메뉴 건너뛰기




Volumn 33, Issue 15, 2014, Pages 1890-1903

Signaling through cyclin D-dependent kinases

Author keywords

apoptosis; CDK4; CDK6; cell cycle; cyclin; senescence

Indexed keywords

ANIMALS; CELL CYCLE; CELL TRANSFORMATION, NEOPLASTIC; CYCLIN D; CYCLIN-DEPENDENT KINASES; HUMANS; PROTEIN UNFOLDING; SIGNAL TRANSDUCTION;

EID: 84899434901     PISSN: 09509232     EISSN: 14765594     Source Type: Journal    
DOI: 10.1038/onc.2013.137     Document Type: Review
Times cited : (237)

References (203)
  • 1
    • 60749109846 scopus 로고    scopus 로고
    • Cell cycle CDKs and cancer: A changing paradigm
    • Malumbres M, Barbacid M. Cell cycle, CDKs and cancer: A changing paradigm. Nat Rev Cancer 2009; 9: 153-166
    • (2009) Nat Rev Cancer , vol.9 , pp. 153-166
    • Malumbres, M.1    Barbacid, M.2
  • 2
    • 0028978274 scopus 로고
    • A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma
    • Wolfel T, Hauer M, Schneider J, Serrano M, Wolfel C, Klehmann-Hieb E, et al. A p16INK4a-insensitive CDK4 mutant targeted by cytolytic T lymphocytes in a human melanoma. Science 1995; 269: 1281-1284
    • (1995) Science , vol.269 , pp. 1281-1284
    • Wolfel, T.1    Hauer, M.2    Schneider, J.3    Serrano, M.4    Wolfel, C.5    Klehmann-Hieb, E.6
  • 3
    • 0028652269 scopus 로고
    • CDKN2 (p16/MTS1) gene deletion or CDK4 amplification occurs in the majority of glioblastomas
    • Schmidt EE, Ichimura K, Reifenberger G, Collins VP. CDKN2 (p16/MTS1) gene deletion or CDK4 amplification occurs in the majority of glioblastomas. Cancer Res 1994; 54: 6321-6324
    • (1994) Cancer Res , vol.54 , pp. 6321-6324
    • Schmidt, E.E.1    Ichimura, K.2    Reifenberger, G.3    Collins, V.P.4
  • 4
    • 0028061974 scopus 로고
    • CDK4 amplification is an alternative mechanism to p16 gene homozygous deletion in glioma cell lines
    • He J, Allen JR, Collins VP, Allalunis-Turner MJ, Godbout R, Day 3rd RS, et al. CDK4 amplification is an alternative mechanism to p16 gene homozygous deletion in glioma cell lines. Cancer Res 1994; 54: 5804-5807
    • (1994) Cancer Res , vol.54 , pp. 5804-5807
    • He, J.1    Allen, J.R.2    Collins, V.P.3    Allalunis-Turner, M.J.4    Godbout, R.5    Day III, R.S.6
  • 6
    • 0030982897 scopus 로고    scopus 로고
    • Cyclindependent kinase 6 (CDK6) amplification in human gliomas identified using twodimensional separation of genomic DNA
    • Costello JF, Plass C, Arap W, Chapman VM, Held WA, Berger MS, et al. Cyclindependent kinase 6 (CDK6) amplification in human gliomas identified using twodimensional separation of genomic DNA. Cancer Res 1997; 57: 1250-1254
    • (1997) Cancer Res , vol.57 , pp. 1250-1254
    • Costello, J.F.1    Plass, C.2    Arap, W.3    Chapman, V.M.4    Held, W.A.5    Berger, M.S.6
  • 9
    • 52149123619 scopus 로고    scopus 로고
    • Core signaling pathways in human pancreatic cancers revealed by global genomic analyses
    • Jones S, Zhang X, Parsons DW, Lin JC, Leary RJ, Angenendt P, et al. Core signaling pathways in human pancreatic cancers revealed by global genomic analyses. Science 2008; 321: 1801-1806
    • (2008) Science , vol.321 , pp. 1801-1806
    • Jones, S.1    Zhang, X.2    Parsons, D.W.3    Lin, J.C.4    Leary, R.J.5    Angenendt, P.6
  • 12
    • 30344479175 scopus 로고    scopus 로고
    • Cyclin D1-dependent kinase activity in murine development and mammary tumorigenesis
    • Landis MW, Pawlyk BS, Li T, Sicinski P, Hinds PW. Cyclin D1-dependent kinase activity in murine development and mammary tumorigenesis. Cancer Cell 2006; 9: 13-22
    • (2006) Cancer Cell , vol.9 , pp. 13-22
    • Landis, M.W.1    Pawlyk, B.S.2    Li, T.3    Sicinski, P.4    Hinds, P.W.5
  • 13
    • 77954279920 scopus 로고    scopus 로고
    • A synthetic lethal interaction between K-Ras oncogenes and Cdk4 unveils a therapeutic strategy for non-small cell lung carcinoma
    • Puyol M, Martin A, Dubus P, Mulero F, Pizcueta P, Khan G, et al. A synthetic lethal interaction between K-Ras oncogenes and Cdk4 unveils a therapeutic strategy for non-small cell lung carcinoma. Cancer Cell 2010; 18: 63-73
    • (2010) Cancer Cell , vol.18 , pp. 63-73
    • Puyol, M.1    Martin, A.2    Dubus, P.3    Mulero, F.4    Pizcueta, P.5    Khan, G.6
  • 15
    • 81255205373 scopus 로고    scopus 로고
    • A systematic screen for CDK4/6 substrates links FOXM1 phosphorylation to senescence suppression in cancer cells
    • Anders L, Ke N, Hydbring P, Choi YJ, Widlund HR, Chick JM, et al. A systematic screen for CDK4/6 substrates links FOXM1 phosphorylation to senescence suppression in cancer cells. Cancer Cell 2011; 20: 620-634
    • (2011) Cancer Cell , vol.20 , pp. 620-634
    • Anders, L.1    Ke, N.2    Hydbring, P.3    Choi, Y.J.4    Widlund, H.R.5    Chick, J.M.6
  • 16
    • 0037112178 scopus 로고    scopus 로고
    • Cdk4 disruption renders primary mouse cells resistant to oncogenic transformation, leading to Arf/p53-independent senescence
    • Zou X, Ray D, Aziyu A, Christov K, Boiko AD, Gudkov AV, et al. Cdk4 disruption renders primary mouse cells resistant to oncogenic transformation, leading to Arf/p53-independent senescence. Genes Dev 2002; 16: 2923-2934
    • (2002) Genes Dev , vol.16 , pp. 2923-2934
    • Zou, X.1    Ray, D.2    Aziyu, A.3    Christov, K.4    Boiko, A.D.5    Gudkov, A.V.6
  • 17
    • 34250215990 scopus 로고    scopus 로고
    • CDK4 and CDK6 delay senescence by kinase-dependent and p16INK4a-independent mechanisms
    • Ruas M, Gregory F, Jones R, Poolman R, Starborg M, Rowe J, et al. CDK4 and CDK6 delay senescence by kinase-dependent and p16INK4a-independent mechanisms. Mol Cell Biol 2007; 27: 4273-4282
    • (2007) Mol Cell Biol , vol.27 , pp. 4273-4282
    • Ruas, M.1    Gregory, F.2    Jones, R.3    Poolman, R.4    Starborg, M.5    Rowe, J.6
  • 18
    • 77951082119 scopus 로고    scopus 로고
    • Pharmacologic inhibition of cyclin-dependent kinases 4 and 6 arrests the growth of glioblastoma multiforme intracranial xenografts
    • Michaud K, Solomon DA, Oermann E, Kim JS, Zhong WZ, Prados MD, et al. Pharmacologic inhibition of cyclin-dependent kinases 4 and 6 arrests the growth of glioblastoma multiforme intracranial xenografts. Cancer Res 2010; 70: 3228-3238
    • (2010) Cancer Res , vol.70 , pp. 3228-3238
    • Michaud, K.1    Solomon, D.A.2    Oermann, E.3    Kim, J.S.4    Zhong, W.Z.5    Prados, M.D.6
  • 19
    • 0036134935 scopus 로고    scopus 로고
    • Germ line transmission of the Cdk4(R24C) mutation facilitates tumorigenesis and escape from cellular senescence
    • Rane SG, Cosenza SC, Mettus RV, Reddy EP. Germ line transmission of the Cdk4(R24C) mutation facilitates tumorigenesis and escape from cellular senescence. Mol Cell Biol 2002; 22: 644-656
    • (2002) Mol Cell Biol , vol.22 , pp. 644-656
    • Rane, S.G.1    Cosenza, S.C.2    Mettus, R.V.3    Reddy, E.P.4
  • 20
    • 0021133314 scopus 로고
    • The chromosome 14 breakpoint in neoplastic B cells with the t(11;14) translocation involves the immunoglobulin heavy chain locus
    • Erikson J, Finan J, Tsujimoto Y, Nowell PC, Croce CM. The chromosome 14 breakpoint in neoplastic B cells with the t(11;14) translocation involves the immunoglobulin heavy chain locus. Proc Natl Acad Sci USA 1984; 81: 4144-4148
    • (1984) Proc Natl Acad Sci USA , vol.81 , pp. 4144-4148
    • Erikson, J.1    Finan, J.2    Tsujimoto, Y.3    Nowell, P.C.4    Croce, C.M.5
  • 21
    • 0021829149 scopus 로고
    • Clustering of breakpoints on chromosome 11 in human B-cell neoplasms with the t(11;14) chromosome translocation
    • Tsujimoto Y, Jaffe E, Cossman J, Gorham J, Nowell PC, Croce CM. Clustering of breakpoints on chromosome 11 in human B-cell neoplasms with the t(11;14) chromosome translocation. Nature 1985; 315: 340-343
    • (1985) Nature , vol.315 , pp. 340-343
    • Tsujimoto, Y.1    Jaffe, E.2    Cossman, J.3    Gorham, J.4    Nowell, P.C.5    Croce, C.M.6
  • 22
    • 0021270716 scopus 로고
    • Molecular cloning of the chromosomal breakpoint of B-cell lymphomas and leukemias with the t(11;14) chromosome translocation
    • Tsujimoto Y, Yunis J, Onorato-Showe L, Erikson J, Nowell PC, Croce CM. Molecular cloning of the chromosomal breakpoint of B-cell lymphomas and leukemias with the t(11;14) chromosome translocation. Science 1984; 224: 1403-1406
    • (1984) Science , vol.224 , pp. 1403-1406
    • Tsujimoto, Y.1    Yunis, J.2    Onorato-Showe, L.3    Erikson, J.4    Nowell, P.C.5    Croce, C.M.6
  • 24
    • 0024374960 scopus 로고
    • Molecular cloning and chromosomal mapping of DNA rearranged with the parathyroid hormone gene in a parathyroid adenoma
    • Arnold A, Kim HG, Gaz RD, Eddy RL, Fukushima Y, Byers MG, et al. Molecular cloning and chromosomal mapping of DNA rearranged with the parathyroid hormone gene in a parathyroid adenoma. J Clin Invest 1989; 83: 2034-2040
    • (1989) J Clin Invest , vol.83 , pp. 2034-2040
    • Arnold, A.1    Kim, H.G.2    Gaz, R.D.3    Eddy, R.L.4    Fukushima, Y.5    Byers, M.G.6
  • 27
    • 0025819962 scopus 로고
    • Colony-stimulating factor 1 regulates novel cyclins during the G1 phase of the cell cycle
    • Matsushime H, Roussel MF, Ashmun RA, Sherr CJ. Colony-stimulating factor 1 regulates novel cyclins during the G1 phase of the cell cycle. Cell 1991; 65: 701-713
    • (1991) Cell , vol.65 , pp. 701-713
    • Matsushime, H.1    Roussel, M.F.2    Ashmun, R.A.3    Sherr, C.J.4
  • 28
    • 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, et al. Identification and properties of an atypical catalytic subunit (p34PSK-J3/cdk4) for mammalian D type G1 cyclins. Cell 1992; 71: 323-334
    • (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
  • 29
    • 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 1993; 7: 331-342
    • (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
  • 30
  • 31
    • 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, et al. CDK6 (PLSTIRE) and CDK4 (PSK-J3) are a distinct subset of the cyclin-dependent kinases that associate with cyclin D1. Oncogene 1994; 9: 71-79
    • (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
  • 32
    • 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 1994; 14: 2077-2086
    • (1994) Mol Cell Biol , vol.14 , pp. 2077-2086
    • Meyerson, M.1    Harlow, E.2
  • 33
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1-phase progression
    • Sherr CJ, Roberts JM. CDK inhibitors: Positive and negative regulators of G1-phase progression. Genes Dev 1999; 13: 1501-1512
    • (1999) Genes Dev , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 34
    • 0033214080 scopus 로고    scopus 로고
    • Direct induction of cyclin D2 by Myc contributes to cell cycle progression and sequestration of p27
    • Bouchard C, Thieke K, Maier A, Saffrich R, Hanley-Hyde J, Ansorge W, et al. Direct induction of cyclin D2 by Myc contributes to cell cycle progression and sequestration of p27. EMBO J 1999; 18: 5321-5333
    • (1999) EMBO J , vol.18 , pp. 5321-5333
    • Bouchard, C.1    Thieke, K.2    Maier, A.3    Saffrich, R.4    Hanley-Hyde, J.5    Ansorge, W.6
  • 35
    • 59349108429 scopus 로고    scopus 로고
    • Transcriptional regulation of the cyclin D1 gene at a glance
    • Klein EA, Assoian RK. Transcriptional regulation of the cyclin D1 gene at a glance. J Cell Sci 2008; 121: 3853-3857
    • (2008) J Cell Sci , vol.121 , pp. 3853-3857
    • Klein, E.A.1    Assoian, R.K.2
  • 36
    • 0034902568 scopus 로고    scopus 로고
    • Induction of cyclin D1 transcription and CDK2 activity by Notch(ic implication for cell cycle disruption in transformation by Notch(ic)
    • Ronchini C, Capobianco AJ. Induction of cyclin D1 transcription and CDK2 activity by Notch(ic): Implication for cell cycle disruption in transformation by Notch(ic). Mol Cell Biol 2001; 21: 5925-5934
    • (2001) Mol Cell Biol , vol.21 , pp. 5925-5934
    • Ronchini, C.1    Capobianco, A.J.2
  • 39
    • 0032491579 scopus 로고    scopus 로고
    • Cyclin D expression is controlled post-Transcriptionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway
    • Muise-Helmericks RC, Grimes HL, Bellacosa A, Malstrom SE, Tsichlis PN, Rosen N. Cyclin D expression is controlled post-Transcriptionally via a phosphatidylinositol 3-kinase/Akt-dependent pathway. J Biol Chem 1998; 273: 29864-29872
    • (1998) J Biol Chem , vol.273 , pp. 29864-29872
    • Muise-Helmericks, R.C.1    Grimes, H.L.2    Bellacosa, A.3    Malstrom, S.E.4    Tsichlis, P.N.5    Rosen, N.6
  • 40
    • 9644303169 scopus 로고    scopus 로고
    • Cooperation between fibroblast growth factor receptor-4 and ErbB2 in regulation of cyclin D1 translation
    • Koziczak M, Hynes NE. Cooperation between fibroblast growth factor receptor-4 and ErbB2 in regulation of cyclin D1 translation. J Biol Chem 2004; 279: 50004-50011
    • (2004) J Biol Chem , vol.279 , pp. 50004-50011
    • Koziczak, M.1    Hynes, N.E.2
  • 41
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization
    • Diehl JA, Cheng M, Roussel MF, Sherr CJ. Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev 1998; 12: 3499-3511
    • (1998) Genes Dev , vol.12 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 42
    • 0030916209 scopus 로고    scopus 로고
    • Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway
    • Diehl JA, Zindy F, Sherr CJ. Inhibition of cyclin D1 phosphorylation on threonine-286 prevents its rapid degradation via the ubiquitin-proteasome pathway. Genes Dev 1997; 11: 957-972
    • (1997) Genes Dev , vol.11 , pp. 957-972
    • Diehl, J.A.1    Zindy, F.2    Sherr, C.J.3
  • 43
    • 0034671768 scopus 로고    scopus 로고
    • Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation
    • Alt JR, Cleveland JL, Hannink M, Diehl JA. Phosphorylation-dependent regulation of cyclin D1 nuclear export and cyclin D1-dependent cellular transformation. Genes Dev 2000; 14: 3102-3114
    • (2000) Genes Dev , vol.14 , pp. 3102-3114
    • Alt, J.R.1    Cleveland, J.L.2    Hannink, M.3    Diehl, J.A.4
  • 44
    • 67649352637 scopus 로고    scopus 로고
    • Nuclear cyclin D1: An oncogenic driver in human cancer
    • Kim JK, Diehl JA. Nuclear cyclin D1: An oncogenic driver in human cancer. J Cell Physiol 2009; 220: 292-296
    • (2009) J Cell Physiol , vol.220 , pp. 292-296
    • Kim, J.K.1    Diehl, J.A.2
  • 46
    • 45849131324 scopus 로고    scopus 로고
    • Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer
    • Barbash O, Zamfirova P, Lin DI, Chen X, Yang K, Nakagawa H, et al. Mutations in Fbx4 inhibit dimerization of the SCF(Fbx4) ligase and contribute to cyclin D1 overexpression in human cancer. Cancer Cell 2008; 14: 68-78
    • (2008) Cancer Cell , vol.14 , pp. 68-78
    • Barbash, O.1    Zamfirova, P.2    Lin, D.I.3    Chen, X.4    Yang, K.5    Nakagawa, H.6
  • 47
    • 66649117243 scopus 로고    scopus 로고
    • F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest after DNA damage
    • Santra MK, Wajapeyee N, Green MR. F-box protein FBXO31 mediates cyclin D1 degradation to induce G1 arrest after DNA damage. Nature 2009; 459: 722-725
    • (2009) Nature , vol.459 , pp. 722-725
    • Santra, M.K.1    Wajapeyee, N.2    Green, M.R.3
  • 50
    • 42449087261 scopus 로고    scopus 로고
    • Switching cyclin D-Cdk4 kinase activity on and off
    • Blain SW. Switching cyclin D-Cdk4 kinase activity on and off. Cell Cycle 2008; 7: 892-898
    • (2008) Cell Cycle , vol.7 , pp. 892-898
    • Blain, S.W.1
  • 52
    • 0030845187 scopus 로고    scopus 로고
    • Differential interaction of the cyclin-dependent kinase (Cdk) inhibitor p27Kip1 with cyclin A-Cdk2 and cyclin D2-Cdk4
    • Blain SW, Montalvo E, Massague J. Differential interaction of the cyclin-dependent kinase (Cdk) inhibitor p27Kip1 with cyclin A-Cdk2 and cyclin D2-Cdk4. J Biol Chem 1997; 272: 25863-25872
    • (1997) J Biol Chem , vol.272 , pp. 25863-25872
    • Blain, S.W.1    Montalvo, E.2    Massague, J.3
  • 54
    • 0033559264 scopus 로고    scopus 로고
    • The p21(Cip1 and p 27(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, et al. The p21(Cip1)and p27(Kip1) CDK 'inhibitors' are essential activators of cyclin D-dependent kinases in murine fibroblasts. EMBO J 1999; 18: 1571-1583
    • (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
  • 55
    • 0030614715 scopus 로고    scopus 로고
    • The subcellular locations of p15(Ink4b) and p27(Kip1) coordinate their inhibitory interactions with cdk4 and cdk2
    • Reynisdottir I, Massague J. The subcellular locations of p15(Ink4b) and p27(Kip1) coordinate their inhibitory interactions with cdk4 and cdk2. Genes Dev 1997; 11: 492-503
    • (1997) Genes Dev , vol.11 , pp. 492-503
    • Reynisdottir, I.1    Massague, J.2
  • 57
    • 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 1994; 78: 67-74
    • (1994) Cell , vol.78 , pp. 67-74
    • Toyoshima, H.1    Hunter, T.2
  • 58
    • 0028176483 scopus 로고
    • Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals
    • Polyak K, Lee MH, Erdjument-Bromage H, Koff A, Roberts JM, Tempst P, et al. Cloning of p27Kip1, a cyclin-dependent kinase inhibitor and a potential mediator of extracellular antimitogenic signals. Cell 1994; 78: 59-66
    • (1994) Cell , vol.78 , pp. 59-66
    • Polyak, K.1    Lee, M.H.2    Erdjument-Bromage, H.3    Koff, A.4    Roberts, J.M.5    Tempst, P.6
  • 59
    • 0028179669 scopus 로고
    • P27KIP1, a cyclin-Cdk inhibitor, links transforming growth factor-beta and contact inhibition to cell cycle arrest
    • Polyak K, Kato JY, Solomon MJ, Sherr CJ, Massague J, Roberts JM, et al. p27Kip1, a cyclin-Cdk inhibitor, links transforming growth factor-beta and contact inhibition to cell cycle arrest. Genes Dev 1994; 8: 9-22
    • (1994) Genes Dev , vol.8 , pp. 9-22
    • Polyak, K.1    Kato, J.Y.2    Solomon, M.J.3    Sherr, C.J.4    Massague, J.5    Roberts, J.M.6
  • 61
    • 33846268807 scopus 로고    scopus 로고
    • P27 phosphorylation by Src regulates inhibition of cyclin E-Cdk2
    • Chu I, Sun J, Arnaout A, Kahn H, Hanna W, Narod S, et al. p27 phosphorylation by Src regulates inhibition of cyclin E-Cdk2. Cell 2007; 128: 281-294
    • (2007) Cell , vol.128 , pp. 281-294
    • Chu, I.1    Sun, J.2    Arnaout, A.3    Kahn, H.4    Hanna, W.5    Narod, S.6
  • 62
    • 33846321913 scopus 로고    scopus 로고
    • Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases
    • Grimmler M, Wang Y, Mund T, Cilensek Z, Keidel EM, Waddell MB, et al. Cdk-inhibitory activity and stability of p27Kip1 are directly regulated by oncogenic tyrosine kinases. Cell 2007; 128: 269-280
    • (2007) Cell , vol.128 , pp. 269-280
    • Grimmler, M.1    Wang, Y.2    Mund, T.3    Cilensek, Z.4    Keidel, E.M.5    Waddell, M.B.6
  • 63
    • 84869006754 scopus 로고    scopus 로고
    • Tyrosine phosphorylation of the p21 cyclin-dependent kinase inhibitor facilitates the development of proneural glioma
    • Hukkelhoven E, Liu Y, Yeh N, Ciznadija D, Blain SW, Koff A. Tyrosine phosphorylation of the p21 cyclin-dependent kinase inhibitor facilitates the development of proneural glioma. J Biol Chem 2012; 287: 38523-38530
    • (2012) J Biol Chem , vol.287 , pp. 38523-38530
    • Hukkelhoven, E.1    Liu, Y.2    Yeh, N.3    Ciznadija, D.4    Blain, S.W.5    Koff, A.6
  • 64
    • 37549061066 scopus 로고    scopus 로고
    • Differential modification of p27Kip1 controls its cyclin D-cdk4 inhibitory activity
    • James MK, Ray A, Leznova D, Blain SW. Differential modification of p27Kip1 controls its cyclin D-cdk4 inhibitory activity. Mol Cell Biol 2008; 28: 498-510
    • (2008) Mol Cell Biol , vol.28 , pp. 498-510
    • James, M.K.1    Ray, A.2    Leznova, D.3    Blain, S.W.4
  • 65
    • 59449106702 scopus 로고    scopus 로고
    • P27KIP1 inhibits cyclin D-cyclin-dependent kinase 4 by two independent modes
    • Ray A, James MK, Larochelle S, Fisher RP, Blain SW. p27Kip1 inhibits cyclin D-cyclin-dependent kinase 4 by two independent modes. Mol Cell Biol 2009; 29: 986-999
    • (2009) Mol Cell Biol , vol.29 , pp. 986-999
    • Ray, A.1    James, M.K.2    Larochelle, S.3    Fisher, R.P.4    Blain, S.W.5
  • 67
    • 0028270189 scopus 로고
    • Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-Activating kinase
    • Kato JY, Matsuoka M, Strom DK, Sherr CJ. Regulation of cyclin D-dependent kinase 4 (cdk4) by cdk4-Activating kinase. Mol Cell Biol 1994; 14: 2713-2721
    • (1994) Mol Cell Biol , vol.14 , pp. 2713-2721
    • Kato, J.Y.1    Matsuoka, M.2    Strom, D.K.3    Sherr, C.J.4
  • 69
    • 33745470981 scopus 로고    scopus 로고
    • Regulated activating Thr172 phosphorylation of cyclin-dependent kinase 4(CDK4 its relationship with cyclins and CDK 'inhibitors'
    • Bockstaele L, Kooken H, Libert F, Paternot S, Dumont JE, De Launoit Y, et al. Regulated activating Thr172 phosphorylation of cyclin-dependent kinase 4(CDK4): Its relationship with cyclins and CDK 'inhibitors'. Mol Cell Biol 2006; 26: 5070-5085
    • (2006) Mol Cell Biol , vol.26 , pp. 5070-5085
    • Bockstaele, L.1    Kooken, H.2    Libert, F.3    Paternot, S.4    Dumont, J.E.5    De Launoit, Y.6
  • 70
    • 67651233668 scopus 로고    scopus 로고
    • Differential regulation of cyclindependent kinase 4 (CDK4) and CDK6, evidence that CDK4 might not be activated by CDK7, and design of a CDK6 activating mutation
    • Bockstaele L, Bisteau X, Paternot S, Roger PP. Differential regulation of cyclindependent kinase 4 (CDK4) and CDK6, evidence that CDK4 might not be activated by CDK7, and design of a CDK6 activating mutation. Mol Cell Biol 2009; 29: 4188-4200
    • (2009) Mol Cell Biol , vol.29 , pp. 4188-4200
    • Bockstaele, L.1    Bisteau, X.2    Paternot, S.3    Roger, P.P.4
  • 71
    • 0032517341 scopus 로고    scopus 로고
    • The p16INK4a/CDKN2A tumor suppressor and its relatives
    • Ruas M, Peters G. The p16INK4a/CDKN2A tumor suppressor and its relatives. Biochim Biophys Acta 1998; 1378: F115-F177
    • (1998) Biochim Biophys Acta , vol.1378
    • Ruas, M.1    Peters, G.2
  • 72
    • 0029671263 scopus 로고    scopus 로고
    • Isolation and characterization of p19INK4d, a p16-related inhibitor specific to CDK6 and CDK4
    • Guan KL, Jenkins CW, Li Y, O'Keefe CL, Noh S, Wu X, et al. Isolation and characterization of p19INK4d, a p16-related inhibitor specific to CDK6 and CDK4. Mol Biol Cell 1996; 7: 57-70
    • (1996) Mol Biol Cell , vol.7 , pp. 57-70
    • Guan, K.L.1    Jenkins, C.W.2    Li, Y.3    O'Keefe, C.L.4    Noh, S.5    Wu, X.6
  • 73
    • 0027769876 scopus 로고
    • A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4
    • Serrano M, Hannon GJ, Beach D. A new regulatory motif in cell-cycle control causing specific inhibition of cyclin D/CDK4. Nature 1993; 366: 704-707
    • (1993) Nature , vol.366 , pp. 704-707
    • Serrano, M.1    Hannon, G.J.2    Beach, D.3
  • 74
    • 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 1995; 15: 2672-2681
    • (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
  • 75
    • 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 1995; 83: 993-1000
    • (1995) Cell , vol.83 , pp. 993-1000
    • Quelle, D.E.1    Zindy, F.2    Ashmun, R.A.3    Sherr, C.J.4
  • 76
    • 0032541640 scopus 로고    scopus 로고
    • Crystal structure of the complex of the cyclin D-dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d
    • Brotherton DH, Dhanaraj V, Wick S, Brizuela L, Domaille PJ, Volyanik E, et al. Crystal structure of the complex of the cyclin D-dependent kinase Cdk6 bound to the cell-cycle inhibitor p19INK4d. Nature 1998; 395: 244-250
    • (1998) Nature , vol.395 , pp. 244-250
    • Brotherton, D.H.1    Dhanaraj, V.2    Wick, S.3    Brizuela, L.4    Domaille, P.J.5    Volyanik, E.6
  • 77
    • 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 1998; 395: 237-243
    • (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
  • 78
    • 0034671563 scopus 로고    scopus 로고
    • Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors
    • Jeffrey PD, Tong L, Pavletich NP. Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors. Genes Dev 2000; 14: 3115-3125
    • (2000) Genes Dev , vol.14 , pp. 3115-3125
    • Jeffrey, P.D.1    Tong, L.2    Pavletich, N.P.3
  • 79
    • 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 1999; 19: 1775-1783
    • (1999) Mol Cell Biol , vol.19 , pp. 1775-1783
    • Parry, D.1    Mahony, D.2    Wills, K.3    Lees, E.4
  • 80
    • 0027301324 scopus 로고
    • Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation
    • Xiong Y, Zhang H, Beach D. Subunit rearrangement of the cyclin-dependent kinases is associated with cellular transformation. Genes Dev 1993; 7: 1572-1583
    • (1993) Genes Dev , vol.7 , pp. 1572-1583
    • Xiong, Y.1    Zhang, H.2    Beach, D.3
  • 81
    • 0028168242 scopus 로고
    • P15ink4b is a potential effector of TGF-beta-induced cell cycle arrest
    • Hannon GJ, Beach D. p15INK4B is a potential effector of TGF-beta-induced cell cycle arrest. Nature 1994; 371: 257-261
    • (1994) Nature , vol.371 , pp. 257-261
    • Hannon, G.J.1    Beach, D.2
  • 82
    • 33845235459 scopus 로고    scopus 로고
    • Oncogene-induced senescence is part of the tumorigenesis barrier imposed by DNA damage checkpoints
    • Bartkova J, Rezaei N, Liontos M, Karakaidos P, Kletsas D, Issaeva N, et al. Oncogene-induced senescence is part of the tumorigenesis barrier imposed by DNA damage checkpoints. Nature 2006; 444: 633-637
    • (2006) Nature , vol.444 , pp. 633-637
    • Bartkova, J.1    Rezaei, N.2    Liontos, M.3    Karakaidos, P.4    Kletsas, D.5    Issaeva, N.6
  • 84
    • 0030944985 scopus 로고    scopus 로고
    • Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a
    • Serrano M, Lin AW, McCurrach ME, Beach D, Lowe SW. Oncogenic ras provokes premature cell senescence associated with accumulation of p53 and p16INK4a. Cell 1997; 88: 593-602
    • (1997) Cell , vol.88 , pp. 593-602
    • Serrano, M.1    Lin, A.W.2    McCurrach, M.E.3    Beach, D.4    Lowe, S.W.5
  • 88
    • 33747872306 scopus 로고    scopus 로고
    • A novel orally active small molecule potently induces G1 arrest in primary myeloma cells and prevents tumor growth by specific inhibition of cyclin-dependent kinase 4/6
    • Baughn LB, Di Liberto M, Wu K, Toogood PL, Louie T, Gottschalk R, et al. A novel orally active small molecule potently induces G1 arrest in primary myeloma cells and prevents tumor growth by specific inhibition of cyclin-dependent kinase 4/6. Cancer Res 2006; 66: 7661-7667
    • (2006) Cancer Res , vol.66 , pp. 7661-7667
    • Baughn, L.B.1    Di Liberto, M.2    Wu, K.3    Toogood, P.L.4    Louie, T.5    Gottschalk, R.6
  • 90
    • 77954757207 scopus 로고    scopus 로고
    • Therapeutic CDK4/6 inhibition in breast cancer: Key mechanisms of response and failure
    • Dean JL, Thangavel C, McClendon AK, Reed CA, Knudsen ES. Therapeutic CDK4/6 inhibition in breast cancer: Key mechanisms of response and failure. Oncogene 2010; 29: 4018-4032
    • (2010) Oncogene , vol.29 , pp. 4018-4032
    • Dean, J.L.1    Thangavel, C.2    McClendon, A.K.3    Reed, C.A.4    Knudsen, E.S.5
  • 91
    • 84865254684 scopus 로고    scopus 로고
    • Modification of the DNA damage response by therapeutic CDK4/6 inhibition
    • Dean JL, McClendon AK, Knudsen ES. Modification of the DNA damage response by therapeutic CDK4/6 inhibition. J Biol Chem 2012; 287: 29075-29087
    • (2012) J Biol Chem , vol.287 , pp. 29075-29087
    • Dean, J.L.1    McClendon, A.K.2    Knudsen, E.S.3
  • 92
    • 76049104235 scopus 로고    scopus 로고
    • PD 0332991, a selective cyclin D kinase 4/6 inhibitor, preferentially inhibits proliferation of luminal estrogen receptor-positive human breast cancer cell lines in vitro
    • Finn RS, Dering J, Conklin D, Kalous O, Cohen DJ, Desai AJ, et al. PD 0332991, a selective cyclin D kinase 4/6 inhibitor, preferentially inhibits proliferation of luminal estrogen receptor-positive human breast cancer cell lines in vitro. Breast Cancer Res 2009; 11: R77
    • (2009) Breast Cancer Res , vol.11
    • Finn, R.S.1    Dering, J.2    Conklin, D.3    Kalous, O.4    Cohen, D.J.5    Desai, A.J.6
  • 93
    • 9444228344 scopus 로고    scopus 로고
    • Specific inhibition of cyclin-dependent kinase 4/6 by PD 0332991 and associated antitumor activity in human tumor xenografts
    • Fry DW, Harvey PJ, Keller PR, Elliott WL, Meade M, Trachet E, et al. Specific inhibition of cyclin-dependent kinase 4/6 by PD 0332991 and associated antitumor activity in human tumor xenografts. Mol Cancer Ther 2004; 3: 1427-1438
    • (2004) Mol Cancer Ther , vol.3 , pp. 1427-1438
    • Fry, D.W.1    Harvey, P.J.2    Keller, P.R.3    Elliott, W.L.4    Meade, M.5    Trachet, E.6
  • 95
    • 0036118561 scopus 로고    scopus 로고
    • Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4
    • Leng X, Noble M, Adams PD, Qin J, Harper JW. Reversal of growth suppression by p107 via direct phosphorylation by cyclin D1/cyclin-dependent kinase 4. Mol Cell Biol 2002; 22: 2242-2254
    • (2002) Mol Cell Biol , vol.22 , pp. 2242-2254
    • Leng, X.1    Noble, M.2    Adams, P.D.3    Qin, J.4    Harper, J.W.5
  • 96
    • 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 1995; 9: 1340-1353
    • (1995) Genes Dev , vol.9 , pp. 1340-1353
    • Beijersbergen, R.L.1    Carlee, L.2    Kerkhoven, R.M.3    Bernards, R.4
  • 97
    • 0031019197 scopus 로고    scopus 로고
    • Cyclin D1/Cdk4 regulates retinoblastoma protein-mediated cell cycle arrest by site-specific phosphorylation
    • Connell-Crowley L, Harper JW, Goodrich DW. Cyclin D1/Cdk4 regulates retinoblastoma protein-mediated cell cycle arrest by site-specific phosphorylation. Mol Biol Cell 1997; 8: 287-301
    • (1997) Mol Biol Cell , vol.8 , pp. 287-301
    • Connell-Crowley, L.1    Harper, J.W.2    Goodrich, D.W.3
  • 98
    • 0037178801 scopus 로고    scopus 로고
    • Distinct phosphorylation events regulate p130-And p107-mediated repression of E2F-4
    • Farkas T, Hansen K, Holm K, Lukas J, Bartek J. Distinct phosphorylation events regulate p130-And p107-mediated repression of E2F-4. J Biol Chem 2002; 277: 26741-26752
    • (2002) J Biol Chem , vol.277 , pp. 26741-26752
    • Farkas, T.1    Hansen, K.2    Holm, K.3    Lukas, J.4    Bartek, J.5
  • 99
    • 0035254222 scopus 로고    scopus 로고
    • Phosphorylationdependent and-independent functions of p130 cooperate to evoke a sustained G1 block
    • Hansen K, Farkas T, Lukas J, Holm K, Ronnstrand L, Bartek J. Phosphorylationdependent and-independent functions of p130 cooperate to evoke a sustained G1 block. EMBO J 2001; 20: 422-432
    • (2001) EMBO J , vol.20 , pp. 422-432
    • Hansen, K.1    Farkas, T.2    Lukas, J.3    Holm, K.4    Ronnstrand, L.5    Bartek, J.6
  • 100
    • 0030015264 scopus 로고    scopus 로고
    • Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-Associated kinases
    • Xiao ZX, Ginsberg D, Ewen M, Livingston DM. Regulation of the retinoblastoma protein-related protein p107 by G1 cyclin-Associated kinases. Proc Natl Acad Sci U S A 1996; 93: 4633-4637
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 4633-4637
    • Xiao, Z.X.1    Ginsberg, D.2    Ewen, M.3    Livingston, D.M.4
  • 101
    • 0030918714 scopus 로고    scopus 로고
    • Differential phosphorylation of the retinoblastoma protein by G1/S cyclin-dependent kinases
    • Zarkowska T, Mittnacht S. Differential phosphorylation of the retinoblastoma protein by G1/S cyclin-dependent kinases. J Biol Chem 1997; 272: 12738-12746
    • (1997) J Biol Chem , vol.272 , pp. 12738-12746
    • Zarkowska, T.1    Mittnacht, S.2
  • 102
    • 3142546336 scopus 로고    scopus 로고
    • Cyclin-dependent kinases regulate the antiproliferative function of Smads
    • Matsuura I, Denissova NG, Wang G, He D, Long J, Liu F. Cyclin-dependent kinases regulate the antiproliferative function of Smads. Nature 2004; 430: 226-231
    • (2004) Nature , vol.430 , pp. 226-231
    • Matsuura, I.1    Denissova, N.G.2    Wang, G.3    He, D.4    Long, J.5    Liu, F.6
  • 103
    • 77957966270 scopus 로고    scopus 로고
    • Nuclear cyclin D1/CDK4 kinase regulates CUL4 expression and triggers neoplastic growth via activation of the PRMT5 methyltransferase
    • Aggarwal P, Vaites LP, Kim JK, Mellert H, Gurung B, Nakagawa H, et al. Nuclear cyclin D1/CDK4 kinase regulates CUL4 expression and triggers neoplastic growth via activation of the PRMT5 methyltransferase. Cancer Cell 2010; 18: 329-340
    • (2010) Cancer Cell , vol.18 , pp. 329-340
    • Aggarwal, P.1    Vaites, L.P.2    Kim, J.K.3    Mellert, H.4    Gurung, B.5    Nakagawa, H.6
  • 104
    • 75149175161 scopus 로고    scopus 로고
    • Transcriptional role of cyclin D1 in development revealed by a genetic-proteomic screen
    • Bienvenu F, Jirawatnotai S, Elias JE, Meyer CA, Mizeracka K, Marson A, et al. Transcriptional role of cyclin D1 in development revealed by a genetic-proteomic screen. Nature 2010; 463: 374-378
    • (2010) Nature , vol.463 , pp. 374-378
    • Bienvenu, F.1    Jirawatnotai, S.2    Elias, J.E.3    Meyer, C.A.4    Mizeracka, K.5    Marson, A.6
  • 105
    • 84866274926 scopus 로고    scopus 로고
    • Regulation of transcription and chromatin structure by pRB: Here, there and everywhere
    • Talluri S, Dick FA. Regulation of transcription and chromatin structure by pRB: Here, there and everywhere. Cell Cycle 2012; 11: 3189-3198
    • (2012) Cell Cycle , vol.11 , pp. 3189-3198
    • Talluri, S.1    Dick, F.A.2
  • 106
    • 84856140976 scopus 로고    scopus 로고
    • Conserved RB functions in development and tumor suppression
    • Gordon GM, Du W. Conserved RB functions in development and tumor suppression. Protein Cell 2011; 2: 864-878
    • (2011) Protein Cell , vol.2 , pp. 864-878
    • Gordon, G.M.1    Du, W.2
  • 109
    • 0034811677 scopus 로고    scopus 로고
    • Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase
    • Vandel L, Nicolas E, Vaute O, Ferreira R, Ait-Si-Ali S, Trouche D. Transcriptional repression by the retinoblastoma protein through the recruitment of a histone methyltransferase. Mol Cell Biol 2001; 21: 6484-6494
    • (2001) Mol Cell Biol , vol.21 , pp. 6484-6494
    • Vandel, L.1    Nicolas, E.2    Vaute, O.3    Ferreira, R.4    Ait-Si-Ali, S.5    Trouche, D.6
  • 110
    • 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 1998; 92: 463-473
    • (1998) Cell , vol.92 , pp. 463-473
    • Luo, R.X.1    Postigo, A.A.2    Dean, D.C.3
  • 111
    • 0032168984 scopus 로고    scopus 로고
    • The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase
    • Ferreira R, Magnaghi-Jaulin L, Robin P, Harel-Bellan A, Trouche D. The three members of the pocket proteins family share the ability to repress E2F activity through recruitment of a histone deacetylase. Proc Natl Acad Sci USA 1998; 95: 10493-10498
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 10493-10498
    • Ferreira, R.1    Magnaghi-Jaulin, L.2    Robin, P.3    Harel-Bellan, A.4    Trouche, D.5
  • 112
    • 0034737290 scopus 로고    scopus 로고
    • Exit from G1 and S phase of the cell cycle is regulated by repressor complexes containing HDAC-Rb-hSWI/SNF and Rb-hSWI/SNF
    • Zhang HS, Gavin M, Dahiya A, Postigo AA, Ma D, Luo RX, et al. Exit from G1 and S phase of the cell cycle is regulated by repressor complexes containing HDAC-Rb-hSWI/SNF and Rb-hSWI/SNF. Cell 2000; 101: 79-89
    • (2000) Cell , vol.101 , pp. 79-89
    • Zhang, H.S.1    Gavin, M.2    Dahiya, A.3    Postigo, A.A.4    Ma, D.5    Luo, R.X.6
  • 113
    • 0033578816 scopus 로고    scopus 로고
    • Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1
    • Harbour JW, Luo RX, Dei Santi A, Postigo AA, Dean DC. Cdk phosphorylation triggers sequential intramolecular interactions that progressively block Rb functions as cells move through G1. Cell 1999; 98: 859-869
    • (1999) Cell , vol.98 , pp. 859-869
    • Harbour, J.W.1    Luo, R.X.2    Dei Santi, A.3    Postigo, A.A.4    Dean, D.C.5
  • 114
    • 28944437358 scopus 로고    scopus 로고
    • Structure of the Rb C-Terminal domain bound to E2F1-DP1: A mechanism for phosphorylation-induced E2F release
    • Rubin SM, Gall AL, Zheng N, Pavletich NP. Structure of the Rb C-Terminal domain bound to E2F1-DP1: A mechanism for phosphorylation-induced E2F release. Cell 2005; 123: 1093-1106
    • (2005) Cell , vol.123 , pp. 1093-1106
    • Rubin, S.M.1    Gall, A.L.2    Zheng, N.3    Pavletich, N.P.4
  • 115
    • 77952387813 scopus 로고    scopus 로고
    • Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding
    • Burke JR, Deshong AJ, Pelton JG, Rubin SM. Phosphorylation-induced conformational changes in the retinoblastoma protein inhibit E2F transactivation domain binding. J Biol Chem 2010; 285: 16286-16293
    • (2010) J Biol Chem , vol.285 , pp. 16286-16293
    • Burke, J.R.1    Deshong, A.J.2    Pelton, J.G.3    Rubin, S.M.4
  • 116
    • 0029043782 scopus 로고
    • Mechanism of active transcriptional repression by the retinoblastoma protein
    • Weintraub SJ, Chow KN, Luo RX, Zhang SH, He S, Dean DC. Mechanism of active transcriptional repression by the retinoblastoma protein. Nature 1995; 375: 812-815
    • (1995) Nature , vol.375 , pp. 812-815
    • Weintraub, S.J.1    Chow, K.N.2    Luo, R.X.3    Zhang, S.H.4    He, S.5    Dean, D.C.6
  • 117
    • 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 1997; 17: 7268-7282
    • (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
  • 120
    • 0037080483 scopus 로고    scopus 로고
    • E2F integrates cell cycle progression with DNA repair, replication, and G(2)/M checkpoints
    • Ren B, Cam H, Takahashi Y, Volkert T, Terragni J, Young RA, et al. E2F integrates cell cycle progression with DNA repair, replication, and G(2)/M checkpoints. Genes Dev 2002; 16: 245-256
    • (2002) Genes Dev , vol.16 , pp. 245-256
    • Ren, B.1    Cam, H.2    Takahashi, Y.3    Volkert, T.4    Terragni, J.5    Young, R.A.6
  • 121
    • 80052901782 scopus 로고    scopus 로고
    • Network calisthenics: Control of E2F dynamics in cell cycle entry
    • Wong JV, Dong P, Nevins JR, Mathey-Prevot B, You L. Network calisthenics: Control of E2F dynamics in cell cycle entry. Cell Cycle 2011; 10: 3086-3094
    • (2011) Cell Cycle , vol.10 , pp. 3086-3094
    • Wong, J.V.1    Dong, P.2    Nevins, J.R.3    Mathey-Prevot, B.4    You, L.5
  • 122
    • 81055137232 scopus 로고    scopus 로고
    • FOXM1: From cancer initiation to progression and treatment
    • Koo CY, Muir KW, Lam EW. FOXM1: From cancer initiation to progression and treatment. Biochim Biophys Acta 2012; 1819: 28-37
    • (2012) Biochim Biophys Acta , vol.1819 , pp. 28-37
    • Koo, C.Y.1    Muir, K.W.2    Lam, E.W.3
  • 124
    • 28544449224 scopus 로고    scopus 로고
    • Forkhead box M1 regulates the transcriptional network of genes essential for mitotic progression and genes encoding the SCF (Skp2-Cks1) ubiquitin ligase
    • Wang IC, Chen YJ, Hughes D, Petrovic V, Major ML, Park HJ, et al. Forkhead box M1 regulates the transcriptional network of genes essential for mitotic progression and genes encoding the SCF (Skp2-Cks1) ubiquitin ligase. Mol Cell Biol 2005; 25: 10875-10894
    • (2005) Mol Cell Biol , vol.25 , pp. 10875-10894
    • Wang, I.C.1    Chen, Y.J.2    Hughes, D.3    Petrovic, V.4    Major, M.L.5    Park, H.J.6
  • 126
    • 0037168526 scopus 로고    scopus 로고
    • The Forkhead Box m1b transcription factor is essential for hepatocyte DNA replication and mitosis during mouse liver regeneration
    • Wang X, Kiyokawa H, Dennewitz MB, Costa RH. The Forkhead Box m1b transcription factor is essential for hepatocyte DNA replication and mitosis during mouse liver regeneration. Proc Natl Acad Sci USA 2002; 99: 16881-16886
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 16881-16886
    • Wang, X.1    Kiyokawa, H.2    Dennewitz, M.B.3    Costa, R.H.4
  • 127
    • 84870790059 scopus 로고    scopus 로고
    • Role of the forkhead transcription factor FOXO-FOXM1 axis in cancer and drug resistance
    • Zhao F, Lam EW. Role of the forkhead transcription factor FOXO-FOXM1 axis in cancer and drug resistance. Front Med 2012; 6: 376-380
    • (2012) Front Med , vol.6 , pp. 376-380
    • Zhao, F.1    Lam, E.W.2
  • 128
    • 84866742560 scopus 로고    scopus 로고
    • TGFbeta signalling in context
    • Massague J. TGFbeta signalling in context. Nat Rev Mol Cell Biol 2012; 13: 616-630
    • (2012) Nat Rev Mol Cell Biol , vol.13 , pp. 616-630
    • Massague, J.1
  • 129
    • 67650466368 scopus 로고    scopus 로고
    • Smad2 and Smad3 phosphorylated at both linker and COOH-Terminal regions transmit malignant TGF-beta signal in later stages of human colorectal cancer
    • Matsuzaki K, Kitano C, Murata M, Sekimoto G, Yoshida K, Uemura Y, et al. Smad2 and Smad3 phosphorylated at both linker and COOH-Terminal regions transmit malignant TGF-beta signal in later stages of human colorectal cancer. Cancer Res 2009; 69: 5321-5330
    • (2009) Cancer Res , vol.69 , pp. 5321-5330
    • Matsuzaki, K.1    Kitano, C.2    Murata, M.3    Sekimoto, G.4    Yoshida, K.5    Uemura, Y.6
  • 131
    • 0037040912 scopus 로고    scopus 로고
    • A novel WD repeat protein component of the methylosome binds Sm proteins
    • Friesen WJ, Wyce A, Paushkin S, Abel L, Rappsilber J, Mann M, et al. A novel WD repeat protein component of the methylosome binds Sm proteins. J Biol Chem 2002; 277: 8243-8247
    • (2002) J Biol Chem , vol.277 , pp. 8243-8247
    • Friesen, W.J.1    Wyce, A.2    Paushkin, S.3    Abel, L.4    Rappsilber, J.5    Mann, M.6
  • 133
    • 0037067653 scopus 로고    scopus 로고
    • E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression
    • Chen CR, Kang Y, Siegel PM, Massague J. E2F4/5 and p107 as Smad cofactors linking the TGFbeta receptor to c-myc repression. Cell 2002; 110: 19-32
    • (2002) Cell , vol.110 , pp. 19-32
    • Chen, C.R.1    Kang, Y.2    Siegel, P.M.3    Massague, J.4
  • 134
  • 135
    • 33746216564 scopus 로고    scopus 로고
    • Transcription factor FOXM1c is repressed by RB and activated by cyclin D1/Cdk4
    • Wierstra I, Alves J. Transcription factor FOXM1c is repressed by RB and activated by cyclin D1/Cdk4. Biol Chem 2006; 387: 949-962
    • (2006) Biol Chem , vol.387 , pp. 949-962
    • Wierstra, I.1    Alves, J.2
  • 137
    • 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 1995; 92: 12146-12150
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 12146-12150
    • Ohtani, K.1    DeGregori, J.2    Nevins, J.R.3
  • 138
    • 0033176887 scopus 로고    scopus 로고
    • SKP2 is required for ubiquitinmediated degradation of the CDK inhibitor p27
    • Carrano AC, Eytan E, Hershko A, Pagano M. SKP2 is required for ubiquitinmediated degradation of the CDK inhibitor p27. Nat Cell Biol 1999; 1: 193-199
    • (1999) Nat Cell Biol , vol.1 , pp. 193-199
    • Carrano, A.C.1    Eytan, E.2    Hershko, A.3    Pagano, M.4
  • 139
    • 0033135878 scopus 로고    scopus 로고
    • Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation
    • Montagnoli A, Fiore F, Eytan E, Carrano AC, Draetta GF, Hershko A, et al. Ubiquitination of p27 is regulated by Cdk-dependent phosphorylation and trimeric complex formation. Genes Dev 1999; 13: 1181-1189
    • (1999) Genes Dev , vol.13 , pp. 1181-1189
    • Montagnoli, A.1    Fiore, F.2    Eytan, E.3    Carrano, A.C.4    Draetta, G.F.5    Hershko, A.6
  • 140
    • 33846148370 scopus 로고    scopus 로고
    • Prb family proteins are required for H3K27 trimethylation and Polycomb repression complexes binding to and silencing p16INK4alpha tumor suppressor gene
    • Kotake Y, Cao R, Viatour P, Sage J, Zhang Y, Xiong Y. pRB family proteins are required for H3K27 trimethylation and Polycomb repression complexes binding to and silencing p16INK4alpha tumor suppressor gene. Genes Dev 2007; 21: 49-54
    • (2007) Genes Dev , vol.21 , pp. 49-54
    • Kotake, Y.1    Cao, R.2    Viatour, P.3    Sage, J.4    Zhang, Y.5    Xiong, Y.6
  • 141
    • 0028108451 scopus 로고
    • Cyclin D1 induction in breast cancer cells shortens G1 and is sufficient for cells arrested in G1 to complete the cell cycle
    • Musgrove EA, Lee CS, Buckley MF, Sutherland RL. Cyclin D1 induction in breast cancer cells shortens G1 and is sufficient for cells arrested in G1 to complete the cell cycle. Proc Natl Acad Sci USA 1994; 91: 8022-8026
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 8022-8026
    • Musgrove, E.A.1    Lee, C.S.2    Buckley, M.F.3    Sutherland, R.L.4
  • 142
    • 84864551707 scopus 로고    scopus 로고
    • Prolonged early G(1) arrest by selective CDK4/CDK6 inhibition sensitizes myeloma cells to cytotoxic killing through cell cycle-coupled loss of IRF4
    • Huang X, Di Liberto M, Jayabalan D, Liang J, Ely S, Bretz J, et al. Prolonged early G(1) arrest by selective CDK4/CDK6 inhibition sensitizes myeloma cells to cytotoxic killing through cell cycle-coupled loss of IRF4. Blood 2012; 120: 1095-1106
    • (2012) Blood , vol.120 , pp. 1095-1106
    • Huang, X.1    Di Liberto, M.2    Jayabalan, D.3    Liang, J.4    Ely, S.5    Bretz, J.6
  • 143
    • 0034660892 scopus 로고    scopus 로고
    • The Pezcoller lecture: Cancer cell cycles revisited
    • Sherr CJ. The Pezcoller lecture: Cancer cell cycles revisited. Cancer Res 2000; 60: 3689-3695
    • (2000) Cancer Res , vol.60 , pp. 3689-3695
    • Sherr, C.J.1
  • 144
    • 0024473604 scopus 로고
    • G1 events and regulation of cell proliferation
    • Pardee AB. G1 events and regulation of cell proliferation. Science 1989; 246: 603-608
    • (1989) Science , vol.246 , pp. 603-608
    • Pardee, A.B.1
  • 146
    • 4444247138 scopus 로고    scopus 로고
    • Mammalian cells cycle without the D-Type cyclin-dependent kinases Cdk4 and Cdk6
    • Malumbres M, Sotillo R, Santamaria D, Galan J, Cerezo A, Ortega S, et al. Mammalian cells cycle without the D-Type cyclin-dependent kinases Cdk4 and Cdk6. Cell 2004; 118: 493-504
    • (2004) Cell , vol.118 , pp. 493-504
    • Malumbres, M.1    Sotillo, R.2    Santamaria, D.3    Galan, J.4    Cerezo, A.5    Ortega, S.6
  • 147
    • 8644219655 scopus 로고    scopus 로고
    • Living with or without cyclins and cyclin-dependent kinases
    • Sherr CJ, Roberts JM. Living with or without cyclins and cyclin-dependent kinases. Genes Dev 2004; 18: 2699-2711
    • (2004) Genes Dev , vol.18 , pp. 2699-2711
    • Sherr, C.J.1    Roberts, J.M.2
  • 148
    • 0041327168 scopus 로고    scopus 로고
    • Proliferation of cancer cells despite CDK2 inhibition
    • Tetsu O, McCormick F. Proliferation of cancer cells despite CDK2 inhibition. Cancer Cell 2003; 3: 233-245
    • (2003) Cancer Cell , vol.3 , pp. 233-245
    • Tetsu, O.1    McCormick, F.2
  • 150
    • 84873638532 scopus 로고    scopus 로고
    • Aging cellular senescence and cancer
    • Campisi J. Aging, Cellular Senescence, and Cancer. Annu Rev Physiol 2013; 75: 685-705
    • (2013) Annu Rev Physiol , vol.75 , pp. 685-705
    • Campisi, J.1
  • 151
    • 48249084972 scopus 로고    scopus 로고
    • Excess MCM proteins protect human cells from replicative stress by licensing backup origins of replication
    • Ibarra A, Schwob E, Mendez J. Excess MCM proteins protect human cells from replicative stress by licensing backup origins of replication. Proc Natl Acad Sci USA 2008; 105: 8956-8961
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 8956-8961
    • Ibarra, A.1    Schwob, E.2    Mendez, J.3
  • 152
    • 37249025795 scopus 로고    scopus 로고
    • Dormant origins licensed by excess Mcm2-7 are required for human cells to survive replicative stress
    • Ge XQ, Jackson DA, Blow JJ. Dormant origins licensed by excess Mcm2-7 are required for human cells to survive replicative stress. Genes Dev 2007; 21: 3331-3341
    • (2007) Genes Dev , vol.21 , pp. 3331-3341
    • Ge, X.Q.1    Jackson, D.A.2    Blow, J.J.3
  • 153
    • 80053330162 scopus 로고    scopus 로고
    • Brca2, Rad51 and Mre11: Performing balancing acts on replication forks
    • Costanzo V. Brca2, Rad51 and Mre11: Performing balancing acts on replication forks. DNA Repair (Amst) 2011; 10: 1060-1065
    • (2011) DNA Repair (Amst , vol.10 , pp. 1060-1065
    • Costanzo, V.1
  • 154
    • 79951970806 scopus 로고    scopus 로고
    • Stalled fork rescue via dormant replication origins in unchallenged S phase promotes proper chromosome segregation and tumor suppression
    • Kawabata T, Luebben SW, Yamaguchi S, Ilves I, Matise I, Buske T, et al. Stalled fork rescue via dormant replication origins in unchallenged S phase promotes proper chromosome segregation and tumor suppression. Mol Cell 2011; 41: 543-553
    • (2011) Mol Cell , vol.41 , pp. 543-553
    • Kawabata, T.1    Luebben, S.W.2    Yamaguchi, S.3    Ilves, I.4    Matise, I.5    Buske, T.6
  • 155
    • 84866741381 scopus 로고    scopus 로고
    • Crosstalk between chromatin state and DNA damage response in cellular senescence and cancer
    • Sulli G, Di Micco R, d'Adda di Fagagna F. Crosstalk between chromatin state and DNA damage response in cellular senescence and cancer. Nat Rev Cancer 2012; 12: 709-720
    • (2012) Nat Rev Cancer , vol.12 , pp. 709-720
    • Sulli, G.1    Di Micco, R.2    D'adda Di Fagagna, F.3
  • 156
    • 0037667702 scopus 로고    scopus 로고
    • Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence
    • Narita M, Nunez S, Heard E, Lin AW, Hearn SA, Spector DL, et al. Rb-mediated heterochromatin formation and silencing of E2F target genes during cellular senescence. Cell 2003; 113: 703-716
    • (2003) Cell , vol.113 , pp. 703-716
    • Narita, M.1    Nunez, S.2    Heard, E.3    Lin, A.W.4    Hearn, S.A.5    Spector, D.L.6
  • 157
    • 77950486542 scopus 로고    scopus 로고
    • Dissecting the unique role of the retinoblastoma tumor suppressor during cellular senescence
    • Chicas A, Wang X, Zhang C, McCurrach M, Zhao Z, Mert O, et al. Dissecting the unique role of the retinoblastoma tumor suppressor during cellular senescence. Cancer Cell 2010; 17: 376-387
    • (2010) Cancer Cell , vol.17 , pp. 376-387
    • Chicas, A.1    Wang, X.2    Zhang, C.3    McCurrach, M.4    Zhao, Z.5    Mert, O.6
  • 158
    • 0037184817 scopus 로고    scopus 로고
    • History of the events leading to the formulation of the apoptosis concept
    • Kerr JF. History of the events leading to the formulation of the apoptosis concept. Toxicology 2002; 181-182: 471-474
    • (2002) Toxicology , vol.181-182 , pp. 471-474
    • Kerr, J.F.1
  • 160
    • 0029942842 scopus 로고    scopus 로고
    • Exclusive development of T cell neoplasms in mice transplanted with bone marrow expressing activated Notch alleles
    • Pear WS, Aster JC, Scott ML, Hasserjian RP, Soffer B, Sklar J, et al. Exclusive development of T cell neoplasms in mice transplanted with bone marrow expressing activated Notch alleles. J Exp Med 1996; 183: 2283-2291
    • (1996) J Exp Med , vol.183 , pp. 2283-2291
    • Pear, W.S.1    Aster, J.C.2    Scott, M.L.3    Hasserjian, R.P.4    Soffer, B.5    Sklar, J.6
  • 162
    • 84867051939 scopus 로고    scopus 로고
    • Burkitt lymphoma pathogenesis and therapeutic targets from structural and functional genomics
    • Schmitz R, Young RM, Ceribelli M, Jhavar S, Xiao W, Zhang M, et al. Burkitt lymphoma pathogenesis and therapeutic targets from structural and functional genomics. Nature 2012; 490: 116-120
    • (2012) Nature , vol.490 , pp. 116-120
    • Schmitz, R.1    Young, R.M.2    Ceribelli, M.3    Jhavar, S.4    Xiao, W.5    Zhang, M.6
  • 163
    • 9144229104 scopus 로고    scopus 로고
    • Requirement for cyclin D3 in lymphocyte development and T cell leukemias
    • Sicinska E, Aifantis I, Le Cam L, Swat W, Borowski C, Yu Q, et al. Requirement for cyclin D3 in lymphocyte development and T cell leukemias. Cancer Cell 2003; 4: 451-461
    • (2003) Cancer Cell , vol.4 , pp. 451-461
    • Sicinska, E.1    Aifantis, I.2    Le Cam, L.3    Swat, W.4    Borowski, C.5    Yu, Q.6
  • 164
    • 78751688466 scopus 로고    scopus 로고
    • Cyclin D3 is selectively required for proliferative expansion of germinal center B cells
    • Cato MH, Chintalapati SK, Yau IW, Omori SA, Rickert RC. Cyclin D3 is selectively required for proliferative expansion of germinal center B cells. Mol Cell Biol 2011; 31: 127-137
    • (2011) Mol Cell Biol , vol.31 , pp. 127-137
    • Cato, M.H.1    Chintalapati, S.K.2    Yau, I.W.3    Omori, S.A.4    Rickert, R.C.5
  • 166
    • 0035963435 scopus 로고    scopus 로고
    • Specific protection against breast cancers by cyclin D1 ablation
    • Yu Q, Geng Y, Sicinski P. Specific protection against breast cancers by cyclin D1 ablation. Nature 2001; 411: 1017-1021
    • (2001) Nature , vol.411 , pp. 1017-1021
    • Yu, Q.1    Geng, Y.2    Sicinski, P.3
  • 167
    • 33748184149 scopus 로고    scopus 로고
    • Mantle cell lymphoma cells express predominantly cyclin D1a isoform and are highly sensitive to selective inhibition of CDK4 kinase activity
    • Marzec M, Kasprzycka M, Lai R, Gladden AB, Wlodarski P, Tomczak E, et al. Mantle cell lymphoma cells express predominantly cyclin D1a isoform and are highly sensitive to selective inhibition of CDK4 kinase activity. Blood 2006; 108: 1744-1750
    • (2006) Blood , vol.108 , pp. 1744-1750
    • Marzec, M.1    Kasprzycka, M.2    Lai, R.3    Gladden, A.B.4    Wlodarski, P.5    Tomczak, E.6
  • 168
    • 0037075887 scopus 로고    scopus 로고
    • Cyclin D-dependent kinases INK4 inhibitors and cancer
    • Ortega S, Malumbres M, Barbacid M. Cyclin D-dependent kinases, INK4 inhibitors and cancer. Biochim Biophys Acta 2002; 1602: 73-87
    • (2002) Biochim Biophys Acta , vol.1602 , pp. 73-87
    • Ortega, S.1    Malumbres, M.2    Barbacid, M.3
  • 172
    • 84877028141 scopus 로고    scopus 로고
    • Comprehensive molecular portraits of human breast tumours
    • TCGA
    • TCGA. Comprehensive molecular portraits of human breast tumours. Nature 2012; 490: 61-70
    • (2012) Nature , vol.490 , pp. 61-70
  • 174
    • 34648824397 scopus 로고    scopus 로고
    • Genetic and molecular pathogenesis of mantle cell lymphoma: Perspectives for new targeted therapeutics
    • Jares P, Colomer D, Campo E. Genetic and molecular pathogenesis of mantle cell lymphoma: Perspectives for new targeted therapeutics. Nat Rev Cancer 2007; 7: 750-762
    • (2007) Nat Rev Cancer , vol.7 , pp. 750-762
    • Jares, P.1    Colomer, D.2    Campo, E.3
  • 175
    • 17844399285 scopus 로고    scopus 로고
    • The enigmatic role of cyclin D1 in multiple myeloma
    • Lesage D, Troussard X, Sola B. The enigmatic role of cyclin D1 in multiple myeloma. Int J Cancer 2005; 115: 171-176
    • (2005) Int J Cancer , vol.115 , pp. 171-176
    • Lesage, D.1    Troussard, X.2    Sola, B.3
  • 177
    • 0242526150 scopus 로고    scopus 로고
    • An alternatively spliced cyclin D1 isoform, cyclin D1b, is a nuclear oncogene
    • Lu F, Gladden AB, Diehl JA. An alternatively spliced cyclin D1 isoform, cyclin D1b, is a nuclear oncogene. Cancer Res 2003; 63: 7056-7061
    • (2003) Cancer Res , vol.63 , pp. 7056-7061
    • Lu, F.1    Gladden, A.B.2    Diehl, J.A.3
  • 178
    • 65049084565 scopus 로고    scopus 로고
    • Cyclin D1b protein expression in breast cancer is independent of cyclin D1a and associated with poor disease outcome
    • Millar EK, Dean JL, McNeil CM, O'Toole SA, Henshall SM, Tran T, et al. Cyclin D1b protein expression in breast cancer is independent of cyclin D1a and associated with poor disease outcome. Oncogene 2009; 28: 1812-1820
    • (2009) Oncogene , vol.28 , pp. 1812-1820
    • Millar, E.K.1    Dean, J.L.2    McNeil, C.M.3    O'Toole, S.A.4    Henshall, S.M.5    Tran, T.6
  • 179
    • 0029664339 scopus 로고    scopus 로고
    • Germline mutations in the p16INK4a binding domain of CDK4 in familial melanoma
    • Zuo L, Weger J, Yang Q, Goldstein AM, Tucker MA, Walker GJ, et al. Germline mutations in the p16INK4a binding domain of CDK4 in familial melanoma. Nat Genet 1996; 12: 97-99
    • (1996) Nat Genet , vol.12 , pp. 97-99
    • Zuo, L.1    Weger, J.2    Yang, Q.3    Goldstein, A.M.4    Tucker, M.A.5    Walker, G.J.6
  • 180
    • 0035803395 scopus 로고    scopus 로고
    • Wide spectrum of tumors in knock-in mice carrying a Cdk4 protein insensitive to INK4 inhibitors
    • Sotillo R, Dubus P, Martin J, De la Cueva E, Ortega S, Malumbres M, et al. Wide spectrum of tumors in knock-in mice carrying a Cdk4 protein insensitive to INK4 inhibitors. EMBO J 2001; 20: 6637-6647
    • (2001) EMBO J , vol.20 , pp. 6637-6647
    • Sotillo, R.1    Dubus, P.2    Martin, J.3    De La Cueva, E.4    Ortega, S.5    Malumbres, M.6
  • 182
    • 0035419867 scopus 로고    scopus 로고
    • ErbB2/neu kinase modulates cellular p27(Kip1) and cyclin D1 through multiple signaling pathways
    • Lenferink AE, Busse D, Flanagan WM, Yakes FM, Arteaga CL. ErbB2/neu kinase modulates cellular p27(Kip1) and cyclin D1 through multiple signaling pathways. Cancer Res 2001; 61: 6583-6591
    • (2001) Cancer Res , vol.61 , pp. 6583-6591
    • Lenferink, A.E.1    Busse, D.2    Flanagan, W.M.3    Yakes, F.M.4    Arteaga, C.L.5
  • 183
    • 39749200927 scopus 로고    scopus 로고
    • Disruption of cyclin D1 nuclear export and proteolysis accelerates mammary carcinogenesis
    • Lin DI, Lessie MD, Gladden AB, Bassing CH, Wagner KU, Diehl JA. Disruption of cyclin D1 nuclear export and proteolysis accelerates mammary carcinogenesis. Oncogene 2008; 27: 1231-1242
    • (2008) Oncogene , vol.27 , pp. 1231-1242
    • Lin, D.I.1    Lessie, M.D.2    Gladden, A.B.3    Bassing, C.H.4    Wagner, K.U.5    Diehl, J.A.6
  • 185
    • 78049250336 scopus 로고    scopus 로고
    • Cyclin D2-cyclin-dependent kinase 4/6 is required for efficient proliferation and tumorigenesis following Apc loss
    • Cole AM, Myant K, Reed KR, Ridgway RA, Athineos D, Van Den Brink GR, et al. Cyclin D2-cyclin-dependent kinase 4/6 is required for efficient proliferation and tumorigenesis following Apc loss. Cancer Res 2010; 70: 8149-8158
    • (2010) Cancer Res , vol.70 , pp. 8149-8158
    • Cole, A.M.1    Myant, K.2    Reed, K.R.3    Ridgway, R.A.4    Athineos, D.5    Van Den Brink, G.R.6
  • 186
    • 4344689970 scopus 로고    scopus 로고
    • Cyclin D1 genetic heterozygosity regulates colonic epithelial cell differentiation and tumor number in ApcMin mice
    • Hulit J, Wang C, Li Z, Albanese C, Rao M, Di Vizio D, et al. Cyclin D1 genetic heterozygosity regulates colonic epithelial cell differentiation and tumor number in ApcMin mice. Mol Cell Biol 2004; 24: 7598-7611
    • (2004) Mol Cell Biol , vol.24 , pp. 7598-7611
    • Hulit, J.1    Wang, C.2    Li, Z.3    Albanese, C.4    Rao, M.5    Di Vizio, D.6
  • 187
    • 61849087835 scopus 로고    scopus 로고
    • Notch signaling mediates G1/S cell-cycle progression in T cells via cyclin D3 and its dependent kinases
    • Joshi I, Minter LM, Telfer J, Demarest RM, Capobianco AJ, Aster JC, et al. Notch signaling mediates G1/S cell-cycle progression in T cells via cyclin D3 and its dependent kinases. Blood 2009; 113: 1689-1698
    • (2009) Blood , vol.113 , pp. 1689-1698
    • Joshi, I.1    Minter, L.M.2    Telfer, J.3    Demarest, R.M.4    Capobianco, A.J.5    Aster, J.C.6
  • 188
    • 18644376449 scopus 로고    scopus 로고
    • PKB/Akt phosphorylates p27, impairs nuclear import of p27 and opposes p27-mediated G1 arrest
    • Liang J, Zubovitz J, Petrocelli T, Kotchetkov R, Connor MK, Han K, et al. PKB/Akt phosphorylates p27, impairs nuclear import of p27 and opposes p27-mediated G1 arrest. Nat Med 2002; 8: 1153-1160
    • (2002) Nat Med , vol.8 , pp. 1153-1160
    • Liang, J.1    Zubovitz, J.2    Petrocelli, T.3    Kotchetkov, R.4    Connor, M.K.5    Han, K.6
  • 189
    • 0036799377 scopus 로고    scopus 로고
    • PKB/Akt mediates cellcycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization
    • Shin I, Yakes FM, Rojo F, Shin NY, Bakin AV, Baselga J, et al. PKB/Akt mediates cellcycle progression by phosphorylation of p27(Kip1) at threonine 157 and modulation of its cellular localization. Nat Med 2002; 8: 1145-1152
    • (2002) Nat Med , vol.8 , pp. 1145-1152
    • Shin, I.1    Yakes, F.M.2    Rojo, F.3    Shin, N.Y.4    Bakin, A.V.5    Baselga, J.6
  • 190
    • 18644370396 scopus 로고    scopus 로고
    • Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer
    • Viglietto G, Motti ML, Bruni P, Melillo RM, D'Alessio A, Califano D, et al. Cytoplasmic relocalization and inhibition of the cyclin-dependent kinase inhibitor p27(Kip1) by PKB/Akt-mediated phosphorylation in breast cancer. Nat Med 2002; 8: 1136-1144
    • (2002) Nat Med , vol.8 , pp. 1136-1144
    • Viglietto, G.1    Motti, M.L.2    Bruni, P.3    Melillo, R.M.4    D'Alessio, A.5    Califano, D.6
  • 191
    • 0034745353 scopus 로고    scopus 로고
    • Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells
    • Zhou BP, Liao Y, Xia W, Spohn B, Lee MH, Hung MC. Cytoplasmic localization of p21Cip1/WAF1 by Akt-induced phosphorylation in HER-2/neu-overexpressing cells. Nat Cell Biol 2001; 3: 245-252
    • (2001) Nat Cell Biol , vol.3 , pp. 245-252
    • Zhou, B.P.1    Liao, Y.2    Xia, W.3    Spohn, B.4    Lee, M.H.5    Hung, M.C.6
  • 192
    • 0032530151 scopus 로고    scopus 로고
    • Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21(CIP1/WAF1) and cyclin D proteins
    • Yu ZK, Gervais JL, Zhang H. Human CUL-1 associates with the SKP1/SKP2 complex and regulates p21(CIP1/WAF1) and cyclin D proteins. Proc Natl Acad Sci USA 1998; 95: 11324-11329
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11324-11329
    • Yu, Z.K.1    Gervais, J.L.2    Zhang, H.3
  • 193
    • 0036124467 scopus 로고    scopus 로고
    • ErbB2/Neu-induced, cyclin D1-dependent transformation is accelerated in p27-haploinsufficient mammary epithelial cells but impaired in p27-null cells
    • Muraoka RS, Lenferink AE, Law B, Hamilton E, Brantley DM, Roebuck LR, et al. ErbB2/Neu-induced, cyclin D1-dependent transformation is accelerated in p27-haploinsufficient mammary epithelial cells but impaired in p27-null cells. Mol Cell Biol 2002; 22: 2204-2219
    • (2002) Mol Cell Biol , vol.22 , pp. 2204-2219
    • Muraoka, R.S.1    Lenferink, A.E.2    Law, B.3    Hamilton, E.4    Brantley, D.M.5    Roebuck, L.R.6
  • 194
    • 4944252223 scopus 로고    scopus 로고
    • An Rb-Skp2-p27 pathway mediates acute cell cycle inhibition by Rb and is retained in a partial-penetrance Rb mutant
    • Ji P, Jiang H, Rekhtman K, Bloom J, Ichetovkin M, Pagano M, et al. An Rb-Skp2-p27 pathway mediates acute cell cycle inhibition by Rb and is retained in a partial-penetrance Rb mutant. Mol Cell 2004; 16: 47-58
    • (2004) Mol Cell , vol.16 , pp. 47-58
    • Ji, P.1    Jiang, H.2    Rekhtman, K.3    Bloom, J.4    Ichetovkin, M.5    Pagano, M.6
  • 196
    • 33745676300 scopus 로고    scopus 로고
    • Toward understanding the structural basis of cyclindependent kinase 6 specific inhibition
    • Lu H, Schulze-Gahmen U. Toward understanding the structural basis of cyclindependent kinase 6 specific inhibition. J Med Chem 2006; 49: 3826-3831
    • (2006) J Med Chem , vol.49 , pp. 3826-3831
    • Lu, H.1    Schulze-Gahmen, U.2
  • 197
    • 84861210266 scopus 로고    scopus 로고
    • Selective CDK4/6 inhibition with tumor responses by PD0332991 in patients with mantle cell lymphoma
    • Leonard JP, LaCasce AS, Smith MR, Noy A, Chirieac LR, Rodig SJ, et al. Selective CDK4/6 inhibition with tumor responses by PD0332991 in patients with mantle cell lymphoma. Blood 2012; 119: 4597-4607
    • (2012) Blood , vol.119 , pp. 4597-4607
    • Leonard, J.P.1    LaCasce, A.S.2    Smith, M.R.3    Noy, A.4    Chirieac, L.R.5    Rodig, S.J.6
  • 198
    • 79958149971 scopus 로고    scopus 로고
    • Phase I study of PD 0332991, a cyclin-dependent kinase inhibitor, administered in 3-week cycles (Schedule 2/1
    • Schwartz GK, LoRusso PM, Dickson MA, Randolph SS, Shaik MN, Wilner KD, et al. Phase I study of PD 0332991, a cyclin-dependent kinase inhibitor, administered in 3-week cycles (Schedule 2/1). Br J Cancer 2011; 104: 1862-1868
    • (2011) Br J Cancer , vol.104 , pp. 1862-1868
    • Schwartz, G.K.1    LoRusso, P.M.2    Dickson, M.A.3    Randolph, S.S.4    Shaik, M.N.5    Wilner, K.D.6
  • 199
    • 84855983664 scopus 로고    scopus 로고
    • Phase I, dose-escalation trial of the oral cyclin-dependent kinase 4/6 inhibitor PD 0332991, administered using a 21-day schedule in patients with advanced cancer
    • Flaherty KT, Lorusso PM, Demichele A, Abramson VG, Courtney R, Randolph SS, et al. Phase I, dose-escalation trial of the oral cyclin-dependent kinase 4/6 inhibitor PD 0332991, administered using a 21-day schedule in patients with advanced cancer. Clin Cancer Res 2012; 18: 568-576
    • (2012) Clin Cancer Res , vol.18 , pp. 568-576
    • Flaherty, K.T.1    Lorusso, P.M.2    Demichele, A.3    Abramson, V.G.4    Courtney, R.5    Randolph, S.S.6
  • 200
    • 79961117100 scopus 로고    scopus 로고
    • The meaning of p16(ink4a) expression in tumors: Functional significance, clinical associations and future developments
    • Witkiewicz AK, Knudsen KE, Dicker AP, Knudsen ES. The meaning of p16(ink4a) expression in tumors: Functional significance, clinical associations and future developments. Cell Cycle 2011; 10: 2497-2503
    • (2011) Cell Cycle , vol.10 , pp. 2497-2503
    • Witkiewicz, A.K.1    Knudsen, K.E.2    Dicker, A.P.3    Knudsen, E.S.4
  • 201
    • 79952710710 scopus 로고    scopus 로고
    • Expression of p16 and retinoblastoma determines response to CDK4/6 inhibition in ovarian cancer
    • Konecny GE, Winterhoff B, Kolarova T, Qi J, Manivong K, Dering J, et al. Expression of p16 and retinoblastoma determines response to CDK4/6 inhibition in ovarian cancer. Clin Cancer Res 2011; 17: 1591-1602
    • (2011) Clin Cancer Res , vol.17 , pp. 1591-1602
    • Konecny, G.E.1    Winterhoff, B.2    Kolarova, T.3    Qi, J.4    Manivong, K.5    Dering, J.6
  • 203
    • 50149084928 scopus 로고    scopus 로고
    • Tailoring to RB: Tumour suppressor status and therapeutic response
    • Knudsen ES, Knudsen KE. Tailoring to RB: Tumour suppressor status and therapeutic response. Nat Rev Cancer 2008; 8: 714-724
    • (2008) Nat Rev Cancer , vol.8 , pp. 714-724
    • Knudsen, E.S.1    Knudsen, K.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.