메뉴 건너뛰기




Volumn 26, Issue 6, 2010, Pages 305-310

An update on the rapid advances in malaria parasite cell biology

Author keywords

[No Author keywords available]

Indexed keywords

APICAL MEMBRANE ANTIGEN 1; CIRCUMSPOROZOITE PROTEIN; FOSMIDOMYCIN; MALARIA VACCINE;

EID: 77952584312     PISSN: 14714922     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pt.2010.03.007     Document Type: Review
Times cited : (9)

References (69)
  • 1
    • 0035103466 scopus 로고    scopus 로고
    • Nuclear-encoded, plastid-targeted genes suggest a single common origin for apicomplexan and dinoflagellate plastids
    • Fast N.M., et al. Nuclear-encoded, plastid-targeted genes suggest a single common origin for apicomplexan and dinoflagellate plastids. Mol. Biol. Evol. 18 (2001) 418-426
    • (2001) Mol. Biol. Evol. , vol.18 , pp. 418-426
    • Fast, N.M.1
  • 2
    • 0028220332 scopus 로고
    • The evolutionary origin of the 35 kb circular DNA of Plasmodium falciparum: new evidence supports a possible rhodophyte ancestry
    • Williamson D.H., et al. The evolutionary origin of the 35 kb circular DNA of Plasmodium falciparum: new evidence supports a possible rhodophyte ancestry. Mol. Gen. Genet. 243 (1994) 249-252
    • (1994) Mol. Gen. Genet. , vol.243 , pp. 249-252
    • Williamson, D.H.1
  • 3
    • 0036307786 scopus 로고    scopus 로고
    • Progress with parasite plastids
    • Wilson R.J. Progress with parasite plastids. J. Mol. Biol. 319 (2002) 257-274
    • (2002) J. Mol. Biol. , vol.319 , pp. 257-274
    • Wilson, R.J.1
  • 4
    • 33745453189 scopus 로고    scopus 로고
    • Membrane transporters in the relict plastid of malaria parasites
    • Mullin K.A., et al. Membrane transporters in the relict plastid of malaria parasites. Proc. Natl. Acad. Sci. USA 103 (2006) 9572-9577
    • (2006) Proc. Natl. Acad. Sci. USA , vol.103 , pp. 9572-9577
    • Mullin, K.A.1
  • 5
    • 0033520336 scopus 로고    scopus 로고
    • Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs
    • Jomaa H., et al. Inhibitors of the nonmevalonate pathway of isoprenoid biosynthesis as antimalarial drugs. Science 285 5433 (1999) 1573-1576
    • (1999) Science , vol.285 , Issue.5433 , pp. 1573-1576
    • Jomaa, H.1
  • 6
    • 0037308581 scopus 로고    scopus 로고
    • Fosmidomycin, a novel chemotherapeutic agent for malaria
    • Lell B., et al. Fosmidomycin, a novel chemotherapeutic agent for malaria. Antimicrob. Agents Chemother. 47 (2003) 735-738
    • (2003) Antimicrob. Agents Chemother. , vol.47 , pp. 735-738
    • Lell, B.1
  • 7
    • 62549103382 scopus 로고    scopus 로고
    • Use of high-density tiling microarrays to identify mutations globally and elucidate mechanisms of drug resistance in Plasmodium falciparum
    • Dharia N.V., et al. Use of high-density tiling microarrays to identify mutations globally and elucidate mechanisms of drug resistance in Plasmodium falciparum. Genome Biol. 10 (2009) R21
    • (2009) Genome Biol. , vol.10
    • Dharia, N.V.1
  • 8
    • 0035126479 scopus 로고    scopus 로고
    • Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum
    • Surolia N., and Surolia A. Triclosan offers protection against blood stages of malaria by inhibiting enoyl-ACP reductase of Plasmodium falciparum. Nat. Med. 7 (2001) 167-173
    • (2001) Nat. Med. , vol.7 , pp. 167-173
    • Surolia, N.1    Surolia, A.2
  • 9
    • 26844461350 scopus 로고    scopus 로고
    • Synthesis, biological activity, and X-ray crystal structural analysis of diaryl ether inhibitors of malarial enoyl acyl carrier protein reductase. Part 1: 4′-substituted triclosan derivatives
    • Freundlich J.S., et al. Synthesis, biological activity, and X-ray crystal structural analysis of diaryl ether inhibitors of malarial enoyl acyl carrier protein reductase. Part 1: 4′-substituted triclosan derivatives. Bioorg. Med. Chem. Lett. 15 (2005) 5247-5252
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 5247-5252
    • Freundlich, J.S.1
  • 10
    • 34548480189 scopus 로고    scopus 로고
    • X-ray structural analysis of Plasmodium falciparum enoyl acyl carrier protein reductase as a pathway toward the optimization of triclosan antimalarial efficacy
    • Freundlich J.S., et al. X-ray structural analysis of Plasmodium falciparum enoyl acyl carrier protein reductase as a pathway toward the optimization of triclosan antimalarial efficacy. J. Biol. Chem. 282 (2007) 25436-25444
    • (2007) J. Biol. Chem. , vol.282 , pp. 25436-25444
    • Freundlich, J.S.1
  • 11
    • 33644802299 scopus 로고    scopus 로고
    • Synthesis and biological activity of diaryl ether inhibitors of malarial enoyl acyl carrier protein reductase. Part 2: 2′-substituted triclosan derivatives
    • Freundlich J.S., et al. Synthesis and biological activity of diaryl ether inhibitors of malarial enoyl acyl carrier protein reductase. Part 2: 2′-substituted triclosan derivatives. Bioorg. Med. Chem. Lett. 16 (2006) 2163-2169
    • (2006) Bioorg. Med. Chem. Lett. , vol.16 , pp. 2163-2169
    • Freundlich, J.S.1
  • 12
    • 33947318051 scopus 로고    scopus 로고
    • Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents
    • Muench S.P., et al. Studies of Toxoplasma gondii and Plasmodium falciparum enoyl acyl carrier protein reductase and implications for the development of antiparasitic agents. Acta Crystallogr. D Biol. Crystallogr. 63 (2007) 328-338
    • (2007) Acta Crystallogr. D Biol. Crystallogr. , vol.63 , pp. 328-338
    • Muench, S.P.1
  • 13
    • 0037066782 scopus 로고    scopus 로고
    • Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase
    • Perozzo R., et al. Structural elucidation of the specificity of the antibacterial agent triclosan for malarial enoyl acyl carrier protein reductase. J. Biol. Chem. 277 (2002) 13106-13114
    • (2002) J. Biol. Chem. , vol.277 , pp. 13106-13114
    • Perozzo, R.1
  • 14
    • 4644355051 scopus 로고    scopus 로고
    • Structural basis for the variation in triclosan affinity to enoyl reductases
    • Pidugu L.S., et al. Structural basis for the variation in triclosan affinity to enoyl reductases. J. Mol. Biol. 343 (2004) 147-155
    • (2004) J. Mol. Biol. , vol.343 , pp. 147-155
    • Pidugu, L.S.1
  • 15
    • 57049187017 scopus 로고    scopus 로고
    • The fatty acid biosynthesis enzyme FabI plays a key role in the development of liver-stage malarial parasites
    • Yu M., et al. The fatty acid biosynthesis enzyme FabI plays a key role in the development of liver-stage malarial parasites. Cell Host Microbe 4 (2008) 567-578
    • (2008) Cell Host Microbe , vol.4 , pp. 567-578
    • Yu, M.1
  • 16
    • 59849125892 scopus 로고    scopus 로고
    • Type II fatty acid synthesis is essential only for malaria parasite late liver stage development
    • Vaughan A.M., et al. Type II fatty acid synthesis is essential only for malaria parasite late liver stage development. Cell Microbiol. 11 (2009) 506-520
    • (2009) Cell Microbiol. , vol.11 , pp. 506-520
    • Vaughan, A.M.1
  • 17
    • 76449090046 scopus 로고    scopus 로고
    • Plasmodium pyruvate dehydrogenase activity is only essential for the parasite's progression from liver infection to blood infection
    • Pei Y., et al. Plasmodium pyruvate dehydrogenase activity is only essential for the parasite's progression from liver infection to blood infection. Mol. Microbiol. 75 (2010) 957-971
    • (2010) Mol. Microbiol. , vol.75 , pp. 957-971
    • Pei, Y.1
  • 18
    • 12344312032 scopus 로고    scopus 로고
    • The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast
    • Foth B.J., et al. The malaria parasite Plasmodium falciparum has only one pyruvate dehydrogenase complex, which is located in the apicoplast. Mol. Microbiol. 55 (2005) 39-53
    • (2005) Mol. Microbiol. , vol.55 , pp. 39-53
    • Foth, B.J.1
  • 19
    • 33846965950 scopus 로고    scopus 로고
    • Scavenging of the cofactor lipoate is essential for the survival of the malaria parasite Plasmodium falciparum
    • Allary M., et al. Scavenging of the cofactor lipoate is essential for the survival of the malaria parasite Plasmodium falciparum. Mol. Microbiol. 63 (2007) 1331-1344
    • (2007) Mol. Microbiol. , vol.63 , pp. 1331-1344
    • Allary, M.1
  • 20
    • 37849040526 scopus 로고    scopus 로고
    • Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum
    • Gunther S., et al. Apicoplast lipoic acid protein ligase B is not essential for Plasmodium falciparum. PLoS Pathog. 3 (2007) e189
    • (2007) PLoS Pathog. , vol.3
    • Gunther, S.1
  • 21
    • 59849113706 scopus 로고    scopus 로고
    • Plasmodium falciparum: organelle-specific acquisition of lipoic acid
    • Gunther S., et al. Plasmodium falciparum: organelle-specific acquisition of lipoic acid. Int. J. Biochem. Cell Biol. 41 (2009) 748-752
    • (2009) Int. J. Biochem. Cell Biol. , vol.41 , pp. 748-752
    • Gunther, S.1
  • 22
    • 37249026903 scopus 로고    scopus 로고
    • Distinct physiological states of Plasmodium falciparum in malaria-infected patients
    • Daily J.P., et al. Distinct physiological states of Plasmodium falciparum in malaria-infected patients. Nature 450 (2007) 1091-1095
    • (2007) Nature , vol.450 , pp. 1091-1095
    • Daily, J.P.1
  • 23
    • 66149141833 scopus 로고    scopus 로고
    • Statistical estimation of cell-cycle progression and lineage commitment in Plasmodium falciparum reveals a homogeneous pattern of transcription in ex vivo culture
    • Lemieux J.E., et al. Statistical estimation of cell-cycle progression and lineage commitment in Plasmodium falciparum reveals a homogeneous pattern of transcription in ex vivo culture. Proc. Natl. Acad. Sci. USA 106 (2009) 7559-7564
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 7559-7564
    • Lemieux, J.E.1
  • 24
    • 67650492478 scopus 로고    scopus 로고
    • In vivo profiles in malaria are consistent with a novel physiological state
    • Wirth D., et al. In vivo profiles in malaria are consistent with a novel physiological state. Proc. Natl. Acad. Sci. USA 106 (2009) E70
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106
    • Wirth, D.1
  • 25
    • 64949105863 scopus 로고    scopus 로고
    • 1H NMR spectroscopy
    • 1H NMR spectroscopy. NMR Biomed. 22 (2009) 292-302
    • (2009) NMR Biomed. , vol.22 , pp. 292-302
    • Teng, R.1
  • 26
    • 69149109035 scopus 로고    scopus 로고
    • Preerythrocytic, live-attenuated Plasmodium falciparum vaccine candidates by design
    • VanBuskirk K.M., et al. Preerythrocytic, live-attenuated Plasmodium falciparum vaccine candidates by design. Proc. Natl. Acad. Sci. USA 106 (2009) 13004-13009
    • (2009) Proc. Natl. Acad. Sci. USA , vol.106 , pp. 13004-13009
    • VanBuskirk, K.M.1
  • 27
    • 74949087025 scopus 로고    scopus 로고
    • Genetically engineered, attenuated whole-cell vaccine approaches for malaria
    • Vaughan A.M., et al. Genetically engineered, attenuated whole-cell vaccine approaches for malaria. Hum. Vaccin. 6 (2010) 107-113
    • (2010) Hum. Vaccin. , vol.6 , pp. 107-113
    • Vaughan, A.M.1
  • 28
    • 10344245559 scopus 로고    scopus 로고
    • A host-targeting signal in virulence proteins reveals a secretome in malarial infection
    • Hiller N.L., et al. A host-targeting signal in virulence proteins reveals a secretome in malarial infection. Science 306 (2004) 1934-1937
    • (2004) Science , vol.306 , pp. 1934-1937
    • Hiller, N.L.1
  • 29
    • 10344250457 scopus 로고    scopus 로고
    • Targeting malaria virulence and remodeling proteins to the host erythrocyte
    • Marti M., et al. 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
  • 30
    • 46449088780 scopus 로고    scopus 로고
    • The malaria secretome: from algorithms to essential function in blood stage infection
    • van Ooij C., et al. The malaria secretome: from algorithms to essential function in blood stage infection. PLoS Pathog. 4 (2008) 1-15
    • (2008) PLoS Pathog. , vol.4 , pp. 1-15
    • van Ooij, C.1
  • 31
    • 46149093701 scopus 로고    scopus 로고
    • Exported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytes
    • Maier A.G., et al. Exported proteins required for virulence and rigidity of Plasmodium falciparum-infected human erythrocytes. Cell 134 (2008) 48-61
    • (2008) Cell , vol.134 , pp. 48-61
    • Maier, A.G.1
  • 32
    • 62449295335 scopus 로고    scopus 로고
    • Measuring erythrocyte deformability with fluorescence, fluid forces, and optical trapping
    • Bambardekar K., et al. Measuring erythrocyte deformability with fluorescence, fluid forces, and optical trapping. J. Biomed. Opt. 13 (2008) 064021
    • (2008) J. Biomed. Opt. , vol.13 , pp. 064021
    • Bambardekar, K.1
  • 33
    • 67649277651 scopus 로고    scopus 로고
    • A newly discovered protein export machine in malaria parasites
    • de Koning-Ward T.F., et al. A newly discovered protein export machine in malaria parasites. Nature 459 (2009) 945-949
    • (2009) Nature , vol.459 , pp. 945-949
    • de Koning-Ward, T.F.1
  • 34
    • 58449127326 scopus 로고    scopus 로고
    • Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum
    • Gehde N., et al. Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum. Mol. Microbiol. 71 (2009) 613-628
    • (2009) Mol. Microbiol. , vol.71 , pp. 613-628
    • Gehde, N.1
  • 35
    • 50849084822 scopus 로고    scopus 로고
    • An erythrocyte vesicle protein exported by the malaria parasite promotes tubovesicular lipid import from the host cell surface
    • Tamez P.A., et al. An erythrocyte vesicle protein exported by the malaria parasite promotes tubovesicular lipid import from the host cell surface. PLoS Pathog. 4 (2008) 1-12
    • (2008) PLoS Pathog. , vol.4 , pp. 1-12
    • Tamez, P.A.1
  • 36
    • 47749095577 scopus 로고    scopus 로고
    • Targeted mutagenesis of the ring-exported protein-1 of Plasmodium falciparum disrupts the architecture of Maurer's cleft organelles
    • Hanssen E., et al. Targeted mutagenesis of the ring-exported protein-1 of Plasmodium falciparum disrupts the architecture of Maurer's cleft organelles. Mol. Microbiol. 69 (2008) 938-953
    • (2008) Mol. Microbiol. , vol.69 , pp. 938-953
    • Hanssen, E.1
  • 37
    • 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., et al. 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
  • 38
    • 33846851529 scopus 로고    scopus 로고
    • Skeleton-binding protein 1 functions at the parasitophorous vacuole membrane to traffic PfEMP1 to the Plasmodium falciparum-infected erythrocyte surface
    • Maier A.G., et al. Skeleton-binding protein 1 functions at the parasitophorous vacuole membrane to traffic PfEMP1 to the Plasmodium falciparum-infected erythrocyte surface. Blood 109 (2007) 1289-1297
    • (2007) Blood , vol.109 , pp. 1289-1297
    • Maier, A.G.1
  • 39
    • 43449119499 scopus 로고    scopus 로고
    • The Maurer's cleft protein MAHRP1 is essential for trafficking of PfEMP1 to the surface of Plasmodium falciparum-infected erythrocytes
    • Spycher C., et al. The Maurer's cleft protein MAHRP1 is essential for trafficking of PfEMP1 to the surface of Plasmodium falciparum-infected erythrocytes. Mol. Microbiol. 68 (2008) 1300-1314
    • (2008) Mol. Microbiol. , vol.68 , pp. 1300-1314
    • Spycher, C.1
  • 40
    • 49949152250 scopus 로고    scopus 로고
    • A 3D view of the host cell compartment in P. falciparum-infected erythrocytes
    • Tilley L., and Hanssen E. A 3D view of the host cell compartment in P. falciparum-infected erythrocytes. Transfus. Clin. Biol. 15 (2008) 72-81
    • (2008) Transfus. Clin. Biol. , vol.15 , pp. 72-81
    • Tilley, L.1    Hanssen, E.2
  • 41
    • 38449122179 scopus 로고    scopus 로고
    • Electron tomography of the Maurer's cleft organelles of Plasmodium falciparum-infected erythrocytes reveals novel structural features
    • Hanssen E., et al. Electron tomography of the Maurer's cleft organelles of Plasmodium falciparum-infected erythrocytes reveals novel structural features. Mol. Microbiol. 67 (2008) 703-718
    • (2008) Mol. Microbiol. , vol.67 , pp. 703-718
    • Hanssen, E.1
  • 42
    • 40649122026 scopus 로고    scopus 로고
    • Four distinct pathways of hemoglobin uptake in the malaria parasite Plasmodium falciparum
    • Elliott D.A., et al. Four distinct pathways of hemoglobin uptake in the malaria parasite Plasmodium falciparum. Proc. Natl. Acad. Sci. USA 105 (2008) 2463-2468
    • (2008) Proc. Natl. Acad. Sci. USA , vol.105 , pp. 2463-2468
    • Elliott, D.A.1
  • 43
    • 33750090345 scopus 로고    scopus 로고
    • Spinning disk confocal microscopy of live, intraerythrocytic malarial parasites. 2. Altered vacuolar volume regulation in drug resistant malaria
    • Gligorijevic B., et al. Spinning disk confocal microscopy of live, intraerythrocytic malarial parasites. 2. Altered vacuolar volume regulation in drug resistant malaria. Biochemistry 45 (2006) 12411-12423
    • (2006) Biochemistry , vol.45 , pp. 12411-12423
    • Gligorijevic, B.1
  • 44
    • 33750088680 scopus 로고    scopus 로고
    • Spinning disk confocal microscopy of live, intraerythrocytic malarial parasites. 1. Quantification of hemozoin development for drug sensitive versus resistant malaria
    • Gligorijevic B., et al. Spinning disk confocal microscopy of live, intraerythrocytic malarial parasites. 1. Quantification of hemozoin development for drug sensitive versus resistant malaria. Biochemistry 45 (2006) 12400-12410
    • (2006) Biochemistry , vol.45 , pp. 12400-12410
    • Gligorijevic, B.1
  • 45
    • 84981836120 scopus 로고
    • Intracellular phagotrophy by malaria parasites: an electron microscope study of Plasmodium lophurae
    • Rudzinska M.A., and Trager W. Intracellular phagotrophy by malaria parasites: an electron microscope study of Plasmodium lophurae. J. Eukaryot. Microbiol. 4 (1957) 190-199
    • (1957) J. Eukaryot. Microbiol. , vol.4 , pp. 190-199
    • Rudzinska, M.A.1    Trager, W.2
  • 46
    • 0014644053 scopus 로고
    • Fine structure of the erythrocytic stages of Plasmodium knowlesi. A comparison between intracellular and free forms
    • Aikawa M., et al. Fine structure of the erythrocytic stages of Plasmodium knowlesi. A comparison between intracellular and free forms. Z. Zellforsch. Mikrosk. Anat. 100 (1969) 271-284
    • (1969) Z. Zellforsch. Mikrosk. Anat. , vol.100 , pp. 271-284
    • Aikawa, M.1
  • 47
    • 0041331814 scopus 로고
    • Electron microsope studies of motile stages of malaria parasites. II. The fine structure of the sporozoite of Laverania (Plasmodium) falcipara
    • Garnham P.C., et al. Electron microsope studies of motile stages of malaria parasites. II. The fine structure of the sporozoite of Laverania (Plasmodium) falcipara. Trans. R. Soc. Trop. Med. Hyg. 55 (1961) 98-102
    • (1961) Trans. R. Soc. Trop. Med. Hyg. , vol.55 , pp. 98-102
    • Garnham, P.C.1
  • 48
    • 0013882086 scopus 로고
    • The feeding mechanism of avian malarial parasites
    • Aikawa M., et al. The feeding mechanism of avian malarial parasites. J. Cell Biol. 28 (1966) 355-373
    • (1966) J. Cell Biol. , vol.28 , pp. 355-373
    • Aikawa, M.1
  • 49
    • 0025581056 scopus 로고
    • Three-dimensional reconstruction of the feeding process of the malaria parasite
    • Slomianny C. Three-dimensional reconstruction of the feeding process of the malaria parasite. Blood Cells 16 (1990) 369-378
    • (1990) Blood Cells , vol.16 , pp. 369-378
    • Slomianny, C.1
  • 50
    • 0021889727 scopus 로고
    • Ingestion of erythrocytic stroma by Plasmodium chabaudi trophozoites: ultrastructural study by serial sectioning and 3-dimensional reconstruction
    • Slomianny C., et al. Ingestion of erythrocytic stroma by Plasmodium chabaudi trophozoites: ultrastructural study by serial sectioning and 3-dimensional reconstruction. Parasitology 90 (1985) 579-588
    • (1985) Parasitology , vol.90 , pp. 579-588
    • Slomianny, C.1
  • 51
    • 46749085536 scopus 로고    scopus 로고
    • A new model for hemoglobin ingestion and transport by the human malaria parasite Plasmodium falciparum
    • Lazarus M.D., et al. A new model for hemoglobin ingestion and transport by the human malaria parasite Plasmodium falciparum. J. Cell Sci. 121 (2008) 1937-1949
    • (2008) J. Cell Sci. , vol.121 , pp. 1937-1949
    • Lazarus, M.D.1
  • 52
    • 38049140949 scopus 로고    scopus 로고
    • Actin is required for endocytic trafficking in the malaria parasite Plasmodium falciparum
    • Smythe W.A., et al. Actin is required for endocytic trafficking in the malaria parasite Plasmodium falciparum. Cell Microbiol. 10 (2008) 452-464
    • (2008) Cell Microbiol. , vol.10 , pp. 452-464
    • Smythe, W.A.1
  • 53
    • 43849106495 scopus 로고    scopus 로고
    • Comparative genomics of the Rab protein family in Apicomplexan parasites
    • Langsley G., et al. Comparative genomics of the Rab protein family in Apicomplexan parasites. Microbes Infect. 10 (2008) 462-470
    • (2008) Microbes Infect. , vol.10 , pp. 462-470
    • Langsley, G.1
  • 54
    • 70350571664 scopus 로고    scopus 로고
    • The malaria merozoite, forty years on
    • Bannister L.H., and Mitchell G.H. The malaria merozoite, forty years on. Parasitology 136 (2009) 1435-1444
    • (2009) Parasitology , vol.136 , pp. 1435-1444
    • Bannister, L.H.1    Mitchell, G.H.2
  • 55
    • 34250777898 scopus 로고    scopus 로고
    • A long and winding road: the Plasmodium sporozoite's journey in the mammalian host
    • Sinnis P., and Coppi A. A long and winding road: the Plasmodium sporozoite's journey in the mammalian host. Parasitol. Int. 56 (2007) 171-178
    • (2007) Parasitol. Int. , vol.56 , pp. 171-178
    • Sinnis, P.1    Coppi, A.2
  • 56
    • 32244448982 scopus 로고    scopus 로고
    • Quantitative imaging of Plasmodium transmission from mosquito to mammal
    • Amino R., et al. Quantitative imaging of Plasmodium transmission from mosquito to mammal. Nat. Med. 12 (2006) 220-224
    • (2006) Nat. Med. , vol.12 , pp. 220-224
    • Amino, R.1
  • 57
    • 34147127535 scopus 로고    scopus 로고
    • Plasmodium sporozoites trickle out of the injection site
    • Yamauchi L.M., et al. Plasmodium sporozoites trickle out of the injection site. Cell Microbiol. 9 (2007) 1215-1222
    • (2007) Cell Microbiol. , vol.9 , pp. 1215-1222
    • Yamauchi, L.M.1
  • 58
    • 34548276242 scopus 로고    scopus 로고
    • + T lymphocytes protective against malaria liver stages are primed in skin-draining lymph nodes
    • + T lymphocytes protective against malaria liver stages are primed in skin-draining lymph nodes. Nat. Med. 13 (2007) 1035-1041
    • (2007) Nat. Med. , vol.13 , pp. 1035-1041
    • Chakravarty, S.1
  • 59
    • 68049135868 scopus 로고    scopus 로고
    • Plasmodium sporozoite-host interactions from the dermis to the hepatocyte
    • Ejigiri I., and Sinnis P. Plasmodium sporozoite-host interactions from the dermis to the hepatocyte. Curr. Opin. Microbiol. 12 (2009) 401-407
    • (2009) Curr. Opin. Microbiol. , vol.12 , pp. 401-407
    • Ejigiri, I.1    Sinnis, P.2
  • 60
    • 35848931896 scopus 로고    scopus 로고
    • Heparan sulfate proteoglycans provide a signal to Plasmodium sporozoites to stop migrating and productively invade host cells
    • Coppi A., et al. Heparan sulfate proteoglycans provide a signal to Plasmodium sporozoites to stop migrating and productively invade host cells. Cell Host Microbe 2 (2007) 316-327
    • (2007) Cell Host Microbe , vol.2 , pp. 316-327
    • Coppi, A.1
  • 61
    • 10744226228 scopus 로고    scopus 로고
    • A role for apical membrane antigen 1 during invasion of hepatocytes by Plasmodium falciparum sporozoites
    • Silvie O., et al. A role for apical membrane antigen 1 during invasion of hepatocytes by Plasmodium falciparum sporozoites. J. Biol. Chem. 279 (2004) 9490-9496
    • (2004) J. Biol. Chem. , vol.279 , pp. 9490-9496
    • Silvie, O.1
  • 62
    • 59249090408 scopus 로고    scopus 로고
    • Distinct roles of Plasmodium rhomboid 1 in parasite development and malaria pathogenesis
    • Srinivasan P., et al. Distinct roles of Plasmodium rhomboid 1 in parasite development and malaria pathogenesis. PLoS Pathog. 5 (2009) 1-10
    • (2009) PLoS Pathog. , vol.5 , pp. 1-10
    • Srinivasan, P.1
  • 63
    • 33750465167 scopus 로고    scopus 로고
    • Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria
    • Baker R.P., et al. Two Plasmodium rhomboid proteases preferentially cleave different adhesins implicated in all invasive stages of malaria. PLoS Pathog. 2 (2006) e113
    • (2006) PLoS Pathog. , vol.2
    • Baker, R.P.1
  • 64
    • 72749083468 scopus 로고    scopus 로고
    • Reticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparum
    • Triglia T., et al. Reticulocyte binding protein homologues are key adhesins during erythrocyte invasion by Plasmodium falciparum. Cell Microbiol. 11 (2009) 1671-1687
    • (2009) Cell Microbiol. , vol.11 , pp. 1671-1687
    • Triglia, T.1
  • 65
    • 27644581320 scopus 로고    scopus 로고
    • Spreading the seeds of million-murdering death: metamorphoses of malaria in the mosquito
    • Baton L.A., and Ranford-Cartwright L.C. Spreading the seeds of million-murdering death: metamorphoses of malaria in the mosquito. Trends Parasitol. 21 (2005) 573-580
    • (2005) Trends Parasitol. , vol.21 , pp. 573-580
    • Baton, L.A.1    Ranford-Cartwright, L.C.2
  • 66
    • 0021837134 scopus 로고
    • Transformation of sporozoites of Plasmodium berghei into exoerythrocytic forms in the liver of its mammalian host
    • Meis J.F., et al. Transformation of sporozoites of Plasmodium berghei into exoerythrocytic forms in the liver of its mammalian host. Cell Tissue Res. 241 (1985) 353-360
    • (1985) Cell Tissue Res. , vol.241 , pp. 353-360
    • Meis, J.F.1
  • 67
    • 50849098173 scopus 로고    scopus 로고
    • Malaria parasite pre-erythrocytic stage infection: gliding and hiding
    • Vaughan A.M., et al. Malaria parasite pre-erythrocytic stage infection: gliding and hiding. Cell Host Microbe 4 (2008) 209-218
    • (2008) Cell Host Microbe , vol.4 , pp. 209-218
    • Vaughan, A.M.1
  • 68
    • 33947183313 scopus 로고    scopus 로고
    • L-FABP is a critical host factor for successful malaria liver stage development
    • Mikolajczak S.A., et al. L-FABP is a critical host factor for successful malaria liver stage development. Int. J. Parasitol. 37 (2007) 483-489
    • (2007) Int. J. Parasitol. , vol.37 , pp. 483-489
    • Mikolajczak, S.A.1
  • 69
    • 64849101538 scopus 로고    scopus 로고
    • Clonal conditional mutagenesis in malaria parasites
    • Combe A., et al. Clonal conditional mutagenesis in malaria parasites. Cell Host Microbe 5 (2009) 386-396
    • (2009) Cell Host Microbe , vol.5 , pp. 386-396
    • Combe, A.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.