메뉴 건너뛰기




Volumn 1697, Issue 1-2, 2004, Pages 155-168

Protein kinases as targets for anti-parasitic chemotherapy

Author keywords

CDK; Cyclin dependent kinase; Drug screening; Drug target; kDa; Kilodalton; MAPK; Parasite; Phosphorylation; PKA; PKG; Protein kinase A, or cyclic AMP dependent protein kinase; Protein kinase G, or Cyclic GMP dependent protein kinase; Protein kinase inhibitor

Indexed keywords

ANTIPARASITIC AGENT; PAULLONE DERIVATIVE; PROTEIN KINASE; PROTEIN KINASE INHIBITOR; PROTOZOAL PROTEIN; PURVALANOL B; RECOMBINANT ENZYME;

EID: 1542298986     PISSN: 15709639     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbapap.2003.11.021     Document Type: Conference Paper
Times cited : (131)

References (93)
  • 1
    • 0037033984 scopus 로고    scopus 로고
    • The economic and social burden of malaria
    • Sachs J., Malaney P. The economic and social burden of malaria. Nature. 415:2002;680-685.
    • (2002) Nature , vol.415 , pp. 680-685
    • Sachs, J.1    Malaney, P.2
  • 2
    • 0037034009 scopus 로고    scopus 로고
    • Medical need, scientific opportunity and the drive for antimalarial drugs
    • Ridley R.G. Medical need, scientific opportunity and the drive for antimalarial drugs. Nature. 415:2002;686-693.
    • (2002) Nature , vol.415 , pp. 686-693
    • Ridley, R.G.1
  • 3
    • 0032878499 scopus 로고    scopus 로고
    • A compartmentalised model for the estimation of the cost of coccidiosis to the world's chicken production industry
    • Williams R.B. A compartmentalised model for the estimation of the cost of coccidiosis to the world's chicken production industry. Int. J. Parasitol. 29:1999;1209-1229.
    • (1999) Int. J. Parasitol. , vol.29 , pp. 1209-1229
    • Williams, R.B.1
  • 7
    • 0038404516 scopus 로고    scopus 로고
    • The evaluation and management of hirsutism
    • Azziz R. The evaluation and management of hirsutism. Obstet. Gynecol. 101:2003;995-1007.
    • (2003) Obstet. Gynecol. , vol.101 , pp. 995-1007
    • Azziz, R.1
  • 11
    • 0034602344 scopus 로고    scopus 로고
    • A kingdom-level phylogeny of eukaryotes based on combined protein data
    • Baldauf S.L., Roger A.J., Wenk-Siefert I., Doolittle W.F. A kingdom-level phylogeny of eukaryotes based on combined protein data. Science. 290:2000;972-977.
    • (2000) Science , vol.290 , pp. 972-977
    • Baldauf, S.L.1    Roger, A.J.2    Wenk-Siefert, I.3    Doolittle, W.F.4
  • 12
    • 0035339840 scopus 로고    scopus 로고
    • The biology of kinetoplastid parasites: Insights and challenges from genomics and post-genomics
    • Gull K. The biology of kinetoplastid parasites: insights and challenges from genomics and post-genomics. Int. J. Parasitol. 31:2001;443-452.
    • (2001) Int. J. Parasitol. , vol.31 , pp. 443-452
    • Gull, K.1
  • 13
    • 0027997253 scopus 로고
    • The ribosomal RNA genes of Plasmodium
    • Waters A.P. The ribosomal RNA genes of Plasmodium. Adv. Parasitol. 34:1994;33-79.
    • (1994) Adv. Parasitol. , vol.34 , pp. 33-79
    • Waters, A.P.1
  • 17
    • 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 S.P., Gull K., Hyde J.E. Microtubular organization visualized by immunofluorescence microscopy during erythrocytic schizogony in Plasmodium falciparum and investigation of post-translational modifications of parasite tubulin. Parasitology. 106:1993;223-232.
    • (1993) Parasitology , vol.106 , pp. 223-232
    • Read, M.1    Sherwin, T.2    Holloway, S.P.3    Gull, K.4    Hyde, J.E.5
  • 18
    • 0034307767 scopus 로고    scopus 로고
    • Host cell invasion by malaria parasites
    • Chitnis C.E., Blackman M.J. Host cell invasion by malaria parasites. Parasitol. Today. 16:2000;411-415.
    • (2000) Parasitol. Today , vol.16 , pp. 411-415
    • Chitnis, C.E.1    Blackman, M.J.2
  • 19
    • 0032988608 scopus 로고    scopus 로고
    • The apicoplast as a potential therapeutic target in Toxoplasma and other apicomplexan parasites: Some additional thoughts
    • Roos D.S. The apicoplast as a potential therapeutic target in Toxoplasma and other apicomplexan parasites: some additional thoughts. Parasitol. Today. 15:1999;41.
    • (1999) Parasitol. Today , vol.15 , pp. 41
    • Roos, D.S.1
  • 20
    • 0036242661 scopus 로고    scopus 로고
    • Basic cell biology of Trypanosoma cruzi
    • De Souza W. Basic cell biology of Trypanosoma cruzi. Curr. Pharm. Des. 8:2002;269-285.
    • (2002) Curr. Pharm. Des. , vol.8 , pp. 269-285
    • De Souza, W.1
  • 21
    • 0028035122 scopus 로고
    • Staurosporine inhibits invasion of erythrocytes by malarial merozoites
    • Ward G.E., Fujioka H., Aikawa M., Miller L.H. Staurosporine inhibits invasion of erythrocytes by malarial merozoites. Exp. Parasitol. 79:1994;480-487.
    • (1994) Exp. Parasitol. , vol.79 , pp. 480-487
    • Ward, G.E.1    Fujioka, H.2    Aikawa, M.3    Miller, L.H.4
  • 22
    • 0033231908 scopus 로고    scopus 로고
    • An overview of Plasmodium protein kinases
    • (00001527 00001527)
    • Kappes B., Doerig C.D., Graser R. An overview of Plasmodium protein kinases. Parasitol. Today. 15:1999;449-454. (00001527 00001527).
    • (1999) Parasitol. Today , vol.15 , pp. 449-454
    • Kappes, B.1    Doerig, C.D.2    Graser, R.3
  • 23
    • 0036015628 scopus 로고    scopus 로고
    • A novel cyclic GMP-dependent protein kinase is expressed in the ring stage of the Plasmodium falciparum life cycle
    • Deng W., Baker D.A. A novel cyclic GMP-dependent protein kinase is expressed in the ring stage of the Plasmodium falciparum life cycle. Mol. Microbiol. 44:2002;1141-1151.
    • (2002) Mol. Microbiol. , vol.44 , pp. 1141-1151
    • Deng, W.1    Baker, D.A.2
  • 25
    • 0036616356 scopus 로고    scopus 로고
    • Toxoplasma gondii cyclic GMP-dependent kinase: Chemotherapeutic targeting of an essential parasite protein kinase
    • Donald R.G., Allocco J., Singh S.B., Nare B., Salowe S.P., Wiltsie J., Liberator P.A. Toxoplasma gondii cyclic GMP-dependent kinase: chemotherapeutic targeting of an essential parasite protein kinase. Eukaryot. Cell. 1:2002;317-328.
    • (2002) Eukaryot. Cell , vol.1 , pp. 317-328
    • Donald, R.G.1    Allocco, J.2    Singh, S.B.3    Nare, B.4    Salowe, S.P.5    Wiltsie, J.6    Liberator, P.A.7
  • 26
    • 0037006990 scopus 로고    scopus 로고
    • The role of a parasite-specific allosteric site in the distinctive activation behavior of Eimeria tenella cGMP-dependent protein kinase
    • Salowe S.P., Wiltsie J., Liberator P.A., Donald R.G. The role of a parasite-specific allosteric site in the distinctive activation behavior of Eimeria tenella cGMP-dependent protein kinase. Biochemistry. 41:2002;4385-4391.
    • (2002) Biochemistry , vol.41 , pp. 4385-4391
    • Salowe, S.P.1    Wiltsie, J.2    Liberator, P.A.3    Donald, R.G.4
  • 27
    • 0036132994 scopus 로고    scopus 로고
    • Classification and phylogenetic analysis of the cAMP-dependent protein kinase regulatory subunit family
    • Canaves J.M., Taylor S.S. Classification and phylogenetic analysis of the cAMP-dependent protein kinase regulatory subunit family. J. Mol. Evol. 54:2002;17-29.
    • (2002) J. Mol. Evol. , vol.54 , pp. 17-29
    • Canaves, J.M.1    Taylor, S.S.2
  • 28
    • 0032910168 scopus 로고    scopus 로고
    • Organization and regulation of mitogen-activated protein kinase signaling pathways
    • Garrington T.P., Johnson G.L. Organization and regulation of mitogen-activated protein kinase signaling pathways. Curr. Opin. Cell Biol. 11:1999;211-218.
    • (1999) Curr. Opin. Cell Biol. , vol.11 , pp. 211-218
    • Garrington, T.P.1    Johnson, G.L.2
  • 29
    • 0033569722 scopus 로고    scopus 로고
    • An atypical mitogen-activated protein kinase (MAPK) homologue expressed in gametocytes of the human malaria parasite Plasmodium falciparum. Identification of a MAPK signature
    • Dorin D., Alano P., Boccaccio I., Ciceron L., Doerig C., Sulpice R., Parzy D. An atypical mitogen-activated protein kinase (MAPK) homologue expressed in gametocytes of the human malaria parasite Plasmodium falciparum. Identification of a MAPK signature. J. Biol. Chem. 274:1999;29912-29920.
    • (1999) J. Biol. Chem. , vol.274 , pp. 29912-29920
    • Dorin, D.1    Alano, P.2    Boccaccio, I.3    Ciceron, L.4    Doerig, C.5    Sulpice, R.6    Parzy, D.7
  • 30
    • 0033538053 scopus 로고    scopus 로고
    • Molecular cloning and expression of a stress-responsive mitogen-activated protein kinase-related kinase from Tetrahymena cells
    • Nakashima S., Wang S., Hisamoto N., Sakai H., Andoh M., Matsumoto K., Nozawa Y. Molecular cloning and expression of a stress-responsive mitogen-activated protein kinase-related kinase from Tetrahymena cells. J. Biol. Chem. 274:1999;9976-9983.
    • (1999) J. Biol. Chem. , vol.274 , pp. 9976-9983
    • Nakashima, S.1    Wang, S.2    Hisamoto, N.3    Sakai, H.4    Andoh, M.5    Matsumoto, K.6    Nozawa, Y.7
  • 31
    • 0036855223 scopus 로고    scopus 로고
    • Stage-specific requirement of a mitogen-activated protein kinase by Trypanosoma brucei
    • Muller I.B., Domenicali-Pfister D., Roditi I., Vassella E. Stage-specific requirement of a mitogen-activated protein kinase by Trypanosoma brucei. Mol. Biol. Cell. 13:2002;3787-3799.
    • (2002) Mol. Biol. Cell , vol.13 , pp. 3787-3799
    • Muller, I.B.1    Domenicali-Pfister, D.2    Roditi, I.3    Vassella, E.4
  • 32
    • 0034509322 scopus 로고    scopus 로고
    • Protein tyrosine kinase activity in human malaria parasite Plasmodium falciparum
    • Sharma A. Protein tyrosine kinase activity in human malaria parasite Plasmodium falciparum. Indian J. Exp. Biol. 38:2000;1222-1226.
    • (2000) Indian J. Exp. Biol. , vol.38 , pp. 1222-1226
    • Sharma, A.1
  • 34
    • 0027459506 scopus 로고
    • Protein kinases in divergent eukaryotes: Identification of protein kinase activities regulated during trypanosome development
    • Parsons M., Valentine M., Carter V. Protein kinases in divergent eukaryotes: identification of protein kinase activities regulated during trypanosome development. Proc. Natl. Acad. Sci. U. S. A. 90:1993;2656-2660.
    • (1993) Proc. Natl. Acad. Sci. U. S. A. , vol.90 , pp. 2656-2660
    • Parsons, M.1    Valentine, M.2    Carter, V.3
  • 35
    • 0031026008 scopus 로고    scopus 로고
    • The protein kinases of budding yeast: Six score and more
    • Hunter T., Plowman G.D. The protein kinases of budding yeast: six score and more. Trends Biochem. Sci. 22:1997;18-22.
    • (1997) Trends Biochem. Sci. , vol.22 , pp. 18-22
    • Hunter, T.1    Plowman, G.D.2
  • 36
    • 0029896543 scopus 로고    scopus 로고
    • Leishmania chagasi: A gene encoding a protein kinase with a catalytic domain structurally related to MAP kinase kinase
    • Li S., Wilson M.E., Donelson J.E. Leishmania chagasi: a gene encoding a protein kinase with a catalytic domain structurally related to MAP kinase kinase. Exp. Parasitol. 82:1996;87-96.
    • (1996) Exp. Parasitol. , vol.82 , pp. 87-96
    • Li, S.1    Wilson, M.E.2    Donelson, J.E.3
  • 37
    • 85056017700 scopus 로고    scopus 로고
    • A protein kinase involved in flagellar length control
    • (in press).
    • M. Wiese, D. Kuhn, C.G. Grünfelder. A protein kinase involved in flagellar length control. Eukaryotic Cell (in press).
    • Eukaryotic Cell
    • Wiese, M.1    Kuhn, D.2    Grünfelder, C.G.3
  • 38
    • 0034176923 scopus 로고    scopus 로고
    • PfPK6, a novel cyclin-dependent kinase/mitogen-activated protein kinase-related protein kinase from Plasmodium falciparum
    • Bracchi-Ricard V., Barik S., Delvecchio C., Doerig C., Chakrabarti R., Chakrabarti D. PfPK6, a novel cyclin-dependent kinase/mitogen-activated protein kinase-related protein kinase from Plasmodium falciparum. Biochem. J. 347(Pt. 1):2000;255-263.
    • (2000) Biochem. J. , vol.347 , Issue.PT. 1 , pp. 255-263
    • Bracchi-Ricard, V.1    Barik, S.2    Delvecchio, C.3    Doerig, C.4    Chakrabarti, R.5    Chakrabarti, D.6
  • 39
    • 0346131227 scopus 로고    scopus 로고
    • The cell cycle of parasitic protozoa: Potential for chemotherapeutic exploitation
    • Hammarton T., Mottram J.C., Doerig C. The cell cycle of parasitic protozoa: potential for chemotherapeutic exploitation. Prog. Cell Cycle Res. 5:2003;91-101.
    • (2003) Prog. Cell Cycle Res. , vol.5 , pp. 91-101
    • Hammarton, T.1    Mottram, J.C.2    Doerig, C.3
  • 40
    • 0039278089 scopus 로고    scopus 로고
    • A MAP kinase homologue from the human malaria parasite Plasmodium falciparum
    • Doerig C.M., Parzy D., Langsley G., Horrocks P., Carter R., Doerig C.D. A MAP kinase homologue from the human malaria parasite Plasmodium falciparum. Gene. 177:1996;1-6.
    • (1996) Gene , vol.177 , pp. 1-6
    • Doerig, C.M.1    Parzy, D.2    Langsley, G.3    Horrocks, P.4    Carter, R.5    Doerig, C.D.6
  • 41
    • 0034850190 scopus 로고    scopus 로고
    • Pfnek-1, a NIMA-related kinase from the human malaria parasite plasmodium falciparum biochemical properties and possible involvement in MAPK regulation
    • Dorin D., Le Roch K., Sallicandro P., Alano P., Parzy D., Poullet P., Meijer L., Doerig C. Pfnek-1, a NIMA-related kinase from the human malaria parasite plasmodium falciparum biochemical properties and possible involvement in MAPK regulation. Eur. J. Biochem. 268:2001;2600-2608.
    • (2001) Eur. J. Biochem. , vol.268 , pp. 2600-2608
    • Dorin, D.1    Le Roch, K.2    Sallicandro, P.3    Alano, P.4    Parzy, D.5    Poullet, P.6    Meijer, L.7    Doerig, C.8
  • 42
    • 0029114836 scopus 로고
    • A family of trypanosome cdc2-related protein kinases
    • Mottram J.C., Smith G. A family of trypanosome cdc2-related protein kinases. Gene. 162:1995;147-152.
    • (1995) Gene , vol.162 , pp. 147-152
    • Mottram, J.C.1    Smith, G.2
  • 43
    • 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. 32:2002;1575-1585.
    • (2002) Int. J. Parasitol. , vol.32 , pp. 1575-1585
    • Doerig, C.1    Endicott, J.2    Chakrabarti, D.3
  • 44
    • 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., Meijer L., Doerig C. 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    Waters, N.4    Kappes, B.5    Chakrabarti, D.6    Meijer, L.7    Doerig, C.8
  • 45
    • 0035413616 scopus 로고    scopus 로고
    • Cyclin-dependent kinases
    • Harper J.W., Adams P.D. Cyclin-dependent kinases. Chem. Rev. 101:2001;2511-2526.
    • (2001) Chem. Rev. , vol.101 , pp. 2511-2526
    • Harper, J.W.1    Adams, P.D.2
  • 46
    • 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.W., Gussio R., Leost M., Senderowicz A.M., Lahusen T., Kunick C., Meijer L., Sausville E.A. Discovery and initial characterization of the paullones, a novel class of small-molecule inhibitors of cyclin-dependent kinases. Cancer Res. 5:1999;2566-2569.
    • (1999) Cancer Res. , vol.5 , pp. 2566-2569
    • Zaharevitz, D.W.1    Gussio, R.2    Leost, M.3    Senderowicz, A.M.4    Lahusen, T.5    Kunick, C.6    Meijer, L.7    Sausville, E.A.8
  • 47
    • 0033614949 scopus 로고    scopus 로고
    • Paullones, a series of cyclin-dependent kinase inhibitors: Synthesis, evaluation of CDK1/cyclin B inhibition, and in vitro antitumor activity
    • Schultz C., Link A., Leost M., Zaharevitz D.W., Gussio R., Sausville E.A., Meijer L., Kunick C. 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    Link, A.2    Leost, M.3    Zaharevitz, D.W.4    Gussio, R.5    Sausville, E.A.6    Meijer, L.7    Kunick, C.8
  • 51
    • 0028331873 scopus 로고
    • Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases
    • Gleason W.B., Fu Z., Birktoft J., Banaszak L. Refined crystal structure of mitochondrial malate dehydrogenase from porcine heart and the consensus structure for dicarboxylic acid oxidoreductases. Biochemistry. 33:1994;2078-2088.
    • (1994) Biochemistry , vol.33 , pp. 2078-2088
    • Gleason, W.B.1    Fu, Z.2    Birktoft, J.3    Banaszak, L.4
  • 52
    • 0024413884 scopus 로고
    • Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution
    • Birktoft J.J., Rhodes G., Banaszak L.J. Refined crystal structure of cytoplasmic malate dehydrogenase at 2.5-A resolution. Biochemistry. 28:1989;6065-6081.
    • (1989) Biochemistry , vol.28 , pp. 6065-6081
    • Birktoft, J.J.1    Rhodes, G.2    Banaszak, L.J.3
  • 54
    • 0021928596 scopus 로고
    • Purification of particulate malate dehydrogenase and phosphoenolpyruvate carboxykinase from Leishmania mexicana mexicana
    • Mottram J.C., Coombs G.H. Purification of particulate malate dehydrogenase and phosphoenolpyruvate carboxykinase from Leishmania mexicana mexicana. Biochim. Biophys. Acta. 827:1985;310-319.
    • (1985) Biochim. Biophys. Acta , vol.827 , pp. 310-319
    • Mottram, J.C.1    Coombs, G.H.2
  • 55
    • 0026541023 scopus 로고
    • Purification and properties of Plasmodium falciparum malate dehydrogenase
    • Lang-Unnasch N. Purification and properties of Plasmodium falciparum malate dehydrogenase. Mol. Biochem. Parasitol. 50:1992;17-25.
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 17-25
    • Lang-Unnasch, N.1
  • 56
    • 0035427503 scopus 로고    scopus 로고
    • Structure-activity 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., Doerig C., Havlik I. Structure-activity relationships and inhibitory effects of various purine derivatives on the in vitro growth of Plasmodium falciparum. Biochem. Pharmacol. 62:2001;341-348.
    • (2001) Biochem. Pharmacol. , vol.62 , pp. 341-348
    • Harmse, L.1    Van Zyl, R.2    Gray, N.3    Schultz, P.4    Leclerc, S.5    Meijer, L.6    Doerig, C.7    Havlik, I.8
  • 59
    • 0030705190 scopus 로고    scopus 로고
    • Identification, cloning, and mutational analysis of the casein kinase 1 cDNA of the malaria parasite, Plasmodium falciparum. Stage-specific expression of the gene
    • Barik S., Taylor R.E., Chakrabarti D. Identification, cloning, and mutational analysis of the casein kinase 1 cDNA of the malaria parasite, Plasmodium falciparum. Stage-specific expression of the gene. 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
  • 60
    • 0034235518 scopus 로고    scopus 로고
    • Identification of a nucleoside/nucleobase transporter from Plasmodium falciparum, a novel target for anti-malarial chemotherapy
    • Parker M.D., Hyde R.J., Yao S.Y., McRobert L., Cass C.E., Young J.D., McConkey G.A., Baldwin S.A. Identification of a nucleoside/nucleobase transporter from Plasmodium falciparum, a novel target for anti-malarial chemotherapy. Biochem. J. 349:2000;67-75.
    • (2000) Biochem. J. , vol.349 , pp. 67-75
    • Parker, M.D.1    Hyde, R.J.2    Yao, S.Y.3    McRobert, L.4    Cass, C.E.5    Young, J.D.6    McConkey, G.A.7    Baldwin, S.A.8
  • 61
    • 0035798637 scopus 로고    scopus 로고
    • Localization of the Plasmodium falciparum PfNT1 nucleoside transporter to the parasite plasma membrane
    • Rager N., Mamoun C.B., Carter N.S., Goldberg D.E., Ullman B. Localization of the Plasmodium falciparum PfNT1 nucleoside transporter to the parasite plasma membrane. J. Biol. Chem. 276:2001;41095-41099.
    • (2001) J. Biol. Chem. , vol.276 , pp. 41095-41099
    • Rager, N.1    Mamoun, C.B.2    Carter, N.S.3    Goldberg, D.E.4    Ullman, B.5
  • 62
    • 0028307510 scopus 로고
    • Phosphorylation of protein 4.1 in Plasmodium falciparum-infected human red blood cells
    • Chishti A.H., Maalouf G.J., Marfatia S., Palek J., Wang W., Fisher D., Liu S.C. Phosphorylation of protein 4.1 in Plasmodium falciparum-infected human red blood cells. Blood. 83:1994;3339-3345.
    • (1994) Blood , vol.83 , pp. 3339-3345
    • Chishti, A.H.1    Maalouf, G.J.2    Marfatia, S.3    Palek, J.4    Wang, W.5    Fisher, D.6    Liu, S.C.7
  • 63
    • 0025987531 scopus 로고
    • Leishmanial protein kinases phosphorylate components of the complement system
    • Hermoso T., Fishelson Z., Becker S.I., Hirschberg K., Jaffe C.L. Leishmanial protein kinases phosphorylate components of the complement system. EMBO J. 10:1991;4061-4067.
    • (1991) EMBO J. , vol.10 , pp. 4061-4067
    • Hermoso, T.1    Fishelson, Z.2    Becker, S.I.3    Hirschberg, K.4    Jaffe, C.L.5
  • 64
    • 0034306450 scopus 로고    scopus 로고
    • Specificity and mechanism of action of some commonly used protein kinase inhibitors
    • Davies S.P., Reddy H., Caivano M., Cohen P. Specificity and mechanism of action of some commonly used protein kinase inhibitors. Biochem. J. 351:2000;95-105.
    • (2000) Biochem. J. , vol.351 , pp. 95-105
    • Davies, S.P.1    Reddy, H.2    Caivano, M.3    Cohen, P.4
  • 65
    • 0035814077 scopus 로고    scopus 로고
    • Design and synthesis of Pfmrk inhibitors as potential antimalarial agents
    • Xiao Z., Waters N.C., Woodard C.L., Li Z., Li P.K. Design and synthesis of Pfmrk inhibitors as potential antimalarial agents. Bioorg. Med. Chem. Lett. 11:2001;2875-2878.
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 2875-2878
    • Xiao, Z.1    Waters, N.C.2    Woodard, C.L.3    Li, Z.4    Li, P.K.5
  • 66
    • 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 K.M., Hassan P., Anderson J.S., Mottram J.C. The crk3 gene of Leishmania mexicana encodes a stage-regulated cdc2-related histone H1 kinase that associates with p12. J. Biol. Chem. 273:1998;10153-10159.
    • (1998) J. Biol. Chem. , vol.273 , pp. 10153-10159
    • Grant, K.M.1    Hassan, P.2    Anderson, J.S.3    Mottram, J.C.4
  • 67
    • 0036697233 scopus 로고    scopus 로고
    • Protein kinases as drug targets in parasitic protozoa
    • Doerig C., Meijer L., Mottram J.C. Protein kinases as drug targets in parasitic protozoa. Trends Parasitol. 18:2002;366-371.
    • (2002) Trends Parasitol. , vol.18 , pp. 366-371
    • Doerig, C.1    Meijer, L.2    Mottram, J.C.3
  • 68
    • 0035815349 scopus 로고    scopus 로고
    • The CRK3 protein kinase is essential for cell cycle progression of Leishmania mexicana
    • Hassan P., Fergusson D., Grant K.M., Mottram J.C. The CRK3 protein kinase is essential for cell cycle progression of Leishmania mexicana. Mol. Biochem. Parasitol. 113:2001;189-198.
    • (2001) Mol. Biochem. Parasitol. , vol.113 , pp. 189-198
    • Hassan, P.1    Fergusson, D.2    Grant, K.M.3    Mottram, J.C.4
  • 69
    • 0029830610 scopus 로고    scopus 로고
    • Gene disruptions indicate an essential function for the LmmCRK1 cdc2-related kinase of Leishmania mexicana
    • Mottram J.C., McCready B.P., Brown K.G., Grant K.M. Gene disruptions indicate an essential function for the LmmCRK1 cdc2-related kinase of Leishmania mexicana. Mol. Microbiol. 22:1996;573-583.
    • (1996) Mol. Microbiol. , vol.22 , pp. 573-583
    • Mottram, J.C.1    McCready, B.P.2    Brown, K.G.3    Grant, K.M.4
  • 70
    • 0032080107 scopus 로고    scopus 로고
    • A mitogen-activated protein (MAP) kinase homologue of Leishmania mexicana is essential for parasite survival in the infected host
    • Wiese M. A mitogen-activated protein (MAP) kinase homologue of Leishmania mexicana is essential for parasite survival in the infected host. EMBO J. 17:1998;2619-2628.
    • (1998) EMBO J. , vol.17 , pp. 2619-2628
    • Wiese, M.1
  • 71
    • 1542276240 scopus 로고    scopus 로고
    • Stage-specific differences in cell cycle control in Trypanosoma brucei revealed by RNAi of a mitotic cyclin
    • Hammarton T.C., Clark J., Douglas F., Boshart M., Mottram J.C. Stage-specific differences in cell cycle control in Trypanosoma brucei revealed by RNAi of a mitotic cyclin. J. Biol. Chem. 7:2003;7.
    • (2003) J. Biol. Chem. , vol.7 , pp. 7
    • Hammarton, T.C.1    Clark, J.2    Douglas, F.3    Boshart, M.4    Mottram, J.C.5
  • 72
    • 0031253198 scopus 로고    scopus 로고
    • Gene targeting in malaria parasites
    • Menard R., Janse C. Gene targeting in malaria parasites. Methods. 13:1997;148-157.
    • (1997) Methods , vol.13 , pp. 148-157
    • Menard, R.1    Janse, C.2
  • 75
    • 0035407514 scopus 로고    scopus 로고
    • Current developments in malaria transmission-blocking vaccines
    • Stowers A., Carter R. Current developments in malaria transmission-blocking vaccines. Expert Opin. Biol. Ther. 1:2001;619-628.
    • (2001) Expert Opin. Biol. Ther. , vol.1 , pp. 619-628
    • Stowers, A.1    Carter, R.2
  • 76
    • 0034616295 scopus 로고    scopus 로고
    • Chitinases of the avian malaria parasite Plasmodium gallinaceum, a class of enzymes necessary for parasite invasion of the mosquito midgut
    • Vinetz J.M., Valenzuela J.G., Specht C.A., Aravind L., Langer R.C., Ribeiro J.M., Kaslow D.C. Chitinases of the avian malaria parasite Plasmodium gallinaceum, a class of enzymes necessary for parasite invasion of the mosquito midgut. J. Biol. Chem. 275:2000;10331-10341.
    • (2000) J. Biol. Chem. , vol.275 , pp. 10331-10341
    • Vinetz, J.M.1    Valenzuela, J.G.2    Specht, C.A.3    Aravind, L.4    Langer, R.C.5    Ribeiro, J.M.6    Kaslow, D.C.7
  • 77
    • 0025194784 scopus 로고
    • Possible roles of Ca2+ and cGMP as mediators of the exflagellation of Plasmodium berghei and Plasmodium falciparum
    • Kawamoto F., Alejo-Blanco R., Fleck S.L., Kawamoto Y., Sinden R.E. Possible roles of Ca2+ and cGMP as mediators of the exflagellation of Plasmodium berghei and Plasmodium falciparum. Mol. Biochem. Parasitol. 42:1990;101-108.
    • (1990) Mol. Biochem. Parasitol , vol.42 , pp. 101-108
    • Kawamoto, F.1    Alejo-Blanco, R.2    Fleck, S.L.3    Kawamoto, Y.4    Sinden, R.E.5
  • 78
    • 0037133932 scopus 로고    scopus 로고
    • Inhibition of Ca2+/calmodulin-dependent protein kinase blocks morphological differentiation of plasmodium gallinaceum zygotes to ookinetes
    • Silva-Neto M.A., Atella G.C., Shahabuddin M. Inhibition of Ca2+/calmodulin-dependent protein kinase blocks morphological differentiation of plasmodium gallinaceum zygotes to ookinetes. J. Biol. Chem. 277:2002;14085-14091.
    • (2002) J. Biol. Chem. , vol.277 , pp. 14085-14091
    • Silva-Neto, M.A.1    Atella, G.C.2    Shahabuddin, M.3
  • 79
    • 0034083116 scopus 로고    scopus 로고
    • Theileria parva: Taking control of host cell proliferation and survival mechanisms
    • Dobbelaere D.A., Fernandez P.C., Heussler V.T. Theileria parva: taking control of host cell proliferation and survival mechanisms. Cell. Microbiol. 2:2000;91-99.
    • (2000) Cell. Microbiol. , vol.2 , pp. 91-99
    • Dobbelaere, D.A.1    Fernandez, P.C.2    Heussler, V.T.3
  • 81
  • 82
    • 0032740614 scopus 로고    scopus 로고
    • Extracellular signal-related kinase (ERK) and p38 mitogen-activated protein (MAP) kinases differentially regulate the lipopolysaccharide-mediated induction of inducible nitric oxide synthase and IL-12 in macrophages: Leishmania phosphoglycans subvert macrophage IL-12 production by targeting ERK MAP kinase
    • Feng G.J., Goodridge H.S., Harnett M.M., Wei X.Q., Nikolaev A.V., Higson A.P., Liew F.Y. Extracellular signal-related kinase (ERK) and p38 mitogen-activated protein (MAP) kinases differentially regulate the lipopolysaccharide-mediated induction of inducible nitric oxide synthase and IL-12 in macrophages: Leishmania phosphoglycans subvert macrophage IL-12 production by targeting ERK MAP kinase. J. Immunol. 163:1999;6403-6412.
    • (1999) J. Immunol. , vol.163 , pp. 6403-6412
    • Feng, G.J.1    Goodridge, H.S.2    Harnett, M.M.3    Wei, X.Q.4    Nikolaev, A.V.5    Higson, A.P.6    Liew, F.Y.7
  • 83
    • 0034101539 scopus 로고    scopus 로고
    • Dual role for transforming growth factor beta-dependent signaling in Trypanosoma cruzi infection of mammalian cells
    • Hall B.S., Pereira M.A. Dual role for transforming growth factor beta-dependent signaling in Trypanosoma cruzi infection of mammalian cells. Infect. Immun. 68:2000;2077-2081.
    • (2000) Infect. Immun. , vol.68 , pp. 2077-2081
    • Hall, B.S.1    Pereira, M.A.2
  • 84
    • 0036527429 scopus 로고    scopus 로고
    • Protein kinases-the major drug targets of the twenty-first century?
    • Cohen P. Protein kinases-the major drug targets of the twenty-first century? Nat. Rev. Drug Discov. 1:2002;309-315.
    • (2002) Nat. Rev. Drug Discov. , vol.1 , pp. 309-315
    • Cohen, P.1
  • 85
    • 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., 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
  • 86
    • 0028296130 scopus 로고
    • Calcium-binding properties of a calcium-dependent protein kinase from Plasmodium falciparum and the significance of individual calcium-binding sites for kinase activation
    • Zhao Y., Pokutta S., Maurer P., Lindt M., Franklin R.M., Kappes B. Calcium-binding properties of a calcium-dependent protein kinase from Plasmodium falciparum and the significance of individual calcium-binding sites for kinase activation. Biochemistry. 33:1994;3714-3721.
    • (1994) Biochemistry , vol.33 , pp. 3714-3721
    • Zhao, Y.1    Pokutta, S.2    Maurer, P.3    Lindt, M.4    Franklin, R.M.5    Kappes, B.6
  • 87
    • 0028121976 scopus 로고
    • Plasmodium falciparum calcium-dependent protein kinase phosphorylates proteins of the host erythrocytic membrane
    • Zhao Y., Franklin R.M., Kappes B. Plasmodium falciparum calcium-dependent protein kinase phosphorylates proteins of the host erythrocytic membrane. Mol. Biochem. Parasitol. 66:1994;329-343.
    • (1994) Mol. Biochem. Parasitol. , vol.66 , pp. 329-343
    • Zhao, Y.1    Franklin, R.M.2    Kappes, B.3
  • 88
    • 0036062618 scopus 로고    scopus 로고
    • A protein kinase specifically associated with proliferative forms of Trypanosoma brucei is functionally related to a yeast kinase involved in the co-ordination of cell shape and division
    • Garcia-Salcedo J.A., Nolan D.P., Gijon P., Gomez-Rodriguez J., Pays E. A protein kinase specifically associated with proliferative forms of Trypanosoma brucei is functionally related to a yeast kinase involved in the co-ordination of cell shape and division. Mol. Microbiol. 45:2002;307-319.
    • (2002) Mol. Microbiol. , vol.45 , pp. 307-319
    • Garcia-Salcedo, J.A.1    Nolan, D.P.2    Gijon, P.3    Gomez-Rodriguez, J.4    Pays, E.5
  • 90
    • 0037449812 scopus 로고    scopus 로고
    • Potential involvement of extracellular signal-regulated kinase 1 and 2 in encystation of a primitive eukaryote, Giardia lamblia. Stage-specific activation and intracellular localization
    • Ellis J.G.t., Davila M.R., Chakrabarti R. Potential involvement of extracellular signal-regulated kinase 1 and 2 in encystation of a primitive eukaryote, Giardia lamblia. Stage-specific activation and intracellular localization. J. Biol. Chem. 278:2003;1936-1945.
    • (2003) J. Biol. Chem. , vol.278 , pp. 1936-1945
    • T. G., E.J.1    Davila, M.R.2    Chakrabarti, R.3
  • 91
    • 0035971085 scopus 로고    scopus 로고
    • Possible roles of protein kinase a in cell motility and excystation of the early diverging eukaryote Giardia lamblia
    • Abel E.S., Davids B.J., Robles L.D., Loflin C.E., Gillin F.D., Chakrabarti R. Possible roles of protein kinase A in cell motility and excystation of the early diverging eukaryote Giardia lamblia. J. Biol. Chem. 276:2001;10320-10329.
    • (2001) J. Biol. Chem. , vol.276 , pp. 10320-10329
    • Abel, E.S.1    Davids, B.J.2    Robles, L.D.3    Loflin, C.E.4    Gillin, F.D.5    Chakrabarti, R.6
  • 92
    • 0242710962 scopus 로고    scopus 로고
    • Structures of P. falciparum PfPK5: Testing the CDK regulation paradigm and mechanisms of small molecules inhibition
    • Holton S., Merckx A., Burgess D., Doerig C., Noble M., Endicott J. Structures of P. falciparum PfPK5: testing the CDK regulation paradigm and mechanisms of small molecules inhibition. Structure. 11:2003;1329-1337.
    • (2003) Structure , vol.11 , pp. 1329-1337
    • Holton, S.1    Merckx, A.2    Burgess, D.3    Doerig, C.4    Noble, M.5    Endicott, J.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.