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Volumn 302, Issue 4-5, 2012, Pages 195-202

Does protein phosphorylation govern host cell entry and egress by the Apicomplexa?

Author keywords

Apicomplexa; Gliding motility; Invasion; Kinase; Phosphorylation; Signaling

Indexed keywords

ACTIN; CALCIUM DEPENDANT PROTEIN KINASE 1; CALCIUM DEPENDENT PROTEIN KINASE 1; CALMODULIN; CYCLIC AMP DEPENDENT PROTEIN KINASE; CYCLIC GMP DEPENDENT PROTEIN KINASE; MYOSIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN LIGHT CHAIN; PROTEIN KINASE; PROTEOME; UNCLASSIFIED DRUG;

EID: 84866604909     PISSN: 14384221     EISSN: 16180607     Source Type: Journal    
DOI: 10.1016/j.ijmm.2012.07.012     Document Type: Short Survey
Times cited : (18)

References (97)
  • 1
    • 10844221661 scopus 로고    scopus 로고
    • A genomic perspective of protein kinases in Plasmodium falciparum
    • Anamika, Srinivasan N., Krupa A. A genomic perspective of protein kinases in Plasmodium falciparum. Proteins 2005, 58:180-189.
    • (2005) Proteins , vol.58 , pp. 180-189
    • Anamika, S.N.1    Krupa, A.2
  • 2
    • 84857530326 scopus 로고    scopus 로고
    • Spatial localisation of actin filaments across developmental stages of the malaria parasite
    • Angrisano F., Riglar D.T., Sturm A., Volz J.C., Delves M.J., et al. Spatial localisation of actin filaments across developmental stages of the malaria parasite. PLoS One 2012, 7:e32188.
    • (2012) PLoS One , vol.7
    • Angrisano, F.1    Riglar, D.T.2    Sturm, A.3    Volz, J.C.4    Delves, M.J.5
  • 4
    • 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., et al. A conserved molecular motor drives cell invasion and gliding motility across malaria life cycle stages and other apicomplexan parasites. J. Biol. Chem. 2006, 281:5197-5208.
    • (2006) J. Biol. Chem. , vol.281 , pp. 5197-5208
    • Baum, J.1    Richard, D.2    Healer, J.3    Rug, M.4    Krnajski, Z.5
  • 5
    • 40149100618 scopus 로고    scopus 로고
    • A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion
    • Baum J., Tonkin C.J., Paul A.S., Rug M., Smith B.J., et al. A malaria parasite formin regulates actin polymerization and localizes to the parasite-erythrocyte moving junction during invasion. Cell Host Microbe 2008, 3:188-198.
    • (2008) Cell Host Microbe , vol.3 , pp. 188-198
    • Baum, J.1    Tonkin, C.J.2    Paul, A.S.3    Rug, M.4    Smith, B.J.5
  • 6
    • 0037242399 scopus 로고    scopus 로고
    • Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites
    • Bergman L.W., Kaiser K., Fujioka H., Coppens I., Daly T.M., et al. Myosin A tail domain interacting protein (MTIP) localizes to the inner membrane complex of Plasmodium sporozoites. J. Cell Sci. 2003, 116:39-49.
    • (2003) J. Cell Sci. , vol.116 , pp. 39-49
    • Bergman, L.W.1    Kaiser, K.2    Fujioka, H.3    Coppens, I.4    Daly, T.M.5
  • 7
    • 79955948463 scopus 로고    scopus 로고
    • The moving junction of apicomplexan parasites: a key structure for invasion
    • Besteiro S., Dubremetz J.F., Lebrun M. The moving junction of apicomplexan parasites: a key structure for invasion. Cell. Microbiol. 2011, 13:797-805.
    • (2011) Cell. Microbiol. , vol.13 , pp. 797-805
    • Besteiro, S.1    Dubremetz, J.F.2    Lebrun, M.3
  • 8
    • 67649399023 scopus 로고    scopus 로고
    • Calcium-dependent signaling and kinases in apicomplexan parasites
    • Billker O., Lourido S., Sibley L.D. Calcium-dependent signaling and kinases in apicomplexan parasites. Cell Host Microbe 2009, 5:612-622.
    • (2009) Cell Host Microbe , vol.5 , pp. 612-622
    • Billker, O.1    Lourido, S.2    Sibley, L.D.3
  • 9
    • 51449114441 scopus 로고    scopus 로고
    • Malarial proteases and host cell egress: an 'emerging' cascade
    • Blackman M.J. Malarial proteases and host cell egress: an 'emerging' cascade. Cell. Microbiol. 2008, 10:1925-1934.
    • (2008) Cell. Microbiol. , vol.10 , pp. 1925-1934
    • Blackman, M.J.1
  • 11
    • 77954078996 scopus 로고    scopus 로고
    • Rhomboid 4 (ROM4) affects the processing of surface adhesins and facilitates host cell invasion by Toxoplasma gondii
    • Buguliskis J.S., Brossier F., Shuman J., Sibley L.D. Rhomboid 4 (ROM4) affects the processing of surface adhesins and facilitates host cell invasion by Toxoplasma gondii. PLoS Pathog. 2010, 6:e1000858.
    • (2010) PLoS Pathog. , vol.6
    • Buguliskis, J.S.1    Brossier, F.2    Shuman, J.3    Sibley, L.D.4
  • 12
    • 0033224351 scopus 로고    scopus 로고
    • Secretion of micronemal proteins is associated with toxoplasma invasion of host cells
    • Carruthers V.B., Giddings O.K., Sibley L.D. Secretion of micronemal proteins is associated with toxoplasma invasion of host cells. Cell. Microbiol. 1999, 1:225-235.
    • (1999) Cell. Microbiol. , vol.1 , pp. 225-235
    • Carruthers, V.B.1    Giddings, O.K.2    Sibley, L.D.3
  • 13
    • 0032927424 scopus 로고    scopus 로고
    • Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii
    • Carruthers V.B., Sibley L.D. Mobilization of intracellular calcium stimulates microneme discharge in Toxoplasma gondii. Mol. Microbiol. 1999, 31:421-428.
    • (1999) Mol. Microbiol. , vol.31 , pp. 421-428
    • Carruthers, V.B.1    Sibley, L.D.2
  • 14
    • 79952523494 scopus 로고    scopus 로고
    • Aurora B regulates formin mDia3 in achieving metaphase chromosome alignment
    • Cheng L., Zhang J., Ahmad S., Rozier L., Yu H., et al. Aurora B regulates formin mDia3 in achieving metaphase chromosome alignment. Dev. Cell 2011, 20:342-352.
    • (2011) Dev. Cell , vol.20 , pp. 342-352
    • Cheng, L.1    Zhang, J.2    Ahmad, S.3    Rozier, L.4    Yu, H.5
  • 15
    • 0034383949 scopus 로고    scopus 로고
    • The regulation of protein function by multisite phosphorylation - a 25 year update
    • Cohen P. The regulation of protein function by multisite phosphorylation - a 25 year update. Trends Biochem. Sci. 2000, 25:596-601.
    • (2000) Trends Biochem. Sci. , vol.25 , pp. 596-601
    • Cohen, P.1
  • 16
    • 84857702296 scopus 로고    scopus 로고
    • Molecular characterization of Toxoplasma gondii formin 3, an actin nucleator dispensable for tachyzoite growth and motility
    • Daher W., Klages N., Carlier M.F., Soldati-Favre D. Molecular characterization of Toxoplasma gondii formin 3, an actin nucleator dispensable for tachyzoite growth and motility. Eukaryot. Cell 2012, 11:343-352.
    • (2012) Eukaryot. Cell , vol.11 , pp. 343-352
    • Daher, W.1    Klages, N.2    Carlier, M.F.3    Soldati-Favre, D.4
  • 17
    • 78449238637 scopus 로고    scopus 로고
    • Concerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondii
    • Daher W., Plattner F., Carlier M.F., Soldati-Favre D. Concerted action of two formins in gliding motility and host cell invasion by Toxoplasma gondii. PLoS Pathog. 2010, 6:e1001132.
    • (2010) PLoS Pathog. , vol.6
    • Daher, W.1    Plattner, F.2    Carlier, M.F.3    Soldati-Favre, D.4
  • 18
    • 68049137458 scopus 로고    scopus 로고
    • Mechanisms controlling glideosome function in apicomplexans
    • Daher W., Soldati-Favre D. Mechanisms controlling glideosome function in apicomplexans. Curr. Opin. Microbiol. 2009, 12:408-414.
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 408-414
    • Daher, W.1    Soldati-Favre, D.2
  • 19
    • 0030754072 scopus 로고    scopus 로고
    • Actin in the parasite Toxoplasma gondii is encoded by a single copy gene, ACT1 and exists primarily in a globular form
    • Dobrowolski J.M., Niesman I.R., Sibley L.D. Actin in the parasite Toxoplasma gondii is encoded by a single copy gene, ACT1 and exists primarily in a globular form. Cell Motil. Cytoskeleton 1997, 37:253-262.
    • (1997) Cell Motil. Cytoskeleton , vol.37 , pp. 253-262
    • Dobrowolski, J.M.1    Niesman, I.R.2    Sibley, L.D.3
  • 21
    • 0036616356 scopus 로고    scopus 로고
    • Toxoplasma gondii cyclic GMP-dependent kinase: chemotherapeutic targeting of an essential parasite protein kinase
    • Donald R.G., Allocco J., Singh S.B., Nare B., Salowe S.P., et al. Toxoplasma gondii cyclic GMP-dependent kinase: chemotherapeutic targeting of an essential parasite protein kinase. Eukaryot. Cell 2002, 1:317-328.
    • (2002) Eukaryot. Cell , vol.1 , pp. 317-328
    • Donald, R.G.1    Allocco, J.2    Singh, S.B.3    Nare, B.4    Salowe, S.P.5
  • 22
    • 77952378704 scopus 로고    scopus 로고
    • A plant-like kinase in Plasmodium falciparum regulates parasite egress from erythrocytes
    • Dvorin J.D., Martyn D.C., Patel S.D., Grimley J.S., Collins C.R., et al. A plant-like kinase in Plasmodium falciparum regulates parasite egress from erythrocytes. Science 2010, 328:910-912.
    • (2010) Science , vol.328 , pp. 910-912
    • Dvorin, J.D.1    Martyn, D.C.2    Patel, S.D.3    Grimley, J.S.4    Collins, C.R.5
  • 23
    • 0019993146 scopus 로고
    • Toxoplasma gondii: calcium ionophore A23187-mediated exit of trophozoites from infected murine macrophages
    • Endo T., Sethi K.K., Piekarski G. Toxoplasma gondii: calcium ionophore A23187-mediated exit of trophozoites from infected murine macrophages. Exp. Parasitol. 1982, 53:179-188.
    • (1982) Exp. Parasitol. , vol.53 , pp. 179-188
    • Endo, T.1    Sethi, K.K.2    Piekarski, G.3
  • 24
    • 77449109151 scopus 로고    scopus 로고
    • Role of Plasmodium berghei cGMP-dependent protein kinase in late liver stage development
    • Falae A., Combe A., Amaladoss A., Carvalho T., Menard R., et al. Role of Plasmodium berghei cGMP-dependent protein kinase in late liver stage development. J. Biol. Chem. 2010, 285:3282-3288.
    • (2010) J. Biol. Chem. , vol.285 , pp. 3282-3288
    • Falae, A.1    Combe, A.2    Amaladoss, A.3    Carvalho, T.4    Menard, R.5
  • 26
    • 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., et al. Identification of the membrane receptor of a class XIV myosin in Toxoplasma gondii. J. Cell Biol. 2004, 165:383-393.
    • (2004) J. Cell Biol. , vol.165 , pp. 383-393
    • Gaskins, E.1    Gilk, S.2    DeVore, N.3    Mann, T.4    Ward, G.5
  • 27
    • 59249083317 scopus 로고    scopus 로고
    • GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex
    • Gilk S.D., Gaskins E., Ward G.E., Beckers C.J. GAP45 phosphorylation controls assembly of the Toxoplasma myosin XIV complex. Eukaryot. Cell 2009, 8:190-196.
    • (2009) Eukaryot. Cell , vol.8 , pp. 190-196
    • Gilk, S.D.1    Gaskins, E.2    Ward, G.E.3    Beckers, C.J.4
  • 28
    • 57649221595 scopus 로고    scopus 로고
    • The motor complex of Plasmodium falciparum: phosphorylation by a calcium-dependent protein kinase
    • Green J.L., Rees-Channer R.R., Howell S.A., Martin S.R., Knuepfer E., et al. The motor complex of Plasmodium falciparum: phosphorylation by a calcium-dependent protein kinase. J. Biol. Chem. 2008, 283:30980-30989.
    • (2008) J. Biol. Chem. , vol.283 , pp. 30980-30989
    • Green, J.L.1    Rees-Channer, R.R.2    Howell, S.A.3    Martin, S.R.4    Knuepfer, E.5
  • 30
    • 0034440542 scopus 로고    scopus 로고
    • Toxoplasma gondii homologue of plasmodium apical membrane antigen 1 is involved in invasion of host cells
    • Hehl A.B., Lekutis C., Grigg M.E., Bradley P.J., Dubremetz J.F., et al. Toxoplasma gondii homologue of plasmodium apical membrane antigen 1 is involved in invasion of host cells. Infect. Immun. 2000, 68:7078-7086.
    • (2000) Infect. Immun. , vol.68 , pp. 7078-7086
    • Hehl, A.B.1    Lekutis, C.2    Grigg, M.E.3    Bradley, P.J.4    Dubremetz, J.F.5
  • 31
    • 18344362027 scopus 로고    scopus 로고
    • Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor
    • Herm-Gotz A., Weiss S., Stratmann R., Fujita-Becker S., Ruff C., et al. Toxoplasma gondii myosin A and its light chain: a fast, single-headed, plus-end-directed motor. EMBO J. 2002, 21:2149-2158.
    • (2002) EMBO J. , vol.21 , pp. 2149-2158
    • Herm-Gotz, A.1    Weiss, S.2    Stratmann, R.3    Fujita-Becker, S.4    Ruff, C.5
  • 33
    • 84863846071 scopus 로고    scopus 로고
    • The role of cGMP signalling in regulating life cycle progression of Plasmodium
    • 10.1016/j.micinf.2012.04.011 (E-pub ahead of print)
    • Hopp C.S., Bowyer P.W., Baker D.A. The role of cGMP signalling in regulating life cycle progression of Plasmodium. Microbes Infect. 2012, 10.1016/j.micinf.2012.04.011 (E-pub ahead of print).
    • (2012) Microbes Infect.
    • Hopp, C.S.1    Bowyer, P.W.2    Baker, D.A.3
  • 34
    • 0038267453 scopus 로고    scopus 로고
    • A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage
    • Howell S.A., Well I., Fleck S.L., Kettleborough C., Collins C.R., et al. A single malaria merozoite serine protease mediates shedding of multiple surface proteins by juxtamembrane cleavage. J. Biol. Chem. 2003, 278:23890-23898.
    • (2003) J. Biol. Chem. , vol.278 , pp. 23890-23898
    • Howell, S.A.1    Well, I.2    Fleck, S.L.3    Kettleborough, C.4    Collins, C.R.5
  • 35
    • 33748066307 scopus 로고    scopus 로고
    • Toxoplasma MIC2 is a major determinant of invasion and virulence
    • Huynh M.H., Carruthers V.B. Toxoplasma MIC2 is a major determinant of invasion and virulence. PLoS Pathog. 2006, 2:e84.
    • (2006) PLoS Pathog. , vol.2
    • Huynh, M.H.1    Carruthers, V.B.2
  • 36
    • 78650078032 scopus 로고    scopus 로고
    • Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance
    • Iskratsch T., Lange S., Dwyer J., Kho A.L., dos Remedios C., et al. Formin follows function: a muscle-specific isoform of FHOD3 is regulated by CK2 phosphorylation and promotes myofibril maintenance. J. Cell Biol. 2010, 191:1159-1172.
    • (2010) J. Cell Biol. , vol.191 , pp. 1159-1172
    • Iskratsch, T.1    Lange, S.2    Dwyer, J.3    Kho, A.L.4    dos Remedios, C.5
  • 37
    • 0038637915 scopus 로고    scopus 로고
    • Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites
    • Jewett T.J., Sibley L.D. Aldolase forms a bridge between cell surface adhesins and the actin cytoskeleton in apicomplexan parasites. Mol. Cell 2003, 11:885-894.
    • (2003) Mol. Cell , vol.11 , pp. 885-894
    • Jewett, T.J.1    Sibley, L.D.2
  • 38
    • 84863229482 scopus 로고    scopus 로고
    • Development of Toxoplasma gondii calcium-dependent protein kinase 1 (TgCDPK1) inhibitors with potent anti-toxoplasma activity
    • Johnson S.M., Murphy R.C., Geiger J.A., Derocher A.E., Zhang Z., et al. Development of Toxoplasma gondii calcium-dependent protein kinase 1 (TgCDPK1) inhibitors with potent anti-toxoplasma activity. J. Med. Chem. 2012, 55:2416-2426.
    • (2012) J. Med. Chem. , vol.55 , pp. 2416-2426
    • Johnson, S.M.1    Murphy, R.C.2    Geiger, J.A.3    Derocher, A.E.4    Zhang, Z.5
  • 39
    • 68749112446 scopus 로고    scopus 로고
    • Effects of calcium signaling on Plasmodium falciparum erythrocyte invasion and post-translational modification of gliding-associated protein 45 (PfGAP45)
    • Jones M.L., Cottingham C., Rayner J.C. Effects of calcium signaling on Plasmodium falciparum erythrocyte invasion and post-translational modification of gliding-associated protein 45 (PfGAP45). Mol. Biochem. Parasitol. 2009, 168:55-62.
    • (2009) Mol. Biochem. Parasitol. , vol.168 , pp. 55-62
    • Jones, M.L.1    Cottingham, C.2    Rayner, J.C.3
  • 40
    • 43749109597 scopus 로고    scopus 로고
    • Gene expression signatures and small-molecule compounds link a protein kinase to Plasmodium falciparum motility
    • Kato N., Sakata T., Breton G., Le Roch K.G., Nagle A., et al. Gene expression signatures and small-molecule compounds link a protein kinase to Plasmodium falciparum motility. Nat. Chem. Biol. 2008, 4:347-356.
    • (2008) Nat. Chem. Biol. , vol.4 , pp. 347-356
    • Kato, N.1    Sakata, T.2    Breton, G.3    Le Roch, K.G.4    Nagle, A.5
  • 41
    • 43149091439 scopus 로고    scopus 로고
    • Microneme protein 8 - a new essential invasion factor in Toxoplasma gondii
    • Kessler H., Herm-Gotz A., Hegge S., Rauch M., Soldati-Favre D., et al. Microneme protein 8 - a new essential invasion factor in Toxoplasma gondii. J. Cell Sci. 2008, 121:947-956.
    • (2008) J. Cell Sci. , vol.121 , pp. 947-956
    • Kessler, H.1    Herm-Gotz, A.2    Hegge, S.3    Rauch, M.4    Soldati-Favre, D.5
  • 42
    • 0035853753 scopus 로고    scopus 로고
    • Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase
    • Kieschnick H., Wakefield T., Narducci C.A., Beckers C. Toxoplasma gondii attachment to host cells is regulated by a calmodulin-like domain protein kinase. J. Biol. Chem. 2001, 276:12369-12377.
    • (2001) J. Biol. Chem. , vol.276 , pp. 12369-12377
    • Kieschnick, H.1    Wakefield, T.2    Narducci, C.A.3    Beckers, C.4
  • 43
    • 2642554720 scopus 로고    scopus 로고
    • PfPKB, a novel protein kinase B-like enzyme from Plasmodium falciparum. I. Identification, characterization, and possible role in parasite development
    • Kumar A., Vaid A., Syin C., Sharma P. PfPKB, a novel protein kinase B-like enzyme from Plasmodium falciparum. I. Identification, characterization, and possible role in parasite development. J. Biol. Chem. 2004, 279:24255-24264.
    • (2004) J. Biol. Chem. , vol.279 , pp. 24255-24264
    • Kumar, A.1    Vaid, A.2    Syin, C.3    Sharma, P.4
  • 44
    • 79960601918 scopus 로고    scopus 로고
    • Identification of Toxoplasma gondii cAMP dependent protein kinase and its role in the tachyzoite growth
    • Kurokawa H., Kato K., Iwanaga T., Sugi T., Sudo A., et al. Identification of Toxoplasma gondii cAMP dependent protein kinase and its role in the tachyzoite growth. PLoS One 2011, 6:e22492.
    • (2011) PLoS One , vol.6
    • Kurokawa, H.1    Kato, K.2    Iwanaga, T.3    Sugi, T.4    Sudo, A.5
  • 45
    • 79952231758 scopus 로고    scopus 로고
    • The RON2-AMA1 interaction is a critical step in moving junction-dependent invasion by apicomplexan parasites
    • Lamarque M., Besteiro S., Papoin J., Roques M., Vulliez-Le Normand B., et al. The RON2-AMA1 interaction is a critical step in moving junction-dependent invasion by apicomplexan parasites. PLoS Pathog. 2011, 7:e1001276.
    • (2011) PLoS Pathog. , vol.7
    • Lamarque, M.1    Besteiro, S.2    Papoin, J.3    Roques, M.4    Vulliez-Le Normand, B.5
  • 46
    • 84863855283 scopus 로고    scopus 로고
    • Insights into the P. falciparum schizont phospho-proteome
    • 10.1016/j.micinf.2012.04.008 (E-pub ahead of print)
    • Lasonder E., Treeck M., Alam M., Tobin A.B. Insights into the P. falciparum schizont phospho-proteome. Microbes Infect. 2012, 10.1016/j.micinf.2012.04.008 (E-pub ahead of print).
    • (2012) Microbes Infect.
    • Lasonder, E.1    Treeck, M.2    Alam, M.3    Tobin, A.B.4
  • 47
    • 77954665296 scopus 로고    scopus 로고
    • Protein kinase a dependent phosphorylation of apical membrane antigen 1 plays an important role in erythrocyte invasion by the malaria parasite
    • Leykauf K., Treeck M., Gilson P.R., Nebl T., Braulke T., et al. Protein kinase a dependent phosphorylation of apical membrane antigen 1 plays an important role in erythrocyte invasion by the malaria parasite. PLoS Pathog. 2010, 6:e1000941.
    • (2010) PLoS Pathog. , vol.6
    • Leykauf, K.1    Treeck, M.2    Gilson, P.R.3    Nebl, T.4    Braulke, T.5
  • 48
    • 84855190521 scopus 로고    scopus 로고
    • Toxoplasma and Plasmodium protein kinases: roles in invasion and host cell remodelling
    • Lim D.C., Cooke B.M., Doerig C., Saeij J.P. Toxoplasma and Plasmodium protein kinases: roles in invasion and host cell remodelling. Int. J. Parasitol. 2012, 42:21-32.
    • (2012) Int. J. Parasitol. , vol.42 , pp. 21-32
    • Lim, D.C.1    Cooke, B.M.2    Doerig, C.3    Saeij, J.P.4
  • 49
    • 77952723730 scopus 로고    scopus 로고
    • Calcium-dependent protein kinase 1 is an essential regulator of exocytosis in Toxoplasma
    • Lourido S., Shuman J., Zhang C., Shokat K.M., Hui R., et al. Calcium-dependent protein kinase 1 is an essential regulator of exocytosis in Toxoplasma. Nature 2010, 465:359-362.
    • (2010) Nature , vol.465 , pp. 359-362
    • Lourido, S.1    Shuman, J.2    Zhang, C.3    Shokat, K.M.4    Hui, R.5
  • 50
    • 0041402826 scopus 로고    scopus 로고
    • Intracellular calcium stores in Toxoplasma gondii govern invasion of host cells
    • Lovett J.L., Sibley L.D. Intracellular calcium stores in Toxoplasma gondii govern invasion of host cells. J. Cell Sci. 2003, 116:3009-3016.
    • (2003) J. Cell Sci. , vol.116 , pp. 3009-3016
    • Lovett, J.L.1    Sibley, L.D.2
  • 51
    • 45149123080 scopus 로고    scopus 로고
    • Gametogenesis in malaria parasites is mediated by the cGMP-dependent protein kinase
    • McRobert L., Taylor C.J., Deng W., Fivelman Q.L., Cummings R.M., et al. Gametogenesis in malaria parasites is mediated by the cGMP-dependent protein kinase. PLoS Biol. 2008, 6:e139.
    • (2008) PLoS Biol. , vol.6
    • McRobert, L.1    Taylor, C.J.2    Deng, W.3    Fivelman, Q.L.4    Cummings, R.M.5
  • 52
    • 79954584860 scopus 로고    scopus 로고
    • Actin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondii
    • Mehta S., Sibley L.D. Actin depolymerizing factor controls actin turnover and gliding motility in Toxoplasma gondii. Mol. Biol. Cell 2011, 22:1290-1299.
    • (2011) Mol. Biol. Cell , vol.22 , pp. 1290-1299
    • Mehta, S.1    Sibley, L.D.2
  • 53
    • 0037174664 scopus 로고    scopus 로고
    • Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion
    • Meissner M., Schluter D., Soldati D. Role of Toxoplasma gondii myosin A in powering parasite gliding and host cell invasion. Science 2002, 298:837-840.
    • (2002) Science , vol.298 , pp. 837-840
    • Meissner, M.1    Schluter, D.2    Soldati, D.3
  • 54
    • 24344439282 scopus 로고    scopus 로고
    • Conditional expression of Toxoplasma gondii apical membrane antigen-1 (TgAMA1) demonstrates that TgAMA1 plays a critical role in host cell invasion
    • Mital J., Meissner M., Soldati D., Ward G.E. Conditional expression of Toxoplasma gondii apical membrane antigen-1 (TgAMA1) demonstrates that TgAMA1 plays a critical role in host cell invasion. Mol. Biol. Cell 2005, 16:4341-4349.
    • (2005) Mol. Biol. Cell , vol.16 , pp. 4341-4349
    • Mital, J.1    Meissner, M.2    Soldati, D.3    Ward, G.E.4
  • 56
    • 70349666538 scopus 로고    scopus 로고
    • A cyclic GMP signalling module that regulates gliding motility in a malaria parasite
    • Moon R.W., Taylor C.J., Bex C., Schepers R., Goulding D., et al. A cyclic GMP signalling module that regulates gliding motility in a malaria parasite. PLoS Pathog. 2009, 5:e1000599.
    • (2009) PLoS Pathog. , vol.5
    • Moon, R.W.1    Taylor, C.J.2    Bex, C.3    Schepers, R.4    Goulding, D.5
  • 57
    • 0042195182 scopus 로고    scopus 로고
    • Calcium regulation in protozoan parasites
    • Moreno S.N., Docampo R. Calcium regulation in protozoan parasites. Curr. Opin. Microbiol. 2003, 6:359-364.
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 359-364
    • Moreno, S.N.1    Docampo, R.2
  • 58
    • 70350451571 scopus 로고    scopus 로고
    • Progress towards understanding the immunobiology of Theileria parasites
    • Morrison W.I. Progress towards understanding the immunobiology of Theileria parasites. Parasitology 2009, 136:1415-1426.
    • (2009) Parasitology , vol.136 , pp. 1415-1426
    • Morrison, W.I.1
  • 59
    • 0031018273 scopus 로고    scopus 로고
    • Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii
    • Morrissette N.S., Murray J.M., Roos D.S. Subpellicular microtubules associate with an intramembranous particle lattice in the protozoan parasite Toxoplasma gondii. J. Cell Sci. 1997, 110:35-42.
    • (1997) J. Cell Sci. , vol.110 , pp. 35-42
    • Morrissette, N.S.1    Murray, J.M.2    Roos, D.S.3
  • 60
    • 84856679687 scopus 로고    scopus 로고
    • Global malaria mortality between 1980 and 2010: a systematic analysis
    • Murray C.J., Rosenfeld L.C., Lim S.S., Andrews K.G., Foreman K.J., et al. Global malaria mortality between 1980 and 2010: a systematic analysis. Lancet 2012, 379:413-431.
    • (2012) Lancet , vol.379 , pp. 413-431
    • Murray, C.J.1    Rosenfeld, L.C.2    Lim, S.S.3    Andrews, K.G.4    Foreman, K.J.5
  • 61
    • 80053458415 scopus 로고    scopus 로고
    • Quantitative in vivo analyses reveal calcium-dependent phosphorylation sites and identifies a novel component of the Toxoplasma invasion motor complex
    • Nebl T., Prieto J.H., Kapp E., Smith B.J., Williams M.J., et al. Quantitative in vivo analyses reveal calcium-dependent phosphorylation sites and identifies a novel component of the Toxoplasma invasion motor complex. PLoS Pathog. 2011, 7:e1002222.
    • (2011) PLoS Pathog. , vol.7
    • Nebl, T.1    Prieto, J.H.2    Kapp, E.3    Smith, B.J.4    Williams, M.J.5
  • 62
    • 77951969562 scopus 로고    scopus 로고
    • Toxoplasma gondii calcium-dependent protein kinase 1 is a target for selective kinase inhibitors
    • Ojo K.K., Larson E.T., Keyloun K.R., Castaneda L.J., Derocher A.E., et al. Toxoplasma gondii calcium-dependent protein kinase 1 is a target for selective kinase inhibitors. Nat. Struct. Mol. Biol. 2010, 17:602-607.
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 602-607
    • Ojo, K.K.1    Larson, E.T.2    Keyloun, K.R.3    Castaneda, L.J.4    Derocher, A.E.5
  • 63
    • 84855282762 scopus 로고    scopus 로고
    • Juxtamembrane shedding of Plasmodium falciparum AMA1 is sequence independent and essential, and helps evade invasion-inhibitory antibodies
    • Olivieri A., Collins C.R., Hackett F., Withers-Martinez C., Marshall J., et al. Juxtamembrane shedding of Plasmodium falciparum AMA1 is sequence independent and essential, and helps evade invasion-inhibitory antibodies. PLoS Pathog. 2011, 7:e1002448.
    • (2011) PLoS Pathog. , vol.7
    • Olivieri, A.1    Collins, C.R.2    Hackett, F.3    Withers-Martinez, C.4    Marshall, J.5
  • 64
    • 20444383859 scopus 로고    scopus 로고
    • Protein phosphorylation in signaling - 50 years and counting
    • Pawson T., Scott J.D. Protein phosphorylation in signaling - 50 years and counting. Trends Biochem. Sci. 2005, 30:286-290.
    • (2005) Trends Biochem. Sci. , vol.30 , pp. 286-290
    • Pawson, T.1    Scott, J.D.2
  • 65
    • 77956332686 scopus 로고    scopus 로고
    • Integrative genomic approaches highlight a family of parasite-specific kinases that regulate host responses
    • Peixoto L., Chen F., Harb O.S., Davis P.H., Beiting D.P., et al. Integrative genomic approaches highlight a family of parasite-specific kinases that regulate host responses. Cell Host Microbe 2010, 8:208-218.
    • (2010) Cell Host Microbe , vol.8 , pp. 208-218
    • Peixoto, L.1    Chen, F.2    Harb, O.S.3    Davis, P.H.4    Beiting, D.P.5
  • 66
    • 79957580467 scopus 로고    scopus 로고
    • Drug-resistant malaria: molecular mechanisms and implications for public health
    • Petersen I., Eastman R., Lanzer M. Drug-resistant malaria: molecular mechanisms and implications for public health. FEBS Lett. 2011, 585:1551-1562.
    • (2011) FEBS Lett. , vol.585 , pp. 1551-1562
    • Petersen, I.1    Eastman, R.2    Lanzer, M.3
  • 67
    • 38849095132 scopus 로고    scopus 로고
    • Toxoplasma profilin is essential for host cell invasion and TLR11-dependent induction of an interleukin-12 response
    • Plattner F., Yarovinsky F., Romero S., Didry D., Carlier M.F., et al. Toxoplasma profilin is essential for host cell invasion and TLR11-dependent induction of an interleukin-12 response. Cell Host Microbe 2008, 3:77-87.
    • (2008) Cell Host Microbe , vol.3 , pp. 77-87
    • Plattner, F.1    Yarovinsky, F.2    Romero, S.3    Didry, D.4    Carlier, M.F.5
  • 68
    • 84859152006 scopus 로고    scopus 로고
    • Subcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont development
    • Ridzuan M.A., Moon R.W., Knuepfer E., Black S., Holder A.A., et al. Subcellular location, phosphorylation and assembly into the motor complex of GAP45 during Plasmodium falciparum schizont development. PLoS One 2012, 7:e33845.
    • (2012) PLoS One , vol.7
    • Ridzuan, M.A.1    Moon, R.W.2    Knuepfer, E.3    Black, S.4    Holder, A.A.5
  • 69
    • 79251602713 scopus 로고    scopus 로고
    • Intramembrane cleavage of AMA1 triggers Toxoplasma to switch from an invasive to a replicative mode
    • Santos J.M., Ferguson D.J., Blackman M.J., Soldati-Favre D. Intramembrane cleavage of AMA1 triggers Toxoplasma to switch from an invasive to a replicative mode. Science 2011, 331:473-477.
    • (2011) Science , vol.331 , pp. 473-477
    • Santos, J.M.1    Ferguson, D.J.2    Blackman, M.J.3    Soldati-Favre, D.4
  • 70
    • 77649273530 scopus 로고    scopus 로고
    • Fifteen formins for an actin filament: a molecular view on the regulation of human formins
    • Schonichen A., Geyer M. Fifteen formins for an actin filament: a molecular view on the regulation of human formins. Biochim. Biophys. Acta 2010, 1803:152-163.
    • (2010) Biochim. Biophys. Acta , vol.1803 , pp. 152-163
    • Schonichen, A.1    Geyer, M.2
  • 71
    • 79958708392 scopus 로고    scopus 로고
    • The significance of regulatory light chain phosphorylation in cardiac physiology
    • Scruggs S.B., Solaro R.J. The significance of regulatory light chain phosphorylation in cardiac physiology. Arch. Biochem. Biophys. 2011, 510:129-134.
    • (2011) Arch. Biochem. Biophys. , vol.510 , pp. 129-134
    • Scruggs, S.B.1    Solaro, R.J.2
  • 72
    • 34447097337 scopus 로고    scopus 로고
    • Challenges in the successful control of the avian coccidia
    • Shirley M.W., Smith A.L., Blake D.P. Challenges in the successful control of the avian coccidia. Vaccine 2007, 25:5540-5547.
    • (2007) Vaccine , vol.25 , pp. 5540-5547
    • Shirley, M.W.1    Smith, A.L.2    Blake, D.P.3
  • 73
    • 77649263117 scopus 로고    scopus 로고
    • Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites
    • Singh S., Alam M.M., Pal-Bhowmick I., Brzostowski J.A., Chitnis C.E. Distinct external signals trigger sequential release of apical organelles during erythrocyte invasion by malaria parasites. PLoS Pathog. 2010, 6:e1000746.
    • (2010) PLoS Pathog. , vol.6
    • Singh, S.1    Alam, M.M.2    Pal-Bhowmick, I.3    Brzostowski, J.A.4    Chitnis, C.E.5
  • 74
    • 84859203124 scopus 로고    scopus 로고
    • Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro
    • Skillman K.M., Daher W., Ma C.I., Soldati-Favre D., Sibley L.D. Toxoplasma gondii profilin acts primarily to sequester G-actin while formins efficiently nucleate actin filament formation in vitro. Biochemistry 2012, 51:2486-2495.
    • (2012) Biochemistry , vol.51 , pp. 2486-2495
    • Skillman, K.M.1    Daher, W.2    Ma, C.I.3    Soldati-Favre, D.4    Sibley, L.D.5
  • 75
    • 82555196646 scopus 로고    scopus 로고
    • Global kinomic and phospho-proteomic analyses of the human malaria parasite Plasmodium falciparum
    • Solyakov L., Halbert J., Alam M.M., Semblat J.P., Dorin-Semblat D., et al. Global kinomic and phospho-proteomic analyses of the human malaria parasite Plasmodium falciparum. Nat. Commun. 2011, 2:565.
    • (2011) Nat. Commun. , vol.2 , pp. 565
    • Solyakov, L.1    Halbert, J.2    Alam, M.M.3    Semblat, J.P.4    Dorin-Semblat, D.5
  • 76
    • 33750077590 scopus 로고    scopus 로고
    • Two separate, conserved acidic amino acid domains within the Toxoplasma gondii MIC2 cytoplasmic tail are required for parasite survival
    • Starnes G.L., Jewett T.J., Carruthers V.B., Sibley L.D. Two separate, conserved acidic amino acid domains within the Toxoplasma gondii MIC2 cytoplasmic tail are required for parasite survival. J. Biol. Chem. 2006, 281:30745-30754.
    • (2006) J. Biol. Chem. , vol.281 , pp. 30745-30754
    • Starnes, G.L.1    Jewett, T.J.2    Carruthers, V.B.3    Sibley, L.D.4
  • 77
    • 79958748938 scopus 로고    scopus 로고
    • Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle
    • Stull J.T., Kamm K.E., Vandenboom R. Myosin light chain kinase and the role of myosin light chain phosphorylation in skeletal muscle. Arch. Biochem. Biophys. 2011, 510:120-128.
    • (2011) Arch. Biochem. Biophys. , vol.510 , pp. 120-128
    • Stull, J.T.1    Kamm, K.E.2    Vandenboom, R.3
  • 78
    • 70349744261 scopus 로고    scopus 로고
    • Molecular analyses of Toxoplasma gondii calmodulin-like domain protein kinase isoform 3
    • Sugi T., Kato K., Kobayashi K., Pandey K., Takemae H., et al. Molecular analyses of Toxoplasma gondii calmodulin-like domain protein kinase isoform 3. Parasitol. Int. 2009, 58:416-423.
    • (2009) Parasitol. Int. , vol.58 , pp. 416-423
    • Sugi, T.1    Kato, K.2    Kobayashi, K.3    Pandey, K.4    Takemae, H.5
  • 79
    • 77950524822 scopus 로고    scopus 로고
    • Use of the kinase inhibitor analog 1NM-PP1 reveals a role for Toxoplasma gondii CDPK1 in the invasion step
    • Sugi T., Kato K., Kobayashi K., Watanabe S., Kurokawa H., et al. Use of the kinase inhibitor analog 1NM-PP1 reveals a role for Toxoplasma gondii CDPK1 in the invasion step. Eukaryot. Cell 2010, 9:667-670.
    • (2010) Eukaryot. Cell , vol.9 , pp. 667-670
    • Sugi, T.1    Kato, K.2    Kobayashi, K.3    Watanabe, S.4    Kurokawa, H.5
  • 80
    • 75649116460 scopus 로고    scopus 로고
    • The malaria parasite cyclic GMP-dependent protein kinase plays a central role in blood-stage schizogony
    • Taylor H.M., McRobert L., Grainger M., Sicard A., Dluzewski A.R., et al. The malaria parasite cyclic GMP-dependent protein kinase plays a central role in blood-stage schizogony. Eukaryot. Cell 2010, 9:37-45.
    • (2010) Eukaryot. Cell , vol.9 , pp. 37-45
    • Taylor, H.M.1    McRobert, L.2    Grainger, M.3    Sicard, A.4    Dluzewski, A.R.5
  • 81
    • 77958094517 scopus 로고    scopus 로고
    • The systematic functional analysis of Plasmodium protein kinases identifies essential regulators of mosquito transmission
    • Tewari R., Straschil U., Bateman A., Bohme U., Cherevach I., et al. The systematic functional analysis of Plasmodium protein kinases identifies essential regulators of mosquito transmission. Cell Host Microbe 2010, 8:377-387.
    • (2010) Cell Host Microbe , vol.8 , pp. 377-387
    • Tewari, R.1    Straschil, U.2    Bateman, A.3    Bohme, U.4    Cherevach, I.5
  • 82
    • 84860486844 scopus 로고    scopus 로고
    • Regulation of Plasmodium falciparum glideosome associated protein 45 (PfGAP45) phosphorylation
    • Thomas D.C., Ahmed A., Gilberger T.W., Sharma P. Regulation of Plasmodium falciparum glideosome associated protein 45 (PfGAP45) phosphorylation. PLoS One 2012, 7:e35855.
    • (2012) PLoS One , vol.7
    • Thomas, D.C.1    Ahmed, A.2    Gilberger, T.W.3    Sharma, P.4
  • 83
    • 79960668340 scopus 로고    scopus 로고
    • Host cell invasion by apicomplexan parasites: insights from the co-structure of AMA1 with a RON2 peptide
    • Tonkin M.L., Roques M., Lamarque M.H., Pugniere M., Douguet D., et al. Host cell invasion by apicomplexan parasites: insights from the co-structure of AMA1 with a RON2 peptide. Science 2011, 333:463-467.
    • (2011) Science , vol.333 , pp. 463-467
    • Tonkin, M.L.1    Roques, M.2    Lamarque, M.H.3    Pugniere, M.4    Douguet, D.5
  • 84
    • 80054901700 scopus 로고    scopus 로고
    • The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries
    • Treeck M., Sanders J.L., Elias J.E., Boothroyd J.C. The phosphoproteomes of Plasmodium falciparum and Toxoplasma gondii reveal unusual adaptations within and beyond the parasites' boundaries. Cell Host Microbe 2011, 10:410-419.
    • (2011) Cell Host Microbe , vol.10 , pp. 410-419
    • Treeck, M.1    Sanders, J.L.2    Elias, J.E.3    Boothroyd, J.C.4
  • 85
    • 63449122293 scopus 로고    scopus 로고
    • Functional analysis of the leading malaria vaccine candidate AMA-1 reveals an essential role for the cytoplasmic domain in the invasion process
    • Treeck M., Zacherl S., Herrmann S., Cabrera A., Kono M., et al. Functional analysis of the leading malaria vaccine candidate AMA-1 reveals an essential role for the cytoplasmic domain in the invasion process. PLoS Pathog. 2009, 5:e1000322.
    • (2009) PLoS Pathog. , vol.5
    • Treeck, M.1    Zacherl, S.2    Herrmann, S.3    Cabrera, A.4    Kono, M.5
  • 86
    • 0033636201 scopus 로고    scopus 로고
    • Apical membrane antigen 1 plays a central role in erythrocyte invasion by Plasmodium species
    • Triglia T., Healer J., Caruana S.R., Hodder A.N., Anders R.F., et al. Apical membrane antigen 1 plays a central role in erythrocyte invasion by Plasmodium species. Mol. Microbiol. 2000, 38:706-718.
    • (2000) Mol. Microbiol. , vol.38 , pp. 706-718
    • Triglia, T.1    Healer, J.2    Caruana, S.R.3    Hodder, A.N.4    Anders, R.F.5
  • 87
    • 80051787685 scopus 로고    scopus 로고
    • Focus on the ringleader: the role of AMA1 in apicomplexan invasion and replication
    • Tyler J.S., Treeck M., Boothroyd J.C. Focus on the ringleader: the role of AMA1 in apicomplexan invasion and replication. Trends Parasitol. 2011, 27:410-420.
    • (2011) Trends Parasitol. , vol.27 , pp. 410-420
    • Tyler, J.S.1    Treeck, M.2    Boothroyd, J.C.3
  • 88
    • 34250878954 scopus 로고    scopus 로고
    • Mechanisms of specificity in protein phosphorylation
    • Ubersax J.A., Ferrell J.E. Mechanisms of specificity in protein phosphorylation. Nat. Rev. Mol. Cell Biol. 2007, 8:530-541.
    • (2007) Nat. Rev. Mol. Cell Biol. , vol.8 , pp. 530-541
    • Ubersax, J.A.1    Ferrell, J.E.2
  • 89
    • 41949086426 scopus 로고    scopus 로고
    • 2+/calmodulin-PfPKB signaling pathway in erythrocyte invasion by Plasmodium falciparum
    • 2+/calmodulin-PfPKB signaling pathway in erythrocyte invasion by Plasmodium falciparum. J. Biol. Chem. 2008, 283:5589-5597.
    • (2008) J. Biol. Chem. , vol.283 , pp. 5589-5597
    • Vaid, A.1    Thomas, D.C.2    Sharma, P.3
  • 90
    • 33645235850 scopus 로고    scopus 로고
    • The basic region of the diaphanous-autoregulatory domain (DAD) is required for autoregulatory interactions with the diaphanous-related formin inhibitory domain
    • Wallar B.J., Stropich B.N., Schoenherr J.A., Holman H.A., Kitchen S.M., et al. The basic region of the diaphanous-autoregulatory domain (DAD) is required for autoregulatory interactions with the diaphanous-related formin inhibitory domain. J. Biol. Chem. 2006, 281:4300-4307.
    • (2006) J. Biol. Chem. , vol.281 , pp. 4300-4307
    • Wallar, B.J.1    Stropich, B.N.2    Schoenherr, J.A.3    Holman, H.A.4    Kitchen, S.M.5
  • 91
    • 64849094913 scopus 로고    scopus 로고
    • Regulation of the yeast formin Bni1p by the actin-regulating kinase Prk1p
    • Wang J., Neo S.P., Cai M. Regulation of the yeast formin Bni1p by the actin-regulating kinase Prk1p. Traffic 2009, 10:528-535.
    • (2009) Traffic , vol.10 , pp. 528-535
    • Wang, J.1    Neo, S.P.2    Cai, M.3
  • 92
    • 0242481218 scopus 로고    scopus 로고
    • Intraerythrocytic calcium chelators inhibit the invasion of Plasmodium falciparum
    • Wasserman M., Chaparro J. Intraerythrocytic calcium chelators inhibit the invasion of Plasmodium falciparum. Parasitol. Res. 1996, 82:102-107.
    • (1996) Parasitol. Res. , vol.82 , pp. 102-107
    • Wasserman, M.1    Chaparro, J.2
  • 93
    • 12344253270 scopus 로고    scopus 로고
    • Calcium-mediated protein secretion potentiates motility in Toxoplasma gondii
    • Wetzel D.M., Chen L.A., Ruiz F.A., Moreno S.N., Sibley L.D. Calcium-mediated protein secretion potentiates motility in Toxoplasma gondii. J. Cell Sci. 2004, 117:5739-5748.
    • (2004) J. Cell Sci. , vol.117 , pp. 5739-5748
    • Wetzel, D.M.1    Chen, L.A.2    Ruiz, F.A.3    Moreno, S.N.4    Sibley, L.D.5
  • 94
    • 0037328668 scopus 로고    scopus 로고
    • Actin filament polymerization regulates gliding motility by apicomplexan parasites
    • Wetzel D.M., Hakansson S., Hu K., Roos D., Sibley L.D. Actin filament polymerization regulates gliding motility by apicomplexan parasites. Mol. Biol. Cell 2003, 14:396-406.
    • (2003) Mol. Biol. Cell , vol.14 , pp. 396-406
    • Wetzel, D.M.1    Hakansson, S.2    Hu, K.3    Roos, D.4    Sibley, L.D.5
  • 96
    • 67651004664 scopus 로고    scopus 로고
    • Protein phosphorylation influences proteolytic cleavage and kinase substrate properties exemplified by analysis of in vitro phosphorylated Plasmodium falciparum glideosome-associated protein 45 by nano-ultra performance liquid chromatography-tandem mass spectrometry
    • Winter D., Kugelstadt D., Seidler J., Kappes B., Lehmann W.D. Protein phosphorylation influences proteolytic cleavage and kinase substrate properties exemplified by analysis of in vitro phosphorylated Plasmodium falciparum glideosome-associated protein 45 by nano-ultra performance liquid chromatography-tandem mass spectrometry. Anal. Biochem. 2009, 393:41-47.
    • (2009) Anal. Biochem. , vol.393 , pp. 41-47
    • Winter, D.1    Kugelstadt, D.2    Seidler, J.3    Kappes, B.4    Lehmann, W.D.5
  • 97
    • 72449204677 scopus 로고    scopus 로고
    • Molecular epidemiology of cryptosporidiosis: an update
    • Xiao L. Molecular epidemiology of cryptosporidiosis: an update. Exp. Parasitol. 2010, 124:80-89.
    • (2010) Exp. Parasitol. , vol.124 , pp. 80-89
    • Xiao, L.1


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