메뉴 건너뛰기




Volumn 15, Issue 11, 1999, Pages 449-454

An overview of plasmodium protein kinases

Author keywords

[No Author keywords available]

Indexed keywords

MITOGEN ACTIVATED PROTEIN KINASE; PROTEIN KINASE;

EID: 0033231908     PISSN: 01694758     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0169-4758(99)01527-6     Document Type: Review
Times cited : (61)

References (59)
  • 1
    • 0029020282 scopus 로고
    • Protein kinases 6. The eukaryotic protein kinase superfamily: Kinase (catalytic) domain structure and classification
    • Hanks S.K., Hunter T. Protein kinases 6. The eukaryotic protein kinase superfamily: kinase (catalytic) domain structure and classification. FASEB J. 9:1995;576-596.
    • (1995) FASEB J. , vol.9 , pp. 576-596
    • Hanks, S.K.1    Hunter, T.2
  • 2
    • 0030942699 scopus 로고    scopus 로고
    • Histidine kinases in signal transduction pathways of eukaryotes
    • Loomis W.F.et al. Histidine kinases in signal transduction pathways of eukaryotes. J. Cell Sci. 110:1997;1141-1145.
    • (1997) J. Cell Sci. , vol.110 , pp. 1141-1145
    • Loomis, W.F.1
  • 3
    • 0032809084 scopus 로고    scopus 로고
    • A family of PP2 phosphatases in Plasmodium falciparum and parasitic protozoa
    • Garcia A.et al. A family of PP2 phosphatases in Plasmodium falciparum and parasitic protozoa. Parasitol. Today. 15:1999;90-92.
    • (1999) Parasitol. Today , vol.15 , pp. 90-92
    • Garcia, A.1
  • 5
    • 0029768093 scopus 로고    scopus 로고
    • Targeted disruption of the cyclin-dependent kinase 5 gene results in abnormal corticogenesis, neuronal pathology and perinatal death
    • Ohshima T.et al. Targeted disruption of the cyclin-dependent kinase 5 gene results in abnormal corticogenesis, neuronal pathology and perinatal death. Proc. Natl. Acad. Sci. U. S. A. 93:1996;11173-11178.
    • (1996) Proc. Natl. Acad. Sci. U. S. A. , vol.93 , pp. 11173-11178
    • Ohshima, T.1
  • 6
    • 0032005366 scopus 로고    scopus 로고
    • The cyclin family of budding yeast: Abundant use of a good idea
    • Andrews B., Measday V. The cyclin family of budding yeast: abundant use of a good idea. Trends Genet. 14:1998;66-72.
    • (1998) Trends Genet. , vol.14 , pp. 66-72
    • Andrews, B.1    Measday, V.2
  • 7
    • 0028491074 scopus 로고
    • The cell cycle kinases
    • Pines J. The cell cycle kinases. Semin. Cancer Biol. 5:1994;305-313.
    • (1994) Semin. Cancer Biol. , vol.5 , pp. 305-313
    • Pines, J.1
  • 8
    • 0027943714 scopus 로고
    • Activation of cyclin-dependent kinase 4 (cdk4) by mouse MO15-associated kinase
    • Matsuoka M.et al. Activation of cyclin-dependent kinase 4 (cdk4) by mouse MO15-associated kinase. Mol. Cell. Biol. 14:1994;7265-7275.
    • (1994) Mol. Cell. Biol. , vol.14 , pp. 7265-7275
    • Matsuoka, M.1
  • 9
    • 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.et al. 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
  • 10
    • 0030973423 scopus 로고    scopus 로고
    • Cleavage of PITSLRE kinases by ICE/CASP-1 and CPP32/CASP-3 during apoptosis induced by tumor necrosis factor
    • Beyaert R.et al. Cleavage of PITSLRE kinases by ICE/CASP-1 and CPP32/CASP-3 during apoptosis induced by tumor necrosis factor. J. Biol. Chem. 272:1997;11694-11697.
    • (1997) J. Biol. Chem. , vol.272 , pp. 11694-11697
    • Beyaert, R.1
  • 11
    • 0031809282 scopus 로고    scopus 로고
    • The RNP protein, RNPS1, associates with specific isoforms of the p34 (cdc2)-related PITSLRE protein kinase in vivo
    • Loyer P.et al. The RNP protein, RNPS1, associates with specific isoforms of the p34 (cdc2)-related PITSLRE protein kinase in vivo. J. Cell Sci. 111:1998;1495-1506.
    • (1998) J. Cell Sci. , vol.111 , pp. 1495-1506
    • Loyer, P.1
  • 12
    • 0028224015 scopus 로고
    • Isolation and expression of a gene specifying a cdc2-like protein kinase from the human malaria parasite Plasmodium falciparum
    • Ross-MacDonald P.B.et al. Isolation and expression of a gene specifying a cdc2-like protein kinase from the human malaria parasite Plasmodium falciparum. Eur. J. Biochem. 220:1994;693-701.
    • (1994) Eur. J. Biochem. , vol.220 , pp. 693-701
    • Ross-MacDonald, P.B.1
  • 13
    • 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.et al. 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
  • 14
    • 0028988027 scopus 로고
    • Pfcrk-1, a developmentally regulated cdc2-related protein kinase of Plasmodium falciparum
    • Doerig C.D.et al. Pfcrk-1, a developmentally regulated cdc2-related protein kinase of Plasmodium falciparum. Mol. Biochem. Parasitol. 70:1995;167-174.
    • (1995) Mol. Biochem. Parasitol. , vol.70 , pp. 167-174
    • Doerig, C.D.1
  • 15
    • 0030200306 scopus 로고    scopus 로고
    • Mechanisms of activation of the cdc2-related kinase PfPK5 from Plasmodium falciparum
    • Graeser R.et al. 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
  • 16
    • 0030581694 scopus 로고    scopus 로고
    • Plasmodium falciparum protein kinase 5 and the malarial nuclear division cycles
    • Graeser R.et al. 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
  • 17
    • 0027978170 scopus 로고
    • P35 is a neural-specific regulatory subunit of cyclin-dependent kinase 5
    • Tsai L.H.et al. p35 is a neural-specific regulatory subunit of cyclin-dependent kinase 5. Nature. 371:1994;419-423.
    • (1994) Nature , vol.371 , pp. 419-423
    • Tsai, L.H.1
  • 18
    • 0028333768 scopus 로고
    • Sequential protein kinase reactions controlling cell growth and differentiation
    • Johnson G.L., Vaillancourt R.R. Sequential protein kinase reactions controlling cell growth and differentiation. Curr. Opin. Cell Biol. 6:1994;230-238.
    • (1994) Curr. Opin. Cell Biol. , vol.6 , pp. 230-238
    • Johnson, G.L.1    Vaillancourt, R.R.2
  • 19
    • 0031977016 scopus 로고    scopus 로고
    • The riddle of MAP kinase signaling specificity
    • Madhani H.D., Fink G.R. The riddle of MAP kinase signaling specificity. Trends Genet. 14:1998;151-155.
    • (1998) Trends Genet. , vol.14 , pp. 151-155
    • Madhani, H.D.1    Fink, G.R.2
  • 20
    • 0039278089 scopus 로고    scopus 로고
    • A MAP kinase homologue from the human malaria parasite, Plasmodium falciparum
    • Doerig C.M.et al. 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
  • 21
    • 0029943490 scopus 로고    scopus 로고
    • Stage-specific expression of a Plasmodium falciparum protein related to the eukaryotic mitogen-activated protein kinases
    • Lin D.T.et al. Stage-specific expression of a Plasmodium falciparum protein related to the eukaryotic mitogen-activated protein kinases. Mol. Biochem. Parasitol. 78:1996;67-77.
    • (1996) Mol. Biochem. Parasitol. , vol.78 , pp. 67-77
    • Lin, D.T.1
  • 22
    • 0031031218 scopus 로고    scopus 로고
    • Characterization of a mitogen-activated protein (MAP) kinase from Plasmodium falciparum
    • Graeser R.et al. Characterization of a mitogen-activated protein (MAP) kinase from Plasmodium falciparum. Mol. Microbiol. 23:1997;151-159.
    • (1997) Mol. Microbiol. , vol.23 , pp. 151-159
    • Graeser, R.1
  • 23
    • 0027532627 scopus 로고
    • Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro
    • Robbins D.J.et al. Regulation and properties of extracellular signal-regulated protein kinases 1 and 2 in vitro. J. Biol. Chem. 268:1993;5097-5106.
    • (1993) J. Biol. Chem. , vol.268 , pp. 5097-5106
    • Robbins, D.J.1
  • 24
    • 0028491116 scopus 로고
    • Regulation and functions of the glycogen synthase kinase-3 subfamily
    • Woodgett J.R. Regulation and functions of the glycogen synthase kinase-3 subfamily. Semin. Cancer Biol. 5:1994;269-275.
    • (1994) Semin. Cancer Biol. , vol.5 , pp. 269-275
    • Woodgett, J.R.1
  • 25
    • 0030841793 scopus 로고    scopus 로고
    • PDK1, one of the missing links in insulin signal transduction?
    • Cohen P.et al. PDK1, one of the missing links in insulin signal transduction? FEBS Lett. 410:1997;3-10.
    • (1997) FEBS Lett. , vol.410 , pp. 3-10
    • Cohen, P.1
  • 26
    • 0031306770 scopus 로고    scopus 로고
    • Protein kinase CK2 (`casein kinase-2') and its implication in cell division and proliferation
    • Pinna L.A., Meggio F. Protein kinase CK2 (`casein kinase-2') and its implication in cell division and proliferation. Prog. Cell Cycle Res. 3:1997;77-97.
    • (1997) Prog. Cell Cycle Res. , vol.3 , pp. 77-97
    • Pinna, L.A.1    Meggio, F.2
  • 27
    • 0026321413 scopus 로고
    • Multisite and hierarchal protein phosphorylation
    • Roach P.J. Multisite and hierarchal protein phosphorylation. J. Biol. Chem. 266:1991;14139-14142.
    • (1991) J. Biol. Chem. , vol.266 , pp. 14139-14142
    • Roach, P.J.1
  • 28
    • 0029027844 scopus 로고
    • A Plasmodium falciparum protein kinase with two unusually large kinase inserts
    • Kappes B.et al. A Plasmodium falciparum protein kinase with two unusually large kinase inserts. Mol. Biochem. Parasitol. 72:1995;163-178.
    • (1995) Mol. Biochem. Parasitol. , vol.72 , pp. 163-178
    • Kappes, B.1
  • 29
    • 0028059184 scopus 로고
    • A calcium-dependent protein kinase is present in Tetrahymena
    • Hegyesi H., Csaba G. A calcium-dependent protein kinase is present in Tetrahymena. Cell Biochem. Funct. 12:1994;221-226.
    • (1994) Cell Biochem. Funct. , vol.12 , pp. 221-226
    • Hegyesi, H.1    Csaba, G.2
  • 30
    • 0030152182 scopus 로고    scopus 로고
    • Characterization of eight new members of the calmodulin-like domain protein kinase gene family from Arabidopsis thaliana
    • Hrabak E.M.et al. Characterization of eight new members of the calmodulin-like domain protein kinase gene family from Arabidopsis thaliana. Plant Mol. Biol. 31:1996;405-412.
    • (1996) Plant Mol. Biol. , vol.31 , pp. 405-412
    • Hrabak, E.M.1
  • 31
    • 0029960592 scopus 로고    scopus 로고
    • Sequence, expression and localization of calmodulin-domain protein kinases in Eimeria tenella and Eimeria maxima
    • Dunn P.P.et al. Sequence, expression and localization of calmodulin-domain protein kinases in Eimeria tenella and Eimeria maxima. Parasitology. 113:1996;439-448.
    • (1996) Parasitology , vol.113 , pp. 439-448
    • Dunn, P.P.1
  • 32
    • 0031987352 scopus 로고    scopus 로고
    • 2+-dependent protein kinases of Paramecium - cloning provides evidence of a multigene family
    • 2+-dependent protein kinases of Paramecium - cloning provides evidence of a multigene family. Eur. J. Biochem. 251:1998;605-612.
    • (1998) Eur. J. Biochem. , vol.251 , pp. 605-612
    • Kim, K.1
  • 33
    • 0026594053 scopus 로고
    • Purification and characterization of wheat and pine small basic protein substrates for plant calcium-dependent protein kinase
    • Polya G.M.et al. Purification and characterization of wheat and pine small basic protein substrates for plant calcium-dependent protein kinase. Biochim. Biophys. Acta. 1120:1992;273-280.
    • (1992) Biochim. Biophys. Acta , vol.1120 , pp. 273-280
    • Polya, G.M.1
  • 34
    • 0032146404 scopus 로고    scopus 로고
    • Unusual membrane-associated protein kinases in higher plants
    • Satterlee J.S., Sussman M.R. Unusual membrane-associated protein kinases in higher plants. J. Membr. Biol. 164:1998;205-213.
    • (1998) J. Membr. Biol. , vol.164 , pp. 205-213
    • Satterlee, J.S.1    Sussman, M.R.2
  • 35
    • 0027416648 scopus 로고
    • Gene structure and expression of an unusual protein kinase from Plasmodium falciparum homologous at its carboxyl terminus with the EF hand calcium-binding proteins
    • Zhao Y.et al. Gene structure and expression of an unusual protein kinase from Plasmodium falciparum homologous at its carboxyl terminus with the EF hand calcium-binding proteins. J. Biol. Chem. 268:1993;4347-4354.
    • (1993) J. Biol. Chem. , vol.268 , pp. 4347-4354
    • Zhao, Y.1
  • 36
    • 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.et al. 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
  • 37
    • 0028121976 scopus 로고
    • Plasmodium falciparum calcium-dependent protein kinase phosphorylates proteins of the host erythrocytic membrane
    • Zhao Y.et al. 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
  • 38
    • 0030806327 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a second calcium-dependent protein kinase of Plasmodium falciparum
    • Färber P.M.et al. Molecular cloning and characterization of a second calcium-dependent protein kinase of Plasmodium falciparum. Mol. Biochem. Parasitol. 87:1997;211-216.
    • (1997) Mol. Biochem. Parasitol. , vol.87 , pp. 211-216
    • Färber, P.M.1
  • 39
    • 0031717105 scopus 로고    scopus 로고
    • The AMP-activated/SNF1 protein kinase subfamily: Metabolic sensors of the eukaryotic cell?
    • Hardie D.G.et al. The AMP-activated/SNF1 protein kinase subfamily: metabolic sensors of the eukaryotic cell? Annu. Rev. Biochem. 67:1998;821-855.
    • (1998) Annu. Rev. Biochem. , vol.67 , pp. 821-855
    • Hardie, D.G.1
  • 40
    • 0029927806 scopus 로고    scopus 로고
    • PfKIN, an SNF1 type protein kinase of Plasmodium falciparum predominantly expressed in gametocytes
    • Bracchi V.et al. PfKIN, an SNF1 type protein kinase of Plasmodium falciparum predominantly expressed in gametocytes. Mol. Biochem. Parasitol. 76:1996;299-303.
    • (1996) Mol. Biochem. Parasitol. , vol.76 , pp. 299-303
    • Bracchi, V.1
  • 41
    • 0029944966 scopus 로고    scopus 로고
    • Regulation of 5′-AMP-activated protein kinase activity by the noncatalytic beta and gamma subunits
    • Dyck J.R.B.et al. Regulation of 5′-AMP-activated protein kinase activity by the noncatalytic beta and gamma subunits. J. Biol. Chem. 271:1996;17798-17803.
    • (1996) J. Biol. Chem. , vol.271 , pp. 17798-17803
    • Dyck, J.R.B.1
  • 42
    • 0026638161 scopus 로고
    • Molecular cloning, stage-specific expression and cellular distribution of a putative protein kinase from Plasmodium falciparum
    • Zhao Y.et al. Molecular cloning, stage-specific expression and cellular distribution of a putative protein kinase from Plasmodium falciparum. Eur. J. Biochem. 207:1992;305-313.
    • (1992) Eur. J. Biochem. , vol.207 , pp. 305-313
    • Zhao, Y.1
  • 43
    • 0031923038 scopus 로고    scopus 로고
    • The JAK-STAT pathway: Signal transduction involved in proliferation, differentiation and transformation
    • Weber-Nordt R.M.et al. The JAK-STAT pathway: signal transduction involved in proliferation, differentiation and transformation. Leuk. Lymphoma. 28:1998;459-467.
    • (1998) Leuk. Lymphoma , vol.28 , pp. 459-467
    • Weber-Nordt, R.M.1
  • 44
    • 0027925813 scopus 로고
    • Regulation of Dictyostelium morphogenesis by cAMP-dependent protein kinase
    • Williams J.G.et al. Regulation of Dictyostelium morphogenesis by cAMP-dependent protein kinase. Philos. Trans. R. Soc. Lond. B. Biol. Sci. 340:1993;305-313.
    • (1993) Philos. Trans. R. Soc. Lond. B. Biol. Sci. , vol.340 , pp. 305-313
    • Williams, J.G.1
  • 45
    • 0019307068 scopus 로고
    • Gametocytogenesis by malaria parasites in continuous culture
    • Kaushal D.C.et al. Gametocytogenesis by malaria parasites in continuous culture. Nature. 286:1980;490-492.
    • (1980) Nature , vol.286 , pp. 490-492
    • Kaushal, D.C.1
  • 46
    • 0021077911 scopus 로고
    • Stage-specific inhibitory effect of cyclic AMP on asexual maturation and gametocyte formation of Plasmodium falciparum
    • Inselburg J. Stage-specific inhibitory effect of cyclic AMP on asexual maturation and gametocyte formation of Plasmodium falciparum. J. Parasitol. 69:1983;592-597.
    • (1983) J. Parasitol. , vol.69 , pp. 592-597
    • Inselburg, J.1
  • 47
    • 0025195598 scopus 로고
    • Cyclic AMP- and Ca2(+)-dependent protein kinases in Plasmodium falciparum
    • Read L.K., Mikkelsen R.B. Cyclic AMP- and Ca2(+)-dependent protein kinases in Plasmodium falciparum. Exp. Parasitol. 71:1990;39-48.
    • (1990) Exp. Parasitol. , vol.71 , pp. 39-48
    • Read, L.K.1    Mikkelsen, R.B.2
  • 48
    • 0028846249 scopus 로고
    • Cloning and structural analysis of the gene for cAMP-dependent protein kinase catalytic subunit from Plasmodium yoelii
    • Saito-Ito A.et al. Cloning and structural analysis of the gene for cAMP-dependent protein kinase catalytic subunit from Plasmodium yoelii. Biochim. Biophys. Acta. 1269:1995;1-5.
    • (1995) Biochim. Biophys. Acta , vol.1269 , pp. 1-5
    • Saito-Ito, A.1
  • 49
    • 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.et al. 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
  • 50
    • 0028108406 scopus 로고
    • A prenylation motif is required for plasma membrane localization and biochemical function of casein kinase I in budding yeast
    • Vancura A.et al. A prenylation motif is required for plasma membrane localization and biochemical function of casein kinase I in budding yeast. J. Biol. Chem. 269:1994;19271-19278.
    • (1994) J. Biol. Chem. , vol.269 , pp. 19271-19278
    • Vancura, A.1
  • 51
    • 0029131396 scopus 로고
    • Role of COOH-terminal phosphorylation in the regulation of casein kinase I delta
    • Graves P.R., Roach P.J. Role of COOH-terminal phosphorylation in the regulation of casein kinase I delta. J. Biol. Chem. 270:1995;21689-21694.
    • (1995) J. Biol. Chem. , vol.270 , pp. 21689-21694
    • Graves, P.R.1    Roach, P.J.2
  • 52
    • 0021058894 scopus 로고
    • A Plasmodium protein kinase that is developmentally regulated, stimulated by spermine, and inhibited by quercetin
    • Wiser M.F.et al. A Plasmodium protein kinase that is developmentally regulated, stimulated by spermine, and inhibited by quercetin. J. Cell. Biochem. 21:1983;305-314.
    • (1983) J. Cell. Biochem. , vol.21 , pp. 305-314
    • Wiser, M.F.1
  • 53
    • 0028171125 scopus 로고
    • EIF-2 kinases: Regulators of general and gene-specific translation initiation
    • Wek R.C. eIF-2 kinases: regulators of general and gene-specific translation initiation. Trends Biochem. Sci. 19:1994;491-496.
    • (1994) Trends Biochem. Sci. , vol.19 , pp. 491-496
    • Wek, R.C.1
  • 54
    • 0030665841 scopus 로고    scopus 로고
    • Molecular cloning, characterization and localization of PfPK4, an eIF-2α kinase-related enzyme from the malarial parasite Plasmodium falciparum
    • Möhrle J.J.et al. Molecular cloning, characterization and localization of PfPK4, an eIF-2α kinase-related enzyme from the malarial parasite Plasmodium falciparum. Biochem. J. 328:1997;677-687.
    • (1997) Biochem. J. , vol.328 , pp. 677-687
    • Möhrle, J.J.1
  • 55
    • 0022380342 scopus 로고
    • Accumulation and drainage of hemin in the red cell membrane
    • Shaklai N.et al. Accumulation and drainage of hemin in the red cell membrane. Biochim. Biophys. Acta. 821:1985;355-366.
    • (1985) Biochim. Biophys. Acta , vol.821 , pp. 355-366
    • Shaklai, N.1
  • 56
    • 0030936867 scopus 로고    scopus 로고
    • A putative Plasmodium falciparum exported serine/threonine protein kinase
    • Kun J.F.et al. A putative Plasmodium falciparum exported serine/threonine protein kinase. Mol. Biochem. Parasitol. 85:1997;41-51.
    • (1997) Mol. Biochem. Parasitol. , vol.85 , pp. 41-51
    • Kun, J.F.1
  • 57
    • 85047671892 scopus 로고    scopus 로고
    • Plant transmembrane receptors: New pieces in the signaling puzzle
    • Braun D.M., Walker J.C. Plant transmembrane receptors: new pieces in the signaling puzzle. Trends Biochem. Sci. 21:1996;70-73.
    • (1996) Trends Biochem. Sci. , vol.21 , pp. 70-73
    • Braun, D.M.1    Walker, J.C.2
  • 58
    • 0029830610 scopus 로고    scopus 로고
    • Gene disruptions indicate an essential function for the LmmCRK1 cdc2-related kinase of Leishmania mexicana
    • Mottram J.C.et al. 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
  • 59
    • 0027422291 scopus 로고
    • Site-specific recombinases: Tools for genome engineering
    • Kilby N.J.et al. Site-specific recombinases: tools for genome engineering. Trends Genet. 9:1993;413-421.
    • (1993) Trends Genet. , vol.9 , pp. 413-421
    • Kilby, N.J.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.