메뉴 건너뛰기




Volumn 14, Issue 9, 2008, Pages 917-924

Targeting the cell cycle in the pursuit of novel chemotherapies against parasitic protozoa

Author keywords

Aurora kinase; Cell cycle; Cyclin dependent kinase; Glycogen synthase kinase; Leishmania; Plasmodium; Trypanosoma

Indexed keywords

5 IODO INDIRUBIN 3' MONOXIME; AURORA KINASE; AURORA KINASE INHIBITOR; AZAKENPAULLONE; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE INHIBITOR; CYCLOPROPANECARBOXYLIC ACID [4 [4 (4 METHYL 1 PIPERAZINYL) 6 (5 METHYL 2H PYRAZOL 3 YLAMINO) 2 PYRIMIDINYLTHIO]PHENYL]AMIDE; FLAVOPIRIDOL; GLYCOGEN SYNTHASE KINASE; GLYCOGEN SYNTHASE KINASE 3 INHIBITOR; HESPERADIN; HYMENIALDISINE; INDIRUBIN 3' MONOXIME; N [4 [6 METHOXY 7 (3 MORPHOLINOPROPOXY) 4 QUINAZOLINYLAMINO]PHENYL]BENZAMIDE; OLOMOUCINE; POLO LIKE KINASE; PROTEASOME INHIBITOR; PROTEIN SERINE THREONINE KINASE; ROSCOVITINE;

EID: 44349155924     PISSN: 13816128     EISSN: None     Source Type: Journal    
DOI: 10.2174/138161208784041042     Document Type: Review
Times cited : (11)

References (101)
  • 1
    • 0035110493 scopus 로고    scopus 로고
    • Modulation of host responses to blood-stage malaria by interleukin-12: From therapy to adjuvant activity
    • Stevenson MM, Su Z, Sam H, Mohan K. Modulation of host responses to blood-stage malaria by interleukin-12: From therapy to adjuvant activity. Microbes Infect 2001; 3(1): 49-59.
    • (2001) Microbes Infect , vol.3 , Issue.1 , pp. 49-59
    • Stevenson, M.M.1    Su, Z.2    Sam, H.3    Mohan, K.4
  • 2
    • 0031958697 scopus 로고    scopus 로고
    • Structures of Toxoplasma gondii tachyzoites, bradyzoites, and sporozoites and biology and development of tissue cysts
    • Dubey JP, Lindsay DS, Speer CA. Structures of Toxoplasma gondii tachyzoites, bradyzoites, and sporozoites and biology and development of tissue cysts. Clin Microbiol Rev 1998; 11(2): 267-99.
    • (1998) Clin Microbiol Rev , vol.11 , Issue.2 , pp. 267-299
    • Dubey, J.P.1    Lindsay, D.S.2    Speer, C.A.3
  • 3
    • 0033961307 scopus 로고    scopus 로고
    • Small-molecule inhibitors of the cell cycle
    • Crews CM, Mohan R. Small-molecule inhibitors of the cell cycle. Curr Opin Chem Biol 2000; 4(1): 47-53.
    • (2000) Curr Opin Chem Biol , vol.4 , Issue.1 , pp. 47-53
    • Crews, C.M.1    Mohan, R.2
  • 4
    • 28544443503 scopus 로고    scopus 로고
    • Phase I and pharmacokinetic study of flavopiridol followed by 1-beta-D-arabinofuranosylcytosine and mitoxantrone in relapsed and refractory adult acute leukemias
    • Karp JE, Passaniti A, Gojo I, Kaufmann S, Bible K, Garimella TS, et al. Phase I and pharmacokinetic study of flavopiridol followed by 1-beta-D-arabinofuranosylcytosine and mitoxantrone in relapsed and refractory adult acute leukemias. Clin Cancer Res 2005; 11(23): 8403-12.
    • (2005) Clin Cancer Res , vol.11 , Issue.23 , pp. 8403-8412
    • Karp, J.E.1    Passaniti, A.2    Gojo, I.3    Kaufmann, S.4    Bible, K.5    Garimella, T.S.6
  • 5
    • 33846254185 scopus 로고    scopus 로고
    • A phase I trial of the selective oral cyclin-dependent kinase inhibitor seliciclib (CYC202; R-Roscovitine), administered twice daily for 7 days every 21 days
    • Benson C, White J, De Bono J, O'Donnell A, Raynaud F, Cruickshank C, et al. A phase I trial of the selective oral cyclin-dependent kinase inhibitor seliciclib (CYC202; R-Roscovitine), administered twice daily for 7 days every 21 days. Br J Cancer 2007; 96(1): 29-37.
    • (2007) Br J Cancer , vol.96 , Issue.1 , pp. 29-37
    • Benson, C.1    White, J.2    De Bono, J.3    O'Donnell, A.4    Raynaud, F.5    Cruickshank, C.6
  • 6
    • 0027419976 scopus 로고
    • Microtubular organization visualized by immunofluorescence microscopy during erythrocytic schizogony in Plasmodium falciparum and investigation of post-translational modifications of parasite tubulin
    • Read M, Sherwin T, Holloway SP, Gull K, Hyde JE. Microtubular organization visualized by immunofluorescence microscopy during erythrocytic schizogony in Plasmodium falciparum and investigation of post-translational modifications of parasite tubulin. Parasitology 1993; 106(Pt 3): 223-32.
    • (1993) Parasitology , vol.106 , Issue.PART 3 , pp. 223-232
    • Read, M.1    Sherwin, T.2    Holloway, S.P.3    Gull, K.4    Hyde, J.E.5
  • 7
    • 0033398908 scopus 로고    scopus 로고
    • Evidence for novel cell cycle checkpoints in trypanosomes: Kinetoplast segregation and cytokinesis in the absence of mitosis
    • Ploubidou A, Robinson DR, Docherty RC, Ugbadoyi EO, Gull K. Evidence for novel cell cycle checkpoints in trypanosomes: Kinetoplast segregation and cytokinesis in the absence of mitosis. J Cell Sci 1999; 112(Pt 24): 4641-50.
    • (1999) J Cell Sci , vol.112 , Issue.PART 24 , pp. 4641-4650
    • Ploubidou, A.1    Robinson, D.R.2    Docherty, R.C.3    Ugbadoyi, E.O.4    Gull, K.5
  • 8
    • 0038604023 scopus 로고    scopus 로고
    • Stage-specific differences in cell cycle control in Trypanosoma brucei revealed by RNA interference of a mitotic cyclin
    • Hammarton TC, Clark J, Douglas F, Boshart M, Mottram JC. Stage-specific differences in cell cycle control in Trypanosoma brucei revealed by RNA interference of a mitotic cyclin. J Biol Chem 2003; 278(25): 22877-86.
    • (2003) J Biol Chem , vol.278 , Issue.25 , pp. 22877-22886
    • Hammarton, T.C.1    Clark, J.2    Douglas, F.3    Boshart, M.4    Mottram, J.C.5
  • 9
    • 33644858832 scopus 로고    scopus 로고
    • Flagellar motility is required for the viability of the blood-stream trypanosome
    • Broadhead R, Dawe HR, Farr H, Griffiths S, Hart SR, Portman N, et al. Flagellar motility is required for the viability of the blood-stream trypanosome. Nature 2006; 440(7081): 224-7.
    • (2006) Nature , vol.440 , Issue.7081 , pp. 224-227
    • Broadhead, R.1    Dawe, H.R.2    Farr, H.3    Griffiths, S.4    Hart, S.R.5    Portman, N.6
  • 10
    • 4344562126 scopus 로고    scopus 로고
    • Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation
    • Ha NC, Tonozuka T, Stamos JL, Choi HJ, Weis WI. Mechanism of phosphorylation-dependent binding of APC to beta-catenin and its role in beta-catenin degradation. Mol Cell 2004; 15(4): 511-21.
    • (2004) Mol Cell , vol.15 , Issue.4 , pp. 511-521
    • Ha, N.C.1    Tonozuka, T.2    Stamos, J.L.3    Choi, H.J.4    Weis, W.I.5
  • 12
    • 0034717570 scopus 로고    scopus 로고
    • Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the anaphase-promoting complex
    • Rudner AD, Murray AW. Phosphorylation by Cdc28 activates the Cdc20-dependent activity of the anaphase-promoting complex. J Cell Biol 2000; 149(7): 1377-90.
    • (2000) J Cell Biol , vol.149 , Issue.7 , pp. 1377-1390
    • Rudner, A.D.1    Murray, A.W.2
  • 13
    • 17844382743 scopus 로고    scopus 로고
    • Phosphorylation of cyclin D1 at Thr 286 during S phase leads to its proteasomal degradation and allows efficient DNA synthesis
    • Guo Y, Yang K, Harwalkar J, Nye JM, Mason DR, Garrett MD, et al. Phosphorylation of cyclin D1 at Thr 286 during S phase leads to its proteasomal degradation and allows efficient DNA synthesis. Oncogene 2005; 24(16): 2599-612.
    • (2005) Oncogene , vol.24 , Issue.16 , pp. 2599-2612
    • Guo, Y.1    Yang, K.2    Harwalkar, J.3    Nye, J.M.4    Mason, D.R.5    Garrett, M.D.6
  • 16
    • 0037015614 scopus 로고    scopus 로고
    • Genome sequence or the human malaria parasite Plasmodium falciparum
    • Gardner MJ, Hall N, Fung E, White O, Berriman M, Hyman RW, et al. Genome sequence or the human malaria parasite Plasmodium falciparum. Nature 2002; 419(6906): 498-511.
    • (2002) Nature , vol.419 , Issue.6906 , pp. 498-511
    • Gardner, M.J.1    Hall, N.2    Fung, E.3    White, O.4    Berriman, M.5    Hyman, R.W.6
  • 17
    • 2642581817 scopus 로고    scopus 로고
    • The Trypanosoma brucei cyclin, CYC2, is required for cell cycle progression through G1 phase and for maintenance of procyclic form cell morphology
    • Hammarton TC, Engstler M, Mottram JC. The Trypanosoma brucei cyclin, CYC2, is required for cell cycle progression through G1 phase and for maintenance of procyclic form cell morphology. J Biol Chem 2004; 279(23): 24757-64.
    • (2004) J Biol Chem , vol.279 , Issue.23 , pp. 24757-24764
    • Hammarton, T.C.1    Engstler, M.2    Mottram, J.C.3
  • 18
    • 18044386574 scopus 로고    scopus 로고
    • Pairwise knockdowns of cdc2-related kinases (CRKs) in Trypanosoma brucei identified the CRKs for G1/S and G2/M transitions and demonstrated distinctive cytokinetic regulations between two developmental stages of the organism
    • Tu X, Wang CC. Pairwise knockdowns of cdc2-related kinases (CRKs) in Trypanosoma brucei identified the CRKs for G1/S and G2/M transitions and demonstrated distinctive cytokinetic regulations between two developmental stages of the organism. Eukaryot Cell 2005; 4(4): 755-64.
    • (2005) Eukaryot Cell , vol.4 , Issue.4 , pp. 755-764
    • Tu, X.1    Wang, C.C.2
  • 19
    • 2442427368 scopus 로고    scopus 로고
    • The involvement of two cdc2-related kinases (CRKs) in Trypanosoma brucei cell cycle regulation and the distinctive stage-specilic phenotypes caused by CRK3 depletion
    • Tu X, Wang CC. The involvement of two cdc2-related kinases (CRKs) in Trypanosoma brucei cell cycle regulation and the distinctive stage-specilic phenotypes caused by CRK3 depletion. J Biol Chem 2004; 279(19): 20519-28.
    • (2004) J Biol Chem , vol.279 , Issue.19 , pp. 20519-20528
    • Tu, X.1    Wang, C.C.2
  • 20
    • 0032582841 scopus 로고    scopus 로고
    • Stage-specific activity of the Leishmania major CRK3 kinase and functional rescue of a Schizosaccharomyces pombe cdc2 mutant
    • Wang Y, Dimitrov K, Garrity LK, Sazer S, Beverley SM. Stage-specific activity of the Leishmania major CRK3 kinase and functional rescue of a Schizosaccharomyces pombe cdc2 mutant. Mol Biochem Parasitol 1998; 96(1-2): 139-50.
    • (1998) Mol Biochem Parasitol , vol.96 , Issue.1-2 , pp. 139-150
    • Wang, Y.1    Dimitrov, K.2    Garrity, L.K.3    Sazer, S.4    Beverley, S.M.5
  • 21
    • 0034708437 scopus 로고    scopus 로고
    • Activation of a Plasmodium falciparum cdc2-related kinase by heterologous p25 and cyclin H. Functional characterization of a P. falciparum cyclin homologue
    • Le Roch K, Sestier C, Dorin D, Waters N, Kappes B, Chakrabarti D, et al. Activation of a Plasmodium falciparum cdc2-related kinase by heterologous p25 and cyclin H. Functional characterization of a P. falciparum cyclin homologue. J Biol Chem 2000; 275(12): 8952-8.
    • (2000) J Biol Chem , vol.275 , Issue.12 , pp. 8952-8958
    • Le Roch, K.1    Sestier, C.2    Dorin, D.3    Waters, N.4    Kappes, B.5    Chakrabarti, D.6
  • 22
    • 0141960110 scopus 로고    scopus 로고
    • Identification and initial characterization of three novel cyclin-related proteins of the human malaria parasite Plasmodium falciparum
    • Merckx A, Le Roch K, Nivez MP, Dorin D, Alano P, Gutierrez GJ, et al. Identification and initial characterization of three novel cyclin-related proteins of the human malaria parasite Plasmodium falciparum. J Biol Chem 2003; 278(41): 39839-50.
    • (2003) J Biol Chem , vol.278 , Issue.41 , pp. 39839-39850
    • Merckx, A.1    Le Roch, K.2    Nivez, M.P.3    Dorin, D.4    Alano, P.5    Gutierrez, G.J.6
  • 23
    • 32644477033 scopus 로고    scopus 로고
    • Pbcrk-1, the Plasmodium berghei orrhologue of P. falciparum cdc-2 related kinase-1 (PfcrK- 1), is essential for completion of the intraerythrocytic asexual cycle
    • Rangarajan R, Bei A, Henry N, Madamet M, Parzy D, Nivez MP, et al. Pbcrk-1, the Plasmodium berghei orrhologue of P. falciparum cdc-2 related kinase-1 (PfcrK- 1), is essential for completion of the intraerythrocytic asexual cycle. Exp Parasitol 2006; 112(3): 202-7.
    • (2006) Exp Parasitol , vol.112 , Issue.3 , pp. 202-207
    • Rangarajan, R.1    Bei, A.2    Henry, N.3    Madamet, M.4    Parzy, D.5    Nivez, M.P.6
  • 25
    • 0032821504 scopus 로고    scopus 로고
    • The Leishmania mexicana proteasone
    • Robertson CD. The Leishmania mexicana proteasone. Mol Biochem Parasitol 1999; 103(1): 49-60.
    • (1999) Mol Biochem Parasitol , vol.103 , Issue.1 , pp. 49-60
    • Robertson, C.D.1
  • 26
    • 3943107573 scopus 로고    scopus 로고
    • Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints
    • Sancar A, Lindsey-Boltz LA, Unsal-Kacmaz K, Linn S. Molecular mechanisms of mammalian DNA repair and the DNA damage checkpoints. Annu Rev Biochem 2004; 73: 39-85.
    • (2004) Annu Rev Biochem , vol.73 , pp. 39-85
    • Sancar, A.1    Lindsey-Boltz, L.A.2    Unsal-Kacmaz, K.3    Linn, S.4
  • 27
    • 0028707690 scopus 로고
    • Protein kinases and cell cycle control
    • Pines J. Protein kinases and cell cycle control. Semin Cell Biol 1994; 5(6): 399-408.
    • (1994) Semin Cell Biol , vol.5 , Issue.6 , pp. 399-408
    • Pines, J.1
  • 28
    • 0842324788 scopus 로고    scopus 로고
    • Recycling the cell cycle: Cyclins revisited
    • Murray AW. Recycling the cell cycle: Cyclins revisited. Cell 2004; 116(2): 221-34.
    • (2004) Cell , vol.116 , Issue.2 , pp. 221-234
    • Murray, A.W.1
  • 29
    • 0030724422 scopus 로고    scopus 로고
    • Hershko A Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr Opin Cell Biol 1997; 9(6): 788-99.
    • Hershko A Roles of ubiquitin-mediated proteolysis in cell cycle control. Curr Opin Cell Biol 1997; 9(6): 788-99.
  • 30
    • 25444444192 scopus 로고    scopus 로고
    • CAK-Cyclin-dependent Activating Kinase: A key kinase in cell cycle control and a target for drugs?
    • Lolli G, Johnson LN. CAK-Cyclin-dependent Activating Kinase: A key kinase in cell cycle control and a target for drugs? Cell Cycle 2005; 4(4): 572-7.
    • (2005) Cell Cycle , vol.4 , Issue.4 , pp. 572-577
    • Lolli, G.1    Johnson, L.N.2
  • 31
    • 0346882614 scopus 로고    scopus 로고
    • Weel-dependent mechanisms required for coordination of cell growth and cell division
    • Kellogg DR. Weel-dependent mechanisms required for coordination of cell growth and cell division. J Cell Sci 2003; 116(Pt 24): 4883-90.
    • (2003) J Cell Sci , vol.116 , Issue.PART 24 , pp. 4883-4890
    • Kellogg, D.R.1
  • 32
    • 33750618926 scopus 로고    scopus 로고
    • Mitotic phosphatases: No longer silent partners
    • Trinkle-Mulcahy L, Lamond AI. Mitotic phosphatases: No longer silent partners. Curr Opin Cell Biol 2006; 18(6): 623-31.
    • (2006) Curr Opin Cell Biol , vol.18 , Issue.6 , pp. 623-631
    • Trinkle-Mulcahy, L.1    Lamond, A.I.2
  • 33
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: Engines, clocks, and microprucessors
    • Morgan DO. Cyclin-dependent kinases: Engines, clocks, and microprucessors. Annu Rev Cell Dev Bid 1997; 13: 261-91.
    • (1997) Annu Rev Cell Dev Bid , vol.13 , pp. 261-291
    • Morgan, D.O.1
  • 34
    • 0033659982 scopus 로고    scopus 로고
    • Cell cycle regulation in Schizosaccharomyces pombe
    • Moser BA, Russell P. Cell cycle regulation in Schizosaccharomyces pombe. Curr Opin Microbiol 2000; 3(6): 631-6.
    • (2000) Curr Opin Microbiol , vol.3 , Issue.6 , pp. 631-636
    • Moser, B.A.1    Russell, P.2
  • 35
    • 0031737085 scopus 로고    scopus 로고
    • Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae
    • Mendenhall MD, Hodge AE. Regulation of Cdc28 cyclin-dependent protein kinase activity during the cell cycle of the yeast Saccharomyces cerevisiae. Microbiol Mol Biol Rev 1998; 62(4): 1191-243.
    • (1998) Microbiol Mol Biol Rev , vol.62 , Issue.4 , pp. 1191-1243
    • Mendenhall, M.D.1    Hodge, A.E.2
  • 36
    • 25444512182 scopus 로고    scopus 로고
    • Comparative analysis of the kinomes of three pathogenic trypanosomatids: Leishmania major, Trypanosoma brucei and Trypanosoma cruzi
    • Parsons M, Worthey EA, Ward PN, Mottram JC. Comparative analysis of the kinomes of three pathogenic trypanosomatids: Leishmania major, Trypanosoma brucei and Trypanosoma cruzi. BMC Genomics 2005; 6: 127.
    • (2005) BMC Genomics , vol.6 , pp. 127
    • Parsons, M.1    Worthey, E.A.2    Ward, P.N.3    Mottram, J.C.4
  • 37
    • 9144258616 scopus 로고    scopus 로고
    • Protein kinases of the human malaria parasite Plasmodium falciparum: The kinome of a divergent eukaryote
    • Ward P, Equinet L, Packer J, Doerig C. Protein kinases of the human malaria parasite Plasmodium falciparum: The kinome of a divergent eukaryote. BMC Genomics 2004; 5(1): 79.
    • (2004) BMC Genomics , vol.5 , Issue.1 , pp. 79
    • Ward, P.1    Equinet, L.2    Packer, J.3    Doerig, C.4
  • 38
    • 0037021406 scopus 로고    scopus 로고
    • Cyclin-dependent kinase homologues of Plasmodium falciparum
    • Doerig C, Endicott J, Chakrabarti D. Cyclin-dependent kinase homologues of Plasmodium falciparum. Int J Parasitol 2002; 32(13): 1575-85
    • (2002) Int J Parasitol , vol.32 , Issue.13 , pp. 1575-1585
    • Doerig, C.1    Endicott, J.2    Chakrabarti, D.3
  • 39
    • 34047109097 scopus 로고    scopus 로고
    • Cell cycle regulation in Trynanosoma brucei
    • Hammarion TC. Cell cycle regulation in Trynanosoma brucei. Mol Biochem Parasitol 2007; 153(1): 1-8.
    • (2007) Mol Biochem Parasitol , vol.153 , Issue.1 , pp. 1-8
    • Hammarion, T.C.1
  • 40
    • 14044264288 scopus 로고    scopus 로고
    • The developmental cell biology of Trynanosoma brucei
    • Matthews KR. The developmental cell biology of Trynanosoma brucei. J Cell Sci 2005; 118(Pt 2): 283-90.
    • (2005) J Cell Sci , vol.118 , Issue.PART 2 , pp. 283-290
    • Matthews, K.R.1
  • 41
    • 0032562572 scopus 로고    scopus 로고
    • The crk3 gene of Leishmania mexicana encodes a stage-regulated cdc2-related histone H1 kinase that associates with p12
    • Grant KM, Hassan P, Anderson JS, Mottram JC. The crk3 gene of Leishmania mexicana encodes a stage-regulated cdc2-related histone H1 kinase that associates with p12. J Biol Chem 1998; 273(17): 10153-9.
    • (1998) J Biol Chem , vol.273 , Issue.17 , pp. 10153-10159
    • Grant, K.M.1    Hassan, P.2    Anderson, J.S.3    Mottram, J.C.4
  • 42
    • 0029830610 scopus 로고    scopus 로고
    • Gene disruptions indicate an essential function for the LmmCRK1 cdc2-related kinase of Leishmnania mexicana
    • Mottram JC, McCready BP, Brown KG, Grant KM. Gene disruptions indicate an essential function for the LmmCRK1 cdc2-related kinase of Leishmnania mexicana. Mol Microbiol 1996; 22(3): 573-83.
    • (1996) Mol Microbiol , vol.22 , Issue.3 , pp. 573-583
    • Mottram, J.C.1    McCready, B.P.2    Brown, K.G.3    Grant, K.M.4
  • 43
    • 0029114836 scopus 로고
    • A family of trypanosome cdc2-related protein kinases
    • Mottram JC, Smith G. A family of trypanosome cdc2-related protein kinases. Gene 1995; 162(1): 147-52.
    • (1995) Gene , vol.162 , Issue.1 , pp. 147-152
    • Mottram, J.C.1    Smith, G.2
  • 44
    • 0032521213 scopus 로고    scopus 로고
    • Cloning of a cdc2-related protein kinase from Trypanosoma cruzi that interacts with mammalian cyclins
    • Gomez EB, Kornblihtt, AR, Tellez-Inon MT. Cloning of a cdc2-related protein kinase from Trypanosoma cruzi that interacts with mammalian cyclins. Mol Biochem Parasitol 1998; 91(2): 337-51.
    • (1998) Mol Biochem Parasitol , vol.91 , Issue.2 , pp. 337-351
    • Gomez, E.B.1    Kornblihtt, A.R.2    Tellez-Inon, M.T.3
  • 45
    • 0035091541 scopus 로고    scopus 로고
    • Characterization of the Trypanosoma cruzi Cdc2p-related protein kinase 1 and identification of three novel associating cyclins
    • Gomez EB, Samon ML, Laria S, Engel TC, Swindle J, Eisen H, et al. Characterization of the Trypanosoma cruzi Cdc2p-related protein kinase 1 and identification of three novel associating cyclins. Mol Biochem Parasitol 2001; 113(1): 97-108.
    • (2001) Mol Biochem Parasitol , vol.113 , Issue.1 , pp. 97-108
    • Gomez, E.B.1    Samon, M.L.2    Laria, S.3    Engel, T.C.4    Swindle, J.5    Eisen, H.6
  • 46
    • 0036065205 scopus 로고    scopus 로고
    • Cyclin-dependent kinase TPK2 is a critical cell cycle regulator in Toxoplasma gondii
    • Khan F, Tang J, Qin CL, Kim K. Cyclin-dependent kinase TPK2 is a critical cell cycle regulator in Toxoplasma gondii. Mol Microbiol 2002; 45(2): 321-32.
    • (2002) Mol Microbiol , vol.45 , Issue.2 , pp. 321-332
    • Khan, F.1    Tang, J.2    Qin, C.L.3    Kim, K.4
  • 47
    • 0035965775 scopus 로고    scopus 로고
    • TaCRK3 encodes a novel Theileria annulata protein kinase with motifs characteristic of me family of eukaryotic cyclin dependent kinases: A comparative analysis of its expression with TaCRK2 during the parasite life cycle
    • Kinnaird J, Logan M, Tait A, Langsicy G. TaCRK3 encodes a novel Theileria annulata protein kinase with motifs characteristic of me family of eukaryotic cyclin dependent kinases: A comparative analysis of its expression with TaCRK2 during the parasite life cycle. Gene 2001; 279(2): 1271-35.
    • (2001) Gene , vol.279 , Issue.2 , pp. 1271-1335
    • Kinnaird, J.1    Logan, M.2    Tait, A.3    Langsicy, G.4
  • 48
    • 1942477610 scopus 로고    scopus 로고
    • EtCRK2, a cyclin-dependeni kinase gene expressed during the sexual and asexual phases of the Eimeria tenelia life cycle
    • Kinnnird JH, Bumstend JM, Mann DJ, Rynn R, Shirley MW, Shiels BR, et al. EtCRK2, a cyclin-dependeni kinase gene expressed during the sexual and asexual phases of the Eimeria tenelia life cycle. Int J Parasitol 2004; 34(6): 683-92.
    • (2004) Int J Parasitol , vol.34 , Issue.6 , pp. 683-692
    • Kinnnird, J.H.1    Bumstend, J.M.2    Mann, D.J.3    Rynn, R.4    Shirley, M.W.5    Shiels, B.R.6
  • 49
    • 0029802680 scopus 로고    scopus 로고
    • The isolation and characterization of genomic and cDNA clones coding for a cdc2-rela-ted Own (ThCRK2) from the bovine protozoan parasite Theileria
    • Kinnaird JH, Logan M, Kirvar E, Tait A, Carrington M. The isolation and characterization of genomic and cDNA clones coding for a cdc2-rela-ted Own (ThCRK2) from the bovine protozoan parasite Theileria. Mol Microbiol 1996; 22(2): 293-302.
    • (1996) Mol Microbiol , vol.22 , Issue.2 , pp. 293-302
    • Kinnaird, J.H.1    Logan, M.2    Kirvar, E.3    Tait, A.4    Carrington, M.5
  • 50
    • 0035815349 scopus 로고    scopus 로고
    • The CRK3 protein kinase is essential for cell cycle progression of Leishmania mexicana
    • Hassan P, Fergusson D, Grant KM, Mottram X. The CRK3 protein kinase is essential for cell cycle progression of Leishmania mexicana. Mol Biochem Parasitol 2001; 113(2): 189-98.
    • (2001) Mol Biochem Parasitol , vol.113 , Issue.2 , pp. 189-198
    • Hassan, P.1    Fergusson, D.2    Grant, K.M.3    Mottram, X.4
  • 51
    • 0034708779 scopus 로고    scopus 로고
    • Isolation of Trypanosoma brucei CYC2 arid CYC3 cyclin genes by rescue of a yeast G(1) cyclin mutant. Functional characterization of CYC2
    • Van Hellemond JJ, Neuville P, Schwarz RT, Matthews KR, Mottram JC. Isolation of Trypanosoma brucei CYC2 arid CYC3 cyclin genes by rescue of a yeast G(1) cyclin mutant. Functional characterization of CYC2. J Biol Chem 2000; 275(12): 8315-23.
    • (2000) J Biol Chem , vol.275 , Issue.12 , pp. 8315-8323
    • Van Hellemond, J.J.1    Neuville, P.2    Schwarz, R.T.3    Matthews, K.R.4    Mottram, J.C.5
  • 52
    • 0029862051 scopus 로고    scopus 로고
    • Li JL, Robson KJ, Chen JL, Targett GA, Baker DA. Pfmrk, n MO15-related protein kinase from Plasmodium falciparum. Gene cloning, sequence, stage-specific expression and chromosome localization. Eur J Biochem 1996; 241(3): 805-13.
    • Li JL, Robson KJ, Chen JL, Targett GA, Baker DA. Pfmrk, n MO15-related protein kinase from Plasmodium falciparum. Gene cloning, sequence, stage-specific expression and chromosome localization. Eur J Biochem 1996; 241(3): 805-13.
  • 53
    • 0028224015 scopus 로고
    • Isolation and expression of a gene specifying a cdc2-like protein kinase from the human malaria parasite Plasmodium falciparum
    • Ross-Macdonald PB, Graeser R, Kappes B, Franklin R, Williamson DH. Isolation and expression of a gene specifying a cdc2-like protein kinase from the human malaria parasite Plasmodium falciparum. Eur J Biochem 1994; 220(3): 693-701.
    • (1994) Eur J Biochem , vol.220 , Issue.3 , pp. 693-701
    • Ross-Macdonald, P.B.1    Graeser, R.2    Kappes, B.3    Franklin, R.4    Williamson, D.H.5
  • 54
    • 0030200306 scopus 로고    scopus 로고
    • Mechanisms of activation of the cdc2-related kinase PfPK5 from Plasmodium falciparum
    • Graeser R, Franklin RM, Kappes B. Mechanisms of activation of the cdc2-related kinase PfPK5 from Plasmodium falciparum. Mol Biochem Parasitol 1996; 79(1): 125-7.
    • (1996) Mol Biochem Parasitol , vol.79 , Issue.1 , pp. 125-127
    • Graeser, R.1    Franklin, R.M.2    Kappes, B.3
  • 55
    • 0036710767 scopus 로고    scopus 로고
    • Pharmacological inhibitors of cyclin-dependent kinases
    • Knockaert M, Greengard P, Meijer L. Pharmacological inhibitors of cyclin-dependent kinases. Trends Pharmacol Sci 2002; 23(9): 417-25.
    • (2002) Trends Pharmacol Sci , vol.23 , Issue.9 , pp. 417-425
    • Knockaert, M.1    Greengard, P.2    Meijer, L.3
  • 56
    • 0034654447 scopus 로고    scopus 로고
    • Cyclin H activation and drug susceptibility of the Pfmrk cyclin dependent protein kinase from Plasmodium falciparum
    • Waters NC, Woodard CL, Prigge ST. Cyclin H activation and drug susceptibility of the Pfmrk cyclin dependent protein kinase from Plasmodium falciparum. Mol Biochem Parasiiol 2000; 107(1): 45-55.
    • (2000) Mol Biochem Parasiiol , vol.107 , Issue.1 , pp. 45-55
    • Waters, N.C.1    Woodard, C.L.2    Prigge, S.T.3
  • 57
    • 0030581694 scopus 로고    scopus 로고
    • Plasmodium falcinum protein kinase 5 and the malarial nuclear division cycles
    • Graeser R, Wernli B, Franklin RM, Kappes B. Plasmodium falcinum protein kinase 5 and the malarial nuclear division cycles. Mol Biochem Parasitol 1996; 82(1): 37-49.
    • (1996) Mol Biochem Parasitol , vol.82 , Issue.1 , pp. 37-49
    • Graeser, R.1    Wernli, B.2    Franklin, R.M.3    Kappes, B.4
  • 58
    • 33846827044 scopus 로고    scopus 로고
    • Studies on cell-cycle synchronization in the asexual erythrocytic stages of Plasmodium falciparum
    • Naughton JA, Bell A. Studies on cell-cycle synchronization in the asexual erythrocytic stages of Plasmodium falciparum. Parasitology 2007; 134(Pt 3): 331-7.
    • (2007) Parasitology , vol.134 , Issue.PART 3 , pp. 331-337
    • Naughton, J.A.1    Bell, A.2
  • 59
    • 0035427503 scopus 로고    scopus 로고
    • Structure-activithy relationships and inhibitory effects of various purine derivatives on the in vitro growth of Plasmodium falciparum
    • Harmse L, van Zyl R, Gray N, Schultz P, Leclerc S, Meijer L, et al. Structure-activithy relationships and inhibitory effects of various purine derivatives on the in vitro growth of Plasmodium falciparum. Biochem Pharmacol 2001; 62(3): 341-8.
    • (2001) Biochem Pharmacol , vol.62 , Issue.3 , pp. 341-348
    • Harmse, L.1    van Zyl, R.2    Gray, N.3    Schultz, P.4    Leclerc, S.5    Meijer, L.6
  • 60
    • 0242710962 scopus 로고    scopus 로고
    • Structures of P. falciparum PfPK5 test the CDK regulation paradigm and suggest mechanisms of small molecule inhibition
    • Holton S, Merckx A, Burgess D, Doerig C, Noble M, Endicott J. Structures of P. falciparum PfPK5 test the CDK regulation paradigm and suggest mechanisms of small molecule inhibition. Structure 2003; 11(11): 1329-37.
    • (2003) Structure , vol.11 , Issue.11 , pp. 1329-1337
    • Holton, S.1    Merckx, A.2    Burgess, D.3    Doerig, C.4    Noble, M.5    Endicott, J.6
  • 61
    • 3342936476 scopus 로고    scopus 로고
    • Inhibitors of Leishmania mexicana CRK3 cyclin-dependent kinase: Chemical library screen and antileishmanial activity
    • Grant KM, Dunion MH, Yardley V, Skaltsounis AL, Marko D, Eisenbrand G, et al. Inhibitors of Leishmania mexicana CRK3 cyclin-dependent kinase: Chemical library screen and antileishmanial activity. Antimicrob Agents Chemother 2004; 48(8): 3033-42.
    • (2004) Antimicrob Agents Chemother , vol.48 , Issue.8 , pp. 3033-3042
    • Grant, K.M.1    Dunion, M.H.2    Yardley, V.3    Skaltsounis, A.L.4    Marko, D.5    Eisenbrand, G.6
  • 62
    • 0035808457 scopus 로고    scopus 로고
    • Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors?
    • Leclerc S, Garnier M, Hoessel R, Marko D, Bibb JA, Snyder GL, et al. Indirubins inhibit glycogen synthase kinase-3 beta and CDK5/p25, two protein kinases involved in abnormal tau phosphorylation in Alzheimer's disease. A property common to most cyclin-dependent kinase inhibitors? J Biol Chem 2001; 276(1): 251-60.
    • (2001) J Biol Chem , vol.276 , Issue.1 , pp. 251-260
    • Leclerc, S.1    Garnier, M.2    Hoessel, R.3    Marko, D.4    Bibb, J.A.5    Snyder, G.L.6
  • 63
    • 0033128165 scopus 로고    scopus 로고
    • Indirubin, the active constituent of a Chinese antileukaemia medicine, inhibits cyclin-dependent kinases
    • Hoessel R, Leclerc S, Endicott JA, Nobel ME, Lawrie A, Tunnah P, et al. Indirubin, the active constituent of a Chinese antileukaemia medicine, inhibits cyclin-dependent kinases. Nat Cell Biol 1999; 1(1): 60-7.
    • (1999) Nat Cell Biol , vol.1 , Issue.1 , pp. 60-67
    • Hoessel, R.1    Leclerc, S.2    Endicott, J.A.3    Nobel, M.E.4    Lawrie, A.5    Tunnah, P.6
  • 64
    • 44349138571 scopus 로고    scopus 로고
    • Wells C, McNae I, Walkinshaw M, Westwood NJ, Grant KM. The selective biological activity of indirubin-based inhibitors: Applications in parasitology. in: Meijer L, Guyard N, Skaltsounis LA, Eisenbrand G Eds, Indirubin, the red shade of indigo. Life in Progress ed. Roscoff, France: Station Biologique 2006; 259-67.
    • Wells C, McNae I, Walkinshaw M, Westwood NJ, Grant KM. The selective biological activity of indirubin-based inhibitors: Applications in parasitology. in: Meijer L, Guyard N, Skaltsounis LA, Eisenbrand G Eds, Indirubin, the red shade of indigo. Life in Progress ed. Roscoff, France: Station Biologique 2006; 259-67.
  • 65
    • 0034988970 scopus 로고    scopus 로고
    • Inhibitor binding to active and inactive CDK2: The crystal structure of CDK2-cyclin A/indirubin-5-sulphonate
    • Davies TG, Tunnah P, Meijer L, Marko D, Eisenbrand G, Endicott JA, et al. Inhibitor binding to active and inactive CDK2: The crystal structure of CDK2-cyclin A/indirubin-5-sulphonate. Structure 2001; 9(5): 389-97.
    • (2001) Structure , vol.9 , Issue.5 , pp. 389-397
    • Davies, T.G.1    Tunnah, P.2    Meijer, L.3    Marko, D.4    Eisenbrand, G.5    Endicott, J.A.6
  • 66
    • 24944573556 scopus 로고    scopus 로고
    • Structural model of the, Plasmodium CDK, Pfmrk, a novel target for malaria therapeutics
    • Peng Y, Keenan SM, Welsh WJ. Structural model of the, Plasmodium CDK, Pfmrk, a novel target for malaria therapeutics. J Mol Graph Model 2005; 24(1): 72-80.
    • (2005) J Mol Graph Model , vol.24 , Issue.1 , pp. 72-80
    • Peng, Y.1    Keenan, S.M.2    Welsh, W.J.3
  • 67
    • 0035814077 scopus 로고    scopus 로고
    • Design and synthedsis of Pfmrk inhibitors as potential antimalarial agents
    • Xiao Z, Waters NC, Woodard CL, Li Z, Li PK. Design and synthedsis of Pfmrk inhibitors as potential antimalarial agents. Bioorg Med Chem Lett 2001; 11(21): 2875-8.
    • (2001) Bioorg Med Chem Lett , vol.11 , Issue.21 , pp. 2875-2878
    • Xiao, Z.1    Waters, N.C.2    Woodard, C.L.3    Li, Z.4    Li, P.K.5
  • 68
    • 12744281184 scopus 로고    scopus 로고
    • Rational inhibitor design and iterative screening in the identification of selective plasmodial cyclin dependent kinase inhibitors
    • Keenan SM, Geyer JA, Welsh WJ, Prigge ST, Waters NC. Rational inhibitor design and iterative screening in the identification of selective plasmodial cyclin dependent kinase inhibitors. Comb Chem High Throughput Screen 2005; 8(1): 27-38.
    • (2005) Comb Chem High Throughput Screen , vol.8 , Issue.1 , pp. 27-38
    • Keenan, S.M.1    Geyer, J.A.2    Welsh, W.J.3    Prigge, S.T.4    Waters, N.C.5
  • 69
    • 0034859101 scopus 로고    scopus 로고
    • The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling
    • Grimes CA, Jope RS. The multifaceted roles of glycogen synthase kinase 3beta in cellular signaling. Prog Neurobiol 2001; 65(4): 391-426.
    • (2001) Prog Neurobiol , vol.65 , Issue.4 , pp. 391-426
    • Grimes, C.A.1    Jope, R.S.2
  • 70
    • 0032533225 scopus 로고    scopus 로고
    • Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization
    • Diehl JA, Cheng M, Roussel MF, Sherr CJ. Glycogen synthase kinase-3beta regulates cyclin D1 proteolysis and subcellular localization. Genes Dev 1998; 12(22): 3499-511.
    • (1998) Genes Dev , vol.12 , Issue.22 , pp. 3499-3511
    • Diehl, J.A.1    Cheng, M.2    Roussel, M.F.3    Sherr, C.J.4
  • 71
    • 0037442990 scopus 로고    scopus 로고
    • A role for glycogen synthase kinase-3 in mitotic spindle dynamics and chromosome alignment
    • Wakefield JG, Stephens DJ, Tavare JM. A role for glycogen synthase kinase-3 in mitotic spindle dynamics and chromosome alignment. J Cell Sci 2003; 116(Pt 4): 637-46.
    • (2003) J Cell Sci , vol.116 , Issue.PART 4 , pp. 637-646
    • Wakefield, J.G.1    Stephens, D.J.2    Tavare, J.M.3
  • 73
    • 6344226513 scopus 로고    scopus 로고
    • Regulation of flagellar assembly by glycogen synthase kinase 3 in Chlamydomonas reinhardtii
    • Wilson NF, Lefebvre PA. Regulation of flagellar assembly by glycogen synthase kinase 3 in Chlamydomonas reinhardtii. Eukaryot Cell 2004; 3(5): 1307-19.
    • (2004) Eukaryot Cell , vol.3 , Issue.5 , pp. 1307-1319
    • Wilson, N.F.1    Lefebvre, P.A.2
  • 74
    • 3042635178 scopus 로고    scopus 로고
    • GSK3 inhibitors: Development and therapeutic potential
    • Cohen P, Goedert M. GSK3 inhibitors: Development and therapeutic potential. Nat Rev Drug Discov 2004; 3(6): 479-87.
    • (2004) Nat Rev Drug Discov , vol.3 , Issue.6 , pp. 479-487
    • Cohen, P.1    Goedert, M.2
  • 75
    • 12144287677 scopus 로고    scopus 로고
    • Plasmodium falciparum glycogen synthase kinase-3: Molecular model, expression, intracellular localisation and selective inhibitors
    • Droucheau E, Primot A, Thomas V, Mattei D, Knockaert M, Richardson C, et al. Plasmodium falciparum glycogen synthase kinase-3: molecular model, expression, intracellular localisation and selective inhibitors. Biochim Biophys Acta 2004; 1697(1-2): 191-96.
    • (2004) Biochim Biophys Acta , vol.1697 , Issue.1-2 , pp. 191-196
    • Droucheau, E.1    Primot, A.2    Thomas, V.3    Mattei, D.4    Knockaert, M.5    Richardson, C.6
  • 76
    • 0032101958 scopus 로고    scopus 로고
    • Cloning and in vitro expression of TPK3, a Toxoplasma gondii homologue of shaggy/glycogen synthase kinase-3 kinases
    • Qin CL, Tang J, Kim K. Cloning and in vitro expression of TPK3, a Toxoplasma gondii homologue of shaggy/glycogen synthase kinase-3 kinases. Mol Biochem Parasitol 1998; 93(2): 273-83.
    • (1998) Mol Biochem Parasitol , vol.93 , Issue.2 , pp. 273-283
    • Qin, C.L.1    Tang, J.2    Kim, K.3
  • 77
    • 0242551545 scopus 로고    scopus 로고
    • The cellular geography of aurora kinases
    • Carmena M, Earnshaw WC. The cellular geography of aurora kinases. Nat Rev Mol Cell Biol 2003; 4(11): 842-54.
    • (2003) Nat Rev Mol Cell Biol , vol.4 , Issue.11 , pp. 842-854
    • Carmena, M.1    Earnshaw, W.C.2
  • 78
    • 31544432841 scopus 로고    scopus 로고
    • Dynamic localization and functional implications of Aurora-C kinase during male mouse meiosis
    • Tang CJ, Lin CY, Tang TK. Dynamic localization and functional implications of Aurora-C kinase during male mouse meiosis. Dev Biol 2006- 290(2): 398-410.
    • (2006) Dev Biol , vol.290 , Issue.2 , pp. 398-410
    • Tang, C.J.1    Lin, C.Y.2    Tang, T.K.3
  • 79
    • 0347985493 scopus 로고    scopus 로고
    • Kufer TA: Nigg EA, Sillje HH. Regulation of Aurora-A kinase on the mitotic spindle. Chromosoma, 2003; 112(4): 159-63.
    • Kufer TA: Nigg EA, Sillje HH. Regulation of Aurora-A kinase on the mitotic spindle. Chromosoma, 2003; 112(4): 159-63.
  • 80
    • 0035854776 scopus 로고    scopus 로고
    • Chromatin-associated protein phosphatase 1 regulates aurora-B -and histone H3 phosphorylation
    • Murnion ME, Adams RR, Callister DM, Allis CD, Earnshaw WC, Swedlow JR. Chromatin-associated protein phosphatase 1 regulates aurora-B -and histone H3 phosphorylation. J Biol Chem 2001; 276(28): 26656-65.
    • (2001) J Biol Chem , vol.276 , Issue.28 , pp. 26656-26665
    • Murnion, M.E.1    Adams, R.R.2    Callister, D.M.3    Allis, C.D.4    Earnshaw, W.C.5    Swedlow, J.R.6
  • 81
    • 0035984896 scopus 로고    scopus 로고
    • Castro A, Arlot-Bonnemains Y, Vigneron S, Labbe JC, Prigent C, Lorca T. APC/Fizzy-Related targets Aurora-A kinase for proteolysis. EMBO Rep 2002; 3(5): 457-62.
    • Castro A, Arlot-Bonnemains Y, Vigneron S, Labbe JC, Prigent C, Lorca T. APC/Fizzy-Related targets Aurora-A kinase for proteolysis. EMBO Rep 2002; 3(5): 457-62.
  • 83
    • 2342639645 scopus 로고    scopus 로고
    • VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo
    • Harrington EA, Bebbington D, Moore J, Rasmussen RK, Ajose-Adeogun AO, Nakayama T, et al. VX-680, a potent and selective small-molecule inhibitor of the Aurora kinases, suppresses tumor growth in vivo. Nat Med 2004; 10(3): 262-7.
    • (2004) Nat Med , vol.10 , Issue.3 , pp. 262-267
    • Harrington, E.A.1    Bebbington, D.2    Moore, J.3    Rasmussen, R.K.4    Ajose-Adeogun, A.O.5    Nakayama, T.6
  • 84
    • 0013057087 scopus 로고    scopus 로고
    • Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores
    • Ditchfield C, Johnson VL, Tighe A, Ellston R, Haworth C, Johnson T, et al. Aurora B couples chromosome alignment with anaphase by targeting BubR1, Mad2, and Cenp-E to kinetochores. J Cell Biol 2003; 161(2): 267-80.
    • (2003) J Cell Biol , vol.161 , Issue.2 , pp. 267-280
    • Ditchfield, C.1    Johnson, V.L.2    Tighe, A.3    Ellston, R.4    Haworth, C.5    Johnson, T.6
  • 85
    • 33646935040 scopus 로고    scopus 로고
    • An aurora kinase homologue is involved in regulating both mitosis and cytokinesis in Trypanosoma brucei
    • Tu X, Kumar P, Li Z, Wang CC. An aurora kinase homologue is involved in regulating both mitosis and cytokinesis in Trypanosoma brucei. J Biol Chem 2006; 281(14): 9677-87.
    • (2006) J Biol Chem , vol.281 , Issue.14 , pp. 9677-9687
    • Tu, X.1    Kumar, P.2    Li, Z.3    Wang, C.C.4
  • 86
    • 0035963488 scopus 로고    scopus 로고
    • Identification and cloning of Lmairk, a member of the Aurora/Ipl1p protein kinase family, from the human protozoan parasite Leishmania
    • Siman-Tov MM, Ivens AC, Jaffe CL. Identification and cloning of Lmairk, a member of the Aurora/Ipl1p protein kinase family, from the human protozoan parasite Leishmania. Biochim Biophys Acta 2001; 1519(3): 241-5.
    • (2001) Biochim Biophys Acta , vol.1519 , Issue.3 , pp. 241-245
    • Siman-Tov, M.M.1    Ivens, A.C.2    Jaffe, C.L.3
  • 87
    • 33746268564 scopus 로고    scopus 로고
    • Changing roles of aurora-B kinase in two life cycle stages of Trypanosoma brucei
    • Li Z, Wang CC. Changing roles of aurora-B kinase in two life cycle stages of Trypanosoma brucei. Eukaryot Cell 2006; 5(7): 1026-35
    • (2006) Eukaryot Cell , vol.5 , Issue.7 , pp. 1026-1035
    • Li, Z.1    Wang, C.C.2
  • 88
    • 33645316142 scopus 로고    scopus 로고
    • Targeting polo-like kinase 1 for cancer therapy
    • Strebhardt K, Ullrich A. Targeting polo-like kinase 1 for cancer therapy. Nat Rev Cancer 2006; 6(4): 321-30.
    • (2006) Nat Rev Cancer , vol.6 , Issue.4 , pp. 321-330
    • Strebhardt, K.1    Ullrich, A.2
  • 89
    • 34249286656 scopus 로고    scopus 로고
    • Targeting the ubiquitin-proteasome pathway in cancer therapy. Anticancer Agents
    • Ishii Y, Waxman S, Germain D. Targeting the ubiquitin-proteasome pathway in cancer therapy. Anticancer Agents, Med Chem 2007; 7(3): 359-65.
    • (2007) Med Chem , vol.7 , Issue.3 , pp. 359-365
    • Ishii, Y.1    Waxman, S.2    Germain, D.3
  • 90
    • 0031743063 scopus 로고    scopus 로고
    • Polo-like kinases: Positive regulators of cell division from start to finish
    • Nigg EA. Polo-like kinases: Positive regulators of cell division from start to finish. Curr Opin Cell Biol 1998; 10(6): 776-83.
    • (1998) Curr Opin Cell Biol , vol.10 , Issue.6 , pp. 776-783
    • Nigg, E.A.1
  • 91
    • 33746869956 scopus 로고    scopus 로고
    • Polo-like kinase 1: Target and regulator of anaphase-promoting complex/cyclosome-dependent proteolysis
    • Eckerdt F, Strebhardt K. Polo-like kinase 1: Target and regulator of anaphase-promoting complex/cyclosome-dependent proteolysis. Cancer Res 2006; 66(14): 6895-8.
    • (2006) Cancer Res , vol.66 , Issue.14 , pp. 6895-6898
    • Eckerdt, F.1    Strebhardt, K.2
  • 92
    • 33745914956 scopus 로고    scopus 로고
    • Polo-like kinase Cdc5 controls the local activation of Rho1 to promote cytokinesis
    • Yoshida S, Kono K, Lowery DM, Bartolini S, Yaffe MB, Ohya Y, et al. Polo-like kinase Cdc5 controls the local activation of Rho1 to promote cytokinesis. Science 2006; 313(5783): 108-11.
    • (2006) Science , vol.313 , Issue.5783 , pp. 108-111
    • Yoshida, S.1    Kono, K.2    Lowery, D.M.3    Bartolini, S.4    Yaffe, M.B.5    Ohya, Y.6
  • 93
    • 30944445981 scopus 로고    scopus 로고
    • Dissociation of cytokinesis initiation from mitotic control in a eukaryote
    • Kumar P, Wang CC. Dissociation of cytokinesis initiation from mitotic control in a eukaryote. Eukaryot Cell 2006; 5(1): 92-102.
    • (2006) Eukaryot Cell , vol.5 , Issue.1 , pp. 92-102
    • Kumar, P.1    Wang, C.C.2
  • 94
    • 34547854325 scopus 로고    scopus 로고
    • Trypanosoma brucei Polo-like kinase is essential for basal body duplication, kDNA segregation and cytokinesis
    • Hammarton TC, Kramer S, Tetley L, Boshart M, Mottram JC. Trypanosoma brucei Polo-like kinase is essential for basal body duplication, kDNA segregation and cytokinesis. Mol Microbiol 2007; 65(5): 1229-48.
    • (2007) Mol Microbiol , vol.65 , Issue.5 , pp. 1229-1248
    • Hammarton, T.C.1    Kramer, S.2    Tetley, L.3    Boshart, M.4    Mottram, J.C.5
  • 95
    • 33748336875 scopus 로고    scopus 로고
    • The ubiquitin-proteasome pathway in cell cycle control
    • Reed SI. The ubiquitin-proteasome pathway in cell cycle control. Results Probl Cell Differ 2006; 42: 147-81.
    • (2006) Results Probl Cell Differ , vol.42 , pp. 147-181
    • Reed, S.I.1
  • 96
    • 33747517230 scopus 로고    scopus 로고
    • The proteasome:a novel target for anticancer therapy
    • Montagut C, Rovira A, Albanell J. The proteasome:a novel target for anticancer therapy. Clin Transl Oncol 2006; 8(5): 313-7.
    • (2006) Clin Transl Oncol , vol.8 , Issue.5 , pp. 313-317
    • Montagut, C.1    Rovira, A.2    Albanell, J.3
  • 97
    • 22444449129 scopus 로고    scopus 로고
    • The proteasome inhibitor MLN-273 blocks exoerythrocytic and erythrocytic development of Plasmodium parasites
    • Lindenthal C, Weich N, Chia YS, Heussler V, Klinkert MQ. The proteasome inhibitor MLN-273 blocks exoerythrocytic and erythrocytic development of Plasmodium parasites. Parasitology 2005; 131(Pt 1): 37-44.
    • (2005) Parasitology , vol.131 , Issue.PART 1 , pp. 37-44
    • Lindenthal, C.1    Weich, N.2    Chia, Y.S.3    Heussler, V.4    Klinkert, M.Q.5
  • 99
    • 34548136096 scopus 로고    scopus 로고
    • An integrated computational approach to the phenomenon of potent and selective inhibition of aurora kinases B and C by a series of 7-substituted indirubins
    • Myrianthopoulos V, Magiatis P, Ferandin Y, Skaltsounis AL, Meijer L, Mikros E. An integrated computational approach to the phenomenon of potent and selective inhibition of aurora kinases B and C by a series of 7-substituted indirubins. J Med Chem 2007; 50(17): 4027-37.
    • (2007) J Med Chem , vol.50 , Issue.17 , pp. 4027-4037
    • Myrianthopoulos, V.1    Magiatis, P.2    Ferandin, Y.3    Skaltsounis, A.L.4    Meijer, L.5    Mikros, E.6
  • 100
    • 22144457954 scopus 로고    scopus 로고
    • Understanding and modulating cyclin-dependent kinase inhibitor specificity: Molecular modeling and biochemical evaluation of pyrazolopyrimidinones as CDK2/cyclin A and CDK4/cyclin D1 inhibitors
    • Rossi KA, Markwalder JA, Seitz SP, Chang CH, Cox S, Boisclair MD, et al. Understanding and modulating cyclin-dependent kinase inhibitor specificity: Molecular modeling and biochemical evaluation of pyrazolopyrimidinones as CDK2/cyclin A and CDK4/cyclin D1 inhibitors. J Comput Aided Mol Des 2005; 19(2): 111-22.
    • (2005) J Comput Aided Mol Des , vol.19 , Issue.2 , pp. 111-122
    • Rossi, K.A.1    Markwalder, J.A.2    Seitz, S.P.3    Chang, C.H.4    Cox, S.5    Boisclair, M.D.6
  • 101
    • 33745325007 scopus 로고    scopus 로고
    • Mechanisms of drug inhibition of signalling molecules
    • Sebolt-Leopold JS, English JM. Mechanisms of drug inhibition of signalling molecules. Nature 2006; 441(7092): 457-62.
    • (2006) Nature , vol.441 , Issue.7092 , pp. 457-462
    • Sebolt-Leopold, J.S.1    English, J.M.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.