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Volumn 266, Issue , 2008, Pages 85-156

Plasmodium in the Postgenomic Era: New Insights into the Molecular Cell Biology of Malaria Parasites

Author keywords

Ca2+ signaling; Gene expression; Malaria; Merozoite invasion; Plasmodium transfection; Transcriptional regulation

Indexed keywords

CALCIUM ION; MESSENGER RNA; PROTEINASE; TRYPTOPHAN; CALCIUM; CELL CYCLE PROTEIN;

EID: 48949097073     PISSN: 19376448     EISSN: None     Source Type: Book Series    
DOI: 10.1016/S1937-6448(07)66003-1     Document Type: Review
Times cited : (68)

References (378)
  • 2
    • 0037458563 scopus 로고    scopus 로고
    • The signal sequence of exported protein-1 directs the green fluorescent protein to the parasitophorous vacuole of transfected malaria parasites
    • Adisa A., Rug M., Klonis N., Foley M., Cowman A.F., and Tilley L. The signal sequence of exported protein-1 directs the green fluorescent protein to the parasitophorous vacuole of transfected malaria parasites. J. Biol. Chem. 278 (2003) 6532-6542
    • (2003) J. Biol. Chem. , vol.278 , pp. 6532-6542
    • Adisa, A.1    Rug, M.2    Klonis, N.3    Foley, M.4    Cowman, A.F.5    Tilley, L.6
  • 3
    • 0027194909 scopus 로고
    • Cytosolic free calcium in Plasmodium falciparum-infected erythrocytes and the effect of verapamil: A cytofluorimetric study
    • Adovelande J., Bastide B., Deleze J., and Schrevel J. Cytosolic free calcium in Plasmodium falciparum-infected erythrocytes and the effect of verapamil: A cytofluorimetric study. Exp. Parasitol. 76 (1993) 247-258
    • (1993) Exp. Parasitol. , vol.76 , pp. 247-258
    • Adovelande, J.1    Bastide, B.2    Deleze, J.3    Schrevel, J.4
  • 4
    • 0013930819 scopus 로고
    • The fine structure of the erythrocytic stages of three avian malarial parasites, Plasmodium fallax, P. lophurae, and P. cathemerium
    • Aikawa M. The fine structure of the erythrocytic stages of three avian malarial parasites, Plasmodium fallax, P. lophurae, and P. cathemerium. Am. J. Trop. Med. Hyg. 15 (1966) 449-471
    • (1966) Am. J. Trop. Med. Hyg. , vol.15 , pp. 449-471
    • Aikawa, M.1
  • 5
    • 0014141981 scopus 로고
    • Ultrastructure of the pellicular complex of Plasmodium fallax
    • Aikawa M. Ultrastructure of the pellicular complex of Plasmodium fallax. J. Cell Biol. 35 (1967) 103-113
    • (1967) J. Cell Biol. , vol.35 , pp. 103-113
    • Aikawa, M.1
  • 6
    • 0014106537 scopus 로고
    • Fine structure of the asexual stages of Plasmodium elongatum
    • Aikawa M., Huff C.G., and Sprinz H. Fine structure of the asexual stages of Plasmodium elongatum. J. Cell Biol. 34 (1967) 229-249
    • (1967) J. Cell Biol. , vol.34 , pp. 229-249
    • Aikawa, M.1    Huff, C.G.2    Sprinz, H.3
  • 7
    • 0017879439 scopus 로고
    • Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite
    • Aikawa M., Miller L.H., Johnson J., and Rabbege J. Erythrocyte entry by malarial parasites. A moving junction between erythrocyte and parasite. J. Cell Biol. 77 (1978) 72-82
    • (1978) J. Cell Biol. , vol.77 , pp. 72-82
    • Aikawa, M.1    Miller, L.H.2    Johnson, J.3    Rabbege, J.4
  • 8
    • 0018745109 scopus 로고
    • Freeze-fracture study of malaria sporozoites: Antibody-induced changes of the pellicular membrane
    • Aikawa M., Cochrane A.H., Nussenzweig R.S., and Rabbege J. Freeze-fracture study of malaria sporozoites: Antibody-induced changes of the pellicular membrane. J. Protozool. 26 (1979) 273-279
    • (1979) J. Protozool. , vol.26 , pp. 273-279
    • Aikawa, M.1    Cochrane, A.H.2    Nussenzweig, R.S.3    Rabbege, J.4
  • 9
    • 0019779753 scopus 로고
    • Freeze-fracture study on the erythrocyte membrane during malarial parasite invasion
    • Aikawa M., Miller L.H., Rabbege J.R., and Epstein N. Freeze-fracture study on the erythrocyte membrane during malarial parasite invasion. J. Cell Biol. 91 (1981) 55-62
    • (1981) J. Cell Biol. , vol.91 , pp. 55-62
    • Aikawa, M.1    Miller, L.H.2    Rabbege, J.R.3    Epstein, N.4
  • 10
    • 0025151903 scopus 로고
    • Pf155/RESA antigen is localized in dense granules of Plasmodium falciparum merozoites
    • Aikawa M., Torii M., Sjolander A., Berzins K., Perlmann P., and Miller L.H. Pf155/RESA antigen is localized in dense granules of Plasmodium falciparum merozoites. Exp. Parasitol. 71 (1990) 326-329
    • (1990) Exp. Parasitol. , vol.71 , pp. 326-329
    • Aikawa, M.1    Torii, M.2    Sjolander, A.3    Berzins, K.4    Perlmann, P.5    Miller, L.H.6
  • 11
    • 0030222091 scopus 로고    scopus 로고
    • Structure and polymorphism of the upstream region of the pfg27/25 gene, transcriptionally regulated in gametocytogenesis of Plasmodium falciparum
    • Alano P., Silvestrini F., and Roca L. Structure and polymorphism of the upstream region of the pfg27/25 gene, transcriptionally regulated in gametocytogenesis of Plasmodium falciparum. Mol. Biochem. Parasitol. 79 (1996) 207-217
    • (1996) Mol. Biochem. Parasitol. , vol.79 , pp. 207-217
    • Alano, P.1    Silvestrini, F.2    Roca, L.3
  • 12
    • 77951026559 scopus 로고    scopus 로고
    • Identification of the moving junction complex of Toxoplasma gondii: A collaboration between distinct secretory organelles
    • Alexander D.L., Mital J., Ward G.E., Bradley P., and Boothroyd J.C. Identification of the moving junction complex of Toxoplasma gondii: A collaboration between distinct secretory organelles. PLoS Pathogens 1 (2005) e17
    • (2005) PLoS Pathogens , vol.1
    • Alexander, D.L.1    Mital, J.2    Ward, G.E.3    Bradley, P.4    Boothroyd, J.C.5
  • 13
    • 0034788662 scopus 로고    scopus 로고
    • Calcium regulation in the intraerythrocytic malaria parasite Plasmodium falciparum
    • Alleva L.M., and Kirk K. Calcium regulation in the intraerythrocytic malaria parasite Plasmodium falciparum. Mol. Biochem. Parasitol. 117 (2001) 121-128
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 121-128
    • Alleva, L.M.1    Kirk, K.2
  • 14
    • 10844221661 scopus 로고    scopus 로고
    • A genomic perspective of protein kinases in Plasmodium falciparum
    • Anamika Srinivasan N., and Krupa A. A genomic perspective of protein kinases in Plasmodium falciparum. Proteins 58 (2005) 180-189
    • (2005) Proteins , vol.58 , pp. 180-189
    • Anamika Srinivasan, N.1    Krupa, A.2
  • 15
  • 16
    • 0014527902 scopus 로고
    • Chemical agents effective in mediating control of growth and division synchrony of Plasmodium berghei in pinealectomized mice
    • Arnold J.D., Berger A.E., and Martin D.C. Chemical agents effective in mediating control of growth and division synchrony of Plasmodium berghei in pinealectomized mice. J. Parasitol. 55 (1969) 617-625
    • (1969) J. Parasitol. , vol.55 , pp. 617-625
    • Arnold, J.D.1    Berger, A.E.2    Martin, D.C.3
  • 18
    • 0023574139 scopus 로고
    • Ultrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes
    • Atkinson C.T., Aikawa M., Perry G., Fujino T., Bennett V., Davidson E.A., and Howard R.J. Ultrastructural localization of erythrocyte cytoskeletal and integral membrane proteins in Plasmodium falciparum-infected erythrocytes. Eur. J. Cell Biol. 45 (1988) 192-199
    • (1988) Eur. J. Cell Biol. , vol.45 , pp. 192-199
    • Atkinson, C.T.1    Aikawa, M.2    Perry, G.3    Fujino, T.4    Bennett, V.5    Davidson, E.A.6    Howard, R.J.7
  • 19
    • 0028685490 scopus 로고
    • Fitting a mixture model by expectation maximization to discover motifs in biopolymers
    • Bailey T.L., and Elkan C. Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc. Int. Conf. Intell. Syst. Mol. Biol. 2 (1994) 28-36
    • (1994) Proc. Int. Conf. Intell. Syst. Mol. Biol. , vol.2 , pp. 28-36
    • Bailey, T.L.1    Elkan, C.2
  • 20
    • 33750465167 scopus 로고    scopus 로고
    • Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria
    • Baker R.P., Wijetilaka R., and Urban S. Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria. PLoS Pathogens 2 (2006) e113
    • (2006) PLoS Pathogens , vol.2
    • Baker, R.P.1    Wijetilaka, R.2    Urban, S.3
  • 21
    • 0025205176 scopus 로고
    • The ultrastructure of red cell invasion in malaria infections: A review
    • discussion 293-257
    • Bannister L.H., and Dluzewski A.R. The ultrastructure of red cell invasion in malaria infections: A review. Blood Cells 16 (1990) 257-292 discussion 293-257
    • (1990) Blood Cells , vol.16 , pp. 257-292
    • Bannister, L.H.1    Dluzewski, A.R.2
  • 22
    • 0024389888 scopus 로고
    • The fine structure of secretion by Plasmodium knowlesi merozoites during red cell invasion
    • Bannister L.H., and Mitchell G.H. The fine structure of secretion by Plasmodium knowlesi merozoites during red cell invasion. J. Protozool 36 (1989) 362-367
    • (1989) J. Protozool , vol.36 , pp. 362-367
    • Bannister, L.H.1    Mitchell, G.H.2
  • 23
    • 0029000291 scopus 로고
    • The role of the cytoskeleton in Plasmodium falciparum merozoite biology: An electron-microscopic view
    • Bannister L.H., and Mitchell G.H. The role of the cytoskeleton in Plasmodium falciparum merozoite biology: An electron-microscopic view. Ann Trop Med Parasitol 89 (1995) 105-111
    • (1995) Ann Trop Med Parasitol , vol.89 , pp. 105-111
    • Bannister, L.H.1    Mitchell, G.H.2
  • 24
    • 0016588371 scopus 로고
    • Structure and invasive behaviour of Plasmodium knowlesi merozoites in vitro
    • Bannister L.H., Butcher G.A., Dennis E.D., and Mitchell G.H. Structure and invasive behaviour of Plasmodium knowlesi merozoites in vitro. Parasitology 71 (1975) 483-491
    • (1975) Parasitology , vol.71 , pp. 483-491
    • Bannister, L.H.1    Butcher, G.A.2    Dennis, E.D.3    Mitchell, G.H.4
  • 25
    • 0034307484 scopus 로고    scopus 로고
    • A brief illustrated guide to the ultrastructure of Plasmodium falciparum asexual blood stages
    • Bannister L.H., Hopkins J.M., Fowler R.E., Krishna S., and Mitchell G.H. A brief illustrated guide to the ultrastructure of Plasmodium falciparum asexual blood stages. Parasitol Today 16 (2000) 427-433
    • (2000) Parasitol Today , vol.16 , pp. 427-433
    • Bannister, L.H.1    Hopkins, J.M.2    Fowler, R.E.3    Krishna, S.4    Mitchell, G.H.5
  • 26
    • 0033844536 scopus 로고    scopus 로고
    • Ultrastructure of rhoptry development in Plasmodium falciparum erythrocytic schizonts
    • Bannister L.H., Hopkins J.M., Fowler R.E., Krishna S., and Mitchell G.H. Ultrastructure of rhoptry development in Plasmodium falciparum erythrocytic schizonts. Parasitology 121 Pt 3 (2000) 273-287
    • (2000) Parasitology , vol.121 , Issue.PART 3 , pp. 273-287
    • Bannister, L.H.1    Hopkins, J.M.2    Fowler, R.E.3    Krishna, S.4    Mitchell, G.H.5
  • 27
    • 0141502116 scopus 로고    scopus 로고
    • Plasmodium falciparum apical membrane antigen 1 (PfAMA-1) is translocated within micronemes along subpellicular microtubules during merozoite development
    • Bannister L.H., Hopkins J.M., Dluzewski A.R., Margos G., Williams I.T., Blackman M.J., Kocken C.H., Thomas A.W., and Mitchell G.H. Plasmodium falciparum apical membrane antigen 1 (PfAMA-1) is translocated within micronemes along subpellicular microtubules during merozoite development. J. Cell Sci. 116 (2003) 3825-3834
    • (2003) J. Cell Sci. , vol.116 , pp. 3825-3834
    • Bannister, L.H.1    Hopkins, J.M.2    Dluzewski, A.R.3    Margos, G.4    Williams, I.T.5    Blackman, M.J.6    Kocken, C.H.7    Thomas, A.W.8    Mitchell, G.H.9
  • 28
    • 34249817307 scopus 로고    scopus 로고
    • Making a home for Plasmodium post-genomics: Ultrastructural organization of the blood stages
    • Sherman I. (Ed), ASM Press, Washington, D. C
    • Bannister L.H., Margos M., and Hopkins J.H. Making a home for Plasmodium post-genomics: Ultrastructural organization of the blood stages. In: Sherman I. (Ed). "Molecular Approaches to Malaria" (2005), ASM Press, Washington, D. C 24-49
    • (2005) "Molecular Approaches to Malaria" , pp. 24-49
    • Bannister, L.H.1    Margos, M.2    Hopkins, J.H.3
  • 29
    • 0022590394 scopus 로고
    • Lamellar membranes associated with rhoptries in erythrocytic merozoites of Plasmodium knowlesi: A clue to the mechanism of invasion
    • Bannister L.H., Mitchell G.H., Butcher G.A., and Dennis E.D. Lamellar membranes associated with rhoptries in erythrocytic merozoites of Plasmodium knowlesi: A clue to the mechanism of invasion. Parasitology 92 (1986) 291-303
    • (1986) Parasitology , vol.92 , pp. 291-303
    • Bannister, L.H.1    Mitchell, G.H.2    Butcher, G.A.3    Dennis, E.D.4
  • 30
    • 0022544137 scopus 로고
    • Structure and development of the surface coat of erythrocytic merozoites of Plasmodium knowlesi
    • Bannister L.H., Mitchell G.H., Butcher G.A., Dennis E.D., and Cohen S. Structure and development of the surface coat of erythrocytic merozoites of Plasmodium knowlesi. Cell Tissue Res. 245 (1986) 281-290
    • (1986) Cell Tissue Res. , vol.245 , pp. 281-290
    • Bannister, L.H.1    Mitchell, G.H.2    Butcher, G.A.3    Dennis, E.D.4    Cohen, S.5
  • 32
    • 0029052741 scopus 로고
    • Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes
    • Baruch D.I., Pasloske B.L., Singh H.B., Bi X., Ma X.C., Feldman M., Taraschi T.F., and Howard R.J. Cloning the P. falciparum gene encoding PfEMP1, a malarial variant antigen and adherence receptor on the surface of parasitized human erythrocytes. Cell 82 (1995) 77-87
    • (1995) Cell , vol.82 , pp. 77-87
    • Baruch, D.I.1    Pasloske, B.L.2    Singh, H.B.3    Bi, X.4    Ma, X.C.5    Feldman, M.6    Taraschi, T.F.7    Howard, R.J.8
  • 33
    • 42649129281 scopus 로고    scopus 로고
    • Invasion by P. falciparum merozoites suggests a hierarchy of molecular interactions
    • Baum J., Maier A.G., Good R.T., Simpson K.M., and Cowman A.F. Invasion by P. falciparum merozoites suggests a hierarchy of molecular interactions. PLoS Pathogens 1 (2005) e37
    • (2005) PLoS Pathogens , vol.1
    • Baum, J.1    Maier, A.G.2    Good, R.T.3    Simpson, K.M.4    Cowman, A.F.5
  • 35
    • 33645306878 scopus 로고    scopus 로고
    • A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites
    • Baum J., Richard D., Healer J., Rug M., Krnajski Z., Gilberger T.W., Green J.L., Holder A.A., and Cowman A.F. A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites. J. Biol. Chem. 281 (2006) 5197-5208
    • (2006) J. Biol. Chem. , vol.281 , pp. 5197-5208
    • Baum, J.1    Richard, D.2    Healer, J.3    Rug, M.4    Krnajski, Z.5    Gilberger, T.W.6    Green, J.L.7    Holder, A.A.8    Cowman, A.F.9
  • 37
    • 23944494434 scopus 로고    scopus 로고
    • 2+ release and modulate the cell cycle of Plasmodium falciparum malaria parasites
    • 2+ release and modulate the cell cycle of Plasmodium falciparum malaria parasites. J. Pineal Res. 39 (2005) 224-230
    • (2005) J. Pineal Res. , vol.39 , pp. 224-230
    • Beraldo, F.H.1    Garcia, C.R.2
  • 38
    • 23944454006 scopus 로고    scopus 로고
    • Cyclic AMP and calcium interplay as second messengers in melatonin-dependent regulation of Plasmodium falciparum cell cycle
    • Beraldo F.H., Almeida F.M., da Silva A.M., and Garcia C.R. Cyclic AMP and calcium interplay as second messengers in melatonin-dependent regulation of Plasmodium falciparum cell cycle. J. Cell Biol. 170 (2005) 551-557
    • (2005) J. Cell Biol. , vol.170 , pp. 551-557
    • Beraldo, F.H.1    Almeida, F.M.2    da Silva, A.M.3    Garcia, C.R.4
  • 39
    • 34848850220 scopus 로고    scopus 로고
    • Human malarial parasite, Plasmodium falciparum, displays capacitative calcium entry: 2-aminoethyl diphenylborinate blocks the signal transduction pathway of melatonin action on the P. falciparum cell cycle
    • Beraldo F.H., Mikoshiba K., and Carcia C.R. Human malarial parasite, Plasmodium falciparum, displays capacitative calcium entry: 2-aminoethyl diphenylborinate blocks the signal transduction pathway of melatonin action on the P. falciparum cell cycle. J. Pineal Res. 43 (2005) 360-364
    • (2005) J. Pineal Res. , vol.43 , pp. 360-364
    • Beraldo, F.H.1    Mikoshiba, K.2    Carcia, C.R.3
  • 41
    • 5044220453 scopus 로고    scopus 로고
    • A stepwise epigenetic process controls immunoglobulin allelic exclusion
    • Bergman Y., and Cedar H. A stepwise epigenetic process controls immunoglobulin allelic exclusion. Nat. Rev. Immunol. 4 (2004) 753-761
    • (2004) Nat. Rev. Immunol. , vol.4 , pp. 753-761
    • Bergman, Y.1    Cedar, H.2
  • 45
    • 2342611064 scopus 로고    scopus 로고
    • Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite
    • Billker O., Dechamps S., Tewari R., Wenig G., Franke-Fayard B., and Brinkmann V. Calcium and a calcium-dependent protein kinase regulate gamete formation and mosquito transmission in a malaria parasite. Cell 117 (2004) 503-514
    • (2004) Cell , vol.117 , pp. 503-514
    • Billker, O.1    Dechamps, S.2    Tewari, R.3    Wenig, G.4    Franke-Fayard, B.5    Brinkmann, V.6
  • 47
    • 4544238896 scopus 로고    scopus 로고
    • Proteases in host cell invasion by the malaria parasite
    • Blackman M.J. Proteases in host cell invasion by the malaria parasite. Cell Microbiol. 6 (2004) 893-903
    • (2004) Cell Microbiol. , vol.6 , pp. 893-903
    • Blackman, M.J.1
  • 48
    • 0026514240 scopus 로고
    • Secondary processing of the Plasmodium falciparum merozoite surface protein-1 (MSP1) by a calcium-dependent membrane-bound serine protease: Shedding of MSP133 as a noncovalently associated complex with other fragments of the MSP1
    • Blackman M.J., and Holder A.A. Secondary processing of the Plasmodium falciparum merozoite surface protein-1 (MSP1) by a calcium-dependent membrane-bound serine protease: Shedding of MSP133 as a noncovalently associated complex with other fragments of the MSP1. Mol. Biochem. Parasitol. 50 (1992) 307-315
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 307-315
    • Blackman, M.J.1    Holder, A.A.2
  • 49
    • 0028279254 scopus 로고
    • Antibodies inhibit the protease-mediated processing of a malaria merozoite surface protein
    • Blackman M.J., Scott-Finnigan T.J., Shai S., and Holder A.A. Antibodies inhibit the protease-mediated processing of a malaria merozoite surface protein. J. Exp. Med. 180 (1994) 389-393
    • (1994) J. Exp. Med. , vol.180 , pp. 389-393
    • Blackman, M.J.1    Scott-Finnigan, T.J.2    Shai, S.3    Holder, A.A.4
  • 52
    • 6944226698 scopus 로고    scopus 로고
    • Characterization of PfMyb1 transcription factor during erythrocytic development of 3D7 and F12 Plasmodium falciparum clones
    • Boschet C., Gissot M., Briquet S., Hamid Z., Claudel-Renard C., and Vaquero C. Characterization of PfMyb1 transcription factor during erythrocytic development of 3D7 and F12 Plasmodium falciparum clones. Mol. Biochem. Parasitol. 138 (1996) 159-163
    • (1996) Mol. Biochem. Parasitol. , vol.138 , pp. 159-163
    • Boschet, C.1    Gissot, M.2    Briquet, S.3    Hamid, Z.4    Claudel-Renard, C.5    Vaquero, C.6
  • 53
    • 0030581669 scopus 로고    scopus 로고
    • Disruption of a novel open reading frame of Plasmodium falciparum chromosome 9 by subtelomeric and internal deletions can lead to loss or maintenance of cytoadherence
    • Bourke P.F., Holt D.C., Sutherland C.J., and Kemp D.J. Disruption of a novel open reading frame of Plasmodium falciparum chromosome 9 by subtelomeric and internal deletions can lead to loss or maintenance of cytoadherence. Mol. Biochem. Parasitol. 82 (1996) 25-36
    • (1996) Mol. Biochem. Parasitol. , vol.82 , pp. 25-36
    • Bourke, P.F.1    Holt, D.C.2    Sutherland, C.J.3    Kemp, D.J.4
  • 54
    • 4243071596 scopus 로고    scopus 로고
    • The transcriptome of the intraerythrocytic developmental cycle of Plasmodium falciparum
    • Bozdech Z., Llinás 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    Llinás, M.2    Pulliam, B.L.3    Wong, E.D.4    Zhu, J.5    DeRisi, J.L.6
  • 56
    • 0042357079 scopus 로고    scopus 로고
    • Transcriptional, proteomic, and metabolic responses to lithium in galactose-grown yeast cells
    • Bro C., Regenberg B., Lagniel G., Labarre J., Montero-Lomeli M., and Nielsen J. Transcriptional, proteomic, and metabolic responses to lithium in galactose-grown yeast cells. J. Biol. Chem. 278 (2003) 32141-32149
    • (2003) J. Biol. Chem. , vol.278 , pp. 32141-32149
    • Bro, C.1    Regenberg, B.2    Lagniel, G.3    Labarre, J.4    Montero-Lomeli, M.5    Nielsen, J.6
  • 57
    • 15244360655 scopus 로고    scopus 로고
    • A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma
    • Brossier F., Jewett T.J., Sibley L.D., and Urban S. A spatially localized rhomboid protease cleaves cell surface adhesins essential for invasion by Toxoplasma. Proc. Natl. Acad. Sci. USA 102 (2005) 4146-4151
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 4146-4151
    • Brossier, F.1    Jewett, T.J.2    Sibley, L.D.3    Urban, S.4
  • 58
    • 0034308279 scopus 로고    scopus 로고
    • Cellular calcium imaging: So, what's new?
    • Brownlee C. Cellular calcium imaging: So, what's new?. Trends Cell Biol. 10 (2000) 451-457
    • (2000) Trends Cell Biol. , vol.10 , pp. 451-457
    • Brownlee, C.1
  • 59
    • 0035336844 scopus 로고    scopus 로고
    • Signaling at zero G: G-protein-independent functions for 7-TM receptors
    • Brzostowski J.A., and Kimmel A.R. Signaling at zero G: G-protein-independent functions for 7-TM receptors. Trends Biochem. Sci. 26 (2001) 291-297
    • (2001) Trends Biochem. Sci. , vol.26 , pp. 291-297
    • Brzostowski, J.A.1    Kimmel, A.R.2
  • 62
    • 0034982215 scopus 로고    scopus 로고
    • Cytochemical localisation of calcium ATPase activity during the erythrocytic cell cycle of Plasmodium falciparum
    • Caldas M.L., and Wasserman M. Cytochemical localisation of calcium ATPase activity during the erythrocytic cell cycle of Plasmodium falciparum. Int. J. Parasitol. 31 (2001) 776-782
    • (2001) Int. J. Parasitol. , vol.31 , pp. 776-782
    • Caldas, M.L.1    Wasserman, M.2
  • 63
    • 25444456367 scopus 로고    scopus 로고
    • Prediction of the general transcription factors associated with RNA polymerase II in Plasmodium falciparum: Conserved features and differences relative to other eukaryotes
    • Callebaut I., Prat K., Meurice E., Mornon J.P., and Tomavo S. Prediction of the general transcription factors associated with RNA polymerase II in Plasmodium falciparum: Conserved features and differences relative to other eukaryotes. BMC Genomics 6 (2005) 100
    • (2005) BMC Genomics , vol.6 , pp. 100
    • Callebaut, I.1    Prat, K.2    Meurice, E.3    Mornon, J.P.4    Tomavo, S.5
  • 65
    • 0028116935 scopus 로고
    • Multiple ligands for cytoadherence can be present simultaneously on the surface of Plasmodium falciparum-infected erythrocytes
    • Chaiyaroj S.C., Coppel R.L., Novakovic S., and Brown G.V. Multiple ligands for cytoadherence can be present simultaneously on the surface of Plasmodium falciparum-infected erythrocytes. Proc. Natl. Acad. Sci. USA 91 (1994) 10805-10808
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 10805-10808
    • Chaiyaroj, S.C.1    Coppel, R.L.2    Novakovic, S.3    Brown, G.V.4
  • 67
    • 22544478432 scopus 로고    scopus 로고
    • Evidence that the cADPR signalling pathway controls calcium-mediated microneme secretion in Toxoplasma gondii
    • Chini E.N., Nagamune K., Wetzel D.M., and Sibley L.D. Evidence that the cADPR signalling pathway controls calcium-mediated microneme secretion in Toxoplasma gondii. Biochem. J. 389 (2005) 269-277
    • (2005) Biochem. J. , vol.389 , pp. 269-277
    • Chini, E.N.1    Nagamune, K.2    Wetzel, D.M.3    Sibley, L.D.4
  • 68
    • 0034307767 scopus 로고    scopus 로고
    • Host cell invasion by malaria parasites
    • Chitnis C.E., and 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
  • 69
    • 33750632707 scopus 로고    scopus 로고
    • LC/ESI-MS demonstrates the absence of 5-methyl-2′-deoxycytosine in Plasmodium falciparum genomic DNA
    • Choi S.W., Keyes M.K., and Horrocks P. LC/ESI-MS demonstrates the absence of 5-methyl-2′-deoxycytosine in Plasmodium falciparum genomic DNA. Mol. Biochem. Parasitol. 150 (2006) 350-352
    • (2006) Mol. Biochem. Parasitol. , vol.150 , pp. 350-352
    • Choi, S.W.1    Keyes, M.K.2    Horrocks, P.3
  • 71
    • 0038015442 scopus 로고    scopus 로고
    • Linker scanning mutagenesis of the Plasmodium gallinaceum sexual stage specific gene pgs28 reveals a novel downstream cis-control element
    • Chow C.S., and Wirth D.F. Linker scanning mutagenesis of the Plasmodium gallinaceum sexual stage specific gene pgs28 reveals a novel downstream cis-control element. Mol. Biochem. Parasitol. 129 (2003) 199-208
    • (2003) Mol. Biochem. Parasitol. , vol.129 , pp. 199-208
    • Chow, C.S.1    Wirth, D.F.2
  • 72
    • 0036426972 scopus 로고    scopus 로고
    • A DNA microarray-based approach to elucidate the effects of the immunosuppressant SR31747A on gene expression in Saccharomyces cerevisiae
    • Cinato E., Peleraux A., Silve S., Galiegue S., Dhers C., Picard C., Jbilo O., Loison G., and Casellas P. A DNA microarray-based approach to elucidate the effects of the immunosuppressant SR31747A on gene expression in Saccharomyces cerevisiae. Gene Expression 10 (2002) 213-230
    • (2002) Gene Expression , vol.10 , pp. 213-230
    • Cinato, E.1    Peleraux, A.2    Silve, S.3    Galiegue, S.4    Dhers, C.5    Picard, C.6    Jbilo, O.7    Loison, G.8    Casellas, P.9
  • 73
    • 7444236944 scopus 로고    scopus 로고
    • Protein trafficking in Plasmodium falciparum-infected red blood cells
    • Cooke B.M., Lingelbach K., Bannister L.H., and Tilley L. Protein trafficking in Plasmodium falciparum-infected red blood cells. Trends Parasitol. 20 (2004) 581-589
    • (2004) Trends Parasitol. , vol.20 , pp. 581-589
    • Cooke, B.M.1    Lingelbach, K.2    Bannister, L.H.3    Tilley, L.4
  • 74
    • 33644895382 scopus 로고    scopus 로고
    • A Maurer's cleft-associated protein is essential for expression of the major malaria virulence antigen on the surface of infected red blood cells
    • Cooke B.M., Buckingham D.W., Glenister F.K., Fernandez K.M., Bannister L.H., Marti M., Mohandas N., and Coppel R.L. A Maurer's cleft-associated protein is essential for expression of the major malaria virulence antigen on the surface of infected red blood cells. J. Cell Biol. 172 (2006) 899-908
    • (2006) J. Cell Biol. , vol.172 , pp. 899-908
    • Cooke, B.M.1    Buckingham, D.W.2    Glenister, F.K.3    Fernandez, K.M.4    Bannister, L.H.5    Marti, M.6    Mohandas, N.7    Coppel, R.L.8
  • 75
    • 4444339460 scopus 로고    scopus 로고
    • Comparative genomics of transcriptional control in the human malaria parasite Plasmodium falciparum
    • Coulson R.M., Hall N., and Ouzounis C.A. Comparative genomics of transcriptional control in the human malaria parasite Plasmodium falciparum. Genome Res. 14 (2004) 1548-1554
    • (2004) Genome Res. , vol.14 , pp. 1548-1554
    • Coulson, R.M.1    Hall, N.2    Ouzounis, C.A.3
  • 76
    • 32944458099 scopus 로고    scopus 로고
    • Invasion of red blood cells by malaria parasites
    • Cowman A.F., and Crabb B.S. Invasion of red blood cells by malaria parasites. Cell 124 (2006) 755-766
    • (2006) Cell , vol.124 , pp. 755-766
    • Cowman, A.F.1    Crabb, B.S.2
  • 77
    • 0030006717 scopus 로고    scopus 로고
    • Characterization of promoters and stable transfection by homologous and nonhomologous recombination in Plasmodium falciparum
    • Crabb B.S., and Cowman A.F. Characterization of promoters and stable transfection by homologous and nonhomologous recombination in Plasmodium falciparum. Proc. Natl. Acad. Sci. USA 93 (1996) 7289-7294
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7289-7294
    • Crabb, B.S.1    Cowman, A.F.2
  • 79
    • 0035400253 scopus 로고    scopus 로고
    • Molecules on the surface of the Plasmodium falciparum infected erythrocyte and their role in malaria pathogenesis and immune evasion
    • Craig A., and Scherf A. Molecules on the surface of the Plasmodium falciparum infected erythrocyte and their role in malaria pathogenesis and immune evasion. Mol. Biochem. Parasitol. 115 (2001) 129-143
    • (2001) Mol. Biochem. Parasitol. , vol.115 , pp. 129-143
    • Craig, A.1    Scherf, A.2
  • 80
    • 0018180562 scopus 로고
    • Isolation of malaria merozoites: Release of Plasmodium chabaudi merozoites from schizonts bound to immobilized concanavalin A
    • David P.H., Hommel M., Benichou J.C., Eisen H.A., and da Silva L.H. Isolation of malaria merozoites: Release of Plasmodium chabaudi merozoites from schizonts bound to immobilized concanavalin A. Proc. Natl. Acad. Sci. USA 75 (1978) 5081-5084
    • (1978) Proc. Natl. Acad. Sci. USA , vol.75 , pp. 5081-5084
    • David, P.H.1    Hommel, M.2    Benichou, J.C.3    Eisen, H.A.4    da Silva, L.H.5
  • 81
    • 0027305928 scopus 로고
    • Genes necessary for expression of a virulence determinant and for transmission of Plasmodium falciparum are located on a 0.3-megabase region of chromosome 9
    • Day K.P., Karamalis F., Thompson J., Barnes D.A., Peterson C., Brown H., Brown G.V., and Kemp D.J. Genes necessary for expression of a virulence determinant and for transmission of Plasmodium falciparum are located on a 0.3-megabase region of chromosome 9. Proc. Natl. Acad. Sci. USA 90 (1993) 8292-8296
    • (1993) Proc. Natl. Acad. Sci. USA , vol.90 , pp. 8292-8296
    • Day, K.P.1    Karamalis, F.2    Thompson, J.3    Barnes, D.A.4    Peterson, C.5    Brown, H.6    Brown, G.V.7    Kemp, D.J.8
  • 82
    • 0032939607 scopus 로고    scopus 로고
    • Isolation and functional characterization of two distinct sexual-stage-specific promoters of the human malaria parasite Plasmodium falciparum
    • Dechering K.J., Kaan A.M., Mbacham W., Wirth D.F., Eling W., Konings R.N., and Stunnenberg H.G. Isolation and functional characterization of two distinct sexual-stage-specific promoters of the human malaria parasite Plasmodium falciparum. Mol. Cell. Biol. 19 (1999) 967-978
    • (1999) Mol. Cell. Biol. , vol.19 , pp. 967-978
    • Dechering, K.J.1    Kaan, A.M.2    Mbacham, W.3    Wirth, D.F.4    Eling, W.5    Konings, R.N.6    Stunnenberg, H.G.7
  • 83
    • 0035974802 scopus 로고    scopus 로고
    • Malaria: Cooperative silencing elements in var genes
    • Deitsch K.W., Calderwood M.S., and Wellems T.E. Malaria: Cooperative silencing elements in var genes. Nature 412 (2001) 875-876
    • (2001) Nature , vol.412 , pp. 875-876
    • Deitsch, K.W.1    Calderwood, M.S.2    Wellems, T.E.3
  • 84
    • 0034794238 scopus 로고    scopus 로고
    • Puromycin-N-acetyltransferase as a selectable marker for use in Plasmodium falciparum
    • de Koning-Ward T.F., Waters A.P., and Crabb B.S. Puromycin-N-acetyltransferase as a selectable marker for use in Plasmodium falciparum. Mol. Biochem. Parasitol. 117 (2001) 155-160
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 155-160
    • de Koning-Ward, T.F.1    Waters, A.P.2    Crabb, B.S.3
  • 85
    • 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., and 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
  • 86
    • 14644415904 scopus 로고    scopus 로고
    • Dissection of brefeldin A-sensitive and -insensitive steps in apicoplast protein targeting
    • DeRocher A., Gilbert B., Feagin J.E., and Parsons M. Dissection of brefeldin A-sensitive and -insensitive steps in apicoplast protein targeting. J. Cell Sci. 118 (2005) 565-574
    • (2005) J. Cell Sci. , vol.118 , pp. 565-574
    • DeRocher, A.1    Gilbert, B.2    Feagin, J.E.3    Parsons, M.4
  • 87
    • 0031042435 scopus 로고    scopus 로고
    • Pore size of the malaria parasite's nutrient channel
    • Desai S.A., and Rosenberg R.L. Pore size of the malaria parasite's nutrient channel. Proc. Natl. Acad. Sci. USA 94 (1997) 2045-2049
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 2045-2049
    • Desai, S.A.1    Rosenberg, R.L.2
  • 88
    • 0027401744 scopus 로고
    • A nutrient-permeable channel on the intraerythrocytic malaria parasite
    • Desai S.A., Krogstad D.J., and McCleskey E.W. A nutrient-permeable channel on the intraerythrocytic malaria parasite. Nature 362 (1993) 643-646
    • (1993) Nature , vol.362 , pp. 643-646
    • Desai, S.A.1    Krogstad, D.J.2    McCleskey, E.W.3
  • 89
    • 0034255989 scopus 로고    scopus 로고
    • Identification of differentially regulated genes of Plasmodium by suppression subtractive hybridization
    • Dessens J.T., Margos G., Rodriguez M.C., and Sinden R.E. Identification of differentially regulated genes of Plasmodium by suppression subtractive hybridization. Parasitol. Today 16 (2000) 354-356
    • (2000) Parasitol. Today , vol.16 , pp. 354-356
    • Dessens, J.T.1    Margos, G.2    Rodriguez, M.C.3    Sinden, R.E.4
  • 91
    • 0029947792 scopus 로고    scopus 로고
    • Inhibition of invasion and intraerythrocytic development of Plasmodium falciparum by kinase inhibitors
    • Dluzewski A.R., and Garcia C.R. Inhibition of invasion and intraerythrocytic development of Plasmodium falciparum by kinase inhibitors. Experientia 52 (1996) 621-623
    • (1996) Experientia , vol.52 , pp. 621-623
    • Dluzewski, A.R.1    Garcia, C.R.2
  • 93
    • 0026764460 scopus 로고
    • Origins of the parasitophorous vacuole membrane of the malaria parasite, Plasmodium falciparum, in human red blood cells
    • Dluzewski A.R., Mitchell G.H., Fryer P.R., Griffiths S., Wilson R.J., and Gratzer W.B. Origins of the parasitophorous vacuole membrane of the malaria parasite, Plasmodium falciparum, in human red blood cells. J. Cell Sci. 102 (1992) 527-532
    • (1992) J. Cell Sci. , vol.102 , pp. 527-532
    • Dluzewski, A.R.1    Mitchell, G.H.2    Fryer, P.R.3    Griffiths, S.4    Wilson, R.J.5    Gratzer, W.B.6
  • 94
    • 0029584095 scopus 로고
    • Origins of the parasitophorous vacuole membrane of the malaria parasite: Surface area of the parasitized red cell
    • Dluzewski A.R., Zicha D., Dunn G.A., and Gratzer W.B. Origins of the parasitophorous vacuole membrane of the malaria parasite: Surface area of the parasitized red cell. Eur. J. Cell Biol. 68 (1995) 446-449
    • (1995) Eur. J. Cell Biol. , vol.68 , pp. 446-449
    • Dluzewski, A.R.1    Zicha, D.2    Dunn, G.A.3    Gratzer, W.B.4
  • 95
    • 0032941766 scopus 로고    scopus 로고
    • Characterization of protein Ser/Thr phosphatases of the malaria parasite, Plasmodium falciparum: Inhibition of the parasitic calcineurin by cyclophilin-cyclosporin complex
    • Dobson S., May T., Berriman M., Del Vecchio C., Fairlamb A.H., Chakrabarti D., and Barik S. Characterization of protein Ser/Thr phosphatases of the malaria parasite, Plasmodium falciparum: Inhibition of the parasitic calcineurin by cyclophilin-cyclosporin complex. Mol. Biochem. Parasitol. 99 (1999) 167-181
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 167-181
    • Dobson, S.1    May, T.2    Berriman, M.3    Del Vecchio, C.4    Fairlamb, A.H.5    Chakrabarti, D.6    Barik, S.7
  • 96
    • 0027860430 scopus 로고
    • Calcium homeostasis in Trypanosoma cruzi
    • DoCampo R. Calcium homeostasis in Trypanosoma cruzi. Biol. Res. 26 (1993) 189-196
    • (1993) Biol. Res. , vol.26 , pp. 189-196
    • DoCampo, R.1
  • 98
    • 29144446249 scopus 로고    scopus 로고
    • Protein kinases as targets for antimalarial intervention: Kinomics, structure-based design, transmission-blockade, and targeting host cell enzymes
    • Doerig C., Billker O., Pratt D., and Endicott J. Protein kinases as targets for antimalarial intervention: Kinomics, structure-based design, transmission-blockade, and targeting host cell enzymes. Biochim. Biophys. Acta 1754 (2005) 132-150
    • (2005) Biochim. Biophys. Acta , vol.1754 , pp. 132-150
    • Doerig, C.1    Billker, O.2    Pratt, D.3    Endicott, J.4
  • 99
    • 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., and 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
  • 101
    • 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., and Doerig C. 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    Doerig, C.8
  • 102
    • 12344303646 scopus 로고    scopus 로고
    • PfPK7, an atypical MEK-related protein kinase, reflects the absence of classical three-component MAPK pathways in the human malaria parasite Plasmodium falciparum
    • Dorin D., Semblat J.P., Poullet P., Alano P., Goldring J.P., Whittle C., Patterson S., Chakrabarti D., and Doerig C. PfPK7, an atypical MEK-related protein kinase, reflects the absence of classical three-component MAPK pathways in the human malaria parasite Plasmodium falciparum. Mol. Microbiol. 55 (2005) 184-196
    • (2005) Mol. Microbiol. , vol.55 , pp. 184-196
    • Dorin, D.1    Semblat, J.P.2    Poullet, P.3    Alano, P.4    Goldring, J.P.5    Whittle, C.6    Patterson, S.7    Chakrabarti, D.8    Doerig, C.9
  • 103
    • 0036162628 scopus 로고    scopus 로고
    • Negative selection of Plasmodium falciparum reveals targeted gene deletion by double crossover recombination
    • Duraisingh M.T., Triglia T., and Cowman A.F. Negative selection of Plasmodium falciparum reveals targeted gene deletion by double crossover recombination. Int. J. Parasitol. 32 (2002) 81-89
    • (2002) Int. J. Parasitol. , vol.32 , pp. 81-89
    • Duraisingh, M.T.1    Triglia, T.2    Cowman, A.F.3
  • 104
    • 0037447273 scopus 로고    scopus 로고
    • Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways
    • Duraisingh M.T., Maier A.G., Triglia T., and Cowman A.F. Erythrocyte-binding antigen 175 mediates invasion in Plasmodium falciparum utilizing sialic acid-dependent and -independent pathways. Proc. Natl. Acad. Sci. USA 100 (2003) 4796-4801
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 4796-4801
    • Duraisingh, M.T.1    Maier, A.G.2    Triglia, T.3    Cowman, A.F.4
  • 105
    • 0037416197 scopus 로고    scopus 로고
    • Phenotypic variation of Plasmodium falciparum merozoite proteins directs receptor targeting for invasion of human erythrocytes
    • Duraisingh M.T., Triglia T., Ralph S.A., Rayner J.C., Barnwell J.W., McFadden G.I., and Cowman A.F. Phenotypic variation of Plasmodium falciparum merozoite proteins directs receptor targeting for invasion of human erythrocytes. EMBO J. 22 (2003) 1047-1057
    • (2003) EMBO J. , vol.22 , pp. 1047-1057
    • Duraisingh, M.T.1    Triglia, T.2    Ralph, S.A.3    Rayner, J.C.4    Barnwell, J.W.5    McFadden, G.I.6    Cowman, A.F.7
  • 109
    • 0033527572 scopus 로고    scopus 로고
    • Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum
    • Eggleson K.K., Duffin K.L., and Goldberg D.E. Identification and characterization of falcilysin, a metallopeptidase involved in hemoglobin catabolism within the malaria parasite Plasmodium falciparum. J. Biol. Chem. 274 (1999) 32411-32417
    • (1999) J. Biol. Chem. , vol.274 , pp. 32411-32417
    • Eggleson, K.K.1    Duffin, K.L.2    Goldberg, D.E.3
  • 110
    • 33747177314 scopus 로고    scopus 로고
    • Plasmepsins as potential targets for new antimalarial therapy
    • Ersmark K., Samuelsson B., and Hallberg A. Plasmepsins as potential targets for new antimalarial therapy. Med. Res. Rev. 26 (2006) 626-666
    • (2006) Med. Res. Rev. , vol.26 , pp. 626-666
    • Ersmark, K.1    Samuelsson, B.2    Hallberg, A.3
  • 111
    • 0030885188 scopus 로고    scopus 로고
    • Transformation with human dihydrofolate reductase renders malaria parasites insensitive to WR99210 but does not affect the intrinsic activity of proguanil
    • Fidock D.A., and Wellems T.E. Transformation with human dihydrofolate reductase renders malaria parasites insensitive to WR99210 but does not affect the intrinsic activity of proguanil. Proc. Natl. Acad. Sci. USA 94 (1997) 10931-10936
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 10931-10936
    • Fidock, D.A.1    Wellems, T.E.2
  • 112
    • 0036047420 scopus 로고    scopus 로고
    • Production of stage-specific Plasmodium falciparum cDNA libraries using subtractive hybridization
    • Fidock D.A., Nguyen T.V., Beerntsen B.T., and James A.A. Production of stage-specific Plasmodium falciparum cDNA libraries using subtractive hybridization. Methods Mol. Med. 72 (2002) 277-289
    • (2002) Methods Mol. Med. , vol.72 , pp. 277-289
    • Fidock, D.A.1    Nguyen, T.V.2    Beerntsen, B.T.3    James, A.A.4
  • 113
    • 0025971118 scopus 로고
    • The ring-infected erythrocyte surface antigen of Plasmodium falciparum associates with spectrin in the erythrocyte membrane
    • Foley M., Tilley L., Sawyer W.H., and Anders R.F. The ring-infected erythrocyte surface antigen of Plasmodium falciparum associates with spectrin in the erythrocyte membrane. Mol. Biochem. Parasitol. 46 (1991) 137-147
    • (1991) Mol. Biochem. Parasitol. , vol.46 , pp. 137-147
    • Foley, M.1    Tilley, L.2    Sawyer, W.H.3    Anders, R.F.4
  • 115
    • 0346122785 scopus 로고    scopus 로고
    • The cytoskeleton and motility in apicomplexan invasion
    • Fowler R.E., Margos G., and Mitchell G.H. The cytoskeleton and motility in apicomplexan invasion. Adv. Parasitol. 56 (2004) 213-263
    • (2004) Adv. Parasitol. , vol.56 , pp. 213-263
    • Fowler, R.E.1    Margos, G.2    Mitchell, G.H.3
  • 116
    • 33744524946 scopus 로고    scopus 로고
    • Strict pairing of var promoters and introns is required for var gene silencing in the malaria parasite Plasmodium falciparum
    • Frank M., Dzikowski R., Costantini D., Amulic B., Berdougo E., and Deitsch K. Strict pairing of var promoters and introns is required for var gene silencing in the malaria parasite Plasmodium falciparum. J. Biol. Chem. 281 (2006) 9942-9952
    • (2006) J. Biol. Chem. , vol.281 , pp. 9942-9952
    • Frank, M.1    Dzikowski, R.2    Costantini, D.3    Amulic, B.4    Berdougo, E.5    Deitsch, K.6
  • 118
    • 0029992826 scopus 로고    scopus 로고
    • Adherence of Plasmodium falciparum to chondroitin sulfate A in the human placenta
    • Fried M., and Duffy P.E. Adherence of Plasmodium falciparum to chondroitin sulfate A in the human placenta. Science 272 (1996) 1502-1504
    • (1996) Science , vol.272 , pp. 1502-1504
    • Fried, M.1    Duffy, P.E.2
  • 119
    • 54449084262 scopus 로고    scopus 로고
    • A mechanistic approach to merozoite invasion of red blood cells
    • Sherwin I.R. (Ed), ASM Press, Washington, DC
    • Galinski M.R., Dluzewski A.R., and Barnwell J.W. A mechanistic approach to merozoite invasion of red blood cells. In: Sherwin I.R. (Ed). "Molecular Approaches to Malaria" (2005), ASM Press, Washington, DC 1-61
    • (2005) "Molecular Approaches to Malaria" , pp. 1-61
    • Galinski, M.R.1    Dluzewski, A.R.2    Barnwell, J.W.3
  • 120
    • 13844306877 scopus 로고    scopus 로고
    • A silenced Plasmodium falciparum var promoter can be activated in vivo through spontaneous deletion of a silencing element in the intron
    • Gannoun-Zaki L., Jost A., Mu J., Deitsch K.W., and Wellems T.E. A silenced Plasmodium falciparum var promoter can be activated in vivo through spontaneous deletion of a silencing element in the intron. Eukaryot. Cell 4 (2005) 490-492
    • (2005) Eukaryot. Cell , vol.4 , pp. 490-492
    • Gannoun-Zaki, L.1    Jost, A.2    Mu, J.3    Deitsch, K.W.4    Wellems, T.E.5
  • 121
    • 0033485874 scopus 로고    scopus 로고
    • Calcium homeostasis and signaling in the blood-stage malaria parasite
    • Garcia C.R. Calcium homeostasis and signaling in the blood-stage malaria parasite. Parasitol. Today 15 (1999) 488-491
    • (1999) Parasitol. Today , vol.15 , pp. 488-491
    • Garcia, C.R.1
  • 124
    • 0034782804 scopus 로고    scopus 로고
    • Tertian and quartan fevers: Temporal regulation in malarial infection
    • Garcia C.R., Markus R.P., and Madeira L. Tertian and quartan fevers: Temporal regulation in malarial infection. J. Biol. Rhythms 16 (2001) 436-443
    • (2001) J. Biol. Rhythms , vol.16 , pp. 436-443
    • Garcia, C.R.1    Markus, R.P.2    Madeira, L.3
  • 129
    • 0032910168 scopus 로고    scopus 로고
    • Organization and regulation of mitogen-activated protein kinase signaling pathways
    • Garrington T.P., and 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
  • 130
    • 2442528540 scopus 로고    scopus 로고
    • Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii
    • Gaskins E., Gilk S., DeVore N., Mann T., Ward G., and Beckers C. Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii. J. Cell Biol. 165 (2004) 383-393
    • (2004) J. Cell Biol. , vol.165 , pp. 383-393
    • Gaskins, E.1    Gilk, S.2    DeVore, N.3    Mann, T.4    Ward, G.5    Beckers, C.6
  • 131
    • 0242407575 scopus 로고    scopus 로고
    • Interruption of the blood-stage cycle of the malaria parasite, Plasmodium chabaudi, by protein tyrosine kinase inhibitors
    • Gazarini M.L., and Garcia C.R. Interruption of the blood-stage cycle of the malaria parasite, Plasmodium chabaudi, by protein tyrosine kinase inhibitors. Braz. J. Med. Biol. Res. 36 (2003) 1465-1469
    • (2003) Braz. J. Med. Biol. Res. , vol.36 , pp. 1465-1469
    • Gazarini, M.L.1    Garcia, C.R.2
  • 133
    • 0344805645 scopus 로고    scopus 로고
    • Calcium signaling in a low calcium environment: How the intracellular malaria parasite solves the problem
    • Gazarini M.L., Thomas A.P., Pozzan T., and Garcia C.R. Calcium signaling in a low calcium environment: How the intracellular malaria parasite solves the problem. J. Cell Biol. 161 (2003) 103-110
    • (2003) J. Cell Biol. , vol.161 , pp. 103-110
    • Gazarini, M.L.1    Thomas, A.P.2    Pozzan, T.3    Garcia, C.R.4
  • 135
    • 0037853264 scopus 로고    scopus 로고
    • A novel erythrocyte binding antigen-175 paralogue from Plasmodium falciparum defines a new trypsin-resistant receptor on human erythrocytes
    • Gilberger T.W., Thompson J.K., Triglia T., Good R.T., Duraisingh M.T., and Cowman A.F. A novel erythrocyte binding antigen-175 paralogue from Plasmodium falciparum defines a new trypsin-resistant receptor on human erythrocytes. J. Biol. Chem. 278 (2003) 14480-14486
    • (2003) J. Biol. Chem. , vol.278 , pp. 14480-14486
    • Gilberger, T.W.1    Thompson, J.K.2    Triglia, T.3    Good, R.T.4    Duraisingh, M.T.5    Cowman, A.F.6
  • 136
    • 24944495451 scopus 로고    scopus 로고
    • Membrane transformation during malaria parasite release from human red blood cells
    • Glushakova S., Yin D., Li T., and Zimmerberg J. Membrane transformation during malaria parasite release from human red blood cells. Curr. Biol. 15 (2005) 1645-1650
    • (2005) Curr. Biol. , vol.15 , pp. 1645-1650
    • Glushakova, S.1    Yin, D.2    Li, T.3    Zimmerberg, J.4
  • 137
    • 0034652341 scopus 로고    scopus 로고
    • Elemental propagation of calcium signals in response-specific patterns determined by environmental stimulus strength
    • Goddard H., Manison N.F., Tomos D., and Brownlee C. Elemental propagation of calcium signals in response-specific patterns determined by environmental stimulus strength. Proc. Natl. Acad. Sci. USA 97 (2000) 1932-1937
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 1932-1937
    • Goddard, H.1    Manison, N.F.2    Tomos, D.3    Brownlee, C.4
  • 139
  • 140
    • 0344395003 scopus 로고    scopus 로고
    • Drug-induced alterations in gene expression of the asexual blood forms of Plasmodium falciparum
    • Gunasekera A.M., Patankar S., Schug J., Eisen G., and Wirth D.F. Drug-induced alterations in gene expression of the asexual blood forms of Plasmodium falciparum. Mol. Microbiol. 50 (2003) 1229-1239
    • (2003) Mol. Microbiol. , vol.50 , pp. 1229-1239
    • Gunasekera, A.M.1    Patankar, S.2    Schug, J.3    Eisen, G.4    Wirth, D.F.5
  • 141
    • 0020568103 scopus 로고
    • Plasmodium knowlesi: Studies on invasion of rhesus erythrocytes by merozoites in the presence of protease inhibitors
    • Hadley T., Aikawa M., and Miller L.H. Plasmodium knowlesi: Studies on invasion of rhesus erythrocytes by merozoites in the presence of protease inhibitors. Exp. Parasitol. 55 (1983) 306-311
    • (1983) Exp. Parasitol. , vol.55 , pp. 306-311
    • Hadley, T.1    Aikawa, M.2    Miller, L.H.3
  • 142
    • 0032845689 scopus 로고    scopus 로고
    • The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii
    • Hager K.M., Striepen B., Tilney L.G., and Roos D.S. The nuclear envelope serves as an intermediary between the ER and Golgi complex in the intracellular parasite Toxoplasma gondii. J. Cell Sci. 112 (1999) 2631-2638
    • (1999) J. Cell Sci. , vol.112 , pp. 2631-2638
    • Hager, K.M.1    Striepen, B.2    Tilney, L.G.3    Roos, D.S.4
  • 145
    • 0033620487 scopus 로고    scopus 로고
    • Heptahelical receptor signaling: Beyond the G protein paradigm
    • Hall R.A., Premont R.T., and Lefkowitz R.J. Heptahelical receptor signaling: Beyond the G protein paradigm. J. Cell Biol. 145 (1999) 927-932
    • (1999) J. Cell Biol. , vol.145 , pp. 927-932
    • Hall, R.A.1    Premont, R.T.2    Lefkowitz, R.J.3
  • 148
    • 0025259047 scopus 로고
    • In vitro rosetting, cytoadherence, and microagglutination properties of Plasmodium falciparum-infected erythrocytes from Gambian and Tanzanian patients
    • Hasler T., Handunnetti S.M., Aguiar J.C., van Schravendijk M.R., Greenwood B.M., Lallinger G., Cegielski P., and Howard R.J. In vitro rosetting, cytoadherence, and microagglutination properties of Plasmodium falciparum-infected erythrocytes from Gambian and Tanzanian patients. Blood 76 (1990) 1845-1852
    • (1990) Blood , vol.76 , pp. 1845-1852
    • Hasler, T.1    Handunnetti, S.M.2    Aguiar, J.C.3    van Schravendijk, M.R.4    Greenwood, B.M.5    Lallinger, G.6    Cegielski, P.7    Howard, R.J.8
  • 149
    • 0014807599 scopus 로고
    • The clock of the malaria parasite
    • Hawking F. The clock of the malaria parasite. Sci. Am. 222 (1970) 123-131
    • (1970) Sci. Am. , vol.222 , pp. 123-131
    • Hawking, F.1
  • 150
    • 0014389859 scopus 로고
    • 24- and 48-hour cycles of malaria parasites in the blood: Their purpose, production and control
    • Hawking F., Worms M.J., and Gammage K. 24- and 48-hour cycles of malaria parasites in the blood: Their purpose, production and control. Trans. R. Soc. Trop. Med. Hyg. 62 (1968) 731-765
    • (1968) Trans. R. Soc. Trop. Med. Hyg. , vol.62 , pp. 731-765
    • Hawking, F.1    Worms, M.J.2    Gammage, K.3
  • 151
    • 0015404943 scopus 로고
    • The asexual and sexual circadian rhythms of Plasmodium vinckei chabaudi, of P. berghei and of P. gallinaceum
    • Hawking F., Gammage K., and Worms M.J. The asexual and sexual circadian rhythms of Plasmodium vinckei chabaudi, of P. berghei and of P. gallinaceum. Parasitology 65 (1972) 189-201
    • (1972) Parasitology , vol.65 , pp. 189-201
    • Hawking, F.1    Gammage, K.2    Worms, M.J.3
  • 153
    • 0036784706 scopus 로고    scopus 로고
    • Independent translocation of two micronemal proteins in developing Plasmodium falciparum merozoites
    • Healer J., Crawford S., Ralph S., McFadden G., and Cowman A.F. Independent translocation of two micronemal proteins in developing Plasmodium falciparum merozoites. Infect. Immun. 70 (2002) 5751-5758
    • (2002) Infect. Immun. , vol.70 , pp. 5751-5758
    • Healer, J.1    Crawford, S.2    Ralph, S.3    McFadden, G.4    Cowman, A.F.5
  • 154
    • 33747887924 scopus 로고    scopus 로고
    • Cellular and molecular mechanics of gliding locomotion in eukaryotes
    • Heintzelman M.B. Cellular and molecular mechanics of gliding locomotion in eukaryotes. Int. Rev. Cytol. 251 (2006) 79-129
    • (2006) Int. Rev. Cytol. , vol.251 , pp. 79-129
    • Heintzelman, M.B.1
  • 155
    • 0348111350 scopus 로고    scopus 로고
    • Identification of a stomatin orthologue in vacuoles induced in human erythrocytes by malaria parasites: A role for microbial raft proteins in apicomplexan vacuole biogenesis
    • Hiller N.L., Akompong T., Morrow J.S., Holder A.A., and Haldar K. Identification of a stomatin orthologue in vacuoles induced in human erythrocytes by malaria parasites: A role for microbial raft proteins in apicomplexan vacuole biogenesis. J. Biol. Chem. 278 (2003) 48413-48421
    • (2003) J. Biol. Chem. , vol.278 , pp. 48413-48421
    • Hiller, N.L.1    Akompong, T.2    Morrow, J.S.3    Holder, A.A.4    Haldar, K.5
  • 157
    • 33746743840 scopus 로고    scopus 로고
    • Molecular mechanisms of cytoadherence in malaria
    • Ho M., and White N.J. Molecular mechanisms of cytoadherence in malaria. Am. J. Physiol. 276 (1999) C1231-C1242
    • (1999) Am. J. Physiol. , vol.276
    • Ho, M.1    White, N.J.2
  • 158
    • 0028000871 scopus 로고
    • Proteins on the surface of the malaria parasite and cell invasion
    • Holder A.A. Proteins on the surface of the malaria parasite and cell invasion. Parasitology 108 Suppl. (1994) S5-S18
    • (1994) Parasitology , vol.108 , Issue.SUPPL
    • Holder, A.A.1
  • 161
    • 0033213013 scopus 로고    scopus 로고
    • The plastid in Plasmodium falciparum asexual blood stages: A three-dimensional ultrastructural analysis
    • Hopkins J., Fowler R., Krishna S., Wilson I., Mitchell G., and Bannister L. The plastid in Plasmodium falciparum asexual blood stages: A three-dimensional ultrastructural analysis. Protist 150 (1999) 283-295
    • (1999) Protist , vol.150 , pp. 283-295
    • Hopkins, J.1    Fowler, R.2    Krishna, S.3    Wilson, I.4    Mitchell, G.5    Bannister, L.6
  • 162
    • 0033525726 scopus 로고    scopus 로고
    • Mutational analysis identifies a five base pair cis-acting sequence essential for GBP130 promoter activity in Plasmodium falciparum
    • Horrocks P., and Lanzer M. Mutational analysis identifies a five base pair cis-acting sequence essential for GBP130 promoter activity in Plasmodium falciparum. Mol. Biochem. Parasitol. 99 (1999) 77-87
    • (1999) Mol. Biochem. Parasitol. , vol.99 , pp. 77-87
    • Horrocks, P.1    Lanzer, M.2
  • 163
    • 0030222032 scopus 로고    scopus 로고
    • Stage specific expression of proliferating cell nuclear antigen and DNA polymerase δ from Plasmodium falciparum
    • Horrocks P., Jackson M., Cheesman S., White J.H., and Kilbey B.J. Stage specific expression of proliferating cell nuclear antigen and DNA polymerase δ from Plasmodium falciparum. Mol. Biochem. Parasitol. 79 (1996) 177-182
    • (1996) Mol. Biochem. Parasitol. , vol.79 , pp. 177-182
    • Horrocks, P.1    Jackson, M.2    Cheesman, S.3    White, J.H.4    Kilbey, B.J.5
  • 166
    • 0242490894 scopus 로고    scopus 로고
    • Melatonin and N-acetyl-serotonin cross the red blood cell membrane and evoke calcium mobilization in malarial parasites
    • Hotta C.T., Markus R.P., and Garcia C.R. Melatonin and N-acetyl-serotonin cross the red blood cell membrane and evoke calcium mobilization in malarial parasites. Braz. J. Med. Biol. Res. 36 (2003) 1583-1587
    • (2003) Braz. J. Med. Biol. Res. , vol.36 , pp. 1583-1587
    • Hotta, C.T.1    Markus, R.P.2    Garcia, C.R.3
  • 167
    • 0034628901 scopus 로고    scopus 로고
    • Computational identification of cis-regulatory elements associated with groups of functionally related genes in Saccharomyces cerevisiae
    • Hughes J.D., Estep P.W., Tavazoie S., and Church G.M. Computational identification of cis-regulatory elements associated with groups of functionally related genes in Saccharomyces cerevisiae. J. Mol. Biol. 296 (2000) 1205-1214
    • (2000) J. Mol. Biol. , vol.296 , pp. 1205-1214
    • Hughes, J.D.1    Estep, P.W.2    Tavazoie, S.3    Church, G.M.4
  • 169
    • 33645077874 scopus 로고    scopus 로고
    • A calcium-dependent protein kinase regulates Plasmodium ookinete access to the midgut epithelial cell
    • Ishino T., Orito Y., Chinzei Y., and Yuda M. A calcium-dependent protein kinase regulates Plasmodium ookinete access to the midgut epithelial cell. Mol. Microbiol. 59 (2006) 1175-1184
    • (2006) Mol. Microbiol. , vol.59 , pp. 1175-1184
    • Ishino, T.1    Orito, Y.2    Chinzei, Y.3    Yuda, M.4
  • 170
    • 0035945567 scopus 로고    scopus 로고
    • Genomic binding sites of the yeast cell-cycle transcription factors SBF and MBF
    • Iyer V.R., Horak C.E., Scafe C.S., Botstein D., Snyder M., and Brown P.O. Genomic binding sites of the yeast cell-cycle transcription factors SBF and MBF. Nature 409 (2001) 533-538
    • (2001) Nature , vol.409 , pp. 533-538
    • Iyer, V.R.1    Horak, C.E.2    Scafe, C.S.3    Botstein, D.4    Snyder, M.5    Brown, P.O.6
  • 173
    • 0019302689 scopus 로고
    • Factors affecting the ability of isolated Plasmodium knowlesi merozoites to attach to and invade erythrocytes
    • Johnson J.G., Epstein N., Shiroishi T., and Miller L.H. Factors affecting the ability of isolated Plasmodium knowlesi merozoites to attach to and invade erythrocytes. Parasitology 80 (1980) 539-550
    • (1980) Parasitology , vol.80 , pp. 539-550
    • Johnson, J.G.1    Epstein, N.2    Shiroishi, T.3    Miller, L.H.4
  • 176
    • 0037141150 scopus 로고    scopus 로고
    • MAEBL is essential for malarial sporozoite infection of the mosquito salivary gland
    • Kariu T., Yuda M., Yano K., and Chinzei Y. MAEBL is essential for malarial sporozoite infection of the mosquito salivary gland. J. Exp. Med. 195 (2002) 1317-1323
    • (2002) J. Exp. Med. , vol.195 , pp. 1317-1323
    • Kariu, T.1    Yuda, M.2    Yano, K.3    Chinzei, Y.4
  • 178
    • 33750704849 scopus 로고    scopus 로고
    • Interactions between merozoite surface proteins 1, 6, and 7 of the malaria parasite Plasmodium falciparum
    • Kauth C.W., Woehlbier U., Kern M., Mekonnen Z., Lutz R., Mucke N., Langowski J., and Bujard H. Interactions between merozoite surface proteins 1, 6, and 7 of the malaria parasite Plasmodium falciparum. J. Biol. Chem. 281 (2006) 31517-31527
    • (2006) J. Biol. Chem. , vol.281 , pp. 31517-31527
    • Kauth, C.W.1    Woehlbier, U.2    Kern, M.3    Mekonnen, Z.4    Lutz, R.5    Mucke, N.6    Langowski, J.7    Bujard, H.8
  • 180
    • 0026035547 scopus 로고
    • Plasmodium berghei: Ionic regulation and the induction of gametogenesis
    • Kawamoto F., Alejo-Blanco R., Fleck S.L., and Sinden R.E. Plasmodium berghei: Ionic regulation and the induction of gametogenesis. Exp. Parasitol. 72 (1991) 33-42
    • (1991) Exp. Parasitol. , vol.72 , pp. 33-42
    • Kawamoto, F.1    Alejo-Blanco, R.2    Fleck, S.L.3    Sinden, R.E.4
  • 181
    • 0034853629 scopus 로고    scopus 로고
    • The 235 kDa rhoptry protein of Plasmodium (yoelii) yoelii: Function at the junction
    • Khan S.M., Jarra W., and Preiser P.R. The 235 kDa rhoptry protein of Plasmodium (yoelii) yoelii: Function at the junction. Mol. Biochem. Parasitol. 117 (2001) 1-10
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 1-10
    • Khan, S.M.1    Jarra, W.2    Preiser, P.R.3
  • 182
    • 20444405371 scopus 로고    scopus 로고
    • Proteome analysis of separated male and female gametocytes reveals novel sex-specific Plasmodium biology
    • Khan S.M., Franke-Fayard B., Mair G.R., Lasonder E., Janse C.J., Mann M., and Waters A.P. Proteome analysis of separated male and female gametocytes reveals novel sex-specific Plasmodium biology. Cell 121 (2005) 675-687
    • (2005) Cell , vol.121 , pp. 675-687
    • Khan, S.M.1    Franke-Fayard, B.2    Mair, G.R.3    Lasonder, E.4    Janse, C.J.5    Mann, M.6    Waters, A.P.7
  • 183
    • 8444241483 scopus 로고    scopus 로고
    • A malaria membrane skeletal protein is essential for normal morphogenesis, motility, and infectivity of sporozoites
    • Khater E.I., Sinden R.E., and Dessens J.T. A malaria membrane skeletal protein is essential for normal morphogenesis, motility, and infectivity of sporozoites. J. Cell Biol. 167 (2004) 425-432
    • (2004) J. Cell Biol. , vol.167 , pp. 425-432
    • Khater, E.I.1    Sinden, R.E.2    Dessens, J.T.3
  • 184
    • 33750995294 scopus 로고    scopus 로고
    • Maurer's clefts-restricted localization, orientation and export of a Plasmodium falciparum RIFIN
    • Khattab A., and Klinkert M.Q. Maurer's clefts-restricted localization, orientation and export of a Plasmodium falciparum RIFIN. Traffic 7 (2006) 1654-1665
    • (2006) Traffic , vol.7 , pp. 1654-1665
    • Khattab, A.1    Klinkert, M.Q.2
  • 185
    • 0009536009 scopus 로고
    • Characterization of a protein correlated with the production of knob-like protrusions on membranes of erythrocytes infected with Plasmodium falciparum
    • Kilejian A. Characterization of a protein correlated with the production of knob-like protrusions on membranes of erythrocytes infected with Plasmodium falciparum. Proc. Natl. Acad. Sci. USA 76 (1979) 4650-4653
    • (1979) Proc. Natl. Acad. Sci. USA , vol.76 , pp. 4650-4653
    • Kilejian, A.1
  • 186
    • 0017705160 scopus 로고
    • A histidine-rich protein from Plasmodium falciparum and its interaction with membranes
    • Kilejian A., and Jensen J.B. A histidine-rich protein from Plasmodium falciparum and its interaction with membranes. Bull. World Health Org. 55 (1977) 191-197
    • (1977) Bull. World Health Org. , vol.55 , pp. 191-197
    • Kilejian, A.1    Jensen, J.B.2
  • 188
  • 189
    • 0035069258 scopus 로고    scopus 로고
    • Membrane transport in the malaria-infected erythrocyte
    • Kirk K. Membrane transport in the malaria-infected erythrocyte. Physiol. Rev. 81 (2001) 495-537
    • (2001) Physiol. Rev. , vol.81 , pp. 495-537
    • Kirk, K.1
  • 190
    • 0347122968 scopus 로고    scopus 로고
    • Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum
    • Klemba M., Beatty W., Gluzman I., and Goldberg D.E. Trafficking of plasmepsin II to the food vacuole of the malaria parasite Plasmodium falciparum. J. Cell Biol. 164 (2004) 47-56
    • (2004) J. Cell Biol. , vol.164 , pp. 47-56
    • Klemba, M.1    Beatty, W.2    Gluzman, I.3    Goldberg, D.E.4
  • 191
    • 5644247394 scopus 로고    scopus 로고
    • A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation
    • Klemba M., Gluzman I., and Goldberg D.E. A Plasmodium falciparum dipeptidyl aminopeptidase I participates in vacuolar hemoglobin degradation. J. Biol. Chem. 279 (2004) 43000-43007
    • (2004) J. Biol. Chem. , vol.279 , pp. 43000-43007
    • Klemba, M.1    Gluzman, I.2    Goldberg, D.E.3
  • 192
    • 18544374027 scopus 로고    scopus 로고
    • Trafficking of the major virulence factor to the surface of transfected P. falciparum-infected erythrocytes
    • Knuepfer E., Rug M., Klonis N., Tilley L., and Cowman A.F. Trafficking of the major virulence factor to the surface of transfected P. falciparum-infected erythrocytes. Blood 105 (2005) 4078-4087
    • (2005) Blood , vol.105 , pp. 4078-4087
    • Knuepfer, E.1    Rug, M.2    Klonis, N.3    Tilley, L.4    Cowman, A.F.5
  • 193
    • 0032857534 scopus 로고    scopus 로고
    • Plasmodium cynomolgi: Transfection of blood-stage parasites using heterologous DNA constructs
    • Kocken C.H., van der Wel A., and Thomas A.W. Plasmodium cynomolgi: Transfection of blood-stage parasites using heterologous DNA constructs. Exp. Parasitol. 93 (1999) 58-60
    • (1999) Exp. Parasitol. , vol.93 , pp. 58-60
    • Kocken, C.H.1    van der Wel, A.2    Thomas, A.W.3
  • 194
    • 0036153919 scopus 로고    scopus 로고
    • Plasmodium knowlesi provides a rapid in vitro and in vivo transfection system that enables double-crossover gene knockout studies
    • Kocken C.H., Ozwara H., van der Wel A., Beetsma A.L., Mwenda J.M., and Thomas A.W. Plasmodium knowlesi provides a rapid in vitro and in vivo transfection system that enables double-crossover gene knockout studies. Infect. Immun. 70 (2002) 655-660
    • (2002) Infect. Immun. , vol.70 , pp. 655-660
    • Kocken, C.H.1    Ozwara, H.2    van der Wel, A.3    Beetsma, A.L.4    Mwenda, J.M.5    Thomas, A.W.6
  • 196
    • 0020645789 scopus 로고
    • 2+ uptake by mouse erythrocytes in malarial (Plasmodium berghei) infection
    • 2+ uptake by mouse erythrocytes in malarial (Plasmodium berghei) infection. Mol. Biochem. Parasitol. 7 (1983) 227-235
    • (1983) Mol. Biochem. Parasitol. , vol.7 , pp. 227-235
    • Krungkrai, J.1    Yuthavong, Y.2
  • 197
    • 33845292589 scopus 로고    scopus 로고
    • Raf kinase inhibitor protein affects activity of Plasmodium falciparum calcium-dependent protein kinase 1
    • Kugelstadt D., Winter D., Pluckhahn K., Lehmann W.D., and Kappes B. Raf kinase inhibitor protein affects activity of Plasmodium falciparum calcium-dependent protein kinase 1. Mol. Biochem. Parasitol. 151 (2007) 111-117
    • (2007) Mol. Biochem. Parasitol. , vol.151 , pp. 111-117
    • Kugelstadt, D.1    Winter, D.2    Pluckhahn, K.3    Lehmann, W.D.4    Kappes, B.5
  • 198
    • 33947125517 scopus 로고    scopus 로고
    • Quantitative pH measurements in Plasmodium falciparum-infected erythrocytes using pHluorin
    • Kuhn Y., Rohrbach P., and Lanzer M. Quantitative pH measurements in Plasmodium falciparum-infected erythrocytes using pHluorin. Cell Microbiol. 9 (2007) 1004-1013
    • (2007) Cell Microbiol. , vol.9 , pp. 1004-1013
    • Kuhn, Y.1    Rohrbach, P.2    Lanzer, M.3
  • 200
    • 16244382411 scopus 로고    scopus 로고
    • Plasmodium falciparum calcineurin and its association with heat shock protein 90: Mechanisms for the antimalarial activity of cyclosporin A and synergism with geldanamycin
    • Kumar R., Musiyenko A., and Barik S. Plasmodium falciparum calcineurin and its association with heat shock protein 90: Mechanisms for the antimalarial activity of cyclosporin A and synergism with geldanamycin. Mol. Biochem. Parasitol. 141 (2005) 29-37
    • (2005) Mol. Biochem. Parasitol. , vol.141 , pp. 29-37
    • Kumar, R.1    Musiyenko, A.2    Barik, S.3
  • 201
    • 33846599782 scopus 로고    scopus 로고
    • Plasmodium falciparum var gene expression is developmentally controlled at the level of RNA polymerase II-mediated transcription initiation
    • Kyes S., Christodoulou Z., Pinches R., Kriek N., Horrocks P., and Newbold C. Plasmodium falciparum var gene expression is developmentally controlled at the level of RNA polymerase II-mediated transcription initiation. Mol. Microbiol. 63 (2007) 1237-1247
    • (2007) Mol. Microbiol. , vol.63 , pp. 1237-1247
    • Kyes, S.1    Christodoulou, Z.2    Pinches, R.3    Kriek, N.4    Horrocks, P.5    Newbold, C.6
  • 204
    • 0014532821 scopus 로고
    • Penetration of erythrocytes by merozoites of mammalian and avian malarial parasites
    • Ladda R., Aikawa M., and Sprinz H. Penetration of erythrocytes by merozoites of mammalian and avian malarial parasites. J. Parasitol. 55 (1969) 633-644
    • (1969) J. Parasitol. , vol.55 , pp. 633-644
    • Ladda, R.1    Aikawa, M.2    Sprinz, H.3
  • 205
    • 0030775595 scopus 로고    scopus 로고
    • Identification of an endoplasmic reticulum-resident calcium-binding protein with multiple EF-hand motifs in asexual stages of Plasmodium falciparum
    • La Greca N., Hibbs A.R., Riffkin C., Foley M., and Tilley L. Identification of an endoplasmic reticulum-resident calcium-binding protein with multiple EF-hand motifs in asexual stages of Plasmodium falciparum. Mol. Biochem. Parasitol. 89 (1997) 283-293
    • (1997) Mol. Biochem. Parasitol. , vol.89 , pp. 283-293
    • La Greca, N.1    Hibbs, A.R.2    Riffkin, C.3    Foley, M.4    Tilley, L.5
  • 207
  • 208
    • 0021264123 scopus 로고
    • Identification of a strain-specific malarial antigen exposed on the surface of Plasmodium falciparum-infected erythrocytes
    • Leech J.H., Barnwell J.W., Miller L.H., and Howard R.J. Identification of a strain-specific malarial antigen exposed on the surface of Plasmodium falciparum-infected erythrocytes. J. Exp. Med. 159 (1984) 1567-1575
    • (1984) J. Exp. Med. , vol.159 , pp. 1567-1575
    • Leech, J.H.1    Barnwell, J.W.2    Miller, L.H.3    Howard, R.J.4
  • 211
    • 33947243452 scopus 로고    scopus 로고
    • The molecular choreography of a store-operated calcium channel
    • Lewis R.S. The molecular choreography of a store-operated calcium channel. Nature 446 (2007) 284-287
    • (2007) Nature , vol.446 , pp. 284-287
    • Lewis, R.S.1
  • 213
    • 12544251879 scopus 로고    scopus 로고
    • The role of Plasmodium falciparum food vacuole plasmepsins
    • Liu J., Gluzman I.Y., Drew M.E., and Goldberg D.E. The role of Plasmodium falciparum food vacuole plasmepsins. J. Biol. Chem. 280 (2005) 1432-1437
    • (2005) J. Biol. Chem. , vol.280 , pp. 1432-1437
    • Liu, J.1    Gluzman, I.Y.2    Drew, M.E.3    Goldberg, D.E.4
  • 214
    • 33745041171 scopus 로고    scopus 로고
    • Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems
    • Liu J., Istvan E.S., Gluzman I.Y., Gross J., and Goldberg D.E. Plasmodium falciparum ensures its amino acid supply with multiple acquisition pathways and redundant proteolytic enzyme systems. Proc. Natl. Acad. Sci. USA 103 (2006) 8840-8845
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 8840-8845
    • Liu, J.1    Istvan, E.S.2    Gluzman, I.Y.3    Gross, J.4    Goldberg, D.E.5
  • 215
    • 0036324753 scopus 로고    scopus 로고
    • An algorithm for finding protein-DNA binding sites with applications to chromatin-immunoprecipitation microarray experiments
    • Liu X.S., Brutlag D.L., and Liu J.S. An algorithm for finding protein-DNA binding sites with applications to chromatin-immunoprecipitation microarray experiments. Nat. Biotechnol 20 (2002) 835-839
    • (2002) Nat. Biotechnol , vol.20 , pp. 835-839
    • Liu, X.S.1    Brutlag, D.L.2    Liu, J.S.3
  • 216
    • 33644854445 scopus 로고    scopus 로고
    • Comparative whole genome transcriptome analysis of three Plasmodium falciparum strains
    • Llinás M., Bozdech Z., Wong E.D., Adai A.T., and DeRisi J.L. Comparative whole genome transcriptome analysis of three Plasmodium falciparum strains. Nucleic Acids Res. 34 (2006) 1166-1173
    • (2006) Nucleic Acids Res. , vol.34 , pp. 1166-1173
    • Llinás, M.1    Bozdech, Z.2    Wong, E.D.3    Adai, A.T.4    DeRisi, J.L.5
  • 217
    • 0031594576 scopus 로고    scopus 로고
    • 2+ content and expression of an acidocalcisomal calcium pump are elevated in intracellular forms of Trypanosoma cruzi
    • 2+ content and expression of an acidocalcisomal calcium pump are elevated in intracellular forms of Trypanosoma cruzi. Mol. Cell Biol. 18 (1998) 2309-2323
    • (1998) Mol. Cell Biol. , vol.18 , pp. 2309-2323
    • Lu, H.G.1    Zhong, L.2    de Souza, W.3    Benchimol, M.4    Moreno, S.5    DoCampo, R.6
  • 218
    • 0015123715 scopus 로고
    • Plasmodium falciparum malaria: Ultrastructure of parasitized erythrocytes in cardiac vessels
    • Luse S.A., and Miller L.H. Plasmodium falciparum malaria: Ultrastructure of parasitized erythrocytes in cardiac vessels. Am. J. Trop. Med. Hyg. 20 (1971) 655-660
    • (1971) Am. J. Trop. Med. Hyg. , vol.20 , pp. 655-660
    • Luse, S.A.1    Miller, L.H.2
  • 220
    • 0037234392 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations
    • Maier A.G., Duraisingh M.T., Reeder J.C., Patel S.S., Kazura J.W., Zimmerman P.A., and Cowman A.F. Plasmodium falciparum erythrocyte invasion through glycophorin C and selection for Gerbich negativity in human populations. Nat. Med. 9 (2003) 87-92
    • (2003) Nat. Med. , vol.9 , pp. 87-92
    • Maier, A.G.1    Duraisingh, M.T.2    Reeder, J.C.3    Patel, S.S.4    Kazura, J.W.5    Zimmerman, P.A.6    Cowman, A.F.7
  • 221
    • 33748300551 scopus 로고    scopus 로고
    • Negative selection using yeast cytosine deaminase/uracil phosphoribosyl transferase in Plasmodium falciparum for targeted gene deletion by double crossover recombination
    • Maier A.G., Braks J.A., Waters A.P., and Cowman A.F. Negative selection using yeast cytosine deaminase/uracil phosphoribosyl transferase in Plasmodium falciparum for targeted gene deletion by double crossover recombination. Mol. Biochem. Parasitol. 150 (2006) 118-121
    • (2006) Mol. Biochem. Parasitol. , vol.150 , pp. 118-121
    • Maier, A.G.1    Braks, J.A.2    Waters, A.P.3    Cowman, A.F.4
  • 223
    • 0033587690 scopus 로고    scopus 로고
    • A set of independent selectable markers for transfection of the human malaria parasite Plasmodium falciparum
    • Mamoun C.B., Gluzman I.Y., Goyard S., Beverley S.M., and Goldberg D.E. A set of independent selectable markers for transfection of the human malaria parasite Plasmodium falciparum. Proc. Natl. Acad. Sci. USA 96 (1999) 8716-8720
    • (1999) Proc. Natl. Acad. Sci. USA , vol.96 , pp. 8716-8720
    • Mamoun, C.B.1    Gluzman, I.Y.2    Goyard, S.3    Beverley, S.M.4    Goldberg, D.E.5
  • 224
    • 4644285665 scopus 로고    scopus 로고
    • Correlation of structural development and differential expression of invasion-related molecules in schizonts of Plasmodium falciparum
    • Margos G., Bannister L.H., Dluzewski A.R., Hopkins J., Williams I.T., and Mitchell G.H. Correlation of structural development and differential expression of invasion-related molecules in schizonts of Plasmodium falciparum. Parasitology 129 (2004) 273-287
    • (2004) Parasitology , vol.129 , pp. 273-287
    • Margos, G.1    Bannister, L.H.2    Dluzewski, A.R.3    Hopkins, J.4    Williams, I.T.5    Mitchell, G.H.6
  • 225
    • 10344250457 scopus 로고    scopus 로고
    • Targeting malaria virulence and remodeling proteins to the host erythrocyte
    • Marti M., Good R.T., Rug M., Knuepfer E., and Cowman A.F. Targeting malaria virulence and remodeling proteins to the host erythrocyte. Science 306 (2004) 1930-1933
    • (2004) Science , vol.306 , pp. 1930-1933
    • Marti, M.1    Good, R.T.2    Rug, M.3    Knuepfer, E.4    Cowman, A.F.5
  • 226
    • 24144480800 scopus 로고    scopus 로고
    • The "permeome" of the malaria parasite: An overview of the membrane transport proteins of Plasmodium falciparum
    • Martin R.E., Henry R.I., Abbey J.L., Clements J.D., and Kirk K. The "permeome" of the malaria parasite: An overview of the membrane transport proteins of Plasmodium falciparum. Genome Biol. 6 (2005) R26
    • (2005) Genome Biol. , vol.6
    • Martin, R.E.1    Henry, R.I.2    Abbey, J.L.3    Clements, J.D.4    Kirk, K.5
  • 227
    • 0028260815 scopus 로고
    • Correlation of phosphoinositide hydrolysis with exflagellation in the malaria microgametocyte
    • Martin S.K., Jett M., and Schneider I. Correlation of phosphoinositide hydrolysis with exflagellation in the malaria microgametocyte. J. Parasitol. 80 (1994) 371-378
    • (1994) J. Parasitol. , vol.80 , pp. 371-378
    • Martin, S.K.1    Jett, M.2    Schneider, I.3
  • 228
    • 0023507296 scopus 로고
    • Role of calmodulin in Plasmodium falciparum: Implications for erythrocyte invasion by the merozoite
    • Matsumoto Y., Perry G., Scheibel L.W., and Aikawa M. Role of calmodulin in Plasmodium falciparum: Implications for erythrocyte invasion by the merozoite. Eur. J. Cell Biol. 45 (1987) 36-43
    • (1987) Eur. J. Cell Biol. , vol.45 , pp. 36-43
    • Matsumoto, Y.1    Perry, G.2    Scheibel, L.W.3    Aikawa, M.4
  • 230
    • 33144460574 scopus 로고    scopus 로고
    • The glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL
    • Mayer D.C., Jiang L., Achur R.N., Kakizaki I., Gowda D.C., and Miller L.H. The glycophorin C N-linked glycan is a critical component of the ligand for the Plasmodium falciparum erythrocyte receptor BAEBL. Proc. Natl. Acad. Sci. USA 103 (2006) 2358-2362
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 2358-2362
    • Mayer, D.C.1    Jiang, L.2    Achur, R.N.3    Kakizaki, I.4    Gowda, D.C.5    Miller, L.H.6
  • 231
    • 0035091545 scopus 로고    scopus 로고
    • Deletion analysis of the 5′ flanking sequence of the Plasmodium gallinaceum sexual stage specific gene pgs28 suggests a bipartite arrangement of cis-control elements
    • Mbacham W.F., Chow C.S., Daily J., Golightly L.M., and Wirth D.F. Deletion analysis of the 5′ flanking sequence of the Plasmodium gallinaceum sexual stage specific gene pgs28 suggests a bipartite arrangement of cis-control elements. Mol. Biochem. Parasitol. 113 (2001) 183-187
    • (2001) Mol. Biochem. Parasitol. , vol.113 , pp. 183-187
    • Mbacham, W.F.1    Chow, C.S.2    Daily, J.3    Golightly, L.M.4    Wirth, D.F.5
  • 232
    • 0026571564 scopus 로고
    • The role of calcium in the invasion of human erythrocytes by Plasmodium falciparum
    • McCallum-Deighton N., and Holder A.A. The role of calcium in the invasion of human erythrocytes by Plasmodium falciparum. Mol. Biochem. Parasitol. 50 (1992) 317-323
    • (1992) Mol. Biochem. Parasitol. , vol.50 , pp. 317-323
    • McCallum-Deighton, N.1    Holder, A.A.2
  • 234
    • 0018646809 scopus 로고
    • Freeze fracture studies on the interaction between the malaria parasite and the host erythrocyte in Plasmodium knowlesi infections
    • McLaren D.J., Bannister L.H., Trigg P.I., and Butcher G.A. Freeze fracture studies on the interaction between the malaria parasite and the host erythrocyte in Plasmodium knowlesi infections. Parasitology 79 (1979) 125-139
    • (1979) Parasitology , vol.79 , pp. 125-139
    • McLaren, D.J.1    Bannister, L.H.2    Trigg, P.I.3    Butcher, G.A.4
  • 235
    • 14544291540 scopus 로고    scopus 로고
    • Tetracycline analogue-regulated transgene expression in Plasmodium falciparum blood stages using Toxoplasma gondii transactivators
    • Meissner M., Krejany E., Gilson P.R., de Koning-Ward T.F., Soldati D., and Crabb B.S. Tetracycline analogue-regulated transgene expression in Plasmodium falciparum blood stages using Toxoplasma gondii transactivators. Proc. Natl. Acad. Sci. USA 102 (2005) 2980-2985
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 2980-2985
    • Meissner, M.1    Krejany, E.2    Gilson, P.R.3    de Koning-Ward, T.F.4    Soldati, D.5    Crabb, B.S.6
  • 237
    • 1642554364 scopus 로고    scopus 로고
    • Identification of regulatory elements in the Plasmodium falciparum genome
    • Militello K.T., Dodge M., Bethke L., and Wirth D.F. Identification of regulatory elements in the Plasmodium falciparum genome. Mol. Biochem. Parasitol. 134 (2004) 75-88
    • (2004) Mol. Biochem. Parasitol. , vol.134 , pp. 75-88
    • Militello, K.T.1    Dodge, M.2    Bethke, L.3    Wirth, D.F.4
  • 238
    • 0018777194 scopus 로고
    • Interaction between cytochalasin B-treated malarial parasites and erythrocytes: Attachment and junction formation
    • Miller L.H., Aikawa M., Johnson J.G., and Shiroishi T. Interaction between cytochalasin B-treated malarial parasites and erythrocytes: Attachment and junction formation. J. Exp. Med. 149 (1979) 172-184
    • (1979) J. Exp. Med. , vol.149 , pp. 172-184
    • Miller, L.H.1    Aikawa, M.2    Johnson, J.G.3    Shiroishi, T.4
  • 241
    • 0024336003 scopus 로고
    • Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores
    • Minta A., Kao J.P., and Tsien R.Y. Fluorescent indicators for cytosolic calcium based on rhodamine and fluorescein chromophores. J. Biol. Chem. 264 (1989) 8171-8178
    • (1989) J. Biol. Chem. , vol.264 , pp. 8171-8178
    • Minta, A.1    Kao, J.P.2    Tsien, R.Y.3
  • 242
    • 0346251040 scopus 로고    scopus 로고
    • Apical membrane antigen 1, a major malaria vaccine candidate, mediates the close attachment of invasive merozoites to host red blood cells
    • Mitchell G.H., Thomas A.W., Margos G., Dluzewski A.R., and Bannister L.H. Apical membrane antigen 1, a major malaria vaccine candidate, mediates the close attachment of invasive merozoites to host red blood cells. Infect. Immun. 72 (2004) 154-158
    • (2004) Infect. Immun. , vol.72 , pp. 154-158
    • Mitchell, G.H.1    Thomas, A.W.2    Margos, G.3    Dluzewski, A.R.4    Bannister, L.H.5
  • 243
    • 0042195182 scopus 로고    scopus 로고
    • Calcium regulation in protozoan parasites
    • Moreno S.N., and DoCampo R. Calcium regulation in protozoan parasites. Curr. Opin. Microbiol. 6 (2003) 359-364
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 359-364
    • Moreno, S.N.1    DoCampo, R.2
  • 244
    • 7644221040 scopus 로고    scopus 로고
    • Export of Plasmodium falciparum calcium-dependent protein kinase 1 to the parasitophorous vacuole is dependent on three N-terminal membrane anchor motifs
    • Moskes C., Burghaus P.A., Wernli B., Sauder U., Durrenberger M., and Kappes B. Export of Plasmodium falciparum calcium-dependent protein kinase 1 to the parasitophorous vacuole is dependent on three N-terminal membrane anchor motifs. Mol. Microbiol. 54 (2004) 676-691
    • (2004) Mol. Microbiol. , vol.54 , pp. 676-691
    • Moskes, C.1    Burghaus, P.A.2    Wernli, B.3    Sauder, U.4    Durrenberger, M.5    Kappes, B.6
  • 247
    • 0025148986 scopus 로고
    • 2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum
    • 2+-ATPase of rabbit skeletal muscle sarcoplasmic reticulum. J. Cell Sci. 97 (1990) 487-495
    • (1990) J. Cell Sci. , vol.97 , pp. 487-495
    • Murakami, K.1    Tanabe, K.2    Takada, S.3
  • 248
    • 0141733057 scopus 로고    scopus 로고
    • Plasmodium falciparum falcilysin: A metalloprotease with dual specificity
    • Murata C.E., and Goldberg D.E. Plasmodium falciparum falcilysin: A metalloprotease with dual specificity. J. Biol. Chem. 278 (2003) 38022-38028
    • (2003) J. Biol. Chem. , vol.278 , pp. 38022-38028
    • Murata, C.E.1    Goldberg, D.E.2
  • 250
    • 33748079101 scopus 로고    scopus 로고
    • Comparative genomic and phylogenetic analyses of calcium ATPases and calcium-regulated proteins in the Apicomplexa
    • Nagamune K., and Sibley L.D. Comparative genomic and phylogenetic analyses of calcium ATPases and calcium-regulated proteins in the Apicomplexa. Mol. Biol. Evol. 23 (2006) 1613-1627
    • (2006) Mol. Biol. Evol. , vol.23 , pp. 1613-1627
    • Nagamune, K.1    Sibley, L.D.2
  • 251
    • 0036364352 scopus 로고    scopus 로고
    • Surface antigenic variation in Giardia lamblia
    • Nash T.E. Surface antigenic variation in Giardia lamblia. Mol. Microbiol. 45 (2002) 585-590
    • (2002) Mol. Microbiol. , vol.45 , pp. 585-590
    • Nash, T.E.1
  • 252
    • 0035856691 scopus 로고    scopus 로고
    • A pol I transcriptional body associated with VSG mono-allelic expression in Trypanosoma brucei
    • Navarro M., and Gull K. A pol I transcriptional body associated with VSG mono-allelic expression in Trypanosoma brucei. Nature 414 (2001) 759-763
    • (2001) Nature , vol.414 , pp. 759-763
    • Navarro, M.1    Gull, K.2
  • 253
    • 0032791203 scopus 로고    scopus 로고
    • Cytoadherence, pathogenesis and the infected red cell surface in Plasmodium falciparum
    • Newbold C., Craig A., Kyes S., Rowe A., Fernandez-Reyes D., and Fagan T. Cytoadherence, pathogenesis and the infected red cell surface in Plasmodium falciparum. Int. J. Parasitol. 29 (1999) 927-937
    • (1999) Int. J. Parasitol. , vol.29 , pp. 927-937
    • Newbold, C.1    Craig, A.2    Kyes, S.3    Rowe, A.4    Fernandez-Reyes, D.5    Fagan, T.6
  • 255
    • 22544464433 scopus 로고    scopus 로고
    • The role of malaria merozoite proteases in red blood cell invasion
    • O'Donnell R.A., and Blackman M.J. The role of malaria merozoite proteases in red blood cell invasion. Curr. Opin. Microbiol. 8 (2005) 422-427
    • (2005) Curr. Opin. Microbiol. , vol.8 , pp. 422-427
    • O'Donnell, R.A.1    Blackman, M.J.2
  • 257
    • 0029965089 scopus 로고    scopus 로고
    • A high molecular mass Plasmodium yoelii rhoptry protein binds to erythrocytes
    • Ogun S.A., and Holder A.A. A high molecular mass Plasmodium yoelii rhoptry protein binds to erythrocytes. Mol. Biochem. Parasitol. 76 (1996) 321-324
    • (1996) Mol. Biochem. Parasitol. , vol.76 , pp. 321-324
    • Ogun, S.A.1    Holder, A.A.2
  • 259
    • 0036372942 scopus 로고    scopus 로고
    • "The glideosome": A dynamic complex powering gliding motion and host cell invasion by Toxoplasma gondii
    • Opitz C., and Soldati D. "The glideosome": A dynamic complex powering gliding motion and host cell invasion by Toxoplasma gondii. Mol. Microbiol. 45 (2002) 597-604
    • (2002) Mol. Microbiol. , vol.45 , pp. 597-604
    • Opitz, C.1    Soldati, D.2
  • 260
    • 0037197768 scopus 로고    scopus 로고
    • A 24 bp cis-acting element essential for the transcriptional activity of Plasmodium falciparum CDP-diacylglycerol synthase gene promoter
    • Osta M., Gannoun-Zaki L., Bonnefoy S., Roy C., and Vial H.J. A 24 bp cis-acting element essential for the transcriptional activity of Plasmodium falciparum CDP-diacylglycerol synthase gene promoter. Mol. Biochem. Parasitol. 121 (2002) 87-98
    • (2002) Mol. Biochem. Parasitol. , vol.121 , pp. 87-98
    • Osta, M.1    Gannoun-Zaki, L.2    Bonnefoy, S.3    Roy, C.4    Vial, H.J.5
  • 261
    • 0034846332 scopus 로고    scopus 로고
    • The 22 kDa component of the protein complex on the surface of Plasmodium falciparum merozoites is derived from a larger precursor, merozoite surface protein 7
    • Pachebat J.A., Ling I.T., Grainger M., Trucco C., Howell S., Fernandez-Reyes D., Gunaratne R., and Holder A.A. The 22 kDa component of the protein complex on the surface of Plasmodium falciparum merozoites is derived from a larger precursor, merozoite surface protein 7. Mol. Biochem. Parasitol. 117 (2001) 83-89
    • (2001) Mol. Biochem. Parasitol. , vol.117 , pp. 83-89
    • Pachebat, J.A.1    Ling, I.T.2    Grainger, M.3    Trucco, C.4    Howell, S.5    Fernandez-Reyes, D.6    Gunaratne, R.7    Holder, A.A.8
  • 263
    • 0032492553 scopus 로고    scopus 로고
    • 2+ release from chloroquine-sensitive and -insensitive intracellular stores in the intraerythrocytic stage of the malaria parasite P. chabaudi
    • 2+ release from chloroquine-sensitive and -insensitive intracellular stores in the intraerythrocytic stage of the malaria parasite P. chabaudi. Biochem. Biophys Res. Commun. 245 (1998) 155-160
    • (1998) Biochem. Biophys Res. Commun. , vol.245 , pp. 155-160
    • Passos, A.P.1    Garcia, C.R.2
  • 264
    • 0035171634 scopus 로고    scopus 로고
    • Serial analysis of gene expression in Plasmodium falciparum reveals the global expression profile of erythrocytic stages and the presence of anti-sense transcripts in the malarial parasite
    • Patankar S., Munasinghe A., Shoaibi A., Cummings L.M., and Wirth D.F. Serial analysis of gene expression in Plasmodium falciparum reveals the global expression profile of erythrocytic stages and the presence of anti-sense transcripts in the malarial parasite. Mol. Biol. Cell 12 (2001) 3114-3125
    • (2001) Mol. Biol. Cell , vol.12 , pp. 3114-3125
    • Patankar, S.1    Munasinghe, A.2    Shoaibi, A.3    Cummings, L.M.4    Wirth, D.F.5
  • 265
    • 0035224579 scopus 로고    scopus 로고
    • An algorithm for finding signals of unknown length in DNA sequences
    • Pavesi G., Mauri G., and Pesole G. An algorithm for finding signals of unknown length in DNA sequences. Bioinformatics 17 Suppl 1 (2001) S207-S214
    • (2001) Bioinformatics , vol.17 , Issue.SUPPL. 1
    • Pavesi, G.1    Mauri, G.2    Pesole, G.3
  • 266
    • 16644364007 scopus 로고    scopus 로고
    • In silico representation and discovery of transcription factor binding sites
    • Pavesi G., Mauri G., and Pesole G. In silico representation and discovery of transcription factor binding sites. Brief Bioinform 5 (2004) 217-236
    • (2004) Brief Bioinform , vol.5 , pp. 217-236
    • Pavesi, G.1    Mauri, G.2    Pesole, G.3
  • 267
    • 26844506268 scopus 로고    scopus 로고
    • Regulation of antigen gene expression in Trypanosoma brucei
    • Pays E. Regulation of antigen gene expression in Trypanosoma brucei. Trends Parasitol. 21 (2005) 517-520
    • (2005) Trends Parasitol. , vol.21 , pp. 517-520
    • Pays, E.1
  • 268
    • 34547959977 scopus 로고    scopus 로고
    • The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion
    • Pei X., Guo X., Coppel R., Bhattacharjee S., Haldar K., Gratzer W., Mohandas N., and An X. The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion. Blood 110 3 (2007) 1036-1042
    • (2007) Blood , vol.110 , Issue.3 , pp. 1036-1042
    • Pei, X.1    Guo, X.2    Coppel, R.3    Bhattacharjee, S.4    Haldar, K.5    Gratzer, W.6    Mohandas, N.7    An, X.8
  • 271
    • 33846077153 scopus 로고    scopus 로고
    • A role for falcilysin in transit peptide degradation in the Plasmodium falciparum apicoplast
    • Ponpuak M., Klemba M., Park M., Gluzman I.Y., Lamppa G.K., and Goldberg D.E. A role for falcilysin in transit peptide degradation in the Plasmodium falciparum apicoplast. Mol. Microbiol. 63 (2007) 314-334
    • (2007) Mol. Microbiol. , vol.63 , pp. 314-334
    • Ponpuak, M.1    Klemba, M.2    Park, M.3    Gluzman, I.Y.4    Lamppa, G.K.5    Goldberg, D.E.6
  • 272
    • 0038006258 scopus 로고    scopus 로고
    • The Theodore Bucher lecture. Investigating signal transduction with genetically encoded fluorescent probes
    • Pozzan T., Mongillo M., and Rudolf R. The Theodore Bucher lecture. Investigating signal transduction with genetically encoded fluorescent probes. Eur. J. Biochem. 270 (2003) 2343-2352
    • (2003) Eur. J. Biochem. , vol.270 , pp. 2343-2352
    • Pozzan, T.1    Mongillo, M.2    Rudolf, R.3
  • 273
    • 0033561460 scopus 로고    scopus 로고
    • A rhoptry-protein-associated mechanism of clonal phenotypic variation in rodent malaria
    • Preiser P.R., Jarra W., Capiod T., and Snounou G. A rhoptry-protein-associated mechanism of clonal phenotypic variation in rodent malaria. Nature 398 (1999) 618-622
    • (1999) Nature , vol.398 , pp. 618-622
    • Preiser, P.R.1    Jarra, W.2    Capiod, T.3    Snounou, G.4
  • 277
    • 17244382283 scopus 로고    scopus 로고
    • Antigenic variation in Plasmodium falciparum is associated with movement of var loci between subnuclear locations
    • Ralph S.A., Scheidig-Benatar C., and Scherf A. Antigenic variation in Plasmodium falciparum is associated with movement of var loci between subnuclear locations. Proc. Natl. Acad. Sci. USA 102 (2005) 5414-5419
    • (2005) Proc. Natl. Acad. Sci. USA , vol.102 , pp. 5414-5419
    • Ralph, S.A.1    Scheidig-Benatar, C.2    Scherf, A.3
  • 278
    • 0026699150 scopus 로고
    • A novel 40-kDa membrane-associated EF-hand calcium-binding protein in Plasmodium falciparum
    • Rawlings D.J., and Kaslow D.C. A novel 40-kDa membrane-associated EF-hand calcium-binding protein in Plasmodium falciparum. J. Biol. Chem. 267 (1992) 3976-3982
    • (1992) J. Biol. Chem. , vol.267 , pp. 3976-3982
    • Rawlings, D.J.1    Kaslow, D.C.2
  • 279
    • 0034691137 scopus 로고    scopus 로고
    • Targeted disruption of an erythrocyte binding antigen in Plasmodium falciparum is associated with a switch toward a sialic acid-independent pathway of invasion
    • Reed M.B., Caruana S.R., Batchelor A.H., Thompson J.K., Crabb B.S., and Cowman A.F. Targeted disruption of an erythrocyte binding antigen in Plasmodium falciparum is associated with a switch toward a sialic acid-independent pathway of invasion. Proc. Natl. Acad. Sci. USA 97 (2000) 7509-7514
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 7509-7514
    • Reed, M.B.1    Caruana, S.R.2    Batchelor, A.H.3    Thompson, J.K.4    Crabb, B.S.5    Cowman, A.F.6
  • 283
    • 0026081676 scopus 로고
    • The structure of the calmodulin gene of Plasmodium falciparum
    • Robson K.J., and Jennings M.W. The structure of the calmodulin gene of Plasmodium falciparum. Mol. Biochem. Parasitol. 46 (1991) 19-34
    • (1991) Mol. Biochem. Parasitol. , vol.46 , pp. 19-34
    • Robson, K.J.1    Jennings, M.W.2
  • 285
    • 12744262976 scopus 로고    scopus 로고
    • Cysteine proteases of malaria parasites
    • Rosenthal P.J. Cysteine proteases of malaria parasites. Int. J. Parasitol. 34 (2004) 1489-1499
    • (2004) Int. J. Parasitol. , vol.34 , pp. 1489-1499
    • Rosenthal, P.J.1
  • 286
    • 4644246654 scopus 로고    scopus 로고
    • Correct promoter control is needed for trafficking of the ring-infected erythrocyte surface antigen to the host cytosol in transfected malaria parasites
    • Rug M., Wickham M.E., Foley M., Cowman A.F., and Tilley L. Correct promoter control is needed for trafficking of the ring-infected erythrocyte surface antigen to the host cytosol in transfected malaria parasites. Infect. Immun. 72 (2004) 6095-6105
    • (2004) Infect. Immun. , vol.72 , pp. 6095-6105
    • Rug, M.1    Wickham, M.E.2    Foley, M.3    Cowman, A.F.4    Tilley, L.5
  • 287
    • 33745585336 scopus 로고    scopus 로고
    • The role of KAHRP domains in knob formation and cytoadherence of P. falciparum-infected human erythrocytes
    • Rug M., Prescott S.W., Fernandez K.M., Cooke B.M., and Cowman A.F. The role of KAHRP domains in knob formation and cytoadherence of P. falciparum-infected human erythrocytes. Blood 108 (2006) 370-378
    • (2006) Blood , vol.108 , pp. 370-378
    • Rug, M.1    Prescott, S.W.2    Fernandez, K.M.3    Cooke, B.M.4    Cowman, A.F.5
  • 289
    • 0035793051 scopus 로고    scopus 로고
    • Malaria parasite exit from the host erythrocyte: A two-step process requiring extraerythrocytic proteolysis
    • Salmon B.L., Oksman A., and Goldberg D.E. Malaria parasite exit from the host erythrocyte: A two-step process requiring extraerythrocytic proteolysis. Proc. Natl. Acad. Sci. USA 98 (2001) 271-276
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 271-276
    • Salmon, B.L.1    Oksman, A.2    Goldberg, D.E.3
  • 291
    • 0033232020 scopus 로고    scopus 로고
    • The role of variant surface antigens on malaria-infected red blood cells
    • Saul A. The role of variant surface antigens on malaria-infected red blood cells. Parasitol. Today 15 (1999) 455-457
    • (1999) Parasitol. Today , vol.15 , pp. 455-457
    • Saul, A.1
  • 292
    • 0023432272 scopus 로고
    • Calcium and calmodulin antagonists inhibit human malaria parasites (Plasmodium falciparum): Implications for drug design
    • Scheibel L.W., Colombani P.M., Hess A.D., Aikawa M., Atkinson C.T., and Milhous W.K. Calcium and calmodulin antagonists inhibit human malaria parasites (Plasmodium falciparum): Implications for drug design. Proc. Natl. Acad. Sci. USA 84 (1987) 7310-7314
    • (1987) Proc. Natl. Acad. Sci. USA , vol.84 , pp. 7310-7314
    • Scheibel, L.W.1    Colombani, P.M.2    Hess, A.D.3    Aikawa, M.4    Atkinson, C.T.5    Milhous, W.K.6
  • 293
    • 0032530397 scopus 로고    scopus 로고
    • Antigenic variation in malaria: In situ switching, relaxed and mutually exclusive transcription of var genes during intra-erythrocytic development in Plasmodium falciparum
    • Scherf A., Hernandez-Rivas R., Buffet P., Bottius E., Benatar C., Pouvelle B., Gysin J., and Lanzer M. Antigenic variation in malaria: In situ switching, relaxed and mutually exclusive transcription of var genes during intra-erythrocytic development in Plasmodium falciparum. EMBO J. 17 (1998) 5418-5426
    • (1998) EMBO J. , vol.17 , pp. 5418-5426
    • Scherf, A.1    Hernandez-Rivas, R.2    Buffet, P.3    Bottius, E.4    Benatar, C.5    Pouvelle, B.6    Gysin, J.7    Lanzer, M.8
  • 295
    • 33749515928 scopus 로고    scopus 로고
    • Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins
    • Schuler H., and Matuschewski K. Regulation of apicomplexan microfilament dynamics by a minimal set of actin-binding proteins. Traffic 7 (2006) 1433-1439
    • (2006) Traffic , vol.7 , pp. 1433-1439
    • Schuler, H.1    Matuschewski, K.2
  • 296
    • 0028115808 scopus 로고
    • The parasitophorous vacuole membrane surrounding intracellular Toxoplasma gondii functions as a molecular sieve
    • Schwab J.C., Beckers C.J., and Joiner K.A. The parasitophorous vacuole membrane surrounding intracellular Toxoplasma gondii functions as a molecular sieve. Proc. Natl. Acad. Sci. USA 91 (1994) 509-513
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 509-513
    • Schwab, J.C.1    Beckers, C.J.2    Joiner, K.A.3
  • 298
    • 34548576414 scopus 로고
    • Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea
    • Shimomura O., Johnson F.H., and Saiga Y. Extraction, purification and properties of aequorin, a bioluminescent protein from the luminous hydromedusan, Aequorea. J. Cell. Comp. Physiol. 59 (1962) 223-239
    • (1962) J. Cell. Comp. Physiol. , vol.59 , pp. 223-239
    • Shimomura, O.1    Johnson, F.H.2    Saiga, Y.3
  • 299
    • 0025272167 scopus 로고
    • Chromosome 9 from independent clones and isolates of Plasmodium falciparum undergoes subtelomeric deletions with similar breakpoints in vitro
    • Shirley M.W., Biggs B.A., Forsyth K.P., Brown H.J., Thompson J.K., Brown G.V., and Kemp D.J. Chromosome 9 from independent clones and isolates of Plasmodium falciparum undergoes subtelomeric deletions with similar breakpoints in vitro. Mol. Biochem. Parasitol. 40 (1990) 137-145
    • (1990) Mol. Biochem. Parasitol. , vol.40 , pp. 137-145
    • Shirley, M.W.1    Biggs, B.A.2    Forsyth, K.P.3    Brown, H.J.4    Thompson, J.K.5    Brown, G.V.6    Kemp, D.J.7
  • 300
    • 1842482437 scopus 로고    scopus 로고
    • Intracellular parasite invasion strategies
    • Sibley L.D. Intracellular parasite invasion strategies. Science 304 (2004) 248-253
    • (2004) Science , vol.304 , pp. 248-253
    • Sibley, L.D.1
  • 301
    • 1842533231 scopus 로고    scopus 로고
    • Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum
    • Sijwali P.S., and Rosenthal P.J. Gene disruption confirms a critical role for the cysteine protease falcipain-2 in hemoglobin hydrolysis by Plasmodium falciparum. Proc. Natl. Acad. Sci. USA 101 (2004) 4384-4389
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4384-4389
    • Sijwali, P.S.1    Rosenthal, P.J.2
  • 303
    • 33748328016 scopus 로고    scopus 로고
    • Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum
    • Sijwali P.S., Koo J., Singh N., and Rosenthal P.J. Gene disruptions demonstrate independent roles for the four falcipain cysteine proteases of Plasmodium falciparum. Mol. Biochem. Parasitol. 150 (2006) 96-106
    • (2006) Mol. Biochem. Parasitol. , vol.150 , pp. 96-106
    • Sijwali, P.S.1    Koo, J.2    Singh, N.3    Rosenthal, P.J.4
  • 306
    • 0028122878 scopus 로고
    • Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum
    • Sim B.K., Chitnis C.E., Wasniowska K., Hadley T.J., and Miller L.H. Receptor and ligand domains for invasion of erythrocytes by Plasmodium falciparum. Science 264 (1994) 1941-1944
    • (1994) Science , vol.264 , pp. 1941-1944
    • Sim, B.K.1    Chitnis, C.E.2    Wasniowska, K.3    Hadley, T.J.4    Miller, L.H.5
  • 307
    • 15944368263 scopus 로고    scopus 로고
    • Targeted deletion of Plasmodium knowlesi Duffy binding protein confirms its role in junction formation during invasion
    • Singh A.P., Ozwara H., Kocken C.H., Puri S.K., Thomas A.W., and Chitnis C.E. Targeted deletion of Plasmodium knowlesi Duffy binding protein confirms its role in junction formation during invasion. Mol. Microbiol. 55 (2005) 1925-1934
    • (2005) Mol. Microbiol. , vol.55 , pp. 1925-1934
    • Singh, A.P.1    Ozwara, H.2    Kocken, C.H.3    Puri, S.K.4    Thomas, A.W.5    Chitnis, C.E.6
  • 308
    • 38349145774 scopus 로고    scopus 로고
    • Whole-genome analysis of mRNA decay in Plasmodium falciparum reveals a global lengthening of mRNA half-life during the intra-erythrocytic development cycle
    • Shock J.L., Fisher K.F., and DeRisi J.L. Whole-genome analysis of mRNA decay in Plasmodium falciparum reveals a global lengthening of mRNA half-life during the intra-erythrocytic development cycle. Gen. Biol. 8 (2007) R134
    • (2007) Gen. Biol. , vol.8
    • Shock, J.L.1    Fisher, K.F.2    DeRisi, J.L.3
  • 309
    • 0028982168 scopus 로고
    • Switches in expression of Plasmodium falciparum var genes correlate with changes in antigenic and cytoadherent phenotypes of infected erythrocytes
    • Smith J.D., Chitnis C.E., Craig A.G., Roberts D.J., Hudson-Taylor D.E., Peterson D.S., Pinches R., Newbold C.I., and Miller L.H. Switches in expression of Plasmodium falciparum var genes correlate with changes in antigenic and cytoadherent phenotypes of infected erythrocytes. Cell 82 (1995) 101-110
    • (1995) Cell , vol.82 , pp. 101-110
    • Smith, J.D.1    Chitnis, C.E.2    Craig, A.G.3    Roberts, D.J.4    Hudson-Taylor, D.E.5    Peterson, D.S.6    Pinches, R.7    Newbold, C.I.8    Miller, L.H.9
  • 310
    • 7444240712 scopus 로고    scopus 로고
    • Molecular and functional aspects of parasite invasion
    • Soldati D., Foth B.J., and Cowman A.F. Molecular and functional aspects of parasite invasion. Trends Parasitol. 20 (2004) 567-574
    • (2004) Trends Parasitol. , vol.20 , pp. 567-574
    • Soldati, D.1    Foth, B.J.2    Cowman, A.F.3
  • 311
    • 33646883306 scopus 로고    scopus 로고
    • Genesis of and trafficking to the Maurer's clefts of Plasmodium falciparum-infected erythrocytes
    • Spycher C., Rug M., Klonis N., Ferguson D.J., Cowman A.F., Beck H.P., and Tilley L. Genesis of and trafficking to the Maurer's clefts of Plasmodium falciparum-infected erythrocytes. Mol. Cell. Biol. 26 (2006) 4074-4085
    • (2006) Mol. Cell. Biol. , vol.26 , pp. 4074-4085
    • Spycher, C.1    Rug, M.2    Klonis, N.3    Ferguson, D.J.4    Cowman, A.F.5    Beck, H.P.6    Tilley, L.7
  • 313
    • 0029070914 scopus 로고
    • The large diverse gene family var encodes proteins involved in cytoadherence and antigenic variation of Plasmodium falciparum-infected erythrocytes
    • Su X.Z., Heatwole V.M., Wertheimer S.P., Guinet F., Herrfeldt J.A., Peterson D.S., Ravetch J.A., and Wellems T.E. The large diverse gene family var encodes proteins involved in cytoadherence and antigenic variation of Plasmodium falciparum-infected erythrocytes. Cell 82 (1995) 89-100
    • (1995) Cell , vol.82 , pp. 89-100
    • Su, X.Z.1    Heatwole, V.M.2    Wertheimer, S.P.3    Guinet, F.4    Herrfeldt, J.A.5    Peterson, D.S.6    Ravetch, J.A.7    Wellems, T.E.8
  • 316
    • 0025223897 scopus 로고
    • Ion metabolism in malaria-infected erythrocytes
    • Tanabe K. Ion metabolism in malaria-infected erythrocytes. Blood Cells 16 (1990) 437-449
    • (1990) Blood Cells , vol.16 , pp. 437-449
    • Tanabe, K.1
  • 317
    • 0020313839 scopus 로고
    • Calcium transport of Plasmodium chabaudi-infected erythrocytes
    • Tanabe K., Mikkelsen R.B., and Wallach D.F. Calcium transport of Plasmodium chabaudi-infected erythrocytes. J. Cell Biol. 93 (1982) 680-684
    • (1982) J. Cell Biol. , vol.93 , pp. 680-684
    • Tanabe, K.1    Mikkelsen, R.B.2    Wallach, D.F.3
  • 319
    • 23644436001 scopus 로고    scopus 로고
    • Targeting malaria parasite proteins to the erythrocyte
    • Templeton T.J., and Deitsch K.W. Targeting malaria parasite proteins to the erythrocyte. Trends Parasitol. 21 (2005) 399-402
    • (2005) Trends Parasitol. , vol.21 , pp. 399-402
    • Templeton, T.J.1    Deitsch, K.W.2
  • 320
    • 28244461269 scopus 로고    scopus 로고
    • An atypical mitogen-activated protein kinase controls cytokinesis and flagellar motility during male gamete formation in a malaria parasite
    • Tewari R., Dorin D., Moon R., Doerig C., and Billker O. An atypical mitogen-activated protein kinase controls cytokinesis and flagellar motility during male gamete formation in a malaria parasite. Mol. Microbiol. 58 (2005) 1253-1263
    • (2005) Mol. Microbiol. , vol.58 , pp. 1253-1263
    • Tewari, R.1    Dorin, D.2    Moon, R.3    Doerig, C.4    Billker, O.5
  • 321
    • 0025273675 scopus 로고
    • Sixty-six kilodalton-related antigens of Plasmodium knowlesi are merozoite surface antigens associated with the apical prominence
    • Thomas A.W., Bannister L.H., and Waters A.P. Sixty-six kilodalton-related antigens of Plasmodium knowlesi are merozoite surface antigens associated with the apical prominence. Parasite Immunol. 12 (1990) 105-113
    • (1990) Parasite Immunol. , vol.12 , pp. 105-113
    • Thomas, A.W.1    Bannister, L.H.2    Waters, A.P.3
  • 323
    • 33746284200 scopus 로고    scopus 로고
    • Protein targeting to destinations of the secretory pathway in the malaria parasite Plasmodium falciparum
    • Tonkin C.J., Pearce J.A., McFadden G.I., and Cowman A.F. Protein targeting to destinations of the secretory pathway in the malaria parasite Plasmodium falciparum. Curr. Opin. Microbiol. 9 (2006) 381-387
    • (2006) Curr. Opin. Microbiol. , vol.9 , pp. 381-387
    • Tonkin, C.J.1    Pearce, J.A.2    McFadden, G.I.3    Cowman, A.F.4
  • 324
    • 33746306514 scopus 로고    scopus 로고
    • Evidence for Golgi-independent transport from the early secretory pathway to the plastid in malaria parasites
    • Tonkin C.J., Struck N.S., Mullin K.A., Stimmler L.M., and McFadden G.I. Evidence for Golgi-independent transport from the early secretory pathway to the plastid in malaria parasites. Mol. Microbiol. 61 (2006) 614-630
    • (2006) Mol. Microbiol. , vol.61 , pp. 614-630
    • Tonkin, C.J.1    Struck, N.S.2    Mullin, K.A.3    Stimmler, L.M.4    McFadden, G.I.5
  • 325
    • 8844254777 scopus 로고    scopus 로고
    • Identification and characterisation of RAMA homologues in rodent, simian and human malaria species
    • Topolska A.E., Black C.G., and Coppel R.L. Identification and characterisation of RAMA homologues in rodent, simian and human malaria species. Mol. Biochem. Parasitol. 138 (2004) 237-241
    • (2004) Mol. Biochem. Parasitol. , vol.138 , pp. 237-241
    • Topolska, A.E.1    Black, C.G.2    Coppel, R.L.3
  • 326
    • 2542610005 scopus 로고    scopus 로고
    • Associations between responses to the rhoptry-associated membrane antigen of Plasmodium falciparum and immunity to malaria infection
    • Topolska A.E., Richie T.L., Nhan D.H., and Coppel R.L. Associations between responses to the rhoptry-associated membrane antigen of Plasmodium falciparum and immunity to malaria infection. Infect. Immun. 72 (2004) 3325-3330
    • (2004) Infect. Immun. , vol.72 , pp. 3325-3330
    • Topolska, A.E.1    Richie, T.L.2    Nhan, D.H.3    Coppel, R.L.4
  • 327
    • 1042289743 scopus 로고    scopus 로고
    • Characterization of a membrane-associated rhoptry protein of Plasmodium falciparum
    • Topolska A.E., Lidgett A., Truman D., Fujioka H., and Coppel R.L. Characterization of a membrane-associated rhoptry protein of Plasmodium falciparum. J. Biol. Chem. 279 (2004) 4648-4656
    • (2004) J. Biol. Chem. , vol.279 , pp. 4648-4656
    • Topolska, A.E.1    Lidgett, A.2    Truman, D.3    Fujioka, H.4    Coppel, R.L.5
  • 328
    • 0032776597 scopus 로고    scopus 로고
    • Plasmodium falciparum: Stage-related expression of topoisomerase I
    • Tosh K., Cheesman S., Horrocks P., and Kilbey B. Plasmodium falciparum: Stage-related expression of topoisomerase I. Exp. Parasitol. 91 (1999) 126-132
    • (1999) Exp. Parasitol. , vol.91 , pp. 126-132
    • Tosh, K.1    Cheesman, S.2    Horrocks, P.3    Kilbey, B.4
  • 329
    • 0017311840 scopus 로고
    • Human malaria parasites in continuous culture
    • Trager W., and Jensen J.B. Human malaria parasites in continuous culture. Science 193 (1976) 673-675
    • (1976) Science , vol.193 , pp. 673-675
    • Trager, W.1    Jensen, J.B.2
  • 330
    • 33845974900 scopus 로고    scopus 로고
    • A conserved region in the EBL proteins is implicated in microneme targeting of the malaria parasite Plasmodium falciparum
    • Treeck M., Struck N.S., Haase S., Langer C., Herrmann S., Healer J., Cowman A.F., and Gilberger T.W. A conserved region in the EBL proteins is implicated in microneme targeting of the malaria parasite Plasmodium falciparum. J. Biol. Chem. 281 (2006) 31995-32003
    • (2006) J. Biol. Chem. , vol.281 , pp. 31995-32003
    • Treeck, M.1    Struck, N.S.2    Haase, S.3    Langer, C.4    Herrmann, S.5    Healer, J.6    Cowman, A.F.7    Gilberger, T.W.8
  • 331
    • 0034636036 scopus 로고    scopus 로고
    • clag9: A cytoadherence gene in Plasmodium falciparum essential for binding of parasitized erythrocytes to CD36
    • Trenholme K.R., Gardiner D.L., Holt D.C., Thomas E.A., Cowman A.F., and Kemp D.J. clag9: A cytoadherence gene in Plasmodium falciparum essential for binding of parasitized erythrocytes to CD36. Proc. Natl. Acad. Sci. USA 97 (2000) 4029-4033
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 4029-4033
    • Trenholme, K.R.1    Gardiner, D.L.2    Holt, D.C.3    Thomas, E.A.4    Cowman, A.F.5    Kemp, D.J.6
  • 332
    • 12344304667 scopus 로고    scopus 로고
    • Reticulocyte-binding protein homologue 1 is required for sialic acid-dependent invasion into human erythrocytes by Plasmodium falciparum
    • Triglia T., Duraisingh M.T., Good R.T., and Cowman A.F. Reticulocyte-binding protein homologue 1 is required for sialic acid-dependent invasion into human erythrocytes by Plasmodium falciparum. Mol. Microbiol. 55 (2005) 162-174
    • (2005) Mol. Microbiol. , vol.55 , pp. 162-174
    • Triglia, T.1    Duraisingh, M.T.2    Good, R.T.3    Cowman, A.F.4
  • 333
    • 0028889183 scopus 로고
    • Molecular cloning and sequence of two novel P-type adenosinetriphosphatases from Plasmodium falciparum
    • Trottein F., and Cowman A.F. Molecular cloning and sequence of two novel P-type adenosinetriphosphatases from Plasmodium falciparum. Eur. J. Biochem. 227 (1995) 214-225
    • (1995) Eur. J. Biochem. , vol.227 , pp. 214-225
    • Trottein, F.1    Cowman, A.F.2
  • 335
    • 0019333905 scopus 로고
    • New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures
    • Tsien R.Y. New calcium indicators and buffers with high selectivity against magnesium and protons: Design, synthesis, and properties of prototype structures. Biochemistry 19 (1980) 2396-2404
    • (1980) Biochemistry , vol.19 , pp. 2396-2404
    • Tsien, R.Y.1
  • 336
    • 0019972712 scopus 로고
    • Calcium homeostasis in intact lymphocytes: Cytoplasmic free calcium monitored with a new, intracellularly trapped fluorescent indicator
    • Tsien R.Y., Pozzan T., and Rink T.J. Calcium homeostasis in intact lymphocytes: Cytoplasmic free calcium monitored with a new, intracellularly trapped fluorescent indicator. J. Cell Biol. 94 (1982) 325-334
    • (1982) J. Cell Biol. , vol.94 , pp. 325-334
    • Tsien, R.Y.1    Pozzan, T.2    Rink, T.J.3
  • 337
    • 0019862984 scopus 로고
    • Falciparum malaria-infected erythrocytes specifically bind to cultured human endothelial cells
    • Udeinya I.J., Schmidt J.A., Aikawa M., Miller L.H., and Green I. Falciparum malaria-infected erythrocytes specifically bind to cultured human endothelial cells. Science 213 (1981) 555-557
    • (1981) Science , vol.213 , pp. 555-557
    • Udeinya, I.J.1    Schmidt, J.A.2    Aikawa, M.3    Miller, L.H.4    Green, I.5
  • 338
    • 33748753548 scopus 로고    scopus 로고
    • PfPKB, a protein kinase B-like enzyme from Plasmodium falciparum. II. Identification of calcium/calmodulin as its upstream activator and dissection of a novel signaling pathway
    • Vaid A., and Sharma P. PfPKB, a protein kinase B-like enzyme from Plasmodium falciparum. II. Identification of calcium/calmodulin as its upstream activator and dissection of a novel signaling pathway. J. Biol. Chem. 281 (2006) 27126-27133
    • (2006) J. Biol. Chem. , vol.281 , pp. 27126-27133
    • Vaid, A.1    Sharma, P.2
  • 341
    • 0037189526 scopus 로고    scopus 로고
    • Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme
    • van Dooren G.G., Su V., D'Ombrain M.C., and McFadden G.I. Processing of an apicoplast leader sequence in Plasmodium falciparum and the identification of a putative leader cleavage enzyme. J. Biol. Chem. 277 (2002) 23612-23619
    • (2002) J. Biol. Chem. , vol.277 , pp. 23612-23619
    • van Dooren, G.G.1    Su, V.2    D'Ombrain, M.C.3    McFadden, G.I.4
  • 342
    • 31444437901 scopus 로고    scopus 로고
    • Combinatorial gene regulation in Plasmodium falciparum
    • van Noort V., and Huynen M.A. Combinatorial gene regulation in Plasmodium falciparum. Trends Genet. 22 (2006) 73-78
    • (2006) Trends Genet. , vol.22 , pp. 73-78
    • van Noort, V.1    Huynen, M.A.2
  • 344
    • 0036178372 scopus 로고    scopus 로고
    • Merozoite surface protein-9 of Plasmodium vivax and related simian malaria parasites is orthologous to p101/ABRA of P. falciparum
    • Vargas-Serrato E., Barnwell J.W., Ingravallo P., Perler F.B., and Galinski M.R. Merozoite surface protein-9 of Plasmodium vivax and related simian malaria parasites is orthologous to p101/ABRA of P. falciparum. Mol. Biochem. Parasitol. 120 (2002) 41-52
    • (2002) Mol. Biochem. Parasitol. , vol.120 , pp. 41-52
    • Vargas-Serrato, E.1    Barnwell, J.W.2    Ingravallo, P.3    Perler, F.B.4    Galinski, M.R.5
  • 346
    • 0037072661 scopus 로고    scopus 로고
    • Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi
    • Volpe T.A., Kidner C., Hall I.M., Teng G., Grewal S.I., and Martienssen R.A. Regulation of heterochromatic silencing and histone H3 lysine-9 methylation by RNAi. Science 297 (2002) 1833-1837
    • (2002) Science , vol.297 , pp. 1833-1837
    • Volpe, T.A.1    Kidner, C.2    Hall, I.M.3    Teng, G.4    Grewal, S.I.5    Martienssen, R.A.6
  • 347
    • 0037124114 scopus 로고    scopus 로고
    • Plasmodium falciparum possesses a cell cycle-regulated short type replication protein A large subunit encoded by an unusual transcript
    • Voss T.S., Mini T., Jenoe P., and Beck H.P. Plasmodium falciparum possesses a cell cycle-regulated short type replication protein A large subunit encoded by an unusual transcript. J. Biol. Chem. 277 (2002) 17493-17501
    • (2002) J. Biol. Chem. , vol.277 , pp. 17493-17501
    • Voss, T.S.1    Mini, T.2    Jenoe, P.3    Beck, H.P.4
  • 349
    • 0033452362 scopus 로고    scopus 로고
    • Prediction of gene function by genome-scale expression analysis: Prostate cancer-associated genes
    • Walker M.G., Volkmuth W., Sprinzak E., Hodgson D., and Klingler T. Prediction of gene function by genome-scale expression analysis: Prostate cancer-associated genes. Genome Res. 9 (1999) 1198-1203
    • (1999) Genome Res. , vol.9 , pp. 1198-1203
    • Walker, M.G.1    Volkmuth, W.2    Sprinzak, E.3    Hodgson, D.4    Klingler, T.5
  • 351
    • 0034678922 scopus 로고    scopus 로고
    • Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway
    • Waller R.F., Reed M.B., Cowman A.F., and McFadden G.I. Protein trafficking to the plastid of Plasmodium falciparum is via the secretory pathway. EMBO J. 19 (2000) 1794-1802
    • (2000) EMBO J. , vol.19 , pp. 1794-1802
    • Waller, R.F.1    Reed, M.B.2    Cowman, A.F.3    McFadden, G.I.4
  • 352
    • 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
  • 353
    • 0025616923 scopus 로고
    • The role of calcium ions in the invasion of Plasmodium falciparum
    • Wasserman M. The role of calcium ions in the invasion of Plasmodium falciparum. Blood Cells 16 (1990) 450-451
    • (1990) Blood Cells , vol.16 , pp. 450-451
    • Wasserman, M.1
  • 354
    • 0242481218 scopus 로고    scopus 로고
    • Intraerythrocytic calcium chelators inhibit the invasion of Plasmodium falciparum
    • Wasserman M., and Chaparro J. Intraerythrocytic calcium chelators inhibit the invasion of Plasmodium falciparum. Parasitol. Res. 82 (1996) 102-107
    • (1996) Parasitol. Res. , vol.82 , pp. 102-107
    • Wasserman, M.1    Chaparro, J.2
  • 355
    • 0037193658 scopus 로고    scopus 로고
    • Analysis of transcriptomes of human malaria parasite Plasmodium falciparum using full-length enriched library: Identification of novel genes and diverse transcription start sites of messenger RNAs
    • Watanabe J., Sasaki M., Suzuki Y., and Sugano S. Analysis of transcriptomes of human malaria parasite Plasmodium falciparum using full-length enriched library: Identification of novel genes and diverse transcription start sites of messenger RNAs. Gene 291 (2002) 105-113
    • (2002) Gene , vol.291 , pp. 105-113
    • Watanabe, J.1    Sasaki, M.2    Suzuki, Y.3    Sugano, S.4
  • 356
    • 0347125226 scopus 로고    scopus 로고
    • Full-malaria 2004: An enlarged database for comparative studies of full-length cDNAs of malaria parasites, Plasmodium species
    • Watanabe J., Suzuki Y., Sasaki M., and Sugano S. Full-malaria 2004: An enlarged database for comparative studies of full-length cDNAs of malaria parasites, Plasmodium species. Nucleic Acids Res. 32 (2004) D334-D338
    • (2004) Nucleic Acids Res. , vol.32
    • Watanabe, J.1    Suzuki, Y.2    Sasaki, M.3    Sugano, S.4
  • 357
    • 33846090557 scopus 로고    scopus 로고
    • Comparasite: A database for comparative study of transcriptomes of parasites defined by full-length cDNAs
    • Watanabe J., Wakaguri H., Sasaki M., Suzuki Y., and Sugano S. Comparasite: A database for comparative study of transcriptomes of parasites defined by full-length cDNAs. Nucleic Acids Res. 35 (2007) D431-D438
    • (2007) Nucleic Acids Res. , vol.35
    • Watanabe, J.1    Wakaguri, H.2    Sasaki, M.3    Suzuki, Y.4    Sugano, S.5
  • 358
    • 0034660256 scopus 로고    scopus 로고
    • Targeted mutagenesis of Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) disrupts cytoadherence of malaria-infected red blood cells
    • Waterkeyn J.G., Wickham M.E., Davern K.M., Cooke B.M., Coppel R.L., Reeder J.C., Culvenor J.G., Waller R.F., and Cowman A.F. Targeted mutagenesis of Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) disrupts cytoadherence of malaria-infected red blood cells. EMBO J. 19 (2000) 2813-2823
    • (2000) EMBO J. , vol.19 , pp. 2813-2823
    • Waterkeyn, J.G.1    Wickham, M.E.2    Davern, K.M.3    Cooke, B.M.4    Coppel, R.L.5    Reeder, J.C.6    Culvenor, J.G.7    Waller, R.F.8    Cowman, A.F.9
  • 360
    • 0029989433 scopus 로고    scopus 로고
    • DNA replication in the malaria parasite
    • White J.H., and Kilbey B.J. DNA replication in the malaria parasite. Parasitol. Today 12 (1996) 151-155
    • (1996) Parasitol. Today , vol.12 , pp. 151-155
    • White, J.H.1    Kilbey, B.J.2
  • 361
    • 0035886970 scopus 로고    scopus 로고
    • Trafficking and assembly of the cytoadherence complex in Plasmodium falciparum-infected human erythrocytes
    • Wickham M.E., Rug M., Ralph S.A., Klonis N., McFadden G.I., Tilley L., and Cowman A.F. Trafficking and assembly of the cytoadherence complex in Plasmodium falciparum-infected human erythrocytes. EMBO J. 20 (2001) 5636-5649
    • (2001) EMBO J. , vol.20 , pp. 5636-5649
    • Wickham, M.E.1    Rug, M.2    Ralph, S.A.3    Klonis, N.4    McFadden, G.I.5    Tilley, L.6    Cowman, A.F.7
  • 362
    • 0141509925 scopus 로고    scopus 로고
    • Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte
    • Wickham M.E., Culvenor J.G., and Cowman A.F. Selective inhibition of a two-step egress of malaria parasites from the host erythrocyte. J. Biol. Chem. 278 (2003) 37658-37663
    • (2003) J. Biol. Chem. , vol.278 , pp. 37658-37663
    • Wickham, M.E.1    Culvenor, J.G.2    Cowman, A.F.3
  • 363
    • 0033049507 scopus 로고    scopus 로고
    • Release of merozoites from Plasmodium falciparum-infected erythrocytes could be mediated by a non-explosive event
    • Winograd E., Clavijo C.A., Bustamante L.Y., and Jaramillo M. Release of merozoites from Plasmodium falciparum-infected erythrocytes could be mediated by a non-explosive event. Parasitol. Res. 85 (1999) 621-624
    • (1999) Parasitol. Res. , vol.85 , pp. 621-624
    • Winograd, E.1    Clavijo, C.A.2    Bustamante, L.Y.3    Jaramillo, M.4
  • 367
    • 0030035041 scopus 로고    scopus 로고
    • Transformation of Plasmodium falciparum malaria parasites by homologous integration of plasmids that confer resistance to pyrimethamine
    • Wu Y., Kirkman L.A., and Wellems T.E. Transformation of Plasmodium falciparum malaria parasites by homologous integration of plasmids that confer resistance to pyrimethamine. Proc. Natl. Acad. Sci. USA 93 (1996) 1130-1134
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 1130-1134
    • Wu, Y.1    Kirkman, L.A.2    Wellems, T.E.3
  • 368
    • 0242669367 scopus 로고    scopus 로고
    • Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite
    • Wu Y., Wang X., Liu X., and Wang Y. Data-mining approaches reveal hidden families of proteases in the genome of malaria parasite. Genome Res. 13 (2003) 601-616
    • (2003) Genome Res. , vol.13 , pp. 601-616
    • Wu, Y.1    Wang, X.2    Liu, X.3    Wang, Y.4
  • 370
    • 33748655172 scopus 로고    scopus 로고
    • Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai
    • Yeromin A.V., Zhang S.L., Jiang W., Yu Y., Safrina O., and Cahalan M.D. Molecular identification of the CRAC channel by altered ion selectivity in a mutant of Orai. Nature 443 (2006) 226-229
    • (2006) Nature , vol.443 , pp. 226-229
    • Yeromin, A.V.1    Zhang, S.L.2    Jiang, W.3    Yu, Y.4    Safrina, O.5    Cahalan, M.D.6
  • 372
    • 18044382523 scopus 로고    scopus 로고
    • Transcriptional response of Saccharomyces cerevisiae to the plasma membrane-perturbing compound chitosan
    • Zakrzewska A., Boorsma A., Brul S., Hellingwerf K.J., and Klis F.M. Transcriptional response of Saccharomyces cerevisiae to the plasma membrane-perturbing compound chitosan. Eukaryot. Cell 4 (2005) 703-715
    • (2005) Eukaryot. Cell , vol.4 , pp. 703-715
    • Zakrzewska, A.1    Boorsma, A.2    Brul, S.3    Hellingwerf, K.J.4    Klis, F.M.5
  • 374
    • 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., Kappes B., and Franklin R.M. 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    Kappes, B.2    Franklin, R.M.3
  • 375
    • 0028121976 scopus 로고
    • Plasmodium falciparum calcium-dependent protein kinase phosphorylates proteins of the host erythrocytic membrane
    • Zhao Y., Franklin R.M., and 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
  • 376
    • 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., and 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
  • 377
    • 26644473883 scopus 로고    scopus 로고
    • The opportunistic pathogen Toxoplasma gondii deploys a diverse legion of invasion and survival proteins
    • Zhou X.W., Kafsack B.F., Cole R.N., Beckett P., Shen R.F., and Carruthers V.B. The opportunistic pathogen Toxoplasma gondii deploys a diverse legion of invasion and survival proteins. J. Biol. Chem. 280 (2005) 34233-34244
    • (2005) J. Biol. Chem. , vol.280 , pp. 34233-34244
    • Zhou, X.W.1    Kafsack, B.F.2    Cole, R.N.3    Beckett, P.4    Shen, R.F.5    Carruthers, V.B.6
  • 378
    • 16344366882 scopus 로고    scopus 로고
    • In silico gene function prediction using ontology-based pattern identification
    • Zhou Y., Young J.A., Santrosyan A., Chen K., Yan S.F., and Winzeler E.A. In silico gene function prediction using ontology-based pattern identification. Bioinformatics 21 (2005) 1237-1245
    • (2005) Bioinformatics , vol.21 , pp. 1237-1245
    • Zhou, Y.1    Young, J.A.2    Santrosyan, A.3    Chen, K.4    Yan, S.F.5    Winzeler, E.A.6


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