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Volumn 88, Issue , 2014, Pages 74-88

Fluorescent biosensors for drug discovery new tools for old targets - Screening for inhibitors of cyclin-dependent kinases

Author keywords

Cancer; CDK Cyclin; Fluorescent Biosensor; High throughput screening; Inhibitor

Indexed keywords

ANTINEOPLASTIC AGENT; AT 7519; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE INHIBITOR; CYCLINE; DINACICLIB; FLAVOPIRIDOL; ROSCOVITINE; UNCLASSIFIED DRUG; CYCLIN-DEPENDENT KINASES; PROTEIN KINASE INHIBITORS;

EID: 84911469534     PISSN: 02235234     EISSN: 17683254     Source Type: Journal    
DOI: 10.1002/cbic.201402318     Document Type: Article
Times cited : (14)

References (217)
  • 1
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • D.O. Morgan, Cyclin-dependent kinases: engines, clocks, and microprocessors, Annu. Rev. Cell Dev. Biol. 13 (1997) 261-291.
    • (1997) Annu. Rev. Cell Dev. Biol. , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 2
    • 60749109846 scopus 로고    scopus 로고
    • Cell cycle, CDKs and cancer: A changing paradigm
    • M. Malumbres, M. Barbacid, Cell cycle, CDKs and cancer: a changing paradigm, Nat. Rev. Cancer 9 (2009) 153-166.
    • (2009) Nat Rev. Cancer , vol.9 , pp. 153-166
    • Malumbres, M.1    Barbacid, M.2
  • 3
    • 79960088065 scopus 로고    scopus 로고
    • Physiological relevance of cell cycle kinases
    • M. Malumbres, Physiological relevance of cell cycle kinases, Physiol. Rev. 91 (2011) 973-1007.
    • (2011) Physiol. Rev. , vol.91 , pp. 973-1007
    • Malumbres, M.1
  • 4
    • 84880264045 scopus 로고    scopus 로고
    • Cdks cyclins and CKIs: Roles beyond cell cycle regulation
    • S. Lim, P. Kaldis, Cdks, cyclins and CKIs: roles beyond cell cycle regulation, Development 140 (2013) 3079-3093.
    • (2013) Development , vol.140 , pp. 3079-3093
    • Lim, S.1    Kaldis, P.2
  • 5
    • 0037096158 scopus 로고    scopus 로고
    • From Cdc2 to Cdk1: When did the cell cycle kinase join its cyclin partner?
    • M. Dorée, T. Hunt, From Cdc2 to Cdk1: when did the cell cycle kinase join its cyclin partner? J. Cell Sci. 115 (2002) 2461-2464.
    • (2002) J Cell Sci. , vol.115 , pp. 2461-2464
    • Dorée, M.1    Hunt, T.2
  • 6
    • 0033022375 scopus 로고    scopus 로고
    • The cdk-activating kinase (CAK): From yeast to mammals
    • P. Kaldis, The cdk-activating kinase (CAK): from yeast to mammals, Cell Mol. Life Sci. 55 (1999) 284-296.
    • (1999) Cell Mol. Life Sci. , vol.55 , pp. 284-296
    • Kaldis, P.1
  • 7
    • 29244468847 scopus 로고    scopus 로고
    • Secrets of a double agent: CDK7 in cell-cycle control and transcription
    • R.P. Fisher, Secrets of a double agent: CDK7 in cell-cycle control and transcription, J. Cell Sci. 118 (2005) 5171-5180.
    • (2005) J. Cell Sci. , vol.118 , pp. 5171-5180
    • Fisher, R.P.1
  • 8
    • 77957966270 scopus 로고    scopus 로고
    • Nuclear cyclin D1/CDK4 kinase regulates CUL4 expression and triggers neoplastic growth via activation of the PRMT5 methyltransferase
    • P. Aggarwal, L.P. Vaites, J.K. Kim, H. Mellert, B. Gurung, H. Nakagawa, et al., Nuclear cyclin D1/CDK4 kinase regulates CUL4 expression and triggers neoplastic growth via activation of the PRMT5 methyltransferase, Cancer Cell 18 (2010) 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
  • 9
    • 84555177974 scopus 로고    scopus 로고
    • A novel mechanism for regulating hepatic glycogen synthesis involving serotonin and cyclin-dependent kinase-5
    • S.J. Tudhope, C.-C. Wang, J.L. Petrie, L. Potts, F. Malcomson, J. Kieswich, et al., A novel mechanism for regulating hepatic glycogen synthesis involving serotonin and cyclin-dependent kinase-5, Diabetes 61 (2012) 49-60.
    • (2012) Diabetes , vol.61 , pp. 49-60
    • Tudhope, S.J.1    Wang, C.-C.2    Petrie, J.L.3    Potts, L.4    Malcomson, F.5    Kieswich, J.6
  • 10
    • 84863552454 scopus 로고    scopus 로고
    • Regulation of lipogenesis by cyclin-dependent kinase 8-mediated control of SREBP-1
    • X. Zhao, D. Feng, Q. Wang, A. Abdulla, X.-J. Xie, J. Zhou, et al., Regulation of lipogenesis by cyclin-dependent kinase 8-mediated control of SREBP-1, J. Clin. Invest. 122 (2012) 2417-2427.
    • (2012) J. Clin. Invest. , vol.122 , pp. 2417-2427
    • Zhao, X.1    Feng, D.2    Wang, Q.3    Abdulla, A.4    Xie, X.-J.5    Zhou, J.6
  • 11
    • 84864386776 scopus 로고    scopus 로고
    • Cyclin D1 inhibits hepatic lipogenesis via repression of carbohydrate response element binding protein and hepatocyte nuclear factor 4a
    • E.A. Hanse, D.G. Mashek, J.R. Becker, A.D. Solmonson, L.K. Mullany, M.T. Mashek, et al., Cyclin D1 inhibits hepatic lipogenesis via repression of carbohydrate response element binding protein and hepatocyte nuclear factor 4a, Cell Cycle 11 (2012) 2681-2690.
    • (2012) Cell Cycle , vol.11 , pp. 2681-2690
    • Hanse, E.A.1    Mashek, D.G.2    Becker, J.R.3    Solmonson, A.D.4    Mullany, L.K.5    Mashek, M.T.6
  • 12
    • 0030888270 scopus 로고    scopus 로고
    • Interactions of cyclins with cyclin-dependent kinases: A common interactive mechanism
    • F. Heitz, M.C. Morris, D. Fesquet, J.C. Cavadore, M. Dorée, G. Divita, Interactions of cyclins with cyclin-dependent kinases: a common interactive mechanism, Biochemistry 36 (1997) 4995-5003.
    • (1997) Biochemistry , vol.36 , pp. 4995-5003
    • Heitz, F.1    Morris, M.C.2    Fesquet, D.3    Cavadore, J.C.4    Dorée, M.5    Divita, G.6
  • 13
    • 4444247138 scopus 로고    scopus 로고
    • Mammalian cells cycle without the D-type cyclin-dependent kinases Cdk4 and Cdk6
    • M. Malumbres, R. Sotillo, D. Santamaría, J. Galán, A. Cerezo, S. Ortega, et al., Mammalian cells cycle without the D-type cyclin-dependent kinases Cdk4 and Cdk6, Cell 118 (2004) 493-504.
    • (2004) Cell , vol.118 , pp. 493-504
    • Malumbres, M.1    Sotillo, R.2    Santamaría, D.3    Galán, J.4    Cerezo, A.5    Ortega, S.6
  • 15
    • 8644219655 scopus 로고    scopus 로고
    • Living with or without cyclins and cyclin-dependent kinases
    • C.J. Sherr, J.M. Roberts, Living with or without cyclins and cyclin-dependent kinases, Genes. Dev. 18 (2004) 2699-2711.
    • (2004) Genes. Dev. , vol.18 , pp. 2699-2711
    • Sherr, C.J.1    Roberts, J.M.2
  • 16
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • D.O. Morgan, Principles of CDK regulation, Nature 374 (1995) 131-134.
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 19
    • 0026207472 scopus 로고
    • Cyclins and their partners: From a simple idea to complicated reality
    • T. Hunt, Cyclins and their partners: from a simple idea to complicated reality, Semin. Cell Biol. 2 (1991) 213-222.
    • (1991) Semin. Cell Biol. , vol.2 , pp. 213-222
    • Hunt, T.1
  • 20
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • P.D. Jeffrey, A.A. Russo, K. Polyak, E. Gibbs, J. Hurwitz, J. Massagué, et al., Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex, Nature 376 (1995) 313-320.
    • (1995) Nature , vol.376 , pp. 313-320
    • Jeffrey, P.D.1    Russo, A.A.2    Polyak, K.3    Gibbs, E.4    Hurwitz, J.5    Massagué, J.6
  • 21
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • A.A. Russo, P.D. Jeffrey, N.P. Pavletich, Structural basis of cyclin-dependent kinase activation by phosphorylation, Nat. Struct. Biol. 3 (1996) 696-700.
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 696-700
    • Russo, A.A.1    Jeffrey, P.D.2    Pavletich, N.P.3
  • 22
    • 0033605643 scopus 로고    scopus 로고
    • Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity
    • N.R. Brown, M.E. Noble, A.M. Lawrie, M.C. Morris, P. Tunnah, G. Divita, et al., Effects of phosphorylation of threonine 160 on cyclin-dependent kinase 2 structure and activity, J. Biol. Chem. 274 (1999) 8746-8756.
    • (1999) J. Biol. Chem. , vol.274 , pp. 8746-8756
    • Brown, N.R.1    Noble, M.E.2    Lawrie, A.M.3    Morris, M.C.4    Tunnah, P.5    Divita, G.6
  • 24
    • 0037189530 scopus 로고    scopus 로고
    • Kinetic mechanism of activation of the Cdk2/cyclin A complex. Key role of the C-lobe of the Cdk
    • M.C. Morris, C. Gondeau, J.A. Tainer, G. Divita, Kinetic mechanism of activation of the Cdk2/cyclin A complex. Key role of the C-lobe of the Cdk, J. Biol. Chem. 277 (2002) 23847-23853.
    • (2002) J. Biol. Chem. , vol.277 , pp. 23847-23853
    • Morris, M.C.1    Gondeau, C.2    Tainer, J.A.3    Divita, G.4
  • 25
    • 0035826154 scopus 로고    scopus 로고
    • Polo-like kinase 1 phosphorylates cyclin B1 and targets it to the nucleus during prophase
    • F. Toyoshima-Morimoto, E. Taniguchi, N. Shinya, A. Iwamatsu, E. Nishida, Polo-like kinase 1 phosphorylates cyclin B1 and targets it to the nucleus during prophase, Nature 410 (2001) 215-220.
    • (2001) Nature , vol.410 , pp. 215-220
    • Toyoshima-Morimoto, F.1    Taniguchi, E.2    Shinya, N.3    Iwamatsu, A.4    Nishida, E.5
  • 26
    • 0034671563 scopus 로고    scopus 로고
    • Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors
    • P.D. Jeffrey, L. Tong, N.P. Pavletich, Structural basis of inhibition of CDK-cyclin complexes by INK4 inhibitors, Genes. Dev. 14 (2000) 3115-3125.
    • (2000) Genes. Dev. , vol.14 , pp. 3115-3125
    • Jeffrey, P.D.1    Tong, L.2    Pavletich, N.P.3
  • 27
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: Positive and negative regulators of G1-phase progression
    • C.J. Sherr, J.M. Roberts, CDK inhibitors: positive and negative regulators of G1-phase progression, Genes. Dev. 13 (1999) 1501-1512.
    • (1999) Genes. Dev. , vol.13 , pp. 1501-1512
    • Sherr, C.J.1    Roberts, J.M.2
  • 28
    • 0035754080 scopus 로고    scopus 로고
    • To cycle or not to cycle: A critical decision in cancer
    • M. Malumbres, M. Barbacid, To cycle or not to cycle: a critical decision in cancer, Nat. Rev. Cancer 1 (2001) 222-231.
    • (2001) Nat. Rev. Cancer , vol.1 , pp. 222-231
    • Malumbres, M.1    Barbacid, M.2
  • 30
    • 0034614637 scopus 로고    scopus 로고
    • The hallmarks of cancer
    • D. Hanahan, R.A. Weinberg, The hallmarks of cancer, Cell 100 (2000) 57-70.
    • (2000) Cell , vol.100 , pp. 57-70
    • Hanahan, D.1    Weinberg, R.A.2
  • 31
    • 0029921317 scopus 로고    scopus 로고
    • Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer
    • M. Hall, G. Peters, Genetic alterations of cyclins, cyclin-dependent kinases, and Cdk inhibitors in human cancer, Adv. Cancer Res. 68 (1996) 67-108.
    • (1996) Adv Cancer Res. , vol.68 , pp. 67-108
    • Hall, M.1    Peters, G.2
  • 32
    • 33745698050 scopus 로고    scopus 로고
    • The prognostic value and overexpression of cyclin A is correlated with gene amplification of both cyclin A and cyclin e in breast cancer patient
    • A. Husdal, G. Bukholm, I.R.K. Bukholm, The prognostic value and overexpression of cyclin A is correlated with gene amplification of both cyclin A and cyclin E in breast cancer patient, Cell Oncol. 28 (2006) 107-116.
    • (2006) Cell Oncol. , vol.28 , pp. 107-116
    • Husdal, A.1    Bukholm, G.2    Bukholm, I.R.K.3
  • 33
    • 84864035808 scopus 로고    scopus 로고
    • Cyclin A and cyclin B1 overexpression in differentiated thyroid carcinoma
    • A. Nar, O. Ozen, N.B. Tutuncu, B. Demirhan, Cyclin A and cyclin B1 overexpression in differentiated thyroid carcinoma, Med. Oncol. 29 (2012) 294-300.
    • (2012) Med. Oncol. , vol.29 , pp. 294-300
    • Nar, A.1    Ozen, O.2    Tutuncu, N.B.3    Demirhan, B.4
  • 35
    • 33645118564 scopus 로고    scopus 로고
    • Cyclin D1: Polymorphism aberrant splicing and cancer risk
    • K.E. Knudsen, J.A. Diehl, C.A. Haiman, E.S. Knudsen, Cyclin D1: polymorphism, aberrant splicing and cancer risk, Oncogene 25 (2006) 1620-1628.
    • (2006) Oncogene , vol.25 , pp. 1620-1628
    • Knudsen, K.E.1    Diehl, J.A.2    Haiman, C.A.3    Knudsen, E.S.4
  • 36
    • 34147103220 scopus 로고    scopus 로고
    • Nuclear cyclin B1 in human breast carcinoma as a potent prognostic factor
    • T. Suzuki, T. Urano, Y. Miki, T. Moriya, J. Akahira, T. Ishida, et al., Nuclear cyclin B1 in human breast carcinoma as a potent prognostic factor, Cancer Sci. 98 (2007) 644-651.
    • (2007) Cancer Sci. , vol.98 , pp. 644-651
    • Suzuki, T.1    Urano, T.2    Miki, Y.3    Moriya, T.4    Akahira, J.5    Ishida, T.6
  • 38
    • 77955081225 scopus 로고    scopus 로고
    • Evaluation of cell cycle protein expression in gastric cancer: Cyclin B1 expression and its prognostic implication
    • M.D. Begnami, J.H.T.G. Fregnani, S. Nonogaki, F.A. Soares, Evaluation of cell cycle protein expression in gastric cancer: cyclin B1 expression and its prognostic implication, Hum. Pathol. 41 (2010) 1120-1127.
    • (2010) Hum. Pathol. , vol.41 , pp. 1120-1127
    • Begnami, M.D.1    Fregnani, J.H.T.G.2    Nonogaki, S.3    Soares, F.A.4
  • 39
    • 0033044020 scopus 로고    scopus 로고
    • Determination of the prognostic significance of cyclin B1 overexpression in patients with esophageal squamous cell carcinoma
    • H. Murakami, M. Furihata, Y. Ohtsuki, S. Ogoshi, Determination of the prognostic significance of cyclin B1 overexpression in patients with esophageal squamous cell carcinoma, Virchows Arch. 434 (1999) 153-158.
    • (1999) Virchows Arch. , vol.434 , pp. 153-158
    • Murakami, H.1    Furihata, M.2    Ohtsuki, Y.3    Ogoshi, S.4
  • 40
    • 0033870724 scopus 로고    scopus 로고
    • Overexpression of cyclin B1 in early-stage non-small cell lung cancer and its clinical implication
    • J.-C. Soria, S.J. Jang, F.R. Khuri, K. Hassan, D. Liu, W.K. Hong, L. Mao, Overexpression of cyclin B1 in early-stage non-small cell lung cancer and its clinical implication, Cancer Res. 60 (2000) 4000-4004.
    • (2000) Cancer Res. , vol.60 , pp. 4000-4004
    • Soria, J.-C.1    Jang, S.J.2    Khuri, F.R.3    Hassan, K.4    Liu, D.5    Hong, W.K.6    Mao, L.7
  • 41
    • 67649352637 scopus 로고    scopus 로고
    • Nuclear cyclin D1: An oncogenic driver in human cancer
    • J.K. Kim, J.A. Diehl, Nuclear cyclin D1: an oncogenic driver in human cancer, J. Cell Physiol. 220 (2009) 292-296.
    • (2009) J. Cell Physiol. , vol.220 , pp. 292-296
    • Kim, J.K.1    Diehl, J.A.2
  • 42
    • 33644755629 scopus 로고    scopus 로고
    • Do truncated cyclins contribute to aberrant cyclin expression in cancer?
    • R. Van Dross, P.J. Browning, J.C. Pelling, Do truncated cyclins contribute to aberrant cyclin expression in cancer? Cell Cycle 5 (2006) 472-477.
    • (2006) Cell Cycle , vol.5 , pp. 472-477
    • Van Dross, R.1    Browning, P.J.2    Pelling, J.C.3
  • 43
    • 22444432945 scopus 로고    scopus 로고
    • Expression of cyclin A1 and cell cycle proteins in hematopoietic cells and acute myeloid leukemia and links to patient outcome
    • J. Ekberg, C. Holm, S. Jalili, J. Richter, L. Anagnostaki, G. Landberg, et al., Expression of cyclin A1 and cell cycle proteins in hematopoietic cells and acute myeloid leukemia and links to patient outcome, Eur. J. Haematol. 75 (2005) 106-115.
    • (2005) Eur. J. Haematol. , vol.75 , pp. 106-115
    • Ekberg, J.1    Holm, C.2    Jalili, S.3    Richter, J.4    Anagnostaki, L.5    Landberg, G.6
  • 44
    • 1842477408 scopus 로고    scopus 로고
    • Activation of cyclindependent kinase 2 by full length and low molecular weight forms of cyclin e in breast cancer cells
    • R.M. Harwell, B.B. Mull, D.C. Porter, K. Keyomarsi, Activation of cyclindependent kinase 2 by full length and low molecular weight forms of cyclin E in breast cancer cells, J. Biol. Chem. 279 (2004) 12695-12705.
    • (2004) J. Biol. Chem. , vol.279 , pp. 12695-12705
    • Harwell, R.M.1    Mull, B.B.2    Porter, D.C.3    Keyomarsi, K.4
  • 45
    • 0032923368 scopus 로고    scopus 로고
    • Cyclin e in human cancers
    • R. Donnellan, R. Chetty, Cyclin E in human cancers, FASEB J. 13 (1999) 773-780.
    • (1999) FASEB J. , vol.13 , pp. 773-780
    • Donnellan, R.1    Chetty, R.2
  • 46
    • 85038646047 scopus 로고    scopus 로고
    • Cyclin E1 deregulation occurs early in secretory cell transformation to promote formation of fallopian tube e derived high-grade serous ovarian cancers
    • A.M. Karst, P.M. Jones, N. Vena, A.H. Ligon, J.F. Liu, M.S. Hirsch, D. Etemadmoghadam, D.D.L. Bowtell, R. Drapkin, Cyclin E1 deregulation occurs early in secretory cell transformation to promote formation of fallopian tube e derived high-grade serous ovarian cancers, Cancer Res. (2013).
    • (2013) Cancer Res.
    • Karst, A.M.1    Jones, P.M.2    Vena, N.3    Ligon, A.H.4    Liu, J.F.5    Hirsch, M.S.6    Etemadmoghadam, D.7    Bowtell, D.D.L.8    Drapkin, R.9
  • 48
    • 67650073265 scopus 로고    scopus 로고
    • Cell cycle kinases as therapeutic targets for cancer
    • S. Lapenna, A. Giordano, Cell cycle kinases as therapeutic targets for cancer, Nat. Rev. Drug Discov. 8 (2009) 547-566.
    • (2009) Nat. Rev. Drug Discov. , vol.8 , pp. 547-566
    • Lapenna, S.1    Giordano, A.2
  • 49
    • 84887622751 scopus 로고    scopus 로고
    • Targeting cyclin-dependent kinases in anti-neoplastic therapy
    • C. Bruyére, L. Meijer, Targeting cyclin-dependent kinases in anti-neoplastic therapy, Curr. Opin. Cell Biol. 25 (2013) 772-779.
    • (2013) Curr. Opin. Cell Biol. , vol.25 , pp. 772-779
    • Bruyére, C.1    Meijer, L.2
  • 51
    • 33645033152 scopus 로고    scopus 로고
    • Stable gene silencing of cyclin B1 in tumor cells increases susceptibility to taxol and leads to growth arrest in vivo
    • J. Yuan, A. Krämer, Y. Matthess, R. Yan, B. Spänkuch, R. Gätje, et al., Stable gene silencing of cyclin B1 in tumor cells increases susceptibility to taxol and leads to growth arrest in vivo, Oncogene 25 (2006) 1753-1762.
    • (2006) Oncogene , vol.25 , pp. 1753-1762
    • Yuan, J.1    Krämer, A.2    Matthess, Y.3    Yan, R.4    Spänkuch, B.5    Gätje, R.6
  • 53
    • 60549107035 scopus 로고    scopus 로고
    • Targeting cyclin B1 inhibits proliferation and sensitizes breast cancer cells to taxol
    • I. Androic, A. Krämer, R. Yan, F. Rödel, R. Gätje, M. Kaufmann, et al., Targeting cyclin B1 inhibits proliferation and sensitizes breast cancer cells to taxol, BMC Cancer 8 (2008) 391.
    • (2008) BMC Cancer , vol.8 , pp. 391
    • Androic, I.1    Krämer, A.2    Yan, R.3    Rödel, F.4    Gätje, R.5    Kaufmann, M.6
  • 55
    • 0032030883 scopus 로고    scopus 로고
    • Overexpression of cyclin A but not Skp 2 correlates with the tumor relapse of human hepatocellular carcinoma
    • Y. Chao, Y.L. Shih, J.H. Chiu, G.Y. Chau, W.Y. Lui, W.K. Yang, S.D. Lee, T.S. Huang, Overexpression of cyclin A but not Skp 2 correlates with the tumor relapse of human hepatocellular carcinoma, Cancer Res. 58 (1998) 985-990.
    • (1998) Cancer Res. , vol.58 , pp. 985-990
    • Chao, Y.1    Shih, Y.L.2    Chiu, J.H.3    Chau, G.Y.4    Lui, W.Y.5    Yang, W.K.6    Lee, S.D.7    Huang, T.S.8
  • 56
    • 0025022001 scopus 로고
    • Hepatitis B virus integration in a cyclin A gene in a hepatocellular carcinoma
    • J. Wang, X. Chenivesse, B. Henglein, C. Brechot, Hepatitis B virus integration in a cyclin A gene in a hepatocellular carcinoma, Nature 343 (1990) 555-557.
    • (1990) Nature , vol.343 , pp. 555-557
    • Wang, J.1    Chenivesse, X.2    Henglein, B.3    Brechot, C.4
  • 58
    • 0037075887 scopus 로고    scopus 로고
    • Cyclin D-dependent kinases, INK4 inhibitors and cancer, Biochim
    • S. Ortega, M. Malumbres, M. Barbacid, Cyclin D-dependent kinases, INK4 inhibitors and cancer, Biochim. Biophys. Acta 1602 (2002) 73-87.
    • (2002) Biophys. Acta , vol.1602 , pp. 73-87
    • Ortega, S.1    Malumbres, M.2    Barbacid, M.3
  • 59
    • 84886438147 scopus 로고    scopus 로고
    • The cell-cycle regulator CDK4: An emerging therapeutic target in melanoma
    • K.E. Sheppard, G.A. McArthur, The cell-cycle regulator CDK4: an emerging therapeutic target in melanoma, Clin. Cancer Res. 19 (2013) 5320-5328.
    • (2013) Clin. Cancer Res. , vol.19 , pp. 5320-5328
    • Sheppard, K.E.1    McArthur, G.A.2
  • 60
    • 33845951110 scopus 로고    scopus 로고
    • Cyclin D1 in non-small cell lung cancer: A key driver of malignant transformation
    • O. Gautschi, D. Ratschiller, M. Gugger, D.C. Betticher, J. Heighway, Cyclin D1 in non-small cell lung cancer: a key driver of malignant transformation, Lung Cancer 55 (2007) 1-14.
    • (2007) Lung Cancer , vol.55 , pp. 1-14
    • Gautschi, O.1    Ratschiller, D.2    Gugger, M.3    Betticher, D.C.4    Heighway, J.5
  • 61
    • 0035803395 scopus 로고    scopus 로고
    • Wide spectrum of tumors in knock-in mice carrying a Cdk4 protein insensitive to INK4 inhibitors
    • R. Sotillo, P. Dubus, J. Martín, E. de la Cueva, S. Ortega, M. Malumbres, et al., Wide spectrum of tumors in knock-in mice carrying a Cdk4 protein insensitive to INK4 inhibitors, EMBO J. 20 (2001) 6637-6647.
    • (2001) EMBO J. , vol.20 , pp. 6637-6647
    • Sotillo, R.1    Dubus, P.2    Martín, J.3    De La Cueva, E.4    Ortega, S.5    Malumbres, M.6
  • 62
    • 18144424779 scopus 로고    scopus 로고
    • Cooperation between Cdk4 and p27kip1 in tumor development: A preclinical model to evaluate cell cycle inhibitors with therapeutic activity
    • R. Sotillo, O. Renner, P. Dubus, J. Ruiz-Cabello, J. Martín-Caballero, M. Barbacid, et al., Cooperation between Cdk4 and p27kip1 in tumor development: a preclinical model to evaluate cell cycle inhibitors with therapeutic activity, Cancer Res. 65 (2005) 3846-3852.
    • (2005) Cancer Res. , vol.65 , pp. 3846-3852
    • Sotillo, R.1    Renner, O.2    Dubus, P.3    Ruiz-Cabello, J.4    Martín-Caballero, J.5    Barbacid, M.6
  • 64
    • 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
    • M. Puyol, A. Martín, P. Dubus, F. Mulero, P. Pizcueta, G. Khan, et al., A synthetic lethal interaction between K-Ras oncogenes and Cdk4 unveils a therapeutic strategy for non-small cell lung carcinoma, Cancer Cell 18 (2010) 63-73.
    • (2010) Cancer Cell , vol.18 , pp. 63-73
    • Puyol, M.1    Martín, A.2    Dubus, P.3    Mulero, F.4    Pizcueta, P.5    Khan, G.6
  • 65
    • 84859017982 scopus 로고    scopus 로고
    • A defect of the INK4-Cdk4 checkpoint and Myc collaborate in blastoid mantle cell lymphoma-like lymphoma formation in mice
    • C. Vincent-Fabert, R. Fiancette, P. Rouaud, C. Baudet, V. Truffinet, V. Magnone, et al., A defect of the INK4-Cdk4 checkpoint and Myc collaborate in blastoid mantle cell lymphoma-like lymphoma formation in mice, Am. J. Pathol. 180 (2012) 1688-1701.
    • (2012) Am. J. Pathol. , vol.180 , pp. 1688-1701
    • Vincent-Fabert, C.1    Fiancette, R.2    Rouaud, P.3    Baudet, C.4    Truffinet, V.5    Magnone, V.6
  • 66
    • 2442657980 scopus 로고    scopus 로고
    • Overexpression of cdk4/cyclin D1, a possible mediator of apoptosis and an indicator of prognosis in human primary lung carcinoma
    • Y. Dobashi, A. Goto, M. Fukayama, A. Abe, A. Ooi, Overexpression of cdk4/cyclin D1, a possible mediator of apoptosis and an indicator of prognosis in human primary lung carcinoma, Int. J. Cancer 110 (2004) 532-541.
    • (2004) Int J. Cancer , vol.110 , pp. 532-541
    • Dobashi, Y.1    Goto, A.2    Fukayama, M.3    Abe, A.4    Ooi, A.5
  • 67
    • 79952632471 scopus 로고    scopus 로고
    • Expression analysis and molecular targeting of cyclin-dependent kinases in advanced melanoma
    • C. Abdullah, X. Wang, D. Becker, Expression analysis and molecular targeting of cyclin-dependent kinases in advanced melanoma, Cell Cycle 10 (2011) 977-988.
    • (2011) Cell Cycle , vol.10 , pp. 977-988
    • Abdullah, C.1    Wang, X.2    Becker, D.3
  • 70
    • 82755189259 scopus 로고    scopus 로고
    • A p53 defect sensitizes various stages of B cell development to lymphomagenesis in mice carrying an IgH 30 regulatory region-driven c-myc transgene
    • R. Fiancette, P. Rouaud, C. Vincent-Fabert, B. Laffleur, V. Magnone, M. Cogné, et al., A p53 defect sensitizes various stages of B cell development to lymphomagenesis in mice carrying an IgH 30 regulatory region-driven c-myc transgene, J. Immunol. 187 (2011) 5772-5782.
    • (2011) J. Immunol. , vol.187 , pp. 5772-5782
    • Fiancette, R.1    Rouaud, P.2    Vincent-Fabert, C.3    Laffleur, B.4    Magnone, V.5    Cogné, M.6
  • 71
    • 0028652269 scopus 로고
    • CDKN2 (p16/MTS1) gene deletion or CDK4 amplification occurs in the majority of glioblastomas
    • E.E. Schmidt, K. Ichimura, G. Reifenberger, V.P. Collins, CDKN2 (p16/MTS1) gene deletion or CDK4 amplification occurs in the majority of glioblastomas, Cancer Res. 54 (1994) 6321-6324.
    • (1994) Cancer Res. , vol.54 , pp. 6321-6324
    • Schmidt, E.E.1    Ichimura, K.2    Reifenberger, G.3    Collins, V.P.4
  • 72
    • 0032919173 scopus 로고    scopus 로고
    • Gene amplification and overexpression of CDK4 in sporadic breast carcinomas is associated with high tumor cell proliferation
    • H.X. An, M.W. Beckmann, G. Reifenberger, H.G. Bender, D. Niederacher, Gene amplification and overexpression of CDK4 in sporadic breast carcinomas is associated with high tumor cell proliferation, Am. J. Pathol. 154 (1999) 113-118.
    • (1999) Am. J. Pathol. , vol.154 , pp. 113-118
    • An, H.X.1    Beckmann, M.W.2    Reifenberger, G.3    Bender, H.G.4    Niederacher, D.5
  • 74
    • 0033579870 scopus 로고    scopus 로고
    • CDK4 gene amplification in osteosarcoma: Reciprocal relationship with INK4A gene alterations and mapping of 12q13 amplicons
    • G. Wei, F. Lonardo, T. Ueda, T. Kim, A.G. Huvos, J.H. Healey, M. Ladanyi, CDK4 gene amplification in osteosarcoma: reciprocal relationship with INK4A gene alterations and mapping of 12q13 amplicons, Int. J. Cancer 80 (1999) 199-204.
    • (1999) Int. J. Cancer , vol.80 , pp. 199-204
    • Wei, G.1    Lonardo, F.2    Ueda, T.3    Kim, T.4    Huvos, A.G.5    Healey, J.H.6    Ladanyi, M.7
  • 75
    • 0033590604 scopus 로고    scopus 로고
    • Co-amplification and overexpression of CDK4 SAS and MDM2 occurs frequently in human parosteal osteosarcomas
    • J.S. Wunder, K. Eppert, S.R. Burrow, N. Gokgoz, R.S. Bell, I.L. Andrulis, N. Gogkoz, Co-amplification and overexpression of CDK4, SAS and MDM2 occurs frequently in human parosteal osteosarcomas, Oncogene 18 (1999) 783-788.
    • (1999) Oncogene , vol.18 , pp. 783-788
    • Wunder, J.S.1    Eppert, K.2    Burrow, S.R.3    Gokgoz, N.4    Bell, R.S.5    Andrulis, I.L.6    Gogkoz, N.7
  • 77
    • 0030982897 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 6 (CDK6) amplification in human gliomas identified using two-dimensional separation of genomic DNA
    • J.F. Costello, C. Plass, W. Arap, V.M. Chapman, W.A. Held, M.S. Berger, H.J.S. Huang, W.K. Cavenee, Cyclin-dependent kinase 6 (CDK6) amplification in human gliomas identified using two-dimensional separation of genomic DNA, Cancer Res. 57 (1997) 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    Huang, H.J.S.7    Cavenee, W.K.8
  • 78
    • 0028828550 scopus 로고
    • Cortical and brainstem-type Lewy bodies are immunoreactive for the cyclin-dependent kinase 5
    • J.P. Brion, A.M. Couck, Cortical and brainstem-type Lewy bodies are immunoreactive for the cyclin-dependent kinase 5, Am. J. Pathol. 147 (1995) 1465-1476.
    • (1995) Am. J. Pathol. , vol.147 , pp. 1465-1476
    • Brion, J.P.1    Couck, A.M.2
  • 79
    • 0030749732 scopus 로고    scopus 로고
    • P35nck5a and cyclin-dependent kinase 5 colocalize in Lewy bodies of brains with Parkinson's disease
    • S. Nakamura, Y. Kawamoto, S. Nakano, I. Akiguchi, J. Kimura, p35nck5a and cyclin-dependent kinase 5 colocalize in Lewy bodies of brains with Parkinson's disease, Acta Neuropathol. 94 (1997) 153-157.
    • (1997) Acta Neuropathol. , vol.94 , pp. 153-157
    • Nakamura, S.1    Kawamoto, Y.2    Nakano, S.3    Akiguchi, I.4    Kimura, J.5
  • 80
    • 0027421625 scopus 로고
    • Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments
    • H.K. Paudel, J. Lew, Z. Ali, J.H. Wang, Brain proline-directed protein kinase phosphorylates tau on sites that are abnormally phosphorylated in tau associated with Alzheimer's paired helical filaments, J. Biol. Chem. 268 (1993) 23512-23518.
    • (1993) J. Biol. Chem. , vol.268 , pp. 23512-23518
    • Paudel, H.K.1    Lew, J.2    Ali, Z.3    Wang, J.H.4
  • 81
    • 80053542961 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 5 is amplified and overexpressed in pancreatic cancer and activated by mutant K-Ras
    • J.P. Eggers, P.M. Grandgenett, E.C. Collisson, M.E. Lewallen, J. Tremayne, P.K. Singh, et al., Cyclin-dependent kinase 5 is amplified and overexpressed in pancreatic cancer and activated by mutant K-Ras, Clin. Cancer Res. 17 (2011) 6140-6150.
    • (2011) Clin. Cancer Res. , vol.17 , pp. 6140-6150
    • Eggers, J.P.1    Grandgenett, P.M.2    Collisson, E.C.3    Lewallen, M.E.4    Tremayne, J.5    Singh, P.K.6
  • 82
    • 84857781607 scopus 로고    scopus 로고
    • Cdk5: A multifaceted kinase in neurodegenerative diseases
    • Z.H. Cheung, N.Y. Ip, Cdk5: a multifaceted kinase in neurodegenerative diseases, Trends Cell Biol. 22 (2012) 169-175.
    • (2012) Trends Cell Biol. , vol.22 , pp. 169-175
    • Cheung, Z.H.1    Ip, N.Y.2
  • 83
    • 84869486602 scopus 로고    scopus 로고
    • Level of Cdk5 expression predicts the survival of relapsed multiple myeloma patients
    • Z. Levaque, J.L. Rosales, K.Y. Lee, Level of Cdk5 expression predicts the survival of relapsed multiple myeloma patients, Cell Cycle 11 (2012) 4093-4095.
    • (2012) Cell Cycle , vol.11 , pp. 4093-4095
    • Levaque, Z.1    Rosales, J.L.2    Lee, K.Y.3
  • 84
    • 84905679294 scopus 로고    scopus 로고
    • Cdk5 is essential for TGF-b1-indiced epithelial-mesenchymal transition and breast cancer progression
    • Q. Liang, et al., Cdk5 is essential for TGF-b1-indiced epithelial-mesenchymal transition and breast cancer progression, Sci. Rep. 3 (2013) 1-12.
    • (2013) Sci. Rep. , vol.3 , pp. 1-12
    • Liang, Q.1
  • 85
    • 84872515516 scopus 로고    scopus 로고
    • Kinase drug discoveryewhat's next in the field? ACS Chem
    • P. Cohen, D.R. Alessi, Kinase drug discoveryewhat's next in the field? ACS Chem. Biol. 8 (2013) 96-104.
    • (2013) Biol. , vol.8 , pp. 96-104
    • Cohen, P.1    Alessi, D.R.2
  • 86
    • 84874930946 scopus 로고    scopus 로고
    • Introduction for the special issue on kinase inhibitors
    • H. Galons, Introduction for the special issue on kinase inhibitors, Eur. J. Med. Chem. 61 (2013) 1.
    • (2013) Eur. J. Med. Chem. , vol.61 , pp. 1
    • Galons, H.1
  • 88
    • 0033760789 scopus 로고    scopus 로고
    • Inhibitors of cyclin-dependent kinases as anti-cancer therapeutics
    • P.M. Fischer, D.P. Lane, Inhibitors of cyclin-dependent kinases as anti-cancer therapeutics, Curr. Med. Chem. 7 (2000) 1213-1245.
    • (2000) Curr. Med. Chem. , vol.7 , pp. 1213-1245
    • Fischer, P.M.1    Lane, D.P.2
  • 89
    • 0034162636 scopus 로고    scopus 로고
    • Preclinical and clinical development of cyclin-dependent kinase modulators
    • A.M. Senderowicz, E.A. Sausville, Preclinical and clinical development of cyclin-dependent kinase modulators, J. Natl. Cancer Inst. 92 (2000) 376-387.
    • (2000) J. Natl. Cancer Inst. , vol.92 , pp. 376-387
    • Senderowicz, A.M.1    Sausville, E.A.2
  • 90
  • 92
    • 0038245253 scopus 로고    scopus 로고
    • Small molecules as inhibitors of cyclindependent kinases
    • A. Huwe, R. Mazitschek, A. Giannis, Small molecules as inhibitors of cyclindependent kinases, Angew. Chem. Int. Ed. Engl. 42 (2003) 2122-2138.
    • (2003) Angew. Chem. Int. Ed. Engl. , vol.42 , pp. 2122-2138
    • Huwe, A.1    Mazitschek, R.2    Giannis, A.3
  • 93
    • 0038052805 scopus 로고    scopus 로고
    • The cell cycle: A review of regulation, deregulation and therapeutic targets in cancer
    • K. Vermeulen, D.R. Van Bockstaele, Z.N. Berneman, The cell cycle: a review of regulation, deregulation and therapeutic targets in cancer, Cell Prolif. 36 (2003) 131-149.
    • (2003) Cell Prolif. , vol.36 , pp. 131-149
    • Vermeulen, K.1    Van Bockstaele, D.R.2    Berneman, Z.N.3
  • 94
    • 13244268318 scopus 로고    scopus 로고
    • Clinical anticancer drug development: Targeting the cyclin-dependent kinases
    • C. Benson, S. Kaye, P. Workman, M. Garrett, M. Walton, J. de Bono, Clinical anticancer drug development: targeting the cyclin-dependent kinases, Br. J. Cancer 92 (2005) 7-12.
    • (2005) Br. J. Cancer , vol.92 , pp. 7-12
    • Benson, C.1    Kaye, S.2    Workman, P.3    Garrett, M.4    Walton, M.5    De Bono, J.6
  • 95
    • 33645802169 scopus 로고    scopus 로고
    • Cyclin-dependent kinase pathways as targets for cancer treatment
    • G.I. Shapiro, Cyclin-dependent kinase pathways as targets for cancer treatment, J. Clin. Oncol. 24 (2006) 1770-1783.
    • (2006) J. Clin. Oncol. , vol.24 , pp. 1770-1783
    • Shapiro, G.I.1
  • 96
    • 0033957960 scopus 로고    scopus 로고
    • Targeting hyperproliferative disorders with cyclin dependent kinase inhibitors
    • G.R. Rosania, Y.-T. Chang, Targeting hyperproliferative disorders with cyclin dependent kinase inhibitors, Expert Opin. Ther. Pat. 10 (2000) 215-230.
    • (2000) Expert Opin. Ther. Pat. , vol.10 , pp. 215-230
    • Rosania, G.R.1    Chang, Y.-T.2
  • 97
    • 67650777303 scopus 로고    scopus 로고
    • Development of cell-cycle inhibitors for cancer therapy
    • M.A. Dickson, G.K. Schwartz, Development of cell-cycle inhibitors for cancer therapy, Curr. Oncol. 16 (2009) 36-43.
    • (2009) Curr. Oncol. , vol.16 , pp. 36-43
    • Dickson, M.A.1    Schwartz, G.K.2
  • 98
    • 80054752304 scopus 로고    scopus 로고
    • The CDK inhibitors in cancer research and therapy
    • J. Cicenas, M. Valius, The CDK inhibitors in cancer research and therapy, J. Cancer Res. Clin. Oncol. 137 (2011) 1409-1418.
    • (2011) J. Cancer Res. Clin. Oncol. , vol.137 , pp. 1409-1418
    • Cicenas, J.1    Valius, M.2
  • 99
    • 79959954585 scopus 로고    scopus 로고
    • Peptides or small molecules? Different approaches to develop more effective CDK inhibitors
    • D. Cirillo, F. Pentimalli, A. Giordano, Peptides or small molecules? Different approaches to develop more effective CDK inhibitors, Curr. Med. Chem. 18 (2011) 2854-2866.
    • (2011) Curr. Med. Chem. , vol.18 , pp. 2854-2866
    • Cirillo, D.1    Pentimalli, F.2    Giordano, A.3
  • 102
    • 0036488643 scopus 로고    scopus 로고
    • Natural products in cancer chemotherapy: Past, present and future
    • J. Mann, Natural products in cancer chemotherapy: past, present and future, Nat. Rev. Cancer 2 (2002) 143-148.
    • (2002) Nat Rev. Cancer , vol.2 , pp. 143-148
    • Mann, J.1
  • 105
    • 0027948283 scopus 로고
    • Olomoucine, an inhibitor of the cdc2/cdk2 kinases activity, blocks plant cells at the G1 to S and G2 to M cell cycle transitions
    • N. Glab, B. Labidi, L. X Qin, C. Trehin, C. Bergounioux, L. Meijer, Olomoucine, an inhibitor of the cdc2/cdk2 kinases activity, blocks plant cells at the G1 to S and G2 to M cell cycle transitions, FEBS Lett. 353 (1994) 207-211.
    • (1994) FEBS Lett. , vol.353 , pp. 207-211
    • Glab, N.1    Labidi, B.2    Qin, L.X.3    Trehin, C.4    Bergounioux, C.5    Meijer, L.6
  • 108
    • 0033128165 scopus 로고    scopus 로고
    • Indirubin, the active constituent of a Chinese antileukaemia medicine, inhibits cyclin-dependent kinases
    • R. Hoessel, S. Leclerc, J.A. Endicott, M.E. Nobel, A. Lawrie, P. Tunnah, et al., Indirubin, the active constituent of a Chinese antileukaemia medicine, inhibits cyclin-dependent kinases, Nat. Cell Biol. 1 (1999) 60-67.
    • (1999) Nat Cell Biol. , vol.1 , pp. 60-67
    • Hoessel, R.1    Leclerc, S.2    Endicott, J.A.3    Nobel, M.E.4    Lawrie, A.5    Tunnah, P.6
  • 109
    • 0034721195 scopus 로고    scopus 로고
    • Identification of novel purine and pyrimidine cyclindependent kinase inhibitors with distinct molecular interactions and tumor cell growth inhibition profiles
    • C.E. Arris, F.T. Boyle, A.H. Calvert, N.J. Curtin, J.A. Endicott, E.F. Garman, A.E. Gibson, et al., Identification of novel purine and pyrimidine cyclindependent kinase inhibitors with distinct molecular interactions and tumor cell growth inhibition profiles, J. Med. Chem. 43 (2000) 2797-2804.
    • (2000) J. Med. Chem. , vol.43 , pp. 2797-2804
    • Arris, C.E.1    Boyle, F.T.2    Calvert, A.H.3    Curtin, N.J.4    Endicott, J.A.5    Garman, E.F.6    Gibson, A.E.7
  • 110
    • 0032563315 scopus 로고    scopus 로고
    • Exploiting chemical libraries structure, and genomics in the search for kinase inhibitors
    • N.S. Gray, L. Wodicka, A.M. Thunnissen, T.C. Norman, S. Kwon, F.H. Espinoza, et al., Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors, Science 281 (1998) 533-538.
    • (1998) Science , vol.281 , pp. 533-538
    • Gray, N.S.1    Wodicka, L.2    Thunnissen, A.M.3    Norman, T.C.4    Kwon, S.5    Espinoza, F.H.6
  • 111
    • 33846676987 scopus 로고    scopus 로고
    • Chemical genetics: Where genetics and pharmacology meet
    • Z.A. Knight, K.M. Shokat, Chemical genetics: where genetics and pharmacology meet, Cell 128 (2007) 425-430.
    • (2007) Cell , vol.128 , pp. 425-430
    • Knight, Z.A.1    Shokat, K.M.2
  • 113
    • 84884622576 scopus 로고    scopus 로고
    • Structure-guided inhibitor design expands the scope of analog-sensitive kinase technology
    • C. Zhang, M.S. Lopez, A.C. Dar, E. Ladow, S. Finkbeiner, C.-H. Yun, et al., Structure-guided inhibitor design expands the scope of analog-sensitive kinase technology, ACS Chem. Biol. 8 (2013) 1931-1938.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 1931-1938
    • Zhang, C.1    Lopez, M.S.2    Dar, A.C.3    Ladow, E.4    Finkbeiner, S.5    Yun, C.-H.6
  • 114
    • 84903843882 scopus 로고    scopus 로고
    • Molecular pathways: CDK4 inhibitors for Cancer therapy
    • M.A. Dickson, Molecular pathways: CDK4 inhibitors for Cancer therapy, Clin. Cancer Res. 20 (2014) 3379-3383.
    • (2014) Clin. Cancer Res. , vol.20 , pp. 3379-3383
    • Dickson, M.A.1
  • 115
    • 0031028163 scopus 로고    scopus 로고
    • Inhibition of cyclin-dependent kinases by purine analogues: Crystal structure of human cdk2 complexed with roscovitine
    • W.F. De Azevedo, S. Leclerc, L. Meijer, L. Havlicek, M. Strnad, S.H. Kim, Inhibition of cyclin-dependent kinases by purine analogues: crystal structure of human cdk2 complexed with roscovitine, Eur. J. Biochem. 243 (1997) 518-526.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 518-526
    • De Azevedo, W.F.1    Leclerc, S.2    Meijer, L.3    Havlicek, L.4    Strnad, M.5    Kim, S.H.6
  • 116
    • 0033150476 scopus 로고    scopus 로고
    • Synthesis and application of functionally diverse 2,6,9-trisubstituted purine libraries as CDK inhibitors
    • Y.T. Chang, N.S. Gray, G.R. Rosania, D.P. Sutherlin, S. Kwon, T.C. Norman, et al., Synthesis and application of functionally diverse 2,6,9-trisubstituted purine libraries as CDK inhibitors, Chem. Biol. 6 (1999) 361-375.
    • (1999) Chem. Biol. , vol.6 , pp. 361-375
    • Chang, Y.T.1    Gray, N.S.2    Rosania, G.R.3    Sutherlin, D.P.4    Kwon, S.5    Norman, T.C.6
  • 118
    • 84871004657 scopus 로고    scopus 로고
    • Potent inhibitors of CDK5 derived from roscovitine: Synthesis, biological evaluation and molecular modelling
    • L. Demange, F.N. Abdellah, O. Lozach, Y. Ferandin, N. Gresh, L. Meijer, et al., Potent inhibitors of CDK5 derived from roscovitine: synthesis, biological evaluation and molecular modelling, Bioorg. Med. Chem. Lett. 23 (2013) 125-131.
    • (2013) Bioorg. Med. Chem. Lett. , vol.23 , pp. 125-131
    • Demange, L.1    Abdellah, F.N.2    Lozach, O.3    Ferandin, Y.4    Gresh, N.5    Meijer, L.6
  • 119
    • 53249149292 scopus 로고    scopus 로고
    • CR8, a potent and selective, roscovitine-derived inhibitor of cyclindependent kinases
    • K. Bettayeb, N. Oumata, A. Echalier, Y. Ferandin, J.A. Endicott, H. Galons, et al., CR8, a potent and selective, roscovitine-derived inhibitor of cyclindependent kinases, Oncogene 27 (2008) 5797-5807.
    • (2008) Oncogene , vol.27 , pp. 5797-5807
    • Bettayeb, K.1    Oumata, N.2    Echalier, A.3    Ferandin, Y.4    Endicott, J.A.5    Galons, H.6
  • 120
    • 0032212885 scopus 로고    scopus 로고
    • Flavopiridol, a novel cyclin-dependent kinase inhibitor, suppresses the growth of head and neck squamous cell carcinomas by inducing apoptosis
    • V. Patel, A.M. Senderowicz, D. Pinto, T. Igishi, M. Raffeld, L. Quintanilla- Martinez, et al., Flavopiridol, a novel cyclin-dependent kinase inhibitor, suppresses the growth of head and neck squamous cell carcinomas by inducing apoptosis, J. Clin. Invest 102 (1998) 1674-1681.
    • (1998) J Clin. Invest , vol.102 , pp. 1674-1681
    • Patel, V.1    Senderowicz, A.M.2    Pinto, D.3    Igishi, T.4    Raffeld, M.5    Quintanilla- Martinez, L.6
  • 121
    • 0040932434 scopus 로고    scopus 로고
    • The novel cyclin-dependent kinase inhibitor flavopiridol downregulates Bcl-2 and induces growth arrest and apoptosis in chronic b-cell leukemia lines
    • A. König, G. K Schwartz, R. M Mohammad, A. Al-Katib, J. L Gabrilove, The novel cyclin-dependent kinase inhibitor flavopiridol downregulates Bcl-2 and induces growth arrest and apoptosis in chronic b-cell leukemia lines, Blood 90 (1997) 4307-4312.
    • (1997) Blood , vol.90 , pp. 4307-4312
    • König, A.1    Schwartz, G.K.2    Mohammad, R.M.3    Al-Katib, A.4    Gabrilove, J.L.5
  • 122
    • 73349096649 scopus 로고    scopus 로고
    • Phase II study of flavopiridol in relapsed chronic lymphocytic leukemia demonstrating high response rates in genetically high-risk disease
    • T.S. Lin, A.S. Ruppert, A.J. Johnson, B. Fischer, N.A. Heerema, L.A. Andritsos, et al., Phase II study of flavopiridol in relapsed chronic lymphocytic leukemia demonstrating high response rates in genetically high-risk disease, J. Clin. Oncol. 27 (2009) 6012-6018.
    • (2009) J. Clin. Oncol. , vol.27 , pp. 6012-6018
    • Lin, T.S.1    Ruppert, A.S.2    Johnson, A.J.3    Fischer, B.4    Heerema, N.A.5    Andritsos, L.A.6
  • 123
    • 34848818485 scopus 로고    scopus 로고
    • Flavopiridol in the treatment of chronic lymphocytic leukemia
    • B.A. Christian, M.R. Grever, J.C. Byrd, T.S. Lin, Flavopiridol in the treatment of chronic lymphocytic leukemia, Curr. Opin. Oncol. 19 (2007) 573-578.
    • (2007) Curr. Opin. Oncol. , vol.19 , pp. 573-578
    • Christian, B.A.1    Grever, M.R.2    Byrd, J.C.3    Lin, T.S.4
  • 124
    • 50249083873 scopus 로고    scopus 로고
    • Identification of N-(4-piperidinyl)-4-(2,6- dichlorobenzoylamino)-1H-pyrazole-3-carboxamide (AT7519), a novel cyclin dependent kinase inhibitor using fragment-based X-Ray crystallography and structure based drug design
    • P.G. Wyatt, A.J. Woodhead, V. Berdini, J.A. Boulstridge, G.G. Carr, D.M. Cross, D.J. Davis, et al., Identification of N-(4-piperidinyl)-4-(2,6- dichlorobenzoylamino)-1H-pyrazole-3-carboxamide (AT7519), a novel cyclin dependent kinase inhibitor using fragment-based X-Ray crystallography and structure based drug design, J. Med. Chem. 51 (2008) 4986-4999.
    • (2008) J. Med. Chem. , vol.51 , pp. 4986-4999
    • Wyatt, P.G.1    Woodhead, A.J.2    Berdini, V.3    Boulstridge, J.A.4    Carr, G.G.5    Cross, D.M.6    Davis, D.J.7
  • 125
    • 60849123760 scopus 로고    scopus 로고
    • Biological characterization of AT7519, a small-molecule inhibitor of cyclindependent kinases, in human tumor cell lines
    • M.S. Squires, R.E. Feltell, N.G. Wallis, E.J. Lewis, D.-M. Smith, D.M. Cross, et al., Biological characterization of AT7519, a small-molecule inhibitor of cyclindependent kinases, in human tumor cell lines, Mol. Cancer Ther. 8 (2009) 324-332.
    • (2009) Mol Cancer Ther. , vol.8 , pp. 324-332
    • Squires, M.S.1    Feltell, R.E.2    Wallis, N.G.3    Lewis, E.J.4    Smith, D.-M.5    Cross, D.M.6
  • 126
    • 77950825064 scopus 로고    scopus 로고
    • AT7519, a cyclin-dependent kinase inhibitor, exerts its effects by transcriptional inhibition in leukemia cell lines and patient samples
    • M.S. Squires, L. Cooke, V. Lock, W. Qi, E.J. Lewis, N.T. Thompson, J.F. Lyons, D. Mahadevan, AT7519, a cyclin-dependent kinase inhibitor, exerts its effects by transcriptional inhibition in leukemia cell lines and patient samples, Mol. Cancer Ther. 9 (2010) 920-928.
    • (2010) Mol Cancer Ther. , vol.9 , pp. 920-928
    • Squires, M.S.1    Cooke, L.2    Lock, V.3    Qi, W.4    Lewis, E.J.5    Thompson, N.T.6    Lyons, J.F.7    Mahadevan, D.8
  • 129
    • 77955495152 scopus 로고    scopus 로고
    • Discovery of dinaciclib (SCH 727965): A potent and selective inhibitor of cyclindependent kinases
    • K. Paruch, M.P. Dwyer, C. Alvarez, C. Brown, T.-Y. Chan, R.J. Doll, et al., Discovery of dinaciclib (SCH 727965): a potent and selective inhibitor of cyclindependent kinases, ACS Med. Chem. Lett. 1 (2010) 204-208.
    • (2010) ACS Med. Chem. Lett. , vol.1 , pp. 204-208
    • Paruch, K.1    Dwyer, M.P.2    Alvarez, C.3    Brown, C.4    Chan, T.-Y.5    Doll, R.J.6
  • 131
    • 80053398390 scopus 로고    scopus 로고
    • Cyclin-dependent kinase inhibitor Dinaciclib (SCH727965) inhibits pancreatic cancer growth and progression in murine xenograft models
    • G. Feldmann, A. Mishra, S. Bisht, C. Karikari, I. Garrido-Laguna, Z. Rasheed, et al., Cyclin-dependent kinase inhibitor Dinaciclib (SCH727965) inhibits pancreatic cancer growth and progression in murine xenograft models, Cancer Biol. Ther. 12 (2011) 598-609.
    • (2011) Cancer Biol. Ther. , vol.12 , pp. 598-609
    • Feldmann, G.1    Mishra, A.2    Bisht, S.3    Karikari, C.4    Garrido-Laguna, I.5    Rasheed, Z.6
  • 134
    • 84862877673 scopus 로고    scopus 로고
    • P16-Cdk4-Rb axis controls sensitivity to a cyclin-dependent kinase inhibitor PD0332991 in glioblastoma xenograft cells
    • L. Cen, B.L. Carlson, M.A. Schroeder, J.L. Ostrem, G.J. Kitange, A.C. Mladek, S.R. Fink, et al., p16-Cdk4-Rb axis controls sensitivity to a cyclin-dependent kinase inhibitor PD0332991 in glioblastoma xenograft cells, Neuro Oncol. 14 (2012) 870-881.
    • (2012) Neuro Oncol. , vol.14 , pp. 870-881
    • Cen, L.1    Carlson, B.L.2    Schroeder, M.A.3    Ostrem, J.L.4    Kitange, G.J.5    Mladek, A.C.6    Fink, S.R.7
  • 135
    • 84878102554 scopus 로고    scopus 로고
    • Blockbuster dreams for Pfizer's CDK inhibitor
    • M. Guha, Blockbuster dreams for Pfizer's CDK inhibitor, Nat. Biotechnol. 31 (2013) 187.
    • (2013) Nat. Biotechnol. , vol.31 , pp. 187
    • Guha, M.1
  • 136
    • 84872511666 scopus 로고    scopus 로고
    • Strategies for the selective regulation of kinases with allosteric modulators: Exploiting exclusive structural features
    • Z. Fang, C. Grütter, D. Rauh, Strategies for the selective regulation of kinases with allosteric modulators: exploiting exclusive structural features, ACS Chem. Biol. 8 (2013) 58-70.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 58-70
    • Fang, Z.1    Grütter, C.2    Rauh, D.3
  • 137
    • 14644420930 scopus 로고    scopus 로고
    • Interfacial inhibition of macromolecular interactions: Nature's paradigm for drug discovery
    • Y. Pommier, J. Cherfils, Interfacial inhibition of macromolecular interactions: nature's paradigm for drug discovery, Trends Pharmacol. Sci. 26 (2005) 138-145.
    • (2005) Trends Pharmacol. Sci. , vol.26 , pp. 138-145
    • Pommier, Y.1    Cherfils, J.2
  • 138
    • 33745298429 scopus 로고    scopus 로고
    • Rational design of inhibitors that bind to inactive kinase conformations
    • Y. Liu, N.S. Gray, Rational design of inhibitors that bind to inactive kinase conformations, Nat. Chem. Biol. 2 (2006) 358-364.
    • (2006) Nat. Chem. Biol. , vol.2 , pp. 358-364
    • Liu, Y.1    Gray, N.S.2
  • 140
    • 3142781225 scopus 로고    scopus 로고
    • Small-molecule inhibitors of protein-protein interactions: Progressing towards the dream
    • M.R. Arkin, J.A. Wells, Small-molecule inhibitors of protein-protein interactions: progressing towards the dream, Nat. Rev. Drug Discov. 3 (2004) 301-317.
    • (2004) Nat. Rev. Drug Discov. , vol.3 , pp. 301-317
    • Arkin, M.R.1    Wells, J.A.2
  • 143
    • 79960990847 scopus 로고    scopus 로고
    • Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I)
    • X. Morelli, R. Bourgeas, P. Roche, Chemical and structural lessons from recent successes in protein-protein interaction inhibition (2P2I), Curr. Opin. Chem. Biol. 15 (2011) 475-481.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 475-481
    • Morelli, X.1    Bourgeas, R.2    Roche, P.3
  • 144
    • 29144523190 scopus 로고    scopus 로고
    • Peptide inhibitors of protein kinases-discovery, characterisation and use
    • M.A. Bogoyevitch, R.K. Barr, A.J. Ketterman, Peptide inhibitors of protein kinases-discovery, characterisation and use, Biochim. Biophys. Acta 1754 (2005) 79-99.
    • (2005) Biochim Biophys. Acta , vol.1754 , pp. 79-99
    • Bogoyevitch, M.A.1    Barr, R.K.2    Ketterman, A.J.3
  • 146
    • 0037374549 scopus 로고    scopus 로고
    • Selective cyclin-dependent kinase 2/cyclin A antagonists that differ from ATP site inhibitors block tumor growth
    • N. Mendoza, S. Fong, J. Marsters, H. Koeppen, R. Schwall, D. Wickramasinghe, Selective cyclin-dependent kinase 2/cyclin A antagonists that differ from ATP site inhibitors block tumor growth, Cancer Res. 63 (2003) 1020-1024.
    • (2003) Cancer Res. , vol.63 , pp. 1020-1024
    • Mendoza, N.1    Fong, S.2    Marsters, J.3    Koeppen, H.4    Schwall, R.5    Wickramasinghe, D.6
  • 148
    • 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
    • N. Canela, M. Orzáez, R. Fucho, F. Mateo, R. Gutierrez, A. Pineda-Lucena, 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. 281 (2006) 35942-35953.
    • (2006) J. Biol. Chem. , vol.281 , pp. 35942-35953
    • Canela, N.1    Orzáez, M.2    Fucho, R.3    Mateo, F.4    Gutierrez, R.5    Pineda-Lucena, A.6
  • 149
    • 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
    • L. Bagella, A. Sun, T. Tonini, G. Abbadessa, G. Cottone, M.G. Paggi, 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 26 (2007) 1829-1839.
    • (2007) Oncogene , vol.26 , pp. 1829-1839
    • Bagella, L.1    Sun, A.2    Tonini, T.3    Abbadessa, G.4    Cottone, G.5    Paggi, M.G.6
  • 150
    • 36849053959 scopus 로고    scopus 로고
    • Interaction between the Cdk2/cyclin A complex and a small molecule derived from the pRb2/p130 spacer domain: A theoretical model
    • A. Giordano, E. Bellacchio, L. Bagella, M.G. Paggi, Interaction between the Cdk2/cyclin A complex and a small molecule derived from the pRb2/p130 spacer domain: a theoretical model, Cell Cycle 6 (2007) 2591-2593.
    • (2007) Cell Cycle , vol.6 , pp. 2591-2593
    • Giordano, A.1    Bellacchio, E.2    Bagella, L.3    Paggi, M.G.4
  • 151
    • 79958254609 scopus 로고    scopus 로고
    • Selective anticancer activity of a hexapeptide with sequence homology to a non-kinase domain of cyclin dependent kinase 4
    • H.M. Warenius, J.D. Kilburn, J.W. Essex, R.I. Maurer, J.P. Blaydes, U. Agarwala, et al., Selective anticancer activity of a hexapeptide with sequence homology to a non-kinase domain of cyclin dependent kinase 4, Mol. Cancer 10 (2011) 72.
    • (2011) Mol. Cancer , vol.10 , pp. 72
    • Warenius, H.M.1    Kilburn, J.D.2    Essex, J.W.3    Maurer, R.I.4    Blaydes, J.P.5    Agarwala, U.6
  • 152
    • 0033548711 scopus 로고    scopus 로고
    • Identification and structure characterization of a Cdk inhibitory peptide derived from neuronal-specific Cdk5 activator
    • K.T. Chin, S.Y. Ohki, D. Tang, H.C. Cheng, J.H. Wang, M. Zhang, Identification and structure characterization of a Cdk inhibitory peptide derived from neuronal-specific Cdk5 activator, J. Biol. Chem. 274 (1999) 7120-7127.
    • (1999) J. Biol. Chem. , vol.274 , pp. 7120-7127
    • Chin, K.T.1    Ohki, S.Y.2    Tang, D.3    Cheng, H.C.4    Wang, J.H.5    Zhang, M.6
  • 153
    • 0036379174 scopus 로고    scopus 로고
    • A peptide derived from cyclin-dependent kinase activator (p35) specifically inhibits Cdk5 activity and phosphorylation of tau protein in transfected cells
    • Y.-L. Zheng, B.-S. Li, N.D. Amin, W. Albers, H.C. Pant, A peptide derived from cyclin-dependent kinase activator (p35) specifically inhibits Cdk5 activity and phosphorylation of tau protein in transfected cells, Eur. J. Biochem. 269 (2002) 4427-4434.
    • (2002) Eur. J. Biochem. , vol.269 , pp. 4427-4434
    • Zheng, Y.-L.1    Li, B.-S.2    Amin, N.D.3    Albers, W.4    Pant, H.C.5
  • 154
    • 13244264765 scopus 로고    scopus 로고
    • A Cdk5 inhibitory peptide reduces tau hyperphosphorylation and apoptosis in neurons
    • Y.-L. Zheng, S. Kesavapany, M. Gravell, R.S. Hamilton, M. Schubert, N. Amin, et al., A Cdk5 inhibitory peptide reduces tau hyperphosphorylation and apoptosis in neurons, EMBO J. 24 (2005) 209-220.
    • (2005) EMBO J. , vol.24 , pp. 209-220
    • Zheng, Y.-L.1    Kesavapany, S.2    Gravell, M.3    Hamilton, R.S.4    Schubert, M.5    Amin, N.6
  • 155
    • 77958594810 scopus 로고    scopus 로고
    • A 24-residue peptide (p5), derived from p35, the Cdk5 neuronal activator, specifically inhibits Cdk5-p25 hyperactivity and tau hyperphosphorylation
    • Y.-L. Zheng, N.D. Amin, Y.-F. Hu, P. Rudrabhatla, V. Shukla, J. Kanungo, et al., A 24-residue peptide (p5), derived from p35, the Cdk5 neuronal activator, specifically inhibits Cdk5-p25 hyperactivity and tau hyperphosphorylation, J. Biol. Chem. 285 (2010) 34202-34212.
    • (2010) J. Biol. Chem. , vol.285 , pp. 34202-34212
    • Zheng, Y.-L.1    Amin, N.D.2    Hu, Y.-F.3    Rudrabhatla, P.4    Shukla, V.5    Kanungo, J.6
  • 156
    • 84871862823 scopus 로고    scopus 로고
    • A truncated peptide from p35, a Cdk5 activator, prevents Alzheimer's disease phenotypes in model mice
    • V. Shukla, Y.-L. Zheng, S.K. Mishra, N.D. Amin, J. Steiner, P. Grant, et al., A truncated peptide from p35, a Cdk5 activator, prevents Alzheimer's disease phenotypes in model mice, FASEB J. 27 (2013) 174-186.
    • (2013) FASEB J. , vol.27 , pp. 174-186
    • Shukla, V.1    Zheng, Y.-L.2    Mishra, S.K.3    Amin, N.D.4    Steiner, J.5    Grant, P.6
  • 157
    • 84871744906 scopus 로고    scopus 로고
    • Specific inhibition of p25/Cdk5 activity by the Cdk5 inhibitory peptide reduces neurodegeneration in vivo
    • J.R. Sundaram, C.P. Poore, N.H.B. Sulaimee, T. Pareek, A.B.M.A. Asad, R. Rajkumar, et al., Specific inhibition of p25/Cdk5 activity by the Cdk5 inhibitory peptide reduces neurodegeneration in vivo, J. Neurosci. 33 (2013) 334-343.
    • (2013) J. Neurosci. , vol.33 , pp. 334-343
    • Sundaram, J.R.1    Poore, C.P.2    Sulaimee, N.H.B.3    Pareek, T.4    Asad, A.B.M.A.5    Rajkumar, R.6
  • 158
    • 0032877184 scopus 로고    scopus 로고
    • Therapeutic peptides revisited
    • P.W. Latham, Therapeutic peptides revisited, Nat. Biotechnol. 17 (1999) 755-757.
    • (1999) Nat. Biotechnol. , vol.17 , pp. 755-757
    • Latham, P.W.1
  • 159
    • 33645875308 scopus 로고    scopus 로고
    • Peptide aptamers as guides for small-molecule drug discovery
    • I.C. Baines, P. Colas, Peptide aptamers as guides for small-molecule drug discovery, Drug Discov. Today 11 (2006) 334-341.
    • (2006) Drug Discov. Today , vol.11 , pp. 334-341
    • Baines, I.C.1    Colas, P.2
  • 160
    • 57749188299 scopus 로고    scopus 로고
    • Targeting cancer with small molecule kinase inhibitors
    • J. Zhang, P.L. Yang, N.S. Gray, Targeting cancer with small molecule kinase inhibitors, Nat. Rev. Cancer 9 (2009) 28-39.
    • (2009) Nat. Rev. Cancer , vol.9 , pp. 28-39
    • Zhang, J.1    Yang, P.L.2    Gray, N.S.3
  • 162
    • 79959952716 scopus 로고    scopus 로고
    • First BRET-based screening assay performed in budding yeast leads to the discovery of CDK5/p25 interaction inhibitors
    • C. Corbel, Q. Wang, H. Bousserouel, A. Hamdi, B. Zhang, O. Lozach, et al., First BRET-based screening assay performed in budding yeast leads to the discovery of CDK5/p25 interaction inhibitors, Biotechnol. J. 6 (2011) 860-870.
    • (2011) Biotechnol. J. , vol.6 , pp. 860-870
    • Corbel, C.1    Wang, Q.2    Bousserouel, H.3    Hamdi, A.4    Zhang, B.5    Lozach, O.6
  • 163
    • 77749329022 scopus 로고    scopus 로고
    • Human kinome drug discovery and the emerging importance of atypical allosteric inhibitors
    • R.M. Eglen, T. Reisine, Human kinome drug discovery and the emerging importance of atypical allosteric inhibitors, Expert Opin. Drug Discov. 5 (2010) 277-290.
    • (2010) Expert Opin. Drug Discov. , vol.5 , pp. 277-290
    • Eglen, R.M.1    Reisine, T.2
  • 164
    • 70350357186 scopus 로고    scopus 로고
    • A novel class of cyclin-dependent kinase inhibitors identified by molecular docking act through a unique mechanism
    • P. Corsino, N. Horenstein, D. Ostrov, T. Rowe, M. Law, A. Barrett, et al., A novel class of cyclin-dependent kinase inhibitors identified by molecular docking act through a unique mechanism, J. Biol. Chem. 284 (2009) 29945-29955.
    • (2009) J. Biol. Chem. , vol.284 , pp. 29945-29955
    • Corsino, P.1    Horenstein, N.2    Ostrov, D.3    Rowe, T.4    Law, M.5    Barrett, A.6
  • 168
    • 41649110649 scopus 로고    scopus 로고
    • Imaging in the era of molecular oncology
    • R. Weissleder, M.J. Pittet, Imaging in the era of molecular oncology, Nature 452 (2008) 580-589.
    • (2008) Nature , vol.452 , pp. 580-589
    • Weissleder, R.1    Pittet, M.J.2
  • 170
    • 75149112222 scopus 로고    scopus 로고
    • Designs and applications of fluorescent proteinbased biosensors
    • A. Ibraheem, R.E. Campbell, Designs and applications of fluorescent proteinbased biosensors, Curr. Opin. Chem. Biol. 14 (2010) 30-36.
    • (2010) Curr. Opin. Chem. Biol. , vol.14 , pp. 30-36
    • Ibraheem, A.1    Campbell, R.E.2
  • 171
    • 79951671135 scopus 로고    scopus 로고
    • Design and application of genetically encoded biosensors
    • A.E. Palmer, Y. Qin, J.G. Park, J.E. McCombs, Design and application of genetically encoded biosensors, Trends Biotechnol. 29 (2011) 144-152.
    • (2011) Trends Biotechnol. , vol.29 , pp. 144-152
    • Palmer, A.E.1    Qin, Y.2    Park, J.G.3    McCombs, J.E.4
  • 172
    • 71049131212 scopus 로고    scopus 로고
    • Recent progress in strategies for the creation of protein-based fluorescent biosensors
    • H. Wang, E. Nakata, I. Hamachi, Recent progress in strategies for the creation of protein-based fluorescent biosensors, Chembiochem 10 (2009) 2560-2577.
    • (2009) Chembiochem , vol.10 , pp. 2560-2577
    • Wang, H.1    Nakata, E.2    Hamachi, I.3
  • 174
    • 77951211821 scopus 로고    scopus 로고
    • Fluorescent biosensors of intracellular targets from genetically encoded reporters to modular polypeptide probes
    • M.C. Morris, Fluorescent biosensors of intracellular targets from genetically encoded reporters to modular polypeptide probes, Cell Biochem. Biophys. 56 (2010) 19-37.
    • (2010) Cell Biochem. Biophys. , vol.56 , pp. 19-37
    • Morris, M.C.1
  • 175
    • 84871061446 scopus 로고    scopus 로고
    • Fluorescent sensors of protein kinases: From basics to biomedical applications
    • T.N.N. Van, M.C. Morris, Fluorescent sensors of protein kinases: from basics to biomedical applications, Prog. Mol. Biol. Transl. Sci. 113 (2013) 217-274.
    • (2013) Prog. Mol. Biol. Transl. Sci. , vol.113 , pp. 217-274
    • Van, T.N.N.1    Morris, M.C.2
  • 176
    • 84856854097 scopus 로고    scopus 로고
    • Probing the kinome in real time with fluorescent peptides
    • J.A. Gonzalez-Vera, Probing the kinome in real time with fluorescent peptides, Chem. Soc. Rev. 41 (2012) 1652-1664.
    • (2012) Chem. Soc. Rev. , vol.41 , pp. 1652-1664
    • Gonzalez-Vera, J.A.1
  • 177
    • 84871063660 scopus 로고    scopus 로고
    • Fluorescent biosensors for Cancer cell imaging and diagnostics
    • V. Preedy, J. Hunter (Eds.) CRC Press
    • M.C. Morris, Fluorescent biosensors for Cancer cell imaging and diagnostics, in: V. Preedy, J. Hunter (Eds.), Biosensors and Cancer, CRC Press, 2012, ISBN 978-1-57808-734-1.
    • (2012) Biosensors and Cancer
    • Morris, M.C.1
  • 178
    • 84878827470 scopus 로고    scopus 로고
    • Fluorescent biosensors - Probing protein kinase function in Cancer and drug discovery
    • M.C. Morris, Fluorescent biosensors - probing protein kinase function in Cancer and drug discovery, Biochim. Biophys. Acta 1834 (2013) 1387-1395.
    • (2013) Biochim. Biophys. Acta , vol.1834 , pp. 1387-1395
    • Morris, M.C.1
  • 179
    • 84895074355 scopus 로고    scopus 로고
    • Fluorescent biosensors for high throughput screening of protein kinase inhibitors
    • C. Prével, M. Pellerano, T.N.N. Van, M.C. Morris, Fluorescent biosensors for high throughput screening of protein kinase inhibitors, Biotechnol. J. 9 (2014) 253-265.
    • (2014) Biotechnol. J. , vol.9 , pp. 253-265
    • Prével, C.1    Pellerano, M.2    Van, T.N.N.3    Morris, M.C.4
  • 180
    • 0032031530 scopus 로고    scopus 로고
    • Fluorescent-protein biosensors: New tools for drug discovery
    • K.A. Giuliano, D.L. Taylor, Fluorescent-protein biosensors: new tools for drug discovery, Trends Biotechnol. 16 (1998) 135-140.
    • (1998) Trends Biotechnol. , vol.16 , pp. 135-140
    • Giuliano, K.A.1    Taylor, D.L.2
  • 183
    • 20444432725 scopus 로고    scopus 로고
    • High throughput screening for kinase inhibitors
    • O. von Ahsen, U. Bömer, High throughput screening for kinase inhibitors, ChemBioChem 6 (2005) 481-490.
    • (2005) ChemBioChem , vol.6 , pp. 481-490
    • Von Ahsen, O.1    Bömer, U.2
  • 186
    • 34447502161 scopus 로고    scopus 로고
    • Image-based chemical screening
    • A.E. Carpenter, Image-based chemical screening, Nat. Chem. Biol. 3 (2007) 461-465.
    • (2007) Nat. Chem. Biol. , vol.3 , pp. 461-465
    • Carpenter, A.E.1
  • 187
    • 77951975169 scopus 로고    scopus 로고
    • High content screening: Seeing is believing
    • F. Zanella, J.B. Lorens, W. Link, High content screening: seeing is believing, Trends Biotechnol. 28 (2010) 237-245.
    • (2010) Trends Biotechnol. , vol.28 , pp. 237-245
    • Zanella, F.1    Lorens, J.B.2    Link, W.3
  • 188
    • 84881455207 scopus 로고    scopus 로고
    • Intravital FLIM-FRET imaging reveals dasatinib-induced spatial control of src in pancreatic cancer
    • M. Nobis, N.O. Carragher, E.J. McGhee, J.P. Morton, et al., Intravital FLIM-FRET imaging reveals dasatinib-induced spatial control of src in pancreatic cancer, Cancer Res. 73 (2013) 4674-4686.
    • (2013) Cancer Res. , vol.73 , pp. 4674-4686
    • Nobis, M.1    Carragher, N.O.2    McGhee, E.J.3    Morton, J.P.4
  • 189
    • 42449154333 scopus 로고    scopus 로고
    • Simultaneous recording of multiple cellular events by FRET
    • A. Piljic, C. Schultz, Simultaneous recording of multiple cellular events by FRET, ACS Chem. Biol. 3 (2008) 156-160.
    • (2008) ACS Chem. Biol. , vol.3 , pp. 156-160
    • Piljic, A.1    Schultz, C.2
  • 190
    • 65449153321 scopus 로고    scopus 로고
    • Genetically encoded FRET-based biosensors for multiparameter fluorescence imaging
    • H.J. Carlson, R.E. Campbell, Genetically encoded FRET-based biosensors for multiparameter fluorescence imaging, Curr. Opin. Biotechnol. 20 (2009) 19-27.
    • (2009) Curr. Opin. Biotechnol. , vol.20 , pp. 19-27
    • Carlson, H.J.1    Campbell, R.E.2
  • 191
    • 80054930783 scopus 로고    scopus 로고
    • Imaging the coordination of multiple signalling activities in living cells
    • C.M. Welch, H. Elliott, G. Danuser, K.M. Hahn, Imaging the coordination of multiple signalling activities in living cells, Nat. Rev. Mol. Cell Biol. 12 (2011) 749-756.
    • (2011) Nat. Rev. Mol. Cell Biol. , vol.12 , pp. 749-756
    • Welch, C.M.1    Elliott, H.2    Danuser, G.3    Hahn, K.M.4
  • 192
    • 14044272488 scopus 로고    scopus 로고
    • Positional biosensors: A new tool for high content screening
    • K.A. Giuliano, Y.T. Chen, J.R. Haskins, Positional biosensors: a new tool for high content screening, Mod. Drug Discov. 6 (2003) 33-37.
    • (2003) Mod. Drug Discov. , vol.6 , pp. 33-37
    • Giuliano, K.A.1    Chen, Y.T.2    Haskins, J.R.3
  • 193
    • 33947147539 scopus 로고    scopus 로고
    • Reading dynamic kinase activity in living cells for high-throughput screening
    • M.D. Allen, L.M. DiPilato, M. Rahdar, Y.R. Ren, et al., Reading dynamic kinase activity in living cells for high-throughput screening, ACS Chem. Biol. 1 (2006) 371-376.
    • (2006) ACS Chem. Biol. , vol.1 , pp. 371-376
    • Allen, M.D.1    Dipilato, L.M.2    Rahdar, M.3    Ren, Y.R.4
  • 194
    • 35348887075 scopus 로고    scopus 로고
    • FRET-based biosensors for protein kinases: Illuminating the kinome
    • J. Zhang, M.D. Allen, FRET-based biosensors for protein kinases: illuminating the kinome, Mol. Biosyst. 3 (2007) 759-765.
    • (2007) Mol. Biosyst. , vol.3 , pp. 759-765
    • Zhang, J.1    Allen, M.D.2
  • 195
    • 77955099778 scopus 로고    scopus 로고
    • A novel FRET-based biosensor for the measurement of BCR-ABL activity and its response to drugs in living cells
    • T. Mizutani, T. Kondo, S. Darmanin, M. Tsuda, et al., A novel FRET-based biosensor for the measurement of BCR-ABL activity and its response to drugs in living cells, Clin. Cancer Res. 16 (2010) 3964-3975.
    • (2010) Clin. Cancer Res. , vol.16 , pp. 3964-3975
    • Mizutani, T.1    Kondo, T.2    Darmanin, S.3    Tsuda, M.4
  • 196
    • 18744408814 scopus 로고    scopus 로고
    • A multiplexed homogeneous fluorescence-based assay for protein kinase activity in cell lysates
    • M.D. Shults, K.A. Janes, D.A. Lauffenburger, B. Imperiali, A multiplexed homogeneous fluorescence-based assay for protein kinase activity in cell lysates, Nat. Methods 2 (2005) 277-283.
    • (2005) Nat. Methods , vol.2 , pp. 277-283
    • Shults, M.D.1    Janes, K.A.2    Lauffenburger, D.A.3    Imperiali, B.4
  • 197
    • 33646164175 scopus 로고    scopus 로고
    • Optimal Sox-based fluorescent chemosensor design for serine/threonine protein kinases
    • M.D. Shults, D. Carrico-Moniz, B. Imperiali, Optimal Sox-based fluorescent chemosensor design for serine/threonine protein kinases, Anal. Biochem. 352 (2006) 198-207.
    • (2006) Anal. Biochem. , vol.352 , pp. 198-207
    • Shults, M.D.1    Carrico-Moniz, D.2    Imperiali, B.3
  • 198
    • 69649085747 scopus 로고    scopus 로고
    • Monitoring protein kinases in cellular media with highly selective chimeric reporters
    • E. Luković, E. Vogel Taylor, B. Imperiali, Monitoring protein kinases in cellular media with highly selective chimeric reporters, Angew. Chem. Int. Ed. Engl. 48 (2009) 6828-6831.
    • (2009) Angew. Chem. Int. Ed. Engl. , vol.48 , pp. 6828-6831
    • Luković, E.1    Vogel Taylor, E.2    Imperiali, B.3
  • 199
    • 79251482450 scopus 로고    scopus 로고
    • A p38a-selective chemosensor for use in unfractionated cell lysates
    • C.I. Stains, E. Luković, B. Imperiali, A p38a-selective chemosensor for use in unfractionated cell lysates, ACS Chem. Biol. 6 (2011) 101-105.
    • (2011) ACS Chem. Biol. , vol.6 , pp. 101-105
    • Stains, C.I.1    Luković, E.2    Imperiali, B.3
  • 200
    • 1542298996 scopus 로고    scopus 로고
    • Biosensors of protein kinase action: From in vitro assays to living cells
    • C.A. Chen, R.H. Yeh, X. Yan, D.S. Lawrence, Biosensors of protein kinase action: from in vitro assays to living cells, Biochim. Biophys. Acta 1697 (2004) 39-51.
    • (2004) Biochim. Biophys. Acta , vol.1697 , pp. 39-51
    • Chen, C.A.1    Yeh, R.H.2    Yan, X.3    Lawrence, D.S.4
  • 201
    • 34247851104 scopus 로고    scopus 로고
    • Seeing is believing: Peptide-based fluorescent sensors of protein tyrosine kinase activity
    • D.S. Lawrence, Q. Wang, Seeing is believing: peptide-based fluorescent sensors of protein tyrosine kinase activity, Chembiochem 8 (2007) 373-378.
    • (2007) Chembiochem , vol.8 , pp. 373-378
    • Lawrence, D.S.1    Wang, Q.2
  • 202
    • 38149036581 scopus 로고    scopus 로고
    • Peptide-based fluorescent sensors of protein kinase activity: Design and applications
    • V. Sharma, Q. Wang, D.S. Lawrence, Peptide-based fluorescent sensors of protein kinase activity: design and applications, Biochim. Biophys. Acta 1784 (2008) 94-99.
    • (2008) Biochim. Biophys. Acta , vol.1784 , pp. 94-99
    • Sharma, V.1    Wang, Q.2    Lawrence, D.S.3
  • 203
    • 77956893997 scopus 로고    scopus 로고
    • Multicolor monitoring of dysregulated protein kinases in chronic myelogenous leukemia
    • Q. Wang, E.I. Zimmerman, A. Toutchkine, T.D. Martin, et al., Multicolor monitoring of dysregulated protein kinases in chronic myelogenous leukemia, ACS Chem. Biol. 5 (2010) 887-895.
    • (2010) ACS Chem. Biol. , vol.5 , pp. 887-895
    • Wang, Q.1    Zimmerman, E.I.2    Toutchkine, A.3    Martin, T.D.4
  • 204
    • 67649995940 scopus 로고    scopus 로고
    • Development of a Fluorescent-tagged kinase assay system for detection and characterization of allosteric kinase inhibitors
    • J.R. Simard, M. Getlik, C. Grütter, V. Pawar, et al., Development of a Fluorescent-tagged kinase assay system for detection and characterization of allosteric kinase inhibitors, JACS 131 (2009) 13286-13296.
    • (2009) JACS , vol.131 , pp. 13286-13296
    • Simard, J.R.1    Getlik, M.2    Grütter, C.3    Pawar, V.4
  • 205
    • 77950283692 scopus 로고    scopus 로고
    • Fluorophore labelling of the glycine-rich loop as a method of identifying inhibitors that bind to active and inactive kinase conformations
    • J.R. Simard, M. Getlik, C. Grütter, R. Schneider, et al., Fluorophore labelling of the glycine-rich loop as a method of identifying inhibitors that bind to active and inactive kinase conformations, JACS 132 (2010) 4152-4160.
    • (2010) JACS , vol.132 , pp. 4152-4160
    • Simard, J.R.1    Getlik, M.2    Grütter, C.3    Schneider, R.4
  • 206
    • 67349094019 scopus 로고    scopus 로고
    • A new screening assay for allosteric inhibitors of cSrc
    • J.R. Simard, S. Klüter, C. Grütter, M. Getlik, et al., A new screening assay for allosteric inhibitors of cSrc, Nat. Chem. Biol. 5 (2009) 394-396.
    • (2009) Nat. Chem. Biol. , vol.5 , pp. 394-396
    • Simard, J.R.1    Klüter, S.2    Grütter, C.3    Getlik, M.4
  • 207
    • 84863634917 scopus 로고    scopus 로고
    • Fluorophore labelled kinase detects ligands that bind within the MAPK insert of p38a kinase
    • M. Getlik, J.R. Simard, M. Termathe, C. Grütter, et al., Fluorophore labelled kinase detects ligands that bind within the MAPK insert of p38a kinase, PLoS One 7 (2012) e39713.
    • (2012) PLoS One , vol.7 , pp. e39713
    • Getlik, M.1    Simard, J.R.2    Termathe, M.3    Grütter, C.4
  • 208
    • 75749146563 scopus 로고    scopus 로고
    • Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors
    • J. Zhang, F.J. Adrian, W. Jahnke, S.W. Cowan-Jacob, et al., Targeting Bcr-Abl by combining allosteric with ATP-binding-site inhibitors, Nature 463 (2010) 501-506.
    • (2010) Nature , vol.463 , pp. 501-506
    • Zhang, J.1    Adrian, F.J.2    Jahnke, W.3    Cowan-Jacob, S.W.4
  • 209
    • 84861854598 scopus 로고    scopus 로고
    • Direct binding assay for the detection of type IV allosteric inhibitors of abl
    • R. Schneider, R. Becker, J.R. Simard, M. Getlik, et al., Direct binding assay for the detection of type IV allosteric inhibitors of abl, JACS 134 (2012) 9138-9141.
    • (2012) JACS , vol.134 , pp. 9138-9141
    • Schneider, R.1    Becker, R.2    Simard, J.R.3    Getlik, M.4
  • 210
    • 0033003760 scopus 로고    scopus 로고
    • A simple statistical parameter for use in evaluation and validation of high throughput screening assays
    • J.H. Zhang, T.D. Chung, K.R. Oldenburg, A simple statistical parameter for use in evaluation and validation of high throughput screening assays, J. Biomol. Screen 4 (1999) 67-73.
    • (1999) J. Biomol. Screen , vol.4 , pp. 67-73
    • Zhang, J.H.1    Chung, T.D.2    Oldenburg, K.R.3
  • 211
    • 80054767002 scopus 로고    scopus 로고
    • Fluorescent peptide biosensor for probing the relative abundance of cyclin-dependent kinases in living cells
    • L. Kurzawa, M. Pellerano, J.B. Coppolani, M.C. Morris, Fluorescent peptide biosensor for probing the relative abundance of cyclin-dependent kinases in living cells, PlosOne 6 (2011) e26555.
    • (2011) Plos One , vol.6 , pp. e26555
    • Kurzawa, L.1    Pellerano, M.2    Coppolani, J.B.3    Morris, M.C.4
  • 212
    • 84907834056 scopus 로고    scopus 로고
    • Fluorescent protein biosensor for probing CDK/cyclin activity in vitro and in living cells
    • (Epub ahead of print)
    • T.N.N. Van, M. Pellerano, S. LyKaSo, M.C. Morris, Fluorescent protein biosensor for probing CDK/cyclin activity in vitro and in living cells, ChemBioChem (2014), http://dx.doi.org/10.1002/cbic.201402318 (Epub ahead of print).
    • (2014) ChemBioChem
    • Van, T.N.N.1    Pellerano, M.2    Lykaso, S.3    Morris, M.C.4
  • 214
    • 0035204427 scopus 로고    scopus 로고
    • A peptide carrier for the delivery of biologically active proteins into mammalian cells
    • M.C. Morris, J. Depollier, J. Mery, F. Heitz, G. Divita, A peptide carrier for the delivery of biologically active proteins into mammalian cells, Nat. Biotechnol. 19 (2001) 1173-1176.
    • (2001) Nat. Biotechnol. , vol.19 , pp. 1173-1176
    • Morris, M.C.1    Depollier, J.2    Mery, J.3    Heitz, F.4    Divita, G.5
  • 215
    • 24744449809 scopus 로고    scopus 로고
    • Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors
    • W. Jahnke, M.J. Blommers, C. Fernández, C. Zwingelstein, R. Amstutz, Strategies for the NMR-based identification and optimization of allosteric protein kinase inhibitors, Chembiochem 6 (2005) 1607-1610.
    • (2005) Chembiochem , vol.6 , pp. 1607-1610
    • Jahnke, W.1    Blommers, M.J.2    Fernández, C.3    Zwingelstein, C.4    Amstutz, R.5
  • 217
    • 84862236266 scopus 로고    scopus 로고
    • Detection of allosteric kinase inhibitors by displacement of active site probes
    • C.S. Lebakken, L.J. Reichling, J.M. Ellefson, S.M. Riddle, Detection of allosteric kinase inhibitors by displacement of active site probes, J. Biomol. Screen 17 (2012) 813-821.
    • (2012) J. Biomol. Screen , vol.17 , pp. 813-821
    • Lebakken, C.S.1    Reichling, L.J.2    Ellefson, J.M.3    Riddle, S.M.4


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