메뉴 건너뛰기




Volumn 19, Issue 30, 2013, Pages 5327-5332

Anticancer therapeutic strategies based on CDK inhibitors

Author keywords

Anticancer therapeutics; Cancer; CDK inhibitors; CDKs; Cell cycle

Indexed keywords

AT 7519; ATP COMPETITIVE CYCLIN DEPENDENT KINASE INHIBITOR; CY 202; CYCLIN DEPENDENT KINASE INHIBITOR; DOCETAXEL; FLAVOPIRIDOL; NON ATP COMPETITIVE CYCLIN DEPENDENT KINASE INHIBITOR; P 276 00; R 547; ROSCOVITINE; UNCLASSIFIED DRUG; VORINOSTAT; ZK 304709;

EID: 84881361773     PISSN: 13816128     EISSN: 18734286     Source Type: Journal    
DOI: 10.2174/13816128113199990377     Document Type: Review
Times cited : (28)

References (57)
  • 1
    • 79960088065 scopus 로고    scopus 로고
    • Physiological relevance of cell cycle kinases
    • Malumbres M. Physiological relevance of cell cycle kinases. Physiol Rev 2011; 91(3): 973-1007.
    • (2011) Physiol Rev , vol.91 , Issue.3 , pp. 973-1007
    • Malumbres, M.1
  • 2
    • 27544470656 scopus 로고    scopus 로고
    • Mammalian cyclin-dependent kinases
    • Malumbres M, Barbacid M. Mammalian cyclin-dependent kinases. Trends Biochem Sci 2005; 30(11): 630-41.
    • (2005) Trends Biochem Sci , vol.30 , Issue.11 , pp. 630-641
    • Malumbres, M.1    Barbacid, M.2
  • 3
    • 38849187293 scopus 로고    scopus 로고
    • CDK inhibitors: Cell cycle regulators and beyond
    • Besson A, Dowdy SF, Roberts JM. CDK inhibitors: cell cycle regulators and beyond. Dev Cell 2008; 14(2): 159-69.
    • (2008) Dev Cell , vol.14 , Issue.2 , pp. 159-169
    • Besson, A.1    Dowdy, S.F.2    Roberts, J.M.3
  • 4
    • 67650073265 scopus 로고    scopus 로고
    • Cell cycle kinases as therapeutic targets for cancer
    • Lapenna S, Giordano A. Cell cycle kinases as therapeutic targets for cancer. Nat Rev Drug Discov 2009; 8(7): 547-66.
    • (2009) Nat Rev Drug Discov , vol.8 , Issue.7 , pp. 547-566
    • Lapenna, S.1    Giordano, A.2
  • 5
    • 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(3): 153-66.
    • (2009) Nat Rev Cancer , vol.9 , Issue.3 , pp. 153-166
    • Malumbres, M.1    Barbacid, M.2
  • 6
    • 84861111271 scopus 로고    scopus 로고
    • Cyclin dependent kinases in cancer: Potential for therapeutic intervention
    • Canavese M, Santo L, Raje N. Cyclin dependent kinases in cancer: potential for therapeutic intervention. Cancer Biol Ther 2012; 13(7): 451-7.
    • (2012) Cancer Biol Ther , vol.13 , Issue.7 , pp. 451-457
    • Canavese, M.1    Santo, L.2    Raje, N.3
  • 7
    • 84858055716 scopus 로고    scopus 로고
    • The retinoblastoma family of proteins and their regulatory functions in the mammalian cell division cycle
    • Henley SA, Dick FA. The retinoblastoma family of proteins and their regulatory functions in the mammalian cell division cycle. Cell Div 2012; 7(1): 10.
    • (2012) Cell Div , vol.7 , Issue.1 , pp. 10
    • Henley, S.A.1    Dick, F.A.2
  • 9
    • 0033093250 scopus 로고    scopus 로고
    • Cell cycle and cancer
    • Pucci B, Giordano A. Cell cycle and cancer. Clin Ter 1999; 150(2): 135-41.
    • (1999) Clin Ter , vol.150 , Issue.2 , pp. 135-141
    • Pucci, B.1    Giordano, A.2
  • 10
    • 0042528364 scopus 로고    scopus 로고
    • Cyclin E Ablation In the Mouse
    • Geng Y, Yu Q, Sicinska E, et al. Cyclin E ablation in the mouse. Cell 2003; 114(4): 431-43.
    • (2003) Cell , vol.114 , Issue.4 , pp. 431-443
    • Geng, Y.1    Yu, Q.2    Sicinska, E.3
  • 11
    • 33947498211 scopus 로고    scopus 로고
    • A small molecule based on the pRb2/p130 spacer domain leads to inhibition of cdk2 activity, cell cycle arrest and tumor growth reduction in vivo
    • Bagella L, Sun A, Tonini T, et al. A small molecule based on the pRb2/p130 spacer domain leads to inhibition of cdk2 activity, cell cycle arrest and tumor growth reduction in vivo. Oncogene 2007; 26(13): 1829-39.
    • (2007) Oncogene , vol.26 , Issue.13 , pp. 1829-1839
    • Bagella, L.1    Sun, A.2    Tonini, T.3
  • 12
    • 55449124826 scopus 로고    scopus 로고
    • SnapShot: Cell-cycle regulators I
    • Morgan DO. SnapShot: cell-cycle regulators I. Cell 2008; 135(4): 764-e1.
    • (2008) Cell , vol.135 , Issue.4 , pp. 764
    • Morgan, D.O.1
  • 13
    • 55449124826 scopus 로고    scopus 로고
    • SnapShot: Cell-cycle regulators II
    • Morgan DO. SnapShot: Cell-cycle regulators II. Cell 2008; 135(5): 974-e1.
    • (2008) Cell , vol.135 , Issue.5 , pp. 974
    • Morgan, D.O.1
  • 14
    • 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(1): 73-87.
    • (2002) Biochim Biophys Acta , vol.1602 , Issue.1 , pp. 73-87
    • Ortega, S.1    Malumbres, M.2    Barbacid, M.3
  • 15
    • 34447094967 scopus 로고    scopus 로고
    • A census of mitotic cancer genes: New insights into tumor cell biology and cancer therapy
    • Perez de Castro I, de Carcer G, Malumbres M. A census of mitotic cancer genes: new insights into tumor cell biology and cancer therapy. Carcinogenesis 2007; 28(5): 899-912.
    • (2007) Carcinogenesis , vol.28 , Issue.5 , pp. 899-912
    • de Castro, P.I.1    de Carcer, G.2    Malumbres, M.3
  • 16
    • 57349170148 scopus 로고    scopus 로고
    • Role of the cyclin-dependent kinase 9-related pathway in mammalian gene expression and human diseases
    • Romano G, Giordano A. Role of the cyclin-dependent kinase 9-related pathway in mammalian gene expression and human diseases. Cell Cycle 2008; 7(23): 3664-8.
    • (2008) Cell Cycle , vol.7 , Issue.23 , pp. 3664-3668
    • Romano, G.1    Giordano, A.2
  • 17
    • 73949098573 scopus 로고    scopus 로고
    • Selective control of gene expression by CDK9 in human cells
    • Garriga J, Xie H, Obradovic Z, Grana X. Selective control of gene expression by CDK9 in human cells. J Cell Physiol 2010; 222(1): 200-8.
    • (2010) J Cell Physiol , vol.222 , Issue.1 , pp. 200-208
    • Garriga, J.1    Xie, H.2    Obradovic, Z.3    Grana, X.4
  • 18
    • 40849119789 scopus 로고    scopus 로고
    • Cdk11 is a RanGTP-dependent microtubule stabilization factor that regulates spindle assembly rate
    • Yokoyama H, Gruss OJ, Rybina S, et al. Cdk11 is a RanGTP-dependent microtubule stabilization factor that regulates spindle assembly rate. J Cell Biol 2008; 180(5): 867-75.
    • (2008) J Cell Biol , vol.180 , Issue.5 , pp. 867-875
    • Yokoyama, H.1    Gruss, O.J.2    Rybina, S.3
  • 19
    • 34547767152 scopus 로고    scopus 로고
    • CDK11(p58) is required for the maintenance of sister chromatid cohesion
    • Hu D, Valentine M, Kidd VJ, Lahti JM. CDK11(p58) is required for the maintenance of sister chromatid cohesion. J Cell Sci 2007; 120(Pt 14): 2424-34.
    • (2007) J Cell Sci , vol.120 , Issue.PART 14 , pp. 2424-2434
    • Hu, D.1    Valentine, M.2    Kidd, V.J.3    Lahti, J.M.4
  • 20
    • 34547782947 scopus 로고    scopus 로고
    • Haploinsufficiency of the cdc2l gene contributes to skin cancer development in mice
    • Chandramouli A, Shi J, Feng Y, et al. Haploinsufficiency of the cdc2l gene contributes to skin cancer development in mice. Carcinogenesis 2007; 28(9): 2028-35.
    • (2007) Carcinogenesis , vol.28 , Issue.9 , pp. 2028-2035
    • Chandramouli, A.1    Shi, J.2    Feng, Y.3
  • 21
    • 79959954585 scopus 로고    scopus 로고
    • Peptides or small molecules? Different approaches to develop more effective CDK inhibitors
    • Cirillo D, Pentimalli F, Giordano A. Peptides or small molecules? Different approaches to develop more effective CDK inhibitors. Curr Med Chem 2011; 18(19): 2854-66.
    • (2011) Curr Med Chem , vol.18 , Issue.19 , pp. 2854-2866
    • Cirillo, D.1    Pentimalli, F.2    Giordano, A.3
  • 22
    • 84860342022 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 regulates E2F transcription factor through phosphorylation of Rb protein in neurons
    • Futatsugi A, Utreras E, Rudrabhatla P, Jaffe H, Pant HC, Kulkarni AB. Cyclin-dependent kinase 5 regulates E2F transcription factor through phosphorylation of Rb protein in neurons. Cell Cycle 2012; 11(8): 1603-10.
    • (2012) Cell Cycle , vol.11 , Issue.8 , pp. 1603-1610
    • Futatsugi, A.1    Utreras, E.2    Rudrabhatla, P.3    Jaffe, H.4    Pant, H.C.5    Kulkarni, A.B.6
  • 24
    • 33847066362 scopus 로고    scopus 로고
    • Cyclin dependent kinase 2 and the regulation of human progesterone receptor activity
    • Moore NL, Narayanan R, Weigel NL. Cyclin dependent kinase 2 and the regulation of human progesterone receptor activity. Steroids 2007; 72(2): 202-9.
    • (2007) Steroids , vol.72 , Issue.2 , pp. 202-209
    • Moore, N.L.1    Narayanan, R.2    Weigel, N.L.3
  • 25
    • 33947577413 scopus 로고    scopus 로고
    • Peripheral white blood cell toxicity induced by broad spectrum cyclin-dependent kinase inhibitors
    • Jessen BA, Lee L, Koudriakova T, et al. Peripheral white blood cell toxicity induced by broad spectrum cyclin-dependent kinase inhibitors. J Appl Toxicol 2007; 27(2): 133-42.
    • (2007) J Appl Toxicol , vol.27 , Issue.2 , pp. 133-142
    • Jessen, B.A.1    Lee, L.2    Koudriakova, T.3
  • 26
    • 33846219417 scopus 로고    scopus 로고
    • Flavopiridol administered using a pharmacologically derived schedule is associated with marked clinical efficacy in refractory, genetically high-risk chronic lymphocytic leukemia
    • Byrd JC, Lin TS, Dalton JT, et al. Flavopiridol administered using a pharmacologically derived schedule is associated with marked clinical efficacy in refractory, genetically high-risk chronic lymphocytic leukemia. Blood 2007; 109(2): 399-404.
    • (2007) Blood , vol.109 , Issue.2 , pp. 399-404
    • Byrd, J.C.1    Lin, T.S.2    Dalton, J.T.3
  • 27
    • 37549000240 scopus 로고    scopus 로고
    • Expression of serine/threonine protein-kinases and related factors in normal monkey and human retinas: The mechanistic understanding of a CDK2 inhibitor induced retinal toxicity
    • Saturno G, Pesenti M, Cavazzoli C, et al. Expression of serine/threonine protein-kinases and related factors in normal monkey and human retinas: the mechanistic understanding of a CDK2 inhibitor induced retinal toxicity. Toxicol Pathol 2007; 35(7): 972-83.
    • (2007) Toxicol Pathol , vol.35 , Issue.7 , pp. 972-983
    • Saturno, G.1    Pesenti, M.2    Cavazzoli, C.3
  • 29
    • 34147127727 scopus 로고    scopus 로고
    • In vitro antitumor properties of a novel cyclin-dependent kinase inhibitor, P276-00
    • Joshi KS, Rathos MJ, Joshi RD, et al. In vitro antitumor properties of a novel cyclin-dependent kinase inhibitor, P276-00. Mol Cancer Ther 2007; 6(3): 918-25.
    • (2007) Mol Cancer Ther , vol.6 , Issue.3 , pp. 918-925
    • Joshi, K.S.1    Rathos, M.J.2    Joshi, R.D.3
  • 30
    • 34147167723 scopus 로고    scopus 로고
    • P276-00, a novel cyclin-dependent inhibitor induces G1-G2 arrest, shows antitumor activity on cisplatin-resistant cells and significant in vivo efficacy in tumor models
    • Joshi KS, Rathos MJ, Mahajan P, Wagh V, Shenoy S, Bhatia D, et al. P276-00, a novel cyclin-dependent inhibitor induces G1-G2 arrest, shows antitumor activity on cisplatin-resistant cells and significant in vivo efficacy in tumor models. Mol Cancer Ther 2007; 6(3): 926-34.
    • (2007) Mol Cancer Ther , vol.6 , Issue.3 , pp. 926-934
    • Joshi, K.S.1    Rathos, M.J.2    Mahajan, P.3    Wagh, V.4    Shenoy, S.5    Bhatia, D.6
  • 31
    • 60849123760 scopus 로고    scopus 로고
    • Biological characterization of AT7519, a small-molecule inhibitor of cyclin-dependent kinases, in human tumor cell lines
    • Squires MS, Feltell RE, Wallis NG, et al. Biological characterization of AT7519, a small-molecule inhibitor of cyclin-dependent kinases, in human tumor cell lines. Mol Cancer Ther 2009; 8(2): 324-32.
    • (2009) Mol Cancer Ther , vol.8 , Issue.2 , pp. 324-332
    • Squires, M.S.1    Feltell, R.E.2    Wallis, N.G.3
  • 32
    • 33750469601 scopus 로고    scopus 로고
    • In vitro and in vivo activity of R547: A potent and selective cyclin-dependent kinase inhibitor currently in phase I clinical trials
    • DePinto W, Chu XJ, Yin X, et al. In vitro and in vivo activity of R547: a potent and selective cyclin-dependent kinase inhibitor currently in phase I clinical trials. Mol Cancer Ther 2006; 5(11): 2644-58.
    • (2006) Mol Cancer Ther , vol.5 , Issue.11 , pp. 2644-2658
    • Depinto, W.1    Chu, X.J.2    Yin, X.3
  • 33
    • 33747128468 scopus 로고    scopus 로고
    • Molecular and pharmacodynamic characteristics of the novel multi-target tumor growth inhibitor ZK 304709
    • Siemeister G, Luecking U, Wagner C, Detjen K, McCoy C, Bosslet K. Molecular and pharmacodynamic characteristics of the novel multi-target tumor growth inhibitor ZK 304709. Biomed Pharmacother 2006; 60(6): 269-72.
    • (2006) Biomed Pharmacother , vol.60 , Issue.6 , pp. 269-272
    • Siemeister, G.1    Luecking, U.2    Wagner, C.3    Detjen, K.4    McCoy, C.5    Bosslet, K.6
  • 34
    • 58849089221 scopus 로고    scopus 로고
    • The oral multitarget tumour growth inhibitor, ZK 304709, inhibits growth of pancreatic neuroendocrine tumours in an orthotopic mouse model
    • Scholz A, Wagner K, Welzel M, et al. The oral multitarget tumour growth inhibitor, ZK 304709, inhibits growth of pancreatic neuroendocrine tumours in an orthotopic mouse model. Gut 2009; 58(2): 261-70.
    • (2009) Gut , vol.58 , Issue.2 , pp. 261-270
    • Scholz, A.1    Wagner, K.2    Welzel, M.3
  • 35
    • 84860512314 scopus 로고    scopus 로고
    • The cyclin-dependent kinase inhibitor flavopiridol potentiates doxorubicin efficacy in advanced sarcomas: Preclinical investigations and results of a phase I dose-escalation clinical trial
    • Luke JJ, D'Adamo DR, Dickson MA, et al. The cyclin-dependent kinase inhibitor flavopiridol potentiates doxorubicin efficacy in advanced sarcomas: preclinical investigations and results of a phase I dose-escalation clinical trial. Clin Cancer Res 2012; 18(9): 2638-47.
    • (2012) Clin Cancer Res , vol.18 , Issue.9 , pp. 2638-2647
    • Luke, J.J.1    D'Adamo, D.R.2    Dickson, M.A.3
  • 36
    • 0037674946 scopus 로고    scopus 로고
    • Enhancement of depsipeptide-mediated apoptosis of lung or esophageal cancer cells by flavopiridol: Activation of the mitochondria-dependent deathsignaling pathway
    • Nguyen DM, Schrump WD, Tsai WS, et al. Enhancement of depsipeptide-mediated apoptosis of lung or esophageal cancer cells by flavopiridol: activation of the mitochondria-dependent deathsignaling pathway. J Thorac Cardiovasc Surg 2003; 125(5): 1132-42.
    • (2003) J Thorac Cardiovasc Surg , vol.125 , Issue.5 , pp. 1132-1142
    • Nguyen, D.M.1    Schrump, W.D.2    Tsai, W.S.3
  • 37
    • 1842481018 scopus 로고    scopus 로고
    • Abrogation of p21 expression by flavopiridol enhances depsipeptide-mediated apoptosis in malignant pleural mesothelioma cells
    • Nguyen DM, Schrump WD, Chen GA, et al. Abrogation of p21 expression by flavopiridol enhances depsipeptide-mediated apoptosis in malignant pleural mesothelioma cells. Clin Cancer Res 2004; 10(5): 1813-25.
    • (2004) Clin Cancer Res , vol.10 , Issue.5 , pp. 1813-1825
    • Nguyen, D.M.1    Schrump, W.D.2    Chen, G.A.3
  • 38
    • 0036050151 scopus 로고    scopus 로고
    • Synergistic induction of mitochondrial damage and apoptosis in human leukemia cells by flavopiridol and the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA)
    • Almenara J, Rosato R, Grant S. Synergistic induction of mitochondrial damage and apoptosis in human leukemia cells by flavopiridol and the histone deacetylase inhibitor suberoylanilide hydroxamic acid (SAHA). Leukemia 2002; 16(7): 1331-43.
    • (2002) Leukemia , vol.16 , Issue.7 , pp. 1331-1343
    • Almenara, J.1    Rosato, R.2    Grant, S.3
  • 39
    • 4844224868 scopus 로고    scopus 로고
    • Contribution of disruption of the nuclear factor-kappaB pathway to induction of apoptosis in human leukemia cells by histone deacetylase inhibitors and flavopiridol
    • Gao N, Dai Y, Rahmani M, Dent P, Grant S. Contribution of disruption of the nuclear factor-kappaB pathway to induction of apoptosis in human leukemia cells by histone deacetylase inhibitors and flavopiridol. Mol Pharmacol 2004; 66(4): 956-63.
    • (2004) Mol Pharmacol , vol.66 , Issue.4 , pp. 956-963
    • Gao, N.1    Dai, Y.2    Rahmani, M.3    Dent, P.4    Grant, S.5
  • 40
    • 1342308338 scopus 로고    scopus 로고
    • Evidence of a functional role for p21WAF1/CIP1 down-regulation in synergistic antileukemic interactions between the histone deacetylase inhibitor sodium butyrate and flavopiridol
    • Rosato RR, Almenara JA, Yu C, Grant S. Evidence of a functional role for p21WAF1/CIP1 down-regulation in synergistic antileukemic interactions between the histone deacetylase inhibitor sodium butyrate and flavopiridol. Mol Pharmacol 2004; 65(3): 571-81.
    • (2004) Mol Pharmacol , vol.65 , Issue.3 , pp. 571-581
    • Rosato, R.R.1    Almenara, J.A.2    Yu, C.3    Grant, S.4
  • 41
    • 33847367725 scopus 로고    scopus 로고
    • Mechanism and functional role of XIAP and Mcl-1 down-regulation in flavopiridol/vorinostat antileukemic interactions
    • Rosato RR, Almenara JA, Kolla SS, et al. Mechanism and functional role of XIAP and Mcl-1 down-regulation in flavopiridol/vorinostat antileukemic interactions. Mol Cancer Ther 2007; 6(2): 692-702.
    • (2007) Mol Cancer Ther , vol.6 , Issue.2 , pp. 692-702
    • Rosato, R.R.1    Almenara, J.A.2    Kolla, S.S.3
  • 42
    • 78650438185 scopus 로고    scopus 로고
    • Combination of vorinostat and flavopiridol is selectively cytotoxic to multidrugresistant neuroblastoma cell lines with mutant TP53
    • Huang JM, Sheard MA, Ji L, Sposto R, Keshelava N. Combination of vorinostat and flavopiridol is selectively cytotoxic to multidrugresistant neuroblastoma cell lines with mutant TP53. Mol Cancer Ther 2010; 9(12): 3289-301.
    • (2010) Mol Cancer Ther , vol.9 , Issue.12 , pp. 3289-3301
    • Huang, J.M.1    Sheard, M.A.2    Ji, L.3    Sposto, R.4    Keshelava, N.5
  • 44
    • 52049097040 scopus 로고    scopus 로고
    • Progress in the evaluation of CDK inhibitors as antitumor agents
    • McInnes C. Progress in the evaluation of CDK inhibitors as antitumor agents. Drug Discov Today 2008; 13(19-20): 875-81.
    • (2008) Drug Discov Today , vol.13 , Issue.19-20 , pp. 875-881
    • McInnes, C.1
  • 45
    • 0141499922 scopus 로고    scopus 로고
    • p53 in a crosstalk between DNA repair and cell cycle checkpoints
    • Okorokov AL. p53 in a crosstalk between DNA repair and cell cycle checkpoints. Cell Cycle 2003; 2(3): 233-5.
    • (2003) Cell Cycle , vol.2 , Issue.3 , pp. 233-235
    • Okorokov, A.L.1
  • 46
    • 0030910037 scopus 로고    scopus 로고
    • p53 and ATM: Cell cycle, cell death, and cancer
    • Morgan SE, Kastan MB. p53 and ATM: cell cycle, cell death, and cancer. Adv Cancer Res 1997; 71: 1-25.
    • (1997) Adv Cancer Res , vol.71 , pp. 1-25
    • Morgan, S.E.1    Kastan, M.B.2
  • 47
    • 0031028163 scopus 로고    scopus 로고
    • Inhibition of cyclin-dependent kinases by purine analogues: Crystal structure of human cdk2 complexed with roscovitine
    • De Azevedo WF, Leclerc S, Meijer L, Havlicek L, Strnad M, Kim SH. Inhibition of cyclin-dependent kinases by purine analogues: crystal structure of human cdk2 complexed with roscovitine. Eur J Biochem 1997; 243(1-2): 518-26.
    • (1997) Eur J Biochem , vol.243 , Issue.1-2 , pp. 518-526
    • de Azevedo, W.F.1    Leclerc, S.2    Meijer, L.3    Havlicek, L.4    Strnad, M.5    Kim, S.H.6
  • 48
    • 0034721195 scopus 로고    scopus 로고
    • Identification of novel purine and pyrimidine cyclin-dependent kinase inhibitors with distinct molecular interactions and tumor cell growth inhibition profiles
    • Arris CE, Boyle FT, Calvert AH, et al. Identification of novel purine and pyrimidine cyclin-dependent kinase inhibitors with distinct molecular interactions and tumor cell growth inhibition profiles. J Med Chem 2000; 43(15): 2797-804.
    • (2000) J Med Chem , vol.43 , Issue.15 , pp. 2797-2804
    • Arris, C.E.1    Boyle, F.T.2    Calvert, A.H.3
  • 49
    • 0034647433 scopus 로고    scopus 로고
    • The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A
    • Luciani MG, Hutchins JR, Zheleva D, Hupp TR. The C-terminal regulatory domain of p53 contains a functional docking site for cyclin A. J Mol Biol 2000; 300(3): 503-18.
    • (2000) J Mol Biol , vol.300 , Issue.3 , pp. 503-518
    • Luciani, M.G.1    Hutchins, J.R.2    Zheleva, D.3    Hupp, T.R.4
  • 50
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • Jeffrey PD, Russo AA, Polyak K, et al. Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex. Nature 1995; 376(6538): 313-20.
    • (1995) Nature , vol.376 , Issue.6538 , pp. 313-320
    • Jeffrey, P.D.1    Russo, A.A.2    Polyak, K.3
  • 51
    • 33845980608 scopus 로고    scopus 로고
    • Identification of an hexapeptide that binds to a surface pocket in cyclin A and inhibits the catalytic activity of the complex cyclin-dependent kinase 2-cyclin A
    • Canela N, Orzaez M, Fucho R, et al. Identification of an hexapeptide that binds to a surface pocket in cyclin A and inhibits the catalytic activity of the complex cyclin-dependent kinase 2-cyclin A. J Biol Chem 2006; 281(47): 35942-53.
    • (2006) J Biol Chem , vol.281 , Issue.47 , pp. 35942-55953
    • Canela, N.1    Orzaez, M.2    Fucho, R.3
  • 52
    • 2342595835 scopus 로고    scopus 로고
    • Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis
    • Wadia JS, Stan RV, Dowdy SF. Transducible TAT-HA fusogenic peptide enhances escape of TAT-fusion proteins after lipid raft macropinocytosis. Nat Med 2004; 10(3): 310-5.
    • (2004) Nat Med , vol.10 , Issue.3 , pp. 310-315
    • Wadia, J.S.1    Stan, R.V.2    Dowdy, S.F.3
  • 53
    • 0029973557 scopus 로고    scopus 로고
    • Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors
    • Dec
    • Adams PD, Sellers WR, Sharma SK, Wu AD, Nalin CM, Kaelin WG, Jr. Identification of a cyclin-cdk2 recognition motif present in substrates and p21-like cyclin-dependent kinase inhibitors. Mol Cell Biol 1996 Dec; 16(12): 6623-33.
    • (1996) Mol Cell Biol , vol.16 , Issue.12 , pp. 6623-6633
    • Adams, P.D.1    Sellers, W.R.2    Sharma, S.K.3    Wu, A.D.4    Nalin, C.M.5    Kaelin, W.G.6
  • 54
    • 6344240541 scopus 로고    scopus 로고
    • Design, synthesis, biological activity and structural analysis of cyclic peptide inhibitors targeting the substrate recruitment site of cyclin-dependent kinase complexes
    • Andrews MJ, McInnes C, Kontopidis G, et al. Design, synthesis, biological activity and structural analysis of cyclic peptide inhibitors targeting the substrate recruitment site of cyclin-dependent kinase complexes. Org Biomol Chem 2004; 2(19): 2735-41.
    • (2004) Org Biomol Chem , vol.2 , Issue.19 , pp. 2735-2741
    • Andrews, M.J.1    McInnes, C.2    Kontopidis, G.3
  • 55
    • 0036830109 scopus 로고    scopus 로고
    • Highly potent p21(WAF1)-derived peptide inhibitors of CDKmediated pRb phosphorylation: Delineation and structural insight into their interactions with cyclin A
    • Zheleva DI, McInnes C, Gavine AL, Zhelev NZ, Fischer PM, Lane DP. Highly potent p21(WAF1)-derived peptide inhibitors of CDKmediated pRb phosphorylation: delineation and structural insight into their interactions with cyclin A. J Pept Res 2002; 60(5): 257-70.
    • (2002) J Pept Res , vol.60 , Issue.5 , pp. 257-270
    • Zheleva, D.I.1    McInnes, C.2    Gavine, A.L.3    Zhelev, N.Z.4    Fischer, P.M.5    Lane, D.P.6
  • 56
    • 0037119763 scopus 로고    scopus 로고
    • Peptide inhibitors of CDK2-cyclin A that target the cyclin recruitment-site: Structural variants of the C-terminal Phe
    • Atkinson GE, Cowan A, McInnes C, Zheleva DI, Fischer PM, Chan WC. Peptide inhibitors of CDK2-cyclin A that target the cyclin recruitment-site: structural variants of the C-terminal Phe. Bioorg Med Chem Lett 2002; 12(18): 2501-5.
    • (2002) Bioorg Med Chem Lett , vol.12 , Issue.18 , pp. 2501-2505
    • Atkinson, G.E.1    Cowan, A.2    McInnes, C.3    Zheleva, D.I.4    Fischer, P.M.5    Chan, W.C.6
  • 57
    • 67749106463 scopus 로고    scopus 로고
    • Truncation and optimisation of peptide inhibitors of cyclin-dependent kinase 2-cyclin a through structure-guided design
    • Kontopidis G, Andrews MJ, McInnes C, et al. Truncation and optimisation of peptide inhibitors of cyclin-dependent kinase 2-cyclin a through structure-guided design. Chem Med Chem 2009; 4(7): 1120-8.
    • (2009) Chem Med Chem , vol.4 , Issue.7 , pp. 1120-1128
    • Kontopidis, G.1    Andrews, M.J.2    McInnes, C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.