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Volumn 149, Issue 1, 2006, Pages 48-57

Identification of an effector protein and gain-of-function mutants that activate Pfmrk, a malarial cyclin-dependent protein kinase

Author keywords

CDK; Cell cycle; Inhibitor; Kinase; Malaria; MAT1; Pfmrk; PfPK5; Plasmodium falciparum

Indexed keywords

AMINO ACID; CYCLIN DEPENDENT KINASE; CYCLIN DEPENDENT KINASE 7; CYCLIN DEPENDENT KINASE ACTIVATING KINASE; CYCLINE; ENZYME; MENAGE A TRIOS 1 PROTEIN; MO15 RELATED KINASE; PROTEIN; PROTEIN KINASE 5; RNA POLYMERASE II; UNCLASSIFIED DRUG;

EID: 33745872589     PISSN: 01666851     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molbiopara.2006.04.004     Document Type: Article
Times cited : (30)

References (68)
  • 1
    • 0034972445 scopus 로고    scopus 로고
    • The ears of the hippopotamus: manifestations, determinants, and estimates of the malaria burden
    • Breman J.G. The ears of the hippopotamus: manifestations, determinants, and estimates of the malaria burden. Am J Trop Med Hyg 64 (2001) 1-11
    • (2001) Am J Trop Med Hyg , vol.64 , pp. 1-11
    • Breman, J.G.1
  • 2
    • 0036188537 scopus 로고    scopus 로고
    • Clinical status and implications of antimalarial drug resistance
    • Winstanley P.A., Ward S.A., and Snow R.W. Clinical status and implications of antimalarial drug resistance. Microbes Infect 4 (2002) 157-164
    • (2002) Microbes Infect , vol.4 , pp. 157-164
    • Winstanley, P.A.1    Ward, S.A.2    Snow, R.W.3
  • 3
    • 23244443547 scopus 로고    scopus 로고
    • Drug resistance hampers our capacity to roll back malaria
    • Olliaro P. Drug resistance hampers our capacity to roll back malaria. Clin Infect Dis 41 Suppl. 4 (2005) S247-S257
    • (2005) Clin Infect Dis , vol.41 , Issue.SUPPL. 4
    • Olliaro, P.1
  • 4
    • 12744281184 scopus 로고    scopus 로고
    • Rational inhibitor design and iterative screening in the identification of selective plasmodial cyclin dependent kinase inhibitors
    • Keenan S.M., Geyer J.A., Welsh W.J., Prigge S.T., and Waters N.C. Rational inhibitor design and iterative screening in the identification of selective plasmodial cyclin dependent kinase inhibitors. Comb Chem High Throughput Screen 8 (2005) 27-38
    • (2005) Comb Chem High Throughput Screen , vol.8 , pp. 27-38
    • Keenan, S.M.1    Geyer, J.A.2    Welsh, W.J.3    Prigge, S.T.4    Waters, N.C.5
  • 5
    • 0030296465 scopus 로고    scopus 로고
    • Malaria and the cell cycle
    • Leete T.H., and Rubin H. Malaria and the cell cycle. Parasitol today 12 (1996) 442-444
    • (1996) Parasitol today , vol.12 , pp. 442-444
    • Leete, T.H.1    Rubin, H.2
  • 6
    • 0032087856 scopus 로고    scopus 로고
    • The plasmodium cell-cycle: facts and questions
    • Arnot D.E., and Gull K. The plasmodium cell-cycle: facts and questions. Ann Trop Med Parasitol 92 (1998) 361-365
    • (1998) Ann Trop Med Parasitol , vol.92 , pp. 361-365
    • Arnot, D.E.1    Gull, K.2
  • 7
    • 0033631382 scopus 로고    scopus 로고
    • The cell cycle in protozoan parasites
    • Armelle J., Bernard D., and Laurent M. (Eds), Kluwer Academic
    • Doerig C., Chakrabarti D., Kappes B., and Mathews K. The cell cycle in protozoan parasites. In: Armelle J., Bernard D., and Laurent M. (Eds). Progress in Cell Cycle Research vol. 4 (2000), Kluwer Academic
    • (2000) Progress in Cell Cycle Research , vol.4
    • Doerig, C.1    Chakrabarti, D.2    Kappes, B.3    Mathews, K.4
  • 8
    • 0031466305 scopus 로고    scopus 로고
    • Cyclin-dependent kinases: engines, clocks, and microprocessors
    • Morgan D.O. 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
  • 9
    • 0033564697 scopus 로고    scopus 로고
    • CDK inhibitors: positive and negative regulators of G1-phase progression
    • Sherr C.J., and Roberts J.M. 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
  • 10
    • 0035990906 scopus 로고    scopus 로고
    • Cyclin-dependent kinases as potential targets to improve stroke outcome
    • O'Hare M., Wang F., and Park D.S. Cyclin-dependent kinases as potential targets to improve stroke outcome. Pharmacol Ther 93 (2002) 135-143
    • (2002) Pharmacol Ther , vol.93 , pp. 135-143
    • O'Hare, M.1    Wang, F.2    Park, D.S.3
  • 11
    • 0036924593 scopus 로고    scopus 로고
    • Cyclin-dependent kinases as cellular targets for antiviral drugs
    • Schang L.M. Cyclin-dependent kinases as cellular targets for antiviral drugs. J Antimicrob Chemother 50 (2002) 779-792
    • (2002) J Antimicrob Chemother , vol.50 , pp. 779-792
    • Schang, L.M.1
  • 12
    • 0035141075 scopus 로고    scopus 로고
    • Development of cyclin-dependent kinase modulators as novel therapeutic approaches for hematological malignancies
    • Senderowicz A.M. Development of cyclin-dependent kinase modulators as novel therapeutic approaches for hematological malignancies. Leukemia 15 (2001) 1-9
    • (2001) Leukemia , vol.15 , pp. 1-9
    • Senderowicz, A.M.1
  • 13
    • 0037294203 scopus 로고    scopus 로고
    • Inhibiting cyclin-dependent kinase/cyclin activity for the treatment of cancer and cardiovascular disease
    • Ivorra C., Samyn H., Edo M.D., et al. Inhibiting cyclin-dependent kinase/cyclin activity for the treatment of cancer and cardiovascular disease. Curr Pharm Biotechnol 4 (2003) 21-37
    • (2003) Curr Pharm Biotechnol , vol.4 , pp. 21-37
    • Ivorra, C.1    Samyn, H.2    Edo, M.D.3
  • 14
    • 0028931265 scopus 로고
    • Principles of CDK regulation
    • Morgan D.O. Principles of CDK regulation. Nature 374 (1995) 131-134
    • (1995) Nature , vol.374 , pp. 131-134
    • Morgan, D.O.1
  • 15
    • 0030561611 scopus 로고    scopus 로고
    • The dynamics of cyclin dependent kinase structure
    • Morgan D.O. The dynamics of cyclin dependent kinase structure. Curr Opin Cell Biol 8 (1996) 767-772
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 767-772
    • Morgan, D.O.1
  • 17
    • 0029029617 scopus 로고
    • Mechanism of CDK activation revealed by the structure of a cyclinA-CDK2 complex
    • Jeffrey P.D., Russo A.A., Polyak K., 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
  • 18
    • 0029767016 scopus 로고    scopus 로고
    • Structural basis of cyclin-dependent kinase activation by phosphorylation
    • Russo A.A., Jeffrey P.D., and Pavletich N.P. 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
  • 19
    • 0037021406 scopus 로고    scopus 로고
    • Cyclin-dependent kinase homologues of Plasmodium falciparum
    • Doerig C., Endicott J., and Chakrabarti D. Cyclin-dependent kinase homologues of Plasmodium falciparum. Int J Parasitol 32 (2002) 1575-1585
    • (2002) Int J Parasitol , vol.32 , pp. 1575-1585
    • Doerig, C.1    Endicott, J.2    Chakrabarti, D.3
  • 20
    • 0030581694 scopus 로고    scopus 로고
    • Plasmodium falciparum protein kinase 5 and the malarial nuclear division cycles
    • Graeser R., Wernli B., Franklin R.M., and Kappes B. Plasmodium falciparum protein kinase 5 and the malarial nuclear division cycles. Mol Biochem Parasitol 82 (1996) 37-49
    • (1996) Mol Biochem Parasitol , vol.82 , pp. 37-49
    • Graeser, R.1    Wernli, B.2    Franklin, R.M.3    Kappes, B.4
  • 21
    • 0030200306 scopus 로고    scopus 로고
    • Mechanisms of activation of the cdc2-related kinase PfPK5 from Plasmodium falciparum
    • Graeser R., Franklin R.M., and Kappes B. Mechanisms of activation of the cdc2-related kinase PfPK5 from Plasmodium falciparum. Mol Biochem Parasitol 79 (1996) 125-127
    • (1996) Mol Biochem Parasitol , vol.79 , pp. 125-127
    • Graeser, R.1    Franklin, R.M.2    Kappes, B.3
  • 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 M.P., et al. Identification and initial characterization of three novel cyclin-related proteins of the human malaria parasite Plasmodium falciparum. J Biol Chem 278 (2003) 39839-39850
    • (2003) J Biol Chem , vol.278 , pp. 39839-39850
    • Merckx, A.1    Le Roch, K.2    Nivez, M.P.3
  • 23
    • 0035900603 scopus 로고    scopus 로고
    • Influence of human p16(INK4) and p21(CIP1) on the in vitro activity of recombinant Plasmodium falciparum cyclin-dependent protein kinases
    • Li Z., Le Roch K., Geyer J.A., et al. Influence of human p16(INK4) and p21(CIP1) on the in vitro activity of recombinant Plasmodium falciparum cyclin-dependent protein kinases. Biochem Biophys Res Commun 288 (2001) 1207-1211
    • (2001) Biochem Biophys Res Commun , vol.288 , pp. 1207-1211
    • Li, Z.1    Le Roch, K.2    Geyer, J.A.3
  • 24
    • 0029862051 scopus 로고    scopus 로고
    • Pfmrk, a MO15-related protein kinase from Plasmodium falciparum. Gene cloning, sequence, stage-specific expression and chromosome localization
    • Li J.L., Robson K.J., Chen J.L., Targett G.A., and Baker D.A. Pfmrk, a MO15-related protein kinase from Plasmodium falciparum. Gene cloning, sequence, stage-specific expression and chromosome localization. Eur J Biochem 241 (1996) 805-813
    • (1996) Eur J Biochem , vol.241 , pp. 805-813
    • Li, J.L.1    Robson, K.J.2    Chen, J.L.3    Targett, G.A.4    Baker, D.A.5
  • 25
    • 0027296041 scopus 로고
    • The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues
    • Fesquet D., Labbe J.C., Derancourt J., et al. The MO15 gene encodes the catalytic subunit of a protein kinase that activates cdc2 and other cyclin-dependent kinases (CDKs) through phosphorylation of Thr161 and its homologues. EMBO J 12 (1993) 3111-3121
    • (1993) EMBO J , vol.12 , pp. 3111-3121
    • Fesquet, D.1    Labbe, J.C.2    Derancourt, J.3
  • 26
    • 0027251024 scopus 로고
    • The cdc2-related protein p40MO15 is the catalytic subunit of a protein kinase that can activate p33cdk2 and p34cdc2
    • Poon R.Y., Yamashita K., Adamczewski J.P., Hunt T., and Shuttleworth J. The cdc2-related protein p40MO15 is the catalytic subunit of a protein kinase that can activate p33cdk2 and p34cdc2. EMBO J 12 (1993) 3123-3132
    • (1993) EMBO J , vol.12 , pp. 3123-3132
    • Poon, R.Y.1    Yamashita, K.2    Adamczewski, J.P.3    Hunt, T.4    Shuttleworth, J.5
  • 28
    • 0027994603 scopus 로고
    • A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase
    • Fisher R.P., and Morgan D.O. A novel cyclin associates with MO15/CDK7 to form the CDK-activating kinase. Cell 78 (1994) 713-724
    • (1994) Cell , vol.78 , pp. 713-724
    • Fisher, R.P.1    Morgan, D.O.2
  • 29
    • 0029952160 scopus 로고    scopus 로고
    • Cyclin-dependent kinase 7: at the cross-roads of transcription DNA repair and cell cycle control?
    • Nigg E.A. Cyclin-dependent kinase 7: at the cross-roads of transcription DNA repair and cell cycle control?. Curr Opin Cell Biol 8 (1996) 312-317
    • (1996) Curr Opin Cell Biol , vol.8 , pp. 312-317
    • Nigg, E.A.1
  • 30
    • 0029418115 scopus 로고
    • The regulation and functions of cdk7
    • Shuttleworth J. The regulation and functions of cdk7. Prog Cell Cycle Res 1 (1995) 229-240
    • (1995) Prog Cell Cycle Res , vol.1 , pp. 229-240
    • Shuttleworth, J.1
  • 31
    • 0030976052 scopus 로고    scopus 로고
    • Regulation of CDK7 substrate specificity by MAT1 and TFIIH
    • Yankulov K.Y., and Bentley D.L. Regulation of CDK7 substrate specificity by MAT1 and TFIIH. EMBO J 16 (1997) 1638-1646
    • (1997) EMBO J , vol.16 , pp. 1638-1646
    • Yankulov, K.Y.1    Bentley, D.L.2
  • 32
    • 0029987031 scopus 로고    scopus 로고
    • MAT1, cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH
    • Adamczewski J.P., Rossignol M., Tassan J.P., Nigg E.A., Moncollin V., and Egly J.M. MAT1, cdk7 and cyclin H form a kinase complex which is UV light-sensitive upon association with TFIIH. EMBO J 15 (1996) 1877-1884
    • (1996) EMBO J , vol.15 , pp. 1877-1884
    • Adamczewski, J.P.1    Rossignol, M.2    Tassan, J.P.3    Nigg, E.A.4    Moncollin, V.5    Egly, J.M.6
  • 33
    • 0030998712 scopus 로고    scopus 로고
    • Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH
    • Rossignol M., Kolb-Cheynel I., and Egly J.M. Substrate specificity of the cdk-activating kinase (CAK) is altered upon association with TFIIH. EMBO J 16 (1997) 1628-1637
    • (1997) EMBO J , vol.16 , pp. 1628-1637
    • Rossignol, M.1    Kolb-Cheynel, I.2    Egly, J.M.3
  • 34
    • 0035898652 scopus 로고    scopus 로고
    • T-loop phosphorylation stabilizes the CDK7-cyclin H-MAT1 complex in vivo and regulates its CTD kinase activity
    • Larochelle S., Chen J., Knights R., et al. T-loop phosphorylation stabilizes the CDK7-cyclin H-MAT1 complex in vivo and regulates its CTD kinase activity. EMBO J 20 (2001) 3749-3759
    • (2001) EMBO J , vol.20 , pp. 3749-3759
    • Larochelle, S.1    Chen, J.2    Knights, R.3
  • 35
    • 0028807103 scopus 로고
    • Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase
    • Fisher R.P., Jin P., Chamberlin H.M., and Morgan D.O. Alternative mechanisms of CAK assembly require an assembly factor or an activating kinase. Cell 83 (1995) 47-57
    • (1995) Cell , vol.83 , pp. 47-57
    • Fisher, R.P.1    Jin, P.2    Chamberlin, H.M.3    Morgan, D.O.4
  • 36
    • 0031016629 scopus 로고    scopus 로고
    • Dual phosphorylation of the T-loop in cdk7: its role in controlling cyclin H binding and CAK activity
    • Martinez A.M., Afshar M., Martin F., Cavadore J.C., Labbe J.C., and Doree M. Dual phosphorylation of the T-loop in cdk7: its role in controlling cyclin H binding and CAK activity. EMBO J 16 (1997) 343-354
    • (1997) EMBO J , vol.16 , pp. 343-354
    • Martinez, A.M.1    Afshar, M.2    Martin, F.3    Cavadore, J.C.4    Labbe, J.C.5    Doree, M.6
  • 37
    • 0028856425 scopus 로고
    • MAT1 ('menage a trois') a new RING finger protein subunit stabilizing cyclin H-cdk7 complexes in starfish and Xenopus CAK
    • Devault A., Martinez A.M., Fesquet D., et al. MAT1 ('menage a trois') a new RING finger protein subunit stabilizing cyclin H-cdk7 complexes in starfish and Xenopus CAK. EMBO J 14 (1995) 5027-5036
    • (1995) EMBO J , vol.14 , pp. 5027-5036
    • Devault, A.1    Martinez, A.M.2    Fesquet, D.3
  • 38
    • 0028882228 scopus 로고
    • In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein
    • Tassan J.P., Jaquenoud M., Fry A.M., Frutiger S., Hughes G.J., and Nigg E.A. In vitro assembly of a functional human CDK7-cyclin H complex requires MAT1, a novel 36 kDa RING finger protein. EMBO J 14 (1995) 5608-5617
    • (1995) EMBO J , vol.14 , pp. 5608-5617
    • Tassan, J.P.1    Jaquenoud, M.2    Fry, A.M.3    Frutiger, S.4    Hughes, G.J.5    Nigg, E.A.6
  • 39
    • 0034654447 scopus 로고    scopus 로고
    • Cyclin H activation and drug susceptibility of the Pfmrk cyclin dependent protein kinase from Plasmodium falciparum
    • Waters N.C., Woodard C.L., and Prigge S.T. Cyclin H activation and drug susceptibility of the Pfmrk cyclin dependent protein kinase from Plasmodium falciparum. Mol Biochem Parasitol 107 (2000) 45-55
    • (2000) Mol Biochem Parasitol , vol.107 , pp. 45-55
    • Waters, N.C.1    Woodard, C.L.2    Prigge, S.T.3
  • 40
    • 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., 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 275 (2000) 8952-8958
    • (2000) J Biol Chem , vol.275 , pp. 8952-8958
    • Le Roch, K.1    Sestier, C.2    Dorin, D.3
  • 41
    • 29144433571 scopus 로고    scopus 로고
    • Targeting malaria with specific CDK inhibitors
    • Geyer J.A., Prigge S.T., and Waters N.C. Targeting malaria with specific CDK inhibitors. Biochim Biophys Acta 1754 (2005) 160-170
    • (2005) Biochim Biophys Acta , vol.1754 , pp. 160-170
    • Geyer, J.A.1    Prigge, S.T.2    Waters, N.C.3
  • 42
    • 6044260115 scopus 로고    scopus 로고
    • A three-dimensional in silico pharmacophore model for inhibition of Plasmodium falciparum cyclin-dependent kinases and discovery of different classes of novel Pfmrk specific inhibitors
    • Bhattacharjee A.K., Geyer J.A., Woodard C.L., et al. A three-dimensional in silico pharmacophore model for inhibition of Plasmodium falciparum cyclin-dependent kinases and discovery of different classes of novel Pfmrk specific inhibitors. J Med Chem 47 (2004) 5418-5426
    • (2004) J Med Chem , vol.47 , pp. 5418-5426
    • Bhattacharjee, A.K.1    Geyer, J.A.2    Woodard, C.L.3
  • 43
    • 0042420753 scopus 로고    scopus 로고
    • Oxindole-based compounds are selective inhibitors of Plasmodium falciparum cyclin dependent protein kinases
    • Woodard C.L., Li Z., Kathcart A.K., et al. Oxindole-based compounds are selective inhibitors of Plasmodium falciparum cyclin dependent protein kinases. J Med Chem 46 (2003) 3877-3882
    • (2003) J Med Chem , vol.46 , pp. 3877-3882
    • Woodard, C.L.1    Li, Z.2    Kathcart, A.K.3
  • 45
    • 7944231428 scopus 로고    scopus 로고
    • The crystal structure of human CDK7 and its protein recognition properties
    • Lolli G., Lowe E.D., Brown N.R., and Johnson L.N. The crystal structure of human CDK7 and its protein recognition properties. Structure (Camb) 12 (2004) 2067-2079
    • (2004) Structure (Camb) , vol.12 , pp. 2067-2079
    • Lolli, G.1    Lowe, E.D.2    Brown, N.R.3    Johnson, L.N.4
  • 46
    • 0026319199 scopus 로고
    • Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons
    • Nicholls A., Sharp K.A., and Honig B. Protein folding and association: insights from the interfacial and thermodynamic properties of hydrocarbons. Proteins 11 (1991) 281-296
    • (1991) Proteins , vol.11 , pp. 281-296
    • Nicholls, A.1    Sharp, K.A.2    Honig, B.3
  • 47
    • 0027239790 scopus 로고
    • The RING finger. A novel protein sequence motif related to the zinc finger
    • Freemont P.S. The RING finger. A novel protein sequence motif related to the zinc finger. Ann N Y Acad Sci 684 (1993) 174-192
    • (1993) Ann N Y Acad Sci , vol.684 , pp. 174-192
    • Freemont, P.S.1
  • 48
    • 0035924235 scopus 로고    scopus 로고
    • Structure-based generation of a new class of potent Cdk4 inhibitors: new de novo design strategy and library design
    • Honma T., Hayashi K., Aoyama T., et al. Structure-based generation of a new class of potent Cdk4 inhibitors: new de novo design strategy and library design. J Med Chem 44 (2001) 4615-4627
    • (2001) J Med Chem , vol.44 , pp. 4615-4627
    • Honma, T.1    Hayashi, K.2    Aoyama, T.3
  • 49
    • 0035924240 scopus 로고    scopus 로고
    • A novel approach for the development of selective Cdk4 inhibitors: library design based on locations of Cdk4 specific amino acid residues
    • Honma T., Yoshizumi T., Hashimoto N., et al. A novel approach for the development of selective Cdk4 inhibitors: library design based on locations of Cdk4 specific amino acid residues. J Med Chem 44 (2001) 4628-4640
    • (2001) J Med Chem , vol.44 , pp. 4628-4640
    • Honma, T.1    Yoshizumi, T.2    Hashimoto, N.3
  • 50
    • 0037312866 scopus 로고    scopus 로고
    • Cyclin-dependent protein kinases as therapeutic drug targets for antimalarial drug development
    • Waters N.C., and Geyer J.A. Cyclin-dependent protein kinases as therapeutic drug targets for antimalarial drug development. Expert Opin Ther Targets 7 (2003) 7-17
    • (2003) Expert Opin Ther Targets , vol.7 , pp. 7-17
    • Waters, N.C.1    Geyer, J.A.2
  • 51
    • 24944573556 scopus 로고    scopus 로고
    • Structural model of the plasmodium CDK, Pfmrk, a novel target for malaria therapeutics
    • Peng Y., Keenan S.M., and Welsh W.J. Structural model of the plasmodium CDK, Pfmrk, a novel target for malaria therapeutics. J Mol Graph Model 24 (2005) 72-80
    • (2005) J Mol Graph Model , vol.24 , pp. 72-80
    • Peng, Y.1    Keenan, S.M.2    Welsh, W.J.3
  • 52
    • 0037197839 scopus 로고    scopus 로고
    • Evolution of the RNA polymerase II C-terminal domain
    • Stiller J.W., and Hall B.D. Evolution of the RNA polymerase II C-terminal domain. Proc Natl Acad Sci USA 99 (2002) 6091-6096
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 6091-6096
    • Stiller, J.W.1    Hall, B.D.2
  • 53
    • 29244468847 scopus 로고    scopus 로고
    • Secrets of a double agent: CDK7 in cell-cycle control and transcription
    • Fisher R.P. 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
  • 54
    • 0033197840 scopus 로고    scopus 로고
    • Directed evolution to bypass cyclin requirements for the Cdc28p cyclin-dependent kinase
    • Levine K., Kiang L., Jacobson M.D., Fisher R.P., and Cross F.R. Directed evolution to bypass cyclin requirements for the Cdc28p cyclin-dependent kinase. Mol Cell 4 (1999) 353-363
    • (1999) Mol Cell , vol.4 , pp. 353-363
    • Levine, K.1    Kiang, L.2    Jacobson, M.D.3    Fisher, R.P.4    Cross, F.R.5
  • 55
    • 0035816581 scopus 로고    scopus 로고
    • Isolation of hyperactive mutants of the MAPK p38/Hog1 that are independent of MAPK kinase activation
    • Bell M., Capone R., Pashtan I., Levitzki A., and Engelberg D. Isolation of hyperactive mutants of the MAPK p38/Hog1 that are independent of MAPK kinase activation. J Biol Chem 276 (2001) 25351-25358
    • (2001) J Biol Chem , vol.276 , pp. 25351-25358
    • Bell, M.1    Capone, R.2    Pashtan, I.3    Levitzki, A.4    Engelberg, D.5
  • 56
    • 8744256717 scopus 로고    scopus 로고
    • Active mutants of the human p38alpha mitogen-activated protein kinase
    • Diskin R., Askari N., Capone R., Engelberg D., and Livnah O. Active mutants of the human p38alpha mitogen-activated protein kinase. J Biol Chem 279 (2004) 47040-47049
    • (2004) J Biol Chem , vol.279 , pp. 47040-47049
    • Diskin, R.1    Askari, N.2    Capone, R.3    Engelberg, D.4    Livnah, O.5
  • 57
    • 0029993727 scopus 로고    scopus 로고
    • Active and inactive protein kinases: structural basis for regulation
    • Johnson L.N., Noble M.E., and Owen D.J. Active and inactive protein kinases: structural basis for regulation. Cell 85 (1996) 149-158
    • (1996) Cell , vol.85 , pp. 149-158
    • Johnson, L.N.1    Noble, M.E.2    Owen, D.J.3
  • 58
    • 0037013143 scopus 로고    scopus 로고
    • The conformational plasticity of protein kinases
    • Huse M., and Kuriyan J. The conformational plasticity of protein kinases. Cell 109 (2002) 275-282
    • (2002) Cell , vol.109 , pp. 275-282
    • Huse, M.1    Kuriyan, J.2
  • 59
    • 3343024236 scopus 로고    scopus 로고
    • Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha
    • Kannan N., and Neuwald A.F. Evolutionary constraints associated with functional specificity of the CMGC protein kinases MAPK, CDK, GSK, SRPK, DYRK, and CK2alpha. Protein Sci 13 (2004) 2059-2077
    • (2004) Protein Sci , vol.13 , pp. 2059-2077
    • Kannan, N.1    Neuwald, A.F.2
  • 60
    • 0037417767 scopus 로고    scopus 로고
    • MAP kinases and CDKs: kinetic basis for catalytic activation
    • Lew J. MAP kinases and CDKs: kinetic basis for catalytic activation. Biochemistry 42 (2003) 849-856
    • (2003) Biochemistry , vol.42 , pp. 849-856
    • Lew, J.1
  • 61
    • 2442717698 scopus 로고    scopus 로고
    • Communication pathways between the nucleotide pocket and distal regulatory sites in protein kinases
    • Wong L., Jennings P.A., and Adams J.A. Communication pathways between the nucleotide pocket and distal regulatory sites in protein kinases. Acc Chem Res 37 (2004) 304-311
    • (2004) Acc Chem Res , vol.37 , pp. 304-311
    • Wong, L.1    Jennings, P.A.2    Adams, J.A.3
  • 62
    • 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., and Doerig C. Protein kinases of the human malaria parasite Plasmodium falciparum: the kinome of a divergent eukaryote. BMC Genomics 5 (2004) 79
    • (2004) BMC Genomics , vol.5 , pp. 79
    • Ward, P.1    Equinet, L.2    Packer, J.3    Doerig, C.4
  • 63
    • 9144249813 scopus 로고    scopus 로고
    • Comparative genomics of cyclin-dependent kinases suggest co-evolution of the RNAP II C-terminal domain and CTD-directed CDKs
    • Guo Z., and Stiller J.W. Comparative genomics of cyclin-dependent kinases suggest co-evolution of the RNAP II C-terminal domain and CTD-directed CDKs. BMC Genomics 5 (2004) 69
    • (2004) BMC Genomics , vol.5 , pp. 69
    • Guo, Z.1    Stiller, J.W.2
  • 64
    • 0033945894 scopus 로고    scopus 로고
    • Evolution of cyclin-dependent kinases (CDKs) and CDK-activating kinases (CAKs): differential conservation of CAKs in yeast and metazoa
    • Liu J., and Kipreos E.T. Evolution of cyclin-dependent kinases (CDKs) and CDK-activating kinases (CAKs): differential conservation of CAKs in yeast and metazoa. Mol Biol Evol 17 (2000) 1061-1074
    • (2000) Mol Biol Evol , vol.17 , pp. 1061-1074
    • Liu, J.1    Kipreos, E.T.2
  • 65
    • 0032005801 scopus 로고    scopus 로고
    • Cdk7 is essential for mitosis and for in vivo Cdk-activating kinase activity
    • Larochelle S., Pandur J., Fisher R.P., Salz H.K., and Suter B. Cdk7 is essential for mitosis and for in vivo Cdk-activating kinase activity. Genes Dev 12 (1998) 370-381
    • (1998) Genes Dev , vol.12 , pp. 370-381
    • Larochelle, S.1    Pandur, J.2    Fisher, R.P.3    Salz, H.K.4    Suter, B.5
  • 66
    • 0030669391 scopus 로고    scopus 로고
    • The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors
    • Inamoto S., Segil N., Pan Z.Q., Kimura M., and Roeder R.G. The cyclin-dependent kinase-activating kinase (CAK) assembly factor, MAT1, targets and enhances CAK activity on the POU domains of octamer transcription factors. J Biol Chem 272 (1997) 29852-29858
    • (1997) J Biol Chem , vol.272 , pp. 29852-29858
    • Inamoto, S.1    Segil, N.2    Pan, Z.Q.3    Kimura, M.4    Roeder, R.G.5
  • 67
    • 0030724673 scopus 로고    scopus 로고
    • p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner
    • Ko L.J., Shieh S.Y., Chen X., et al. p53 is phosphorylated by CDK7-cyclin H in a p36MAT1-dependent manner. Mol Cell Biol 17 (1997) 7220-7229
    • (1997) Mol Cell Biol , vol.17 , pp. 7220-7229
    • Ko, L.J.1    Shieh, S.Y.2    Chen, X.3
  • 68
    • 4243071596 scopus 로고    scopus 로고
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
    • Bozdech Z., Llinas M., Pulliam B.L., Wong E.D., Zhu J., and DeRisi J.L. The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum. PLoS Biol 1 (2003) E5
    • (2003) PLoS Biol , vol.1
    • Bozdech, Z.1    Llinas, M.2    Pulliam, B.L.3    Wong, E.D.4    Zhu, J.5    DeRisi, J.L.6


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