메뉴 건너뛰기




Volumn 7, Issue 6, 2000, Pages 411-422

Intracellular targets of cyclin-dependent kinase inhibitors: Identification by affinity chromatography using immobilised inhibitors

Author keywords

Casein kinase 1; Cyclin dependent kinases; erk; Malaria; Purine

Indexed keywords

AFFINITY CHROMATOGRAPHY; CASEIN KINASE I; CULTURE MEDIUM; CYCLIN DEPENDENT KINASE; ENZYME INHIBITOR; LEISHMANIA MEXICANA; OLOMOUCINE; PLASMODIUM FALCIPARUM; PURINE DERIVATIVE; PURVALANOL; TOXOPLASMA GONDII; TRYPANOSOMA CRUZI;

EID: 0034086397     PISSN: 10745521     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1074-5521(00)00124-1     Document Type: Article
Times cited : (222)

References (49)
  • 1
    • 0002411854 scopus 로고    scopus 로고
    • Cell cycle control
    • (ed.)
    • Dunphy, W.G. (ed.) (1997). Cell cycle control. Methods Enzymol., 283, 678.
    • (1997) Methods Enzymol. , vol.283 , pp. 678
    • Dunphy, W.G.1
  • 2
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprocessors
    • Morgan D. 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.1
  • 5
    • 0031670668 scopus 로고    scopus 로고
    • Phase I trial of continuous infusion flavopiridol, a novel cyclin-dependent kinase inhibitor, in patients with refractory neoplasms
    • Senderowicz A., Sausville E.A.et al. Phase I trial of continuous infusion flavopiridol, a novel cyclin-dependent kinase inhibitor, in patients with refractory neoplasms. J. Clin. Oncol. 16:1998;1-17.
    • (1998) J. Clin. Oncol. , vol.16 , pp. 1-17
    • Senderowicz, A.1    Sausville, E.A.2
  • 7
    • 0030271304 scopus 로고    scopus 로고
    • Chemical inhibitors of cyclin-dependent kinases
    • Meijer L. Chemical inhibitors of cyclin-dependent kinases. Trends Cell Biol. 6:1996;393-397.
    • (1996) Trends Cell Biol. , vol.6 , pp. 393-397
    • Meijer, L.1
  • 8
    • 0030753686 scopus 로고    scopus 로고
    • Chemical inhibitors of cyclin-dependent kinases
    • Meijer L., Kim S.H. Chemical inhibitors of cyclin-dependent kinases. Methods Enzymol. 283:1997;113-128.
    • (1997) Methods Enzymol. , vol.283 , pp. 113-128
    • Meijer, L.1    Kim, S.H.2
  • 9
    • 0033036758 scopus 로고    scopus 로고
    • Properties and potential applications of chemical inhibitors of cyclin-dependent kinases
    • Meijer L., Leclerc S., Leost M. Properties and potential applications of chemical inhibitors of cyclin-dependent kinases. Pharmacol. Ther. 82:1999;279-284.
    • (1999) Pharmacol. Ther. , vol.82 , pp. 279-284
    • Meijer, L.1    Leclerc, S.2    Leost, M.3
  • 10
  • 11
    • 0025841808 scopus 로고
    • suc1-coated microtitration plates
    • suc1-coated microtitration plates. Anticancer Res. 11:1991;1581-1590.
    • (1991) Anticancer Res. , vol.11 , pp. 1581-1590
    • Rialet, V.1    Meijer, L.2
  • 12
    • 0027186226 scopus 로고
    • Butyrolactone I, a selective inhibitor of cdk2 and cdc2 kinase
    • Kitagawa M., Okuyama A.et al. Butyrolactone I, a selective inhibitor of cdk2 and cdc2 kinase. Oncogene. 8:1993;2425-2432.
    • (1993) Oncogene , vol.8 , pp. 2425-2432
    • Kitagawa, M.1    Okuyama, A.2
  • 13
    • 0028093182 scopus 로고
    • Inhibition of cyclin-dependent kinases by purine derivatives
    • Vesely J., Meijer L.et al. Inhibition of cyclin-dependent kinases by purine derivatives. Eur. J. Biochem. 224:1994;771-786.
    • (1994) Eur. J. Biochem. , vol.224 , pp. 771-786
    • Vesely, J.1    Meijer, L.2
  • 15
    • 0031028163 scopus 로고    scopus 로고
    • Inhibition of cyclin-dependent kinases by purine analogues: Crystal structure of human cdk2 complexed with roscovitine
    • De Azevedo W.F., Leclerc S., Meijer L., Havlicek L., Strnad M., Kim S-H. 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
  • 16
    • 0031037714 scopus 로고    scopus 로고
    • Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 & cdk5
    • Meijer L., Moulinoux J.P.et al. Biochemical and cellular effects of roscovitine, a potent and selective inhibitor of the cyclin-dependent kinases cdc2, cdk2 & cdk5. Eur. J. Biochem. 243:1997;527-536.
    • (1997) Eur. J. Biochem. , vol.243 , pp. 527-536
    • Meijer, L.1    Moulinoux, J.P.2
  • 17
    • 0032563315 scopus 로고    scopus 로고
    • Exploiting chemical libraries, structure, and genomics in the search for kinase inhibitors
    • Gray N.S., Schultz P.G.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    Schultz, P.G.2
  • 18
    • 0033128165 scopus 로고    scopus 로고
    • Indirubin, the active constituent of a Chinese antileukaemia medicine, inhibits cyclin-dependent kinases
    • Hoessel R., Meijer L.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    Meijer, L.2
  • 19
    • 0033614949 scopus 로고    scopus 로고
    • The Paullones, a series of cyclin-dependent kinase inhibitors: Synthesis, evaluation of CDK1/cyclin B inhibition, and in vitro antitumor activity
    • Schultz C., Kunick C.et al. The Paullones, a series of cyclin-dependent kinase inhibitors: synthesis, evaluation of CDK1/cyclin B inhibition, and in vitro antitumor activity. J. Med. Chem. 42:1999;2909-2919.
    • (1999) J. Med. Chem. , vol.42 , pp. 2909-2919
    • Schultz, C.1    Kunick, C.2
  • 20
    • 0033152122 scopus 로고    scopus 로고
    • Discovery and initial characterization of the paullones, a novel class of small-molecule inhibitors of cyclin-dependent kinases
    • Zaharevitz D., Sausville E.A.et al. Discovery and initial characterization of the paullones, a novel class of small-molecule inhibitors of cyclin-dependent kinases. Cancer Res. 59:1999;2566-2569.
    • (1999) Cancer Res. , vol.59 , pp. 2566-2569
    • Zaharevitz, D.1    Sausville, E.A.2
  • 21
    • 0034010742 scopus 로고    scopus 로고
    • Inhibition of cyclin-dependent kinases 1, 2 & 5, GSK-3β and casein kinase 1 by hymenialdisine, a marine sponge constituent
    • Meijer L., Pettit G.R.et al. Inhibition of cyclin-dependent kinases 1, 2 & 5, GSK-3β and casein kinase 1 by hymenialdisine, a marine sponge constituent. Chem. Biol. 7:2000;51-63.
    • (2000) Chem. Biol. , vol.7 , pp. 51-63
    • Meijer, L.1    Pettit, G.R.2
  • 22
    • 15444355744 scopus 로고    scopus 로고
    • CVT-313, a specific and potent inhibitor of CDK2 that prevents neointimal proliferation
    • Brooks E.E., Shiffman D.et al. CVT-313, a specific and potent inhibitor of CDK2 that prevents neointimal proliferation. J. Biol. Chem. 272:1997;29207-29211.
    • (1997) J. Biol. Chem. , vol.272 , pp. 29207-29211
    • Brooks, E.E.1    Shiffman, D.2
  • 23
    • 0030877852 scopus 로고    scopus 로고
    • Prevention of graft coronary arteriosclerosis by antisense cdk2 kinase oligonucleotide
    • Suzuki J.I., Sekiguchi M.et al. Prevention of graft coronary arteriosclerosis by antisense cdk2 kinase oligonucleotide. Nature Med. 3:1997;900-903.
    • (1997) Nature Med. , vol.3 , pp. 900-903
    • Suzuki, J.I.1    Sekiguchi, M.2
  • 24
    • 0030781307 scopus 로고    scopus 로고
    • Direct in vivo inhibition of the nuclear cell cycle cascade in experimental mesangial proliferative glomerulonephritis with roscovitine, a novel CDK2 antagonist
    • Pippin J.W., Qu Q., Meijer L., Shankland S.J. Direct in vivo inhibition of the nuclear cell cycle cascade in experimental mesangial proliferative glomerulonephritis with roscovitine, a novel CDK2 antagonist. J. Clin. Invest. 100:1997;2512-2520.
    • (1997) J. Clin. Invest. , vol.100 , pp. 2512-2520
    • Pippin, J.W.1    Qu, Q.2    Meijer, L.3    Shankland, S.J.4
  • 25
    • 0030751147 scopus 로고    scopus 로고
    • Cell-cycle control and renal disease
    • Shankland S.J. Cell-cycle control and renal disease. Kidney Int. 52:1997;294-308.
    • (1997) Kidney Int. , vol.52 , pp. 294-308
    • Shankland, S.J.1
  • 26
    • 0031009357 scopus 로고    scopus 로고
    • Inhibition of cellular cdk2 activity blocks human cytomegalovirus replication
    • Bresnahan W.A., Boldogh I., Chi P., Thompson E.A., Albrecht T. Inhibition of cellular cdk2 activity blocks human cytomegalovirus replication. Virology. 231:1997;239-247.
    • (1997) Virology , vol.231 , pp. 239-247
    • Bresnahan, W.A.1    Boldogh, I.2    Chi, P.3    Thompson, E.A.4    Albrecht, T.5
  • 27
    • 14444281157 scopus 로고    scopus 로고
    • P-TEFb kinase is required for HIV Tat transcriptional activation in vivo and in vitro
    • Mancebo H.S.Y., Flores O.et al. P-TEFb kinase is required for HIV Tat transcriptional activation in vivo and in vitro. Genes Dev. 11:1997;2633-2644.
    • (1997) Genes Dev. , vol.11 , pp. 2633-2644
    • Mancebo, H.S.Y.1    Flores, O.2
  • 28
    • 0031746015 scopus 로고    scopus 로고
    • Requirement for cellular cyclin-dependent kinases in herpes simplex virus replication and transcription
    • Schang L.M., Phillips J., Schaffer P.A. Requirement for cellular cyclin-dependent kinases in herpes simplex virus replication and transcription. J. Virol. 72:1998;5626-5637.
    • (1998) J. Virol. , vol.72 , pp. 5626-5637
    • Schang, L.M.1    Phillips, J.2    Schaffer, P.A.3
  • 29
    • 0032901995 scopus 로고    scopus 로고
    • Varicella-zoster virus Fc receptor component gI is phosphorylated on its endodomain by a cyclin-dependent kinase
    • Ye M., Duus K.M., Peng J., Price D.H., Grose C. Varicella-zoster virus Fc receptor component gI is phosphorylated on its endodomain by a cyclin-dependent kinase. J. Virol. 73:1999;1320-1330.
    • (1999) J. Virol. , vol.73 , pp. 1320-1330
    • Ye, M.1    Duus, K.M.2    Peng, J.3    Price, D.H.4    Grose, C.5
  • 30
    • 0031045216 scopus 로고    scopus 로고
    • Physiology and pathology of tau protein kinases in relation to Alzheimer's disease
    • Imahori K., Uchida T. Physiology and pathology of tau protein kinases in relation to Alzheimer's disease. J. Biochem. 121:1997;179-188.
    • (1997) J. Biochem. , vol.121 , pp. 179-188
    • Imahori, K.1    Uchida, T.2
  • 32
    • 0023867410 scopus 로고
    • 1 kinase during the sea urchin egg mitotic divisions
    • 1 kinase during the sea urchin egg mitotic divisions. Exp. Cell Res. 174:1988;116-129.
    • (1988) Exp. Cell Res. , vol.174 , pp. 116-129
    • Meijer, L.1    Pondaven, P.2
  • 33
    • 0023945117 scopus 로고
    • 6-Dimethylaminopurine blocks starfish oocyte maturation by inhibiting a relevant protein kinase activity
    • Néant I., Guerrier P. 6-Dimethylaminopurine blocks starfish oocyte maturation by inhibiting a relevant protein kinase activity. Exp. Cell Res. 176:1988;68-79.
    • (1988) Exp. Cell Res. , vol.176 , pp. 68-79
    • Néant, I.1    Guerrier, P.2
  • 34
    • 0032492705 scopus 로고    scopus 로고
    • Synthesis of C2 alkynylated purines, a new family of potent inhibitors of cyclin-dependent kinases
    • Legraverend M., Ludwig O., Bisagni E., Leclerc S., Meijer L. Synthesis of C2 alkynylated purines, a new family of potent inhibitors of cyclin-dependent kinases. Bioorg. Med. Chem. Lett. 8:1998;793-798.
    • (1998) Bioorg. Med. Chem. Lett. , vol.8 , pp. 793-798
    • Legraverend, M.1    Ludwig, O.2    Bisagni, E.3    Leclerc, S.4    Meijer, L.5
  • 35
  • 36
    • 0031575637 scopus 로고    scopus 로고
    • Combinatorial synthesis of 2,9-substituted purines
    • Gray N.S., Schultz P.G. Combinatorial synthesis of 2,9-substituted purines. Tetrahedron Lett. 38:1997;1161-1164.
    • (1997) Tetrahedron Lett. , vol.38 , pp. 1161-1164
    • Gray, N.S.1    Schultz, P.G.2
  • 37
    • 0031013919 scopus 로고    scopus 로고
    • Facile preparation of 2,6-disubstituted purines using solid phase chemistry
    • Nugiel D.A., Cornelius L.A.M., Corbett J.W. Facile preparation of 2,6-disubstituted purines using solid phase chemistry. J. Org. Chem. 62:1997;201-203.
    • (1997) J. Org. Chem. , vol.62 , pp. 201-203
    • Nugiel, D.A.1    Cornelius, L.A.M.2    Corbett, J.W.3
  • 38
    • 0033150476 scopus 로고    scopus 로고
    • Synthesis and application of 2,6,9-trisubstituted purine library towards the development of functionally diverse CDK inhibitors
    • Chang Y.T., Schultz P.G.et al. Synthesis and application of 2,6,9-trisubstituted purine library towards the development of functionally diverse CDK inhibitors. Chem. Biol. 6:1999;361-375.
    • (1999) Chem. Biol. , vol.6 , pp. 361-375
    • Chang, Y.T.1    Schultz, P.G.2
  • 39
    • 0037792445 scopus 로고
    • Starfish oocyte maturation: From prophase to metaphase
    • Meijer L., Mordret G. Starfish oocyte maturation: from prophase to metaphase. Semin. Dev. Biol. 5:1994;165-171.
    • (1994) Semin. Dev. Biol. , vol.5 , pp. 165-171
    • Meijer, L.1    Mordret, G.2
  • 40
    • 0029981099 scopus 로고    scopus 로고
    • cdc2 on its Thr-14 and Tyr-15 residues at the prophase/metaphase transition
    • cdc2 on its Thr-14 and Tyr-15 residues at the prophase/metaphase transition. J. Biol. Chem. 271:1996;27847-27854.
    • (1996) J. Biol. Chem. , vol.271 , pp. 27847-27854
    • Borgne, A.1    Meijer, L.2
  • 41
    • 0005221605 scopus 로고
    • Contrôle neurohormonal de la maturation des ovocytes chez Arenicola marina (Annélide Polychète)
    • Etude in vitro [Neurohormonal control of oocyte maturation in Arericola marina: in vivo study]
    • Meijer L., Durchon M. Contrôle neurohormonal de la maturation des ovocytes chez Arenicola marina (Annélide Polychète). C.R. Acad. Sci. Paris. 285:1977;377-380. Etude in vitro [Neurohormonal control of oocyte maturation in Arericola marina: in vivo study].
    • (1977) C.R. Acad. Sci. Paris , vol.285 , pp. 377-380
    • Meijer, L.1    Durchon, M.2
  • 43
    • 0033609044 scopus 로고    scopus 로고
    • A cyclin-dependent kinase inhibitor inducing cancer cell differentiation: Biochemical identification using Xenopus egg extracts
    • Rosania G.R., Merlie J., Gray N., Chang Y-T., Schultz P.G., Heald R. A cyclin-dependent kinase inhibitor inducing cancer cell differentiation: biochemical identification using Xenopus egg extracts. Proc. Natl. Acad. Sci. USA. 96:1999;4797-4802.
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 4797-4802
    • Rosania, G.R.1    Merlie, J.2    Gray, N.3    Chang, Y.-T.4    Schultz, P.G.5    Heald, R.6
  • 44
    • 0030705190 scopus 로고    scopus 로고
    • Identification, cloning, and mutational analysis of the casein kinase 1 cDNA of the malaria parasite, Plasmodium falciparum
    • Barik S., Taylor R.E., Chakrabarti D. Identification, cloning, and mutational analysis of the casein kinase 1 cDNA of the malaria parasite, Plasmodium falciparum. J. Biol. Chem. 272:1997;26132-26138.
    • (1997) J. Biol. Chem. , vol.272 , pp. 26132-26138
    • Barik, S.1    Taylor, R.E.2    Chakrabarti, D.3
  • 45
    • 0029020282 scopus 로고
    • The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks S.K., Hunter T. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9:1995;576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 46
    • 0029090514 scopus 로고
    • Multiple modes of ligand recognition: Crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine
    • Schulze-Gahmen U., Kim S.-H.et al. Multiple modes of ligand recognition: crystal structures of cyclin-dependent protein kinase 2 in complex with ATP and two inhibitors, olomoucine and isopentenyladenine. Proteins. 22:1995;378-391.
    • (1995) Proteins , vol.22 , pp. 378-391
    • Schulze-Gahmen, U.1    Kim, S.-H.2
  • 47
    • 0029850471 scopus 로고    scopus 로고
    • High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: Bound waters and natural ligand as guides for inhibitor design
    • Schulze-Gahmen U., De Bondt H.L., Kim S.-H. High-resolution crystal structures of human cyclin-dependent kinase 2 with and without ATP: bound waters and natural ligand as guides for inhibitor design. J. Med. Chem. 39:1996;4540-4546.
    • (1996) J. Med. Chem. , vol.39 , pp. 4540-4546
    • Schulze-Gahmen, U.1    De Bondt, H.L.2    Kim, S.-H.3
  • 48
    • 0032530336 scopus 로고    scopus 로고
    • Structural basis of inhibitor selectivity in MAP kinases
    • Wang Z., Goldsmith E.J.et al. Structural basis of inhibitor selectivity in MAP kinases. Structure. 6:1998;1117-1128.
    • (1998) Structure , vol.6 , pp. 1117-1128
    • Wang, Z.1    Goldsmith, E.J.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.