.G.5    Downey, K.M.6    Stillman, B.7
  • 183
    • 0029063745 scopus 로고
    • Cell-cycle inhibition by independent CDK and PCNA binding domains in p21Cip1
    • Luo Y, Hurwitz J, Massague J: Cell-cycle inhibition by independent CDK and PCNA binding domains in p21Cip1. Nature 375: 159-161, 1995
    • (1995) Nature , vol.375 , pp. 159-161
    • Luo, Y.1    Hurwitz, J.2    Massague, J.3
  • 184
    • 0028074603 scopus 로고
    • Differential effects by the p21 CDK inhibitor on PCNA dependent DNA replication and repair
    • Li R, Waga S, Hannon GJ, Beach D, Stillman B: Differential effects by the p21 CDK inhibitor on PCNA dependent DNA replication and repair. Nature 371: 534-537, 1994
    • (1994) Nature , vol.371 , pp. 534-537
    • Li, R.1    Waga, S.2    Hannon, G.J.3    Beach, D.4    Stillman, B.5
  • 185
    • 0028899480 scopus 로고
    • Separate domains of p21 involved in the inhibition of Cdk kinase and PCNA
    • Chen J, Jackson PK, Kirschner MW, Dutta A: Separate domains of p21 involved in the inhibition of Cdk kinase and PCNA. Nature 374: 386-388, 1995
    • (1995) Nature , vol.374 , pp. 386-388
    • Chen, J.1    Jackson, P.K.2    Kirschner, M.W.3    Dutta, A.4
  • 187
    • 0029784513 scopus 로고    scopus 로고
    • Cyclin-binding motifs are essential for the function of p21CIP1
    • Chen J, Saha P, Kornbluth S, Dynlacht BD, Dutta A: Cyclin-binding motifs are essential for the function of p21CIP1. Mol Cell Biol 16: 4673-4682, 1996
    • (1996) Mol Cell Biol , vol.16 , pp. 4673-4682
    • Chen, J.1    Saha, P.2    Kornbluth, S.3    Dynlacht, B.D.4    Dutta, A.5
  • 188
    • 0029948612 scopus 로고    scopus 로고
    • p21 contains independent binding sites for cyclin and cdk2: Both sites are required to inhibit cdk2 kinase activity
    • Fotedar R, Fitzgerald P, Rousselle T, Cannella D, Doree M, Messier H, Fotedar A: p21 contains independent binding sites for cyclin and cdk2: both sites are required to inhibit cdk2 kinase activity. Oncogene 12: 2155-2164, 1996
    • (1996) Oncogene , vol.12 , pp. 2155-2164
    • Fotedar, R.1    Fitzgerald, P.2    Rousselle, T.3    Cannella, D.4    Doree, M.5    Messier, H.6    Fotedar, A.7
  • 193
    • 0028363519 scopus 로고
    • p27, a novel inhibitor of G1 cyclin-cdk protein kinase activity, is related to p21
    • Toyoshima H, Hunter T: p27, a novel inhibitor of G1 cyclin-cdk protein kinase activity, is related to p21. Cell 78: 67-74, 1994
    • (1994) Cell , vol.78 , pp. 67-74
    • Toyoshima, H.1    Hunter, T.2
  • 195
    • 0028263008 scopus 로고
    • The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization
    • Mehlen P, Arrigo AP: The serum-induced phosphorylation of mammalian hsp27 correlates with changes in its intracellular localization and levels of oligomerization. Eur J Biochem 221: 327-334, 1994
    • (1994) Eur J Biochem , vol.221 , pp. 327-334
    • Mehlen, P.1    Arrigo, A.P.2
  • 197
    • 0033561445 scopus 로고    scopus 로고
    • Induced differentiation of U937 cells by 1,25-dihydroxyvitamin D3 involves cell cycle arrest in G1 that is preceded by a transient proliferative burst and an increase in cyclin expression
    • Rots NY, Iavarone A, Bromleigh V, Freedman LP: Induced differentiation of U937 cells by 1,25-dihydroxyvitamin D3 involves cell cycle arrest in G1 that is preceded by a transient proliferative burst and an increase in cyclin expression. Blood 93: 2721-2729, 1999
    • (1999) Blood , vol.93 , pp. 2721-2729
    • Rots, N.Y.1    Iavarone, A.2    Bromleigh, V.3    Freedman, L.P.4
  • 198
    • 0031014017 scopus 로고    scopus 로고
    • Growth inhibitory effect of interferon-beta is associated with the induction of cyclin-dependent kinase inhibitor p27Kip1 in a human gastric carcinoma cell line
    • Kuniyasu H, Yasui W, Kitahara K, Naka K, Yokozaki H, Akama Y, Hamamoto T, Tahara H, Tahara E: Growth inhibitory effect of interferon-beta is associated with the induction of cyclin-dependent kinase inhibitor p27Kip1 in a human gastric carcinoma cell line. Cell Growth Differ 8: 47-52, 1997
    • (1997) Cell Growth Differ , vol.8 , pp. 47-52
    • Kuniyasu, H.1    Yasui, W.2    Kitahara, K.3    Naka, K.4    Yokozaki, H.5    Akama, Y.6    Hamamoto, T.7    Tahara, H.8    Tahara, E.9
  • 199
    • 0032576887 scopus 로고    scopus 로고
    • Differential expression of the p27Kip1 mRNA in IFN-sensitive and resistant cell lines
    • Moro A, Calixto A, Suarez E, Arana MJ, Perea SE: Differential expression of the p27Kip1 mRNA in IFN-sensitive and resistant cell lines. Biochem Biophys Res Commun 245: 752-756, 1998
    • (1998) Biochem Biophys Res Commun , vol.245 , pp. 752-756
    • Moro, A.1    Calixto, A.2    Suarez, E.3    Arana, M.J.4    Perea, S.E.5
  • 201
    • 0033611586 scopus 로고    scopus 로고
    • p27 is involved in N-cadherin-mediated contact inhibition of cell growth and S-phase entry
    • Levenberg S, Yarden A, Kam Z, Geiger B: p27 is involved in N-cadherin-mediated contact inhibition of cell growth and S-phase entry. Oncogene 18: 869-876, 1999
    • (1999) Oncogene , vol.18 , pp. 869-876
    • Levenberg, S.1    Yarden, A.2    Kam, Z.3    Geiger, B.4
  • 202
    • 0033572879 scopus 로고    scopus 로고
    • Activation of a cAMP pathway and induction of melano-genesis correlate with association of p16(INK4) and p27(KIP1) to CDKs, loss of E2F-binding activity, and premature senescence of human melanocytes
    • Haddad MM, Xu W, Schwahn DJ, Liao F, Medrano EE: Activation of a cAMP pathway and induction of melano-genesis correlate with association of p16(INK4) and p27(KIP1) to CDKs, loss of E2F-binding activity, and premature senescence of human melanocytes. Exp Cell Res 253: 561-572, 1999
    • (1999) Exp Cell Res , vol.253 , pp. 561-572
    • Haddad, M.M.1    Xu, W.2    Schwahn, D.J.3    Liao, F.4    Medrano, E.E.5
  • 203
    • 0034602969 scopus 로고    scopus 로고
    • Reentry into the cell cycle of contactinhibited vascular endothelial cells by a phosphatase inhibitor. Possible involvement of extracellular signalregulated kinase and phosphatidylinositol 3-kinase
    • Suzuki E, Nagata D, Yoshizumi M, Kakoki M, Goto A, Omata M, Hirata Y: Reentry into the cell cycle of contactinhibited vascular endothelial cells by a phosphatase inhibitor. Possible involvement of extracellular signalregulated kinase and phosphatidylinositol 3-kinase. J Biol Chem 275: 3637-3644, 2000
    • (2000) J Biol Chem , vol.275 , pp. 3637-3644
    • Suzuki, E.1    Nagata, D.2    Yoshizumi, M.3    Kakoki, M.4    Goto, A.5    Omata, M.6    Hirata, Y.7
  • 205
    • 0029153609 scopus 로고
    • Kip/Cip and Ink4 Cdk inhibitors cooperate to induce cell cycle arrest in response to TGF-beta
    • Reynisdottir I, Polyak K, lavarone A, Massague J: Kip/Cip and Ink4 Cdk inhibitors cooperate to induce cell cycle arrest in response to TGF-beta. Genes Dev 9: 1831-1845, 1995
    • (1995) Genes Dev , vol.9 , pp. 1831-1845
    • Reynisdottir, I.1    Polyak, K.2    Lavarone, A.3    Massague, J.4
  • 206
    • 0030614715 scopus 로고    scopus 로고
    • The subcellular locations of p15(Ink4b) andp27(Kip1) coordinate their inhibitory interactions with cdk4 and cdk2
    • Reynisdottir I, Massague J: The subcellular locations of p15(Ink4b) andp27(Kip1) coordinate their inhibitory interactions with cdk4 and cdk2. Genes Dev 11: 492-503, 1997
    • (1997) Genes Dev , vol.11 , pp. 492-503
    • Reynisdottir, I.1    Massague, J.2
  • 210
    • 0033559264 scopus 로고    scopus 로고
    • The p21(Cip1) and p27(Kip1) CDK 'inhibitors' are essential activators of cyclin D-dependent kinases in murine fibroblasts
    • Cheng M, Olivier P, Diehl JA, Fero M, Roussel MF, Roberts JM, Sherr CJ: The p21(Cip1) and p27(Kip1) CDK 'inhibitors' are essential activators of cyclin D-dependent kinases in murine fibroblasts. Embo J 18: 1571-1583, 1999
    • (1999) Embo J , vol.18 , pp. 1571-1583
    • Cheng, M.1    Olivier, P.2    Diehl, J.A.3    Fero, M.4    Roussel, M.F.5    Roberts, J.M.6    Sherr, C.J.7
  • 212
    • 0032980425 scopus 로고    scopus 로고
    • Cyclin D-CDK subunit arrangement is dependent on the availability of competing INK4 and p21 class inhibitors
    • Parry D, Mahony D, Wills K, Lees E: Cyclin D-CDK subunit arrangement is dependent on the availability of competing INK4 and p21 class inhibitors. Mol Cell Biol 19: 1775-1783, 1999
    • (1999) Mol Cell Biol , vol.19 , pp. 1775-1783
    • Parry, D.1    Mahony, D.2    Wills, K.3    Lees, E.4
  • 215
    • 0028988158 scopus 로고
    • Kip2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution
    • Kip2, a cyclin-dependent kinase inhibitor with unique domain structure and tissue distribution. Genes Dev 9: 639-649, 1995
    • (1995) Genes Dev , vol.9 , pp. 639-649
    • Lee, M.-H.1    Reynisdóttir, I.2    Massague, J.3
  • 216
    • 0032539602 scopus 로고    scopus 로고
    • Suppression of cell transformation by the cyclin-dependent kinase inhibitor p57KIP2 requires binding to proliferating cell nuclear antigen
    • Watanabe H, Pan ZQ, Schreiber-Agus N, DePinho RA, Hurwitz J, Xiong Y: Suppression of cell transformation by the cyclin-dependent kinase inhibitor p57KIP2 requires binding to proliferating cell nuclear antigen. Proc Natl Acad Sci USA 95: 1392-1397, 1998
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 1392-1397
    • Watanabe, H.1    Pan, Z.Q.2    Schreiber-Agus, N.3    DePinho, R.A.4    Hurwitz, J.5    Xiong, Y.6
  • 217
    • 0032568666 scopus 로고    scopus 로고
    • Critical role for the 310 helix region of p57(Kip2) in cyclin-dependent kinase 2 inhibition and growth suppression
    • Hashimoto Y, Kohri K, Kaneko Y, Morisaki H, Kato T, Ikeda K, Nakanishi M: Critical role for the 310 helix region of p57(Kip2) in cyclin-dependent kinase 2 inhibition and growth suppression. J Biol Chem 273: 16544-16550, 1998
    • (1998) J Biol Chem , vol.273 , pp. 16544-16550
    • Hashimoto, Y.1    Kohri, K.2    Kaneko, Y.3    Morisaki, H.4    Kato, T.5    Ikeda, K.6    Nakanishi, M.7
  • 218
    • 0027769876 scopus 로고
    • A new regulatory motif in cell cycle control causing specific inhibition of cyclin D/CDK4
    • Serrano M, Hannon G, Beach D: A new regulatory motif in cell cycle control causing specific inhibition of cyclin D/CDK4. Nature 366: 704-707, 1993
    • (1993) Nature , vol.366 , pp. 704-707
    • Serrano, M.1    Hannon, G.2    Beach, D.3
  • 220
    • 0028168242 scopus 로고
    • Ink4b is a potential effector of cell cycle arrest mediated by TGFb
    • Ink4b is a potential effector of cell cycle arrest mediated by TGFb. Nature 371: 257-261, 1994
    • (1994) Nature , vol.371 , pp. 257-261
    • Hannon, G.J.1    Beach, D.2
  • 222
    • 0028918388 scopus 로고
    • Novel INK4 proteins, p19 and p18, are specific inhibitors of the cyclein D-dependent kinases, cdk4 and cdk6
    • Hirai H, Rouseel MF, Kato J-Y, Ashmun RA, Sherr CJ: Novel INK4 proteins, p19 and p18, are specific inhibitors of the cyclein D-dependent kinases, cdk4 and cdk6. Mol Cell Biol 15: 2672-2681, 1995
    • (1995) Mol Cell Biol , vol.15 , pp. 2672-2681
    • Hirai, H.1    Rouseel, M.F.2    Kato, J.-Y.3    Ashmun, R.A.4    Sherr, C.J.5
  • 225
    • 0032541623 scopus 로고    scopus 로고
    • Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a
    • Russo AA, Tong L, Lee JO, Jeffrey PD, Pavletich NP: Structural basis for inhibition of the cyclin-dependent kinase Cdk6 by the tumour suppressor p16INK4a. Nature 395: 237-243, 1998
    • (1998) Nature , vol.395 , pp. 237-243
    • Russo, A.A.1    Tong, L.2    Lee, J.O.3    Jeffrey, P.D.4    Pavletich, N.P.5
  • 226
    • 0028875086 scopus 로고
    • Evidence for different modes of action of cyclin-dependent kinase inhibitors: P15 and p16 bind to kinases, p21 and p27 bind to cyclins
    • Hall M, Bates S, Peters G: Evidence for different modes of action of cyclin-dependent kinase inhibitors: p15 and p16 bind to kinases, p21 and p27 bind to cyclins. Oncogene 11: 1581-1588, 1995
    • (1995) Oncogene , vol.11 , pp. 1581-1588
    • Hall, M.1    Bates, S.2    Peters, G.3
  • 227
    • 0030053513 scopus 로고    scopus 로고
    • Mutational analysis of the p16 family cyclin-dependent kinase inhibitors p15INK4b and p18INK4c in tumor-derived alleles and primary tumors
    • Zariwala M, Liu E, Xiong Y: Mutational analysis of the p16 family cyclin-dependent kinase inhibitors p15INK4b and p18INK4c in tumor-derived alleles and primary tumors. Oncogene 12: 451-455, 1996
    • (1996) Oncogene , vol.12 , pp. 451-455
    • Zariwala, M.1    Liu, E.2    Xiong, Y.3
  • 228
    • 0028862489 scopus 로고
    • Biochemical and mutagenic analysis of the melanoma tumor suppressor gene product, p16
    • Wick ST, Dubay MM, Imanil I, Brizuela L: Biochemical and mutagenic analysis of the melanoma tumor suppressor gene product, p16. Oncogene 11: 2013-2019, 1995
    • (1995) Oncogene , vol.11 , pp. 2013-2019
    • Wick, S.T.1    Dubay, M.M.2    Imanil, I.3    Brizuela, L.4
  • 229
    • 0028918388 scopus 로고
    • Novel INK4 proteins, p19 and p18, are specific inhibitors of the cyclin D-dependent kinases CDK4 and CDK6
    • Hirai H, Roussel MF, Kato JY, Ashmun RA, Sherr CJ: Novel INK4 proteins, p19 and p18, are specific inhibitors of the cyclin D-dependent kinases CDK4 and CDK6. Mol Cell Biol 15: 2672-2681, 1995
    • (1995) Mol Cell Biol , vol.15 , pp. 2672-2681
    • Hirai, H.1    Roussel, M.F.2    Kato, J.Y.3    Ashmun, R.A.4    Sherr, C.J.5
  • 230
    • 0030612349 scopus 로고    scopus 로고
    • Expression of the p16INK4a tumor suppressor versus other INK4 family members during mouse development and aging
    • Zindy F, Quelle DE, Roussel MF, Sherr CJ: Expression of the p16INK4a tumor suppressor versus other INK4 family members during mouse development and aging. Oncogene 15: 203-211, 1997
    • (1997) Oncogene , vol.15 , pp. 203-211
    • Zindy, F.1    Quelle, D.E.2    Roussel, M.F.3    Sherr, C.J.4
  • 231
  • 234
    • 0032530112 scopus 로고    scopus 로고
    • CDK inhibitors p18(INK4c) and p27(Kip1) mediate two separate pathways to collaboratively suppress pituitary tumorigenesis
    • Franklin DS, Godfrey VL, Lee H, Kovalev GI, Schoonhoven R, Chen-Kiang S, Su L, Xiong Y: CDK inhibitors p18(INK4c) and p27(Kip1) mediate two separate pathways to collaboratively suppress pituitary tumorigenesis. Genes Dev 12: 2899-2911, 1998
    • (1998) Genes Dev , vol.12 , pp. 2899-2911
    • Franklin, D.S.1    Godfrey, V.L.2    Lee, H.3    Kovalev, G.I.4    Schoonhoven, R.5    Chen-Kiang, S.6    Su, L.7    Xiong, Y.8
  • 235
    • 0032981481 scopus 로고    scopus 로고
    • Induced expression of p16(INK4a) inhibits both CDK4-and CDK2-associated kinase activity by reassortment of cyclin-CDK-inhibitor complexes
    • McConnell BB, Gregory FJ, Stott FJ, Hara E, Peters G: Induced expression of p16(INK4a) inhibits both CDK4-and CDK2-associated kinase activity by reassortment of cyclin-CDK-inhibitor complexes. Mol Cell Biol 19: 1981-1989, 1999
    • (1999) Mol Cell Biol , vol.19 , pp. 1981-1989
    • McConnell, B.B.1    Gregory, F.J.2    Stott, F.J.3    Hara, E.4    Peters, G.5
  • 237
    • 0027298902 scopus 로고
    • The cdk2 kinase is required for the G1-to-S transition in mammalian cells
    • Tsai L-H, Lees E, Faha B, Harlow E, Riabowol K: The cdk2 kinase is required for the G1-to-S transition in mammalian cells. Oncogene 8: 1593-1602, 1993
    • (1993) Oncogene , vol.8 , pp. 1593-1602
    • Tsai, L.-H.1    Lees, E.2    Faha, B.3    Harlow, E.4    Riabowol, K.5
  • 238
    • 0031842101 scopus 로고    scopus 로고
    • Requirement of cyclin E-Cdk2 inhibition in p16(INK4a)-mediated growth suppression
    • Jiang H, Chou HS, Zhu L: Requirement of cyclin E-Cdk2 inhibition in p16(INK4a)-mediated growth suppression. Mol Cell Biol 18: 5284-5290, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 5284-5290
    • Jiang, H.1    Chou, H.S.2    Zhu, L.3
  • 240
    • 0029587551 scopus 로고
    • Alternative reading frames of the INK4a tumor suppressor gene encode unrelated proteins capable of inducing cell cycle arrest
    • Quelle DE, Zindy F, Ashmun RA, Sherr CJ: Alternative reading frames of the INK4a tumor suppressor gene encode unrelated proteins capable of inducing cell cycle arrest. Cell 83: 993-1000, 1995
    • (1995) Cell , vol.83 , pp. 993-1000
    • Quelle, D.E.1    Zindy, F.2    Ashmun, R.A.3    Sherr, C.J.4
  • 241
    • 0031771497 scopus 로고    scopus 로고
    • The human ARF cell cycle regulatory gene promoter is a CpG island which can be silenced by DNa methylation and down-regulated by wild-type p53
    • Robertson KD, Jones PA: The human ARF cell cycle regulatory gene promoter is a CpG island which can be silenced by DNA methylation and down-regulated by wild-type p53. Mol Cell Biol 18: 6457-6473, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 6457-6473
    • Robertson, K.D.1    Jones, P.A.2
  • 244
    • 0033166440 scopus 로고    scopus 로고
    • Tissue-specific alternative splicing in the human INK4a/ARF cell cycle regulatory locus
    • Robertson KD, Jones PA: Tissue-specific alternative splicing in the human INK4a/ARF cell cycle regulatory locus. Oncogene 18: 3810-3820, 1999
    • (1999) Oncogene , vol.18 , pp. 3810-3820
    • Robertson, K.D.1    Jones, P.A.2
  • 246
    • 0033000482 scopus 로고    scopus 로고
    • Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53
    • Zhang Y, Xiong Y: Mutations in human ARF exon 2 disrupt its nucleolar localization and impair its ability to block nuclear export of MDM2 and p53. Mol Cell 3: 579-591, 1999
    • (1999) Mol Cell , vol.3 , pp. 579-591
    • Zhang, Y.1    Xiong, Y.2
  • 248
    • 0033521621 scopus 로고    scopus 로고
    • Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53
    • Honda R, Yasuda H: Association of p19(ARF) with Mdm2 inhibits ubiquitin ligase activity of Mdm2 for tumor suppressor p53. Embo J 18: 22-27, 1999
    • (1999) Embo J , vol.18 , pp. 22-27
    • Honda, R.1    Yasuda, H.2
  • 249
    • 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, Yarbrough WG: 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
    • (1998) Cell , vol.92 , pp. 725-734
    • Zhang, Y.1    Xiong, Y.2    Yarbrough, W.G.3
  • 250
    • 0033536063 scopus 로고    scopus 로고
    • P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2
    • Tao W, Levine AJ: P19(ARF) stabilizes p53 by blocking nucleo-cytoplasmic shuttling of Mdm2. Proc Natl Acad Sci USA 96: 6937-6941, 1999
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 6937-6941
    • Tao, W.1    Levine, A.J.2
  • 252
    • 0033614298 scopus 로고    scopus 로고
    • p19ARF prevents G1 cyclin-dependent kinase activation by interacting with MDM2 and activating p53 in mouse fibroblasts
    • Kurokawa K, Tanaka T, Kato J: p19ARF prevents G1 cyclin-dependent kinase activation by interacting with MDM2 and activating p53 in mouse fibroblasts. Oncogene 18: 2718-2727, 1999
    • (1999) Oncogene , vol.18 , pp. 2718-2727
    • Kurokawa, K.1    Tanaka, T.2    Kato, J.3
  • 253
    • 0029587551 scopus 로고
    • Alternative reading frames of the INK4a tumor suppressor gene encode two unrelated proteins capable of inducing cell cycle arrest
    • Quelle DE, Zindy F, Ashmun RA, Sherr CJ: Alternative reading frames of the INK4a tumor suppressor gene encode two unrelated proteins capable of inducing cell cycle arrest. Cell 83: 993-1000, 1995
    • (1995) Cell , vol.83 , pp. 993-1000
    • Quelle, D.E.1    Zindy, F.2    Ashmun, R.A.3    Sherr, C.J.4
  • 254
    • 0033552813 scopus 로고    scopus 로고
    • The oncogene and Polycomb-group gene bmi-1 regulates cell proliferation and senescence through the ink4a locus
    • Jacobs JJ, Kieboom K, Marino S, DePinho RA, van Lohuizen M: The oncogene and Polycomb-group gene bmi-1 regulates cell proliferation and senescence through the ink4a locus. Nature 397: 164-168, 1999
    • (1999) Nature , vol.397 , pp. 164-168
    • Jacobs, J.J.1    Kieboom, K.2    Marino, S.3    DePinho, R.A.4    Van Lohuizen, M.5
  • 255
    • 0033569429 scopus 로고    scopus 로고
    • Bmi-1 collaborates with c-Myc in tumorigenesis by inhibiting c-Myc-induced apoptosis via INK4a/ARF
    • Jacobs JJ, Scheijen B, Voncken JW, Kieboom K, Berns A, van Lohuizen M: Bmi-1 collaborates with c-Myc in tumorigenesis by inhibiting c-Myc-induced apoptosis via INK4a/ARF. Genes Dev 13: 2678-2690, 1999
    • (1999) Genes Dev , vol.13 , pp. 2678-2690
    • Jacobs, J.J.1    Scheijen, B.2    Voncken, J.W.3    Kieboom, K.4    Berns, A.5    Van Lohuizen, M.6
  • 256
    • 0034724446 scopus 로고    scopus 로고
    • Differential requirement for p19ARF in the p53-dependent arrest induced by DNA damage, microtubule disruption, and ribonucleotide depletion (in process citation)
    • Khan SH, Moritsugu J, Wahl GM: Differential requirement for p19ARF in the p53-dependent arrest induced by DNA damage, microtubule disruption, and ribonucleotide depletion (in process citation). Proc Natl Acad Sci USA 97: 3266-3271, 2000
    • (2000) Proc Natl Acad Sci USA , vol.97 , pp. 3266-3271
    • Khan, S.H.1    Moritsugu, J.2    Wahl, G.M.3
  • 259
    • 0032997265 scopus 로고    scopus 로고
    • p53 mediates apoptotic crisis in primary Abelson virus-transformed pre- B cells
    • Unnikrishnan I, Radfar A, Jenab-Wolcott J, Rosenberg N: p53 mediates apoptotic crisis in primary Abelson virus-transformed pre- B cells. Mol Cell Biol 19: 4825-4831, 1999
    • (1999) Mol Cell Biol , vol.19 , pp. 4825-4831
    • Unnikrishnan, I.1    Radfar, A.2    Jenab-Wolcott, J.3    Rosenberg, N.4
  • 260
    • 0032504784 scopus 로고    scopus 로고
    • p19ARF links the tumour suppressor p53 to Ras
    • Palmero I, Pantoja C, Serrano M: p19ARF links the tumour suppressor p53 to Ras (letter). Nature 395: 125-126, 1998
    • (1998) Nature , vol.395 , pp. 125-126
    • Palmero, I.1    Pantoja, C.2    Serrano, M.3
  • 264
    • 0026728326 scopus 로고
    • The retinoblastoma protein region required for interaction with the E2F transcription factor includes the T/E1A binding and carboxy-terminal sequences
    • Huang S, Shin E, Sheppard KA, Chokroverty L, Shan B, Qian YW, Lee EY, Yee, AS: The retinoblastoma protein region required for interaction with the E2F transcription factor includes the T/E1A binding and carboxy-terminal sequences. DNA Cell Biol 11: 539-548, 1992
    • (1992) DNA Cell Biol , vol.11 , pp. 539-548
    • Huang, S.1    Shin, E.2    Sheppard, K.A.3    Chokroverty, L.4    Shan, B.5    Qian, Y.W.6    Lee, E.Y.7    Yee, A.S.8
  • 265
    • 0031862730 scopus 로고    scopus 로고
    • Growth suppression by an E2F-binding-defective retinoblastoma protein (RB): Contribution from the RB C pocket
    • Whitaker LL, Su H, Baskaran R, Knudsen ES, Wang JY: Growth suppression by an E2F-binding-defective retinoblastoma protein (RB): contribution from the RB C pocket. Mol Cell Biol 18: 4032-4042, 1998
    • (1998) Mol Cell Biol , vol.18 , pp. 4032-4042
    • Whitaker, L.L.1    Su, H.2    Baskaran, R.3    Knudsen, E.S.4    Wang, J.Y.5
  • 266
    • 0027212380 scopus 로고
    • Regions of the Retinoblastoma gene product required for its interaction with the E2F transcription factor are necessary for E2-promoter repression and pRB-mediated growth suppression
    • Hiebert SW: Regions of the Retinoblastoma gene product required for its interaction with the E2F transcription factor are necessary for E2-promoter repression and pRB-mediated growth suppression. Molecular and Cellular Biology 13: 3384-3391, 1993
    • (1993) Molecular and Cellular Biology , vol.13 , pp. 3384-3391
    • Hiebert, S.W.1
  • 267
    • 0032545222 scopus 로고    scopus 로고
    • p53-independent role of MDM2 in TGF-betal resistance
    • Sun P, Dong P, Dai K, Hannon GJ, Beach D: p53-independent role of MDM2 in TGF-betal resistance. Science 282: 2270-2272, 1998
    • (1998) Science , vol.282 , pp. 2270-2272
    • Sun, P.1    Dong, P.2    Dai, K.3    Hannon, G.J.4    Beach, D.5
  • 268
    • 0033622003 scopus 로고    scopus 로고
    • p16INK4A and p19ARF act in overlapping pathways in cellular immortalization
    • Carnero A, Hudson JD, Price CM, Beach DH: p16INK4A and p19ARF act in overlapping pathways in cellular immortalization (in process citation). Nat Cell Biol 2: 148-155, 2000
    • (2000) Nat Cell Biol , vol.2 , pp. 148-155
    • Carnero, A.1    Hudson, J.D.2    Price, C.M.3    Beach, D.H.4


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