메뉴 건너뛰기




Volumn 15, Issue 6, 2012, Pages 699-704

Recent insights into the export of PEXEL/HTS-motif containing proteins in Plasmodium parasites

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN; PLASMODIUM TRANSLOCON OF EXPORTED PROTEIN; UNCLASSIFIED DRUG;

EID: 84872275320     PISSN: 13695274     EISSN: 18790364     Source Type: Journal    
DOI: 10.1016/j.mib.2012.09.008     Document Type: Review
Times cited : (11)

References (45)
  • 1
    • 27944471039 scopus 로고    scopus 로고
    • Signal-mediated export of proteins from the malaria parasite to the host erythrocyte
    • Marti M., Baum J., Rug M., Tilley L., Cowman A.F. Signal-mediated export of proteins from the malaria parasite to the host erythrocyte. J Cell Biol 2005, 171:587-592.
    • (2005) J Cell Biol , vol.171 , pp. 587-592
    • Marti, M.1    Baum, J.2    Rug, M.3    Tilley, L.4    Cowman, A.F.5
  • 2
    • 10344250457 scopus 로고    scopus 로고
    • Targeting malaria virulence and remodeling proteins to the host erythrocyte
    • Marti M., Good R.T., Rug M., Knuepfer E., Cowman A.F. Targeting malaria virulence and remodeling proteins to the host erythrocyte. Science 2004, 306:1930-1933.
    • (2004) Science , vol.306 , pp. 1930-1933
    • Marti, M.1    Good, R.T.2    Rug, M.3    Knuepfer, E.4    Cowman, A.F.5
  • 6
    • 0021622987 scopus 로고
    • The ring-infected erythrocyte surface antigen (RESA) polypeptide of Plasmodium falciparum contains two separate blocks of tandem repeats encoding antigenic epitopes that are naturally immunogenic in man
    • Cowman A.F., Coppel R.L., Saint R.B., Favaloro J., Crewther P.E., Stahl H.D., Bianco A.E., Brown G.V., Anders R.F., Kemp D.J. The ring-infected erythrocyte surface antigen (RESA) polypeptide of Plasmodium falciparum contains two separate blocks of tandem repeats encoding antigenic epitopes that are naturally immunogenic in man. Mol Biol Med 1984, 2:207-221.
    • (1984) Mol Biol Med , vol.2 , pp. 207-221
    • Cowman, A.F.1    Coppel, R.L.2    Saint, R.B.3    Favaloro, J.4    Crewther, P.E.5    Stahl, H.D.6    Bianco, A.E.7    Brown, G.V.8    Anders, R.F.9    Kemp, D.J.10
  • 8
    • 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., Anders R.F. The ring-infected erythrocyte surface antigen of Plasmodium falciparum associates with spectrin in the erythrocyte membrane. Mol Biochem Parasitol 1991, 46:137-147.
    • (1991) Mol Biochem Parasitol , vol.46 , pp. 137-147
    • Foley, M.1    Tilley, L.2    Sawyer, W.H.3    Anders, R.F.4
  • 9
    • 24744459649 scopus 로고    scopus 로고
    • Structural and functional studies of interaction between Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and erythrocyte spectrin
    • Pei X., An X., Guo X., Tarnawski M., Coppel R., Mohandas N. Structural and functional studies of interaction between Plasmodium falciparum knob-associated histidine-rich protein (KAHRP) and erythrocyte spectrin. J Biol Chem 2005, 280:31166-31171.
    • (2005) J Biol Chem , vol.280 , pp. 31166-31171
    • Pei, X.1    An, X.2    Guo, X.3    Tarnawski, M.4    Coppel, R.5    Mohandas, N.6
  • 10
    • 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., An X. The ring-infected erythrocyte surface antigen (RESA) of Plasmodium falciparum stabilizes spectrin tetramers and suppresses further invasion. Blood 2007, 110:1036-1042.
    • (2007) Blood , vol.110 , 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
  • 11
    • 34848884573 scopus 로고    scopus 로고
    • Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) destabilizes erythrocyte membrane skeleton
    • Pei X., Guo X., Coppel R., Mohandas N., An X. Plasmodium falciparum erythrocyte membrane protein 3 (PfEMP3) destabilizes erythrocyte membrane skeleton. J Biol Chem 2007, 282:26754-26758.
    • (2007) J Biol Chem , vol.282 , pp. 26754-26758
    • Pei, X.1    Guo, X.2    Coppel, R.3    Mohandas, N.4    An, X.5
  • 12
    • 0023427830 scopus 로고
    • Primary structure and subcellular localization of the knob-associated histidine-rich protein of Plasmodium falciparum
    • Pologe L.G., Pavlovec A., Shio H., Ravetch J.V. Primary structure and subcellular localization of the knob-associated histidine-rich protein of Plasmodium falciparum. Proc Natl Acad Sci USA 1987, 84:7139-7143.
    • (1987) Proc Natl Acad Sci USA , vol.84 , pp. 7139-7143
    • Pologe, L.G.1    Pavlovec, A.2    Shio, H.3    Ravetch, J.V.4
  • 13
    • 84855813613 scopus 로고    scopus 로고
    • Voltage-dependent inactivation of the plasmodial surface anion channel via a cleavable cytoplasmic component
    • Alkhalil A., Hong L., Nguitragool W., Desai S.A. Voltage-dependent inactivation of the plasmodial surface anion channel via a cleavable cytoplasmic component. Biochim Biophys Acta 2012, 1818:367-374.
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 367-374
    • Alkhalil, A.1    Hong, L.2    Nguitragool, W.3    Desai, S.A.4
  • 14
    • 75849161351 scopus 로고    scopus 로고
    • Malaria parasite mutants with altered erythrocyte permeability: a new drug resistance mechanism and important molecular tool
    • Hill D.A., Desai S.A. Malaria parasite mutants with altered erythrocyte permeability: a new drug resistance mechanism and important molecular tool. Future Microbiol 2010, 5:81-97.
    • (2010) Future Microbiol , vol.5 , pp. 81-97
    • Hill, D.A.1    Desai, S.A.2
  • 16
    • 33751167422 scopus 로고    scopus 로고
    • Solute transport via the new permeability pathways in Plasmodium falciparum-infected human red blood cells is not consistent with a simple single-channel model
    • Staines H.M., Ashmore S., Felgate H., Moore J., Powell T., Ellory J.C. Solute transport via the new permeability pathways in Plasmodium falciparum-infected human red blood cells is not consistent with a simple single-channel model. Blood 2006, 108:3187-3194.
    • (2006) Blood , vol.108 , pp. 3187-3194
    • Staines, H.M.1    Ashmore, S.2    Felgate, H.3    Moore, J.4    Powell, T.5    Ellory, J.C.6
  • 17
    • 12744253952 scopus 로고    scopus 로고
    • The new permeability pathways: targets and selective routes for the development of new antimalarial agents
    • Staines H.M., Ellory J.C., Chibale K. The new permeability pathways: targets and selective routes for the development of new antimalarial agents. Comb Chem High Throughput Screen 2005, 8:81-88.
    • (2005) Comb Chem High Throughput Screen , vol.8 , pp. 81-88
    • Staines, H.M.1    Ellory, J.C.2    Chibale, K.3
  • 18
    • 0033962141 scopus 로고    scopus 로고
    • Increased permeability of the malaria-infected erythrocyte to organic cations
    • Staines H.M., Rae C., Kirk K. Increased permeability of the malaria-infected erythrocyte to organic cations. Biochim Biophys Acta 2000, 1463:88-98.
    • (2000) Biochim Biophys Acta , vol.1463 , pp. 88-98
    • Staines, H.M.1    Rae, C.2    Kirk, K.3
  • 19
    • 0345257824 scopus 로고    scopus 로고
    • Characterization of the pathway for transport of the cytoadherence-mediating protein, PfEMP1, to the host cell surface in malaria parasite-infected erythrocytes
    • Kriek N., Tilley L., Horrocks P., Pinches R., Elford B.C., Ferguson D.J., Lingelbach K., Newbold C.I. Characterization of the pathway for transport of the cytoadherence-mediating protein, PfEMP1, to the host cell surface in malaria parasite-infected erythrocytes. Mol Microbiol 2003, 50:1215-1227.
    • (2003) Mol Microbiol , vol.50 , pp. 1215-1227
    • Kriek, N.1    Tilley, L.2    Horrocks, P.3    Pinches, R.4    Elford, B.C.5    Ferguson, D.J.6    Lingelbach, K.7    Newbold, C.I.8
  • 20
    • 64749100258 scopus 로고    scopus 로고
    • Malaria parasite proteins that remodel the host erythrocyte
    • Maier A.G., Cooke B.M., Cowman A.F., Tilley L. Malaria parasite proteins that remodel the host erythrocyte. Nat Rev 2009, 7:341-354.
    • (2009) Nat Rev , vol.7 , pp. 341-354
    • Maier, A.G.1    Cooke, B.M.2    Cowman, A.F.3    Tilley, L.4
  • 21
    • 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., Rug M., O'Neill M.T., Beeson J.G., Marti M., Reeder J., Cowman A.F. Skeleton-binding protein 1 functions at the parasitophorous vacuole membrane to traffic PfEMP1 to the Plasmodium falciparum-infected erythrocyte surface. Blood 2007, 109:1289-1297.
    • (2007) Blood , vol.109 , pp. 1289-1297
    • Maier, A.G.1    Rug, M.2    O'Neill, M.T.3    Beeson, J.G.4    Marti, M.5    Reeder, J.6    Cowman, A.F.7
  • 22
    • 84857711352 scopus 로고    scopus 로고
    • Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope
    • Mayer C., Slater L., Erat M.C., Konrat R., Vakonakis I. Structural analysis of the Plasmodium falciparum erythrocyte membrane protein 1 (PfEMP1) intracellular domain reveals a conserved interaction epitope. J Biol Chem 2012, 287:7182-7189.
    • (2012) J Biol Chem , vol.287 , pp. 7182-7189
    • Mayer, C.1    Slater, L.2    Erat, M.C.3    Konrat, R.4    Vakonakis, I.5
  • 23
    • 59849124093 scopus 로고    scopus 로고
    • Role of the Plasmodium export element in trafficking parasite proteins to the infected erythrocyte
    • Boddey J.A., Moritz R.L., Simpson R.J., Cowman A.F. Role of the Plasmodium export element in trafficking parasite proteins to the infected erythrocyte. Traffic 2009, 10:285-299.
    • (2009) Traffic , vol.10 , pp. 285-299
    • Boddey, J.A.1    Moritz, R.L.2    Simpson, R.J.3    Cowman, A.F.4
  • 24
    • 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., Cowman A.F. Trafficking of the major virulence factor to the surface of transfected P. falciparum-infected erythrocytes. Blood 2005, 105:4078-4087.
    • (2005) Blood , vol.105 , pp. 4078-4087
    • Knuepfer, E.1    Rug, M.2    Klonis, N.3    Tilley, L.4    Cowman, A.F.5
  • 28
    • 77950020574 scopus 로고    scopus 로고
    • Protein export in Plasmodium parasites: from the endoplasmic reticulum to the vacuolar export machine
    • Crabb B.S., de Koning-Ward T.F., Gilson P.R. Protein export in Plasmodium parasites: from the endoplasmic reticulum to the vacuolar export machine. Int J Parasitol 2010, 40:509-513.
    • (2010) Int J Parasitol , vol.40 , pp. 509-513
    • Crabb, B.S.1    de Koning-Ward, T.F.2    Gilson, P.R.3
  • 29
    • 79953325518 scopus 로고    scopus 로고
    • Structural rationale for the recognition of arginine at P(3) in PEXEL motif containing proteins of Plasmodium falciparum by plasmepsin V
    • Guruprasad L., Tanneeru K., Guruprasad K. Structural rationale for the recognition of arginine at P(3) in PEXEL motif containing proteins of Plasmodium falciparum by plasmepsin V. Protein Pept Lett 2011, 18:634-641.
    • (2011) Protein Pept Lett , vol.18 , pp. 634-641
    • Guruprasad, L.1    Tanneeru, K.2    Guruprasad, K.3
  • 30
    • 23944472349 scopus 로고    scopus 로고
    • Characterization of plasmepsin V, a membrane-bound aspartic protease homolog in the endoplasmic reticulum of Plasmodium falciparum
    • Klemba M., Goldberg D.E. Characterization of plasmepsin V, a membrane-bound aspartic protease homolog in the endoplasmic reticulum of Plasmodium falciparum. Mol Biochem Parasitol 2005, 143:183-191.
    • (2005) Mol Biochem Parasitol , vol.143 , pp. 183-191
    • Klemba, M.1    Goldberg, D.E.2
  • 31
    • 84856104303 scopus 로고    scopus 로고
    • Endoplasmic reticulum PI(3)P lipid binding targets malaria proteins to the host cell
    • Bhattacharjee S., Stahelin R.V., Speicher K.D., Speicher D.W., Haldar K. Endoplasmic reticulum PI(3)P lipid binding targets malaria proteins to the host cell. Cell 2012, 148:201-212.
    • (2012) Cell , vol.148 , pp. 201-212
    • Bhattacharjee, S.1    Stahelin, R.V.2    Speicher, K.D.3    Speicher, D.W.4    Haldar, K.5
  • 33
    • 58549092387 scopus 로고    scopus 로고
    • Export of PfSBP1 to the Plasmodium falciparum Maurer's clefts
    • Saridaki T., Frohlich K.S., Braun-Breton C., Lanzer M. Export of PfSBP1 to the Plasmodium falciparum Maurer's clefts. Traffic 2009, 10:137-152.
    • (2009) Traffic , vol.10 , pp. 137-152
    • Saridaki, T.1    Frohlich, K.S.2    Braun-Breton, C.3    Lanzer, M.4
  • 34
    • 84856771094 scopus 로고    scopus 로고
    • Erythrocyte remodeling in Plasmodium berghei infection: the contribution of SEP family members
    • Curra C., Pace T., Franke-Fayard B.M., Picci L., Bertuccini L., Ponzi M. Erythrocyte remodeling in Plasmodium berghei infection: the contribution of SEP family members. Traffic 2012, 13:388-399.
    • (2012) Traffic , vol.13 , pp. 388-399
    • Curra, C.1    Pace, T.2    Franke-Fayard, B.M.3    Picci, L.4    Bertuccini, L.5    Ponzi, M.6
  • 35
    • 72149083014 scopus 로고    scopus 로고
    • Protein export in malaria parasites: do multiple export motifs add up to multiple export pathways?
    • Spielmann T., Gilberger T.W. Protein export in malaria parasites: do multiple export motifs add up to multiple export pathways?. Trends Parasitol 2010, 26:6-10.
    • (2010) Trends Parasitol , vol.26 , pp. 6-10
    • Spielmann, T.1    Gilberger, T.W.2
  • 36
    • 58449127326 scopus 로고    scopus 로고
    • Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum
    • Gehde N., Hinrichs C., Montilla I., Charpian S., Lingelbach K., Przyborski J.M. Protein unfolding is an essential requirement for transport across the parasitophorous vacuolar membrane of Plasmodium falciparum. Mol Microbiol 2009, 71:613-628.
    • (2009) Mol Microbiol , vol.71 , pp. 613-628
    • Gehde, N.1    Hinrichs, C.2    Montilla, I.3    Charpian, S.4    Lingelbach, K.5    Przyborski, J.M.6
  • 43
    • 84859780613 scopus 로고    scopus 로고
    • Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery
    • Sharma A., Dixit S. Structural insights into thioredoxin-2: a component of malaria parasite protein secretion machinery. Sci Rep 2011, 1:179.
    • (2011) Sci Rep , vol.1 , pp. 179
    • Sharma, A.1    Dixit, S.2
  • 45
    • 72049121876 scopus 로고    scopus 로고
    • Whole cell imaging reveals novel modular features of the exomembrane system of the malaria parasite, Plasmodium falciparum
    • Hanssen E., Carlton P., Deed S., Klonis N., Sedat J., DeRisi J., Tilley L. Whole cell imaging reveals novel modular features of the exomembrane system of the malaria parasite, Plasmodium falciparum. Int J Parasitol 2010, 40:123-134.
    • (2010) Int J Parasitol , vol.40 , pp. 123-134
    • Hanssen, E.1    Carlton, P.2    Deed, S.3    Klonis, N.4    Sedat, J.5    DeRisi, J.6    Tilley, L.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.