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Volumn 44, Issue 8, 2014, Pages 551-563

Excreted/secreted Schistosoma mansoni venom allergen-like 9 (SmVAL9) modulates host extracellular matrix remodelling gene expression

Author keywords

Biomphalaria glabrata; Matrix metalloproteinase; Schistosoma mansoni; Venom allergen like

Indexed keywords

MATRIX METALLOPROTEINASE; MICROORGANISM PROTEIN; SCHISTOSOMA MANSONI VENOM ALLERGEN LIKE 9 PROTEIN; TISSUE INHIBITOR OF METALLOPROTEINASE; UNCLASSIFIED DRUG; ALLERGEN; HELMINTH PROTEIN; POLYSACCHARIDE;

EID: 84902775422     PISSN: 00207519     EISSN: 18790135     Source Type: Journal    
DOI: 10.1016/j.ijpara.2014.04.002     Document Type: Article
Times cited : (37)

References (73)
  • 1
    • 84879215676 scopus 로고    scopus 로고
    • Schistosoma eggs induce a proinflammatory, anti-fibrogenic phenotype in hepatic stellate cells
    • Anthony B.J., James K.R., Gobert G.N., Ramm G.A., McManus D.P. Schistosoma eggs induce a proinflammatory, anti-fibrogenic phenotype in hepatic stellate cells. PloS One 2013, 8:e68479.
    • (2013) PloS One , vol.8
    • Anthony, B.J.1    James, K.R.2    Gobert, G.N.3    Ramm, G.A.4    McManus, D.P.5
  • 2
    • 84857501960 scopus 로고    scopus 로고
    • Matrix metalloprotease 16 expression is downregulated by microRNA-146a in spontaneously differentiating Caco-2 cells
    • Astarci E., Erson-Bensan A.E., Banerjee S. Matrix metalloprotease 16 expression is downregulated by microRNA-146a in spontaneously differentiating Caco-2 cells. Dev Growth Differ 2012, 54:216-226.
    • (2012) Dev Growth Differ , vol.54 , pp. 216-226
    • Astarci, E.1    Erson-Bensan, A.E.2    Banerjee, S.3
  • 3
    • 84881251631 scopus 로고    scopus 로고
    • Global trends in neglected tropical disease control and elimination: impact on child health
    • Barry M.A., Simon G.G., Mistry N., Hotez P.J. Global trends in neglected tropical disease control and elimination: impact on child health. Arch Dis Child 2013, 98:635-641.
    • (2013) Arch Dis Child , vol.98 , pp. 635-641
    • Barry, M.A.1    Simon, G.G.2    Mistry, N.3    Hotez, P.J.4
  • 5
    • 0035218399 scopus 로고    scopus 로고
    • Mechanisms of molluscan host resistance and of parasite strategies for survival
    • Bayne C.J., Hahn U.K., Bender R.C. Mechanisms of molluscan host resistance and of parasite strategies for survival. Parasitology 2001, 123(Suppl.):S159-S167.
    • (2001) Parasitology , vol.123 , Issue.SUPPL.
    • Bayne, C.J.1    Hahn, U.K.2    Bender, R.C.3
  • 7
    • 0027515396 scopus 로고
    • Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'
    • Bode W., Gomis-Ruth F.X., Stockler W. Astacins, serralysins, snake venom and matrix metalloproteinases exhibit identical zinc-binding environments (HEXXHXXGXXH and Met-turn) and topologies and should be grouped into a common family, the 'metzincins'. FEBS Lett 1993, 331:134-140.
    • (1993) FEBS Lett , vol.331 , pp. 134-140
    • Bode, W.1    Gomis-Ruth, F.X.2    Stockler, W.3
  • 8
    • 0037985005 scopus 로고    scopus 로고
    • Extra-cellular matrix changes in Schistosoma mansoni-infected Biomphalaria glabrata
    • Borges C.M., Andrade Z.A. Extra-cellular matrix changes in Schistosoma mansoni-infected Biomphalaria glabrata. Mem Inst Oswaldo Cruz 2003, 98:135-139.
    • (2003) Mem Inst Oswaldo Cruz , vol.98 , pp. 135-139
    • Borges, C.M.1    Andrade, Z.A.2
  • 9
    • 40649090624 scopus 로고    scopus 로고
    • Necator americanus: the Na-ASP-2 protein secreted by the infective larvae induces neutrophil recruitment in vivo and in vitro
    • Bower M.A., Constant S.L., Mendez S. Necator americanus: the Na-ASP-2 protein secreted by the infective larvae induces neutrophil recruitment in vivo and in vitro. Exp Parasitol 2008, 118:569-575.
    • (2008) Exp Parasitol , vol.118 , pp. 569-575
    • Bower, M.A.1    Constant, S.L.2    Mendez, S.3
  • 13
    • 84866127853 scopus 로고    scopus 로고
    • Platyhelminth Venom Allergen-Like (VAL) proteins: revealing structural diversity, class-specific features and biological associations across the phylum
    • Chalmers I.W., Hoffmann K.F. Platyhelminth Venom Allergen-Like (VAL) proteins: revealing structural diversity, class-specific features and biological associations across the phylum. Parasitology 2012, 139:1231-1245.
    • (2012) Parasitology , vol.139 , pp. 1231-1245
    • Chalmers, I.W.1    Hoffmann, K.F.2
  • 14
    • 41049105094 scopus 로고    scopus 로고
    • Developmentally regulated expression, alternative splicing and distinct sub-groupings in members of the Schistosoma mansoni venom allergen-like (SmVAL) gene family
    • Chalmers I.W., McArdle A.J., Coulson R.M., Wagner M.A., Schmid R., Hirai H., Hoffmann K.F. Developmentally regulated expression, alternative splicing and distinct sub-groupings in members of the Schistosoma mansoni venom allergen-like (SmVAL) gene family. BMC Genomics 2008, 9:89.
    • (2008) BMC Genomics , vol.9 , pp. 89
    • Chalmers, I.W.1    McArdle, A.J.2    Coulson, R.M.3    Wagner, M.A.4    Schmid, R.5    Hirai, H.6    Hoffmann, K.F.7
  • 15
    • 84883194417 scopus 로고    scopus 로고
    • Membrane localization of membrane type 1 matrix metalloproteinase by CD44 regulates the activation of pro-matrix metalloproteinase 9 in osteoclasts
    • Chellaiah M.A., Ma T. Membrane localization of membrane type 1 matrix metalloproteinase by CD44 regulates the activation of pro-matrix metalloproteinase 9 in osteoclasts. Biomed Res Int 2013, 2013:302392.
    • (2013) Biomed Res Int , vol.2013 , pp. 302392
    • Chellaiah, M.A.1    Ma, T.2
  • 16
    • 84887895214 scopus 로고    scopus 로고
    • Deep sequencing-based identification of pathogen-specific microRNAs in the plasma of rabbits infected with Schistosoma japonicum
    • Cheng G., Luo R., Hu C., Cao J., Jin Y. Deep sequencing-based identification of pathogen-specific microRNAs in the plasma of rabbits infected with Schistosoma japonicum. Parasitology 2013, 1-11.
    • (2013) Parasitology , pp. 1-11
    • Cheng, G.1    Luo, R.2    Hu, C.3    Cao, J.4    Jin, Y.5
  • 17
    • 75449122146 scopus 로고
    • Observations on hearts explanted in vitro from the snail Australorbis glabratus
    • Chernin E. Observations on hearts explanted in vitro from the snail Australorbis glabratus. J Parasitol 1963, 49:353-364.
    • (1963) J Parasitol , vol.49 , pp. 353-364
    • Chernin, E.1
  • 19
    • 33646916258 scopus 로고    scopus 로고
    • Identification of novel proteases and immunomodulators in the secretions of schistosome cercariae that facilitate host entry
    • Curwen R.S., Ashton P.D., Sundaralingam S., Wilson R.A. Identification of novel proteases and immunomodulators in the secretions of schistosome cercariae that facilitate host entry. Mol Cell Proteomics 2006, 5:835-844.
    • (2006) Mol Cell Proteomics , vol.5 , pp. 835-844
    • Curwen, R.S.1    Ashton, P.D.2    Sundaralingam, S.3    Wilson, R.A.4
  • 20
    • 79957971394 scopus 로고    scopus 로고
    • Manipulation of vascular function by blood flukes?
    • Da'dara A., Skelly P.J. Manipulation of vascular function by blood flukes?. Blood Rev 2011, 25:175-179.
    • (2011) Blood Rev , vol.25 , pp. 175-179
    • Da'dara, A.1    Skelly, P.J.2
  • 22
    • 0038015446 scopus 로고    scopus 로고
    • Isolation and molecular cloning of a secreted hookworm platelet inhibitor from adult Ancylostoma caninum
    • Del Valle A., Jones B.F., Harrison L.M., Chadderdon R.C., Cappello M. Isolation and molecular cloning of a secreted hookworm platelet inhibitor from adult Ancylostoma caninum. Mol Biochem Parasitol 2003, 129:167-177.
    • (2003) Mol Biochem Parasitol , vol.129 , pp. 167-177
    • Del Valle, A.1    Jones, B.F.2    Harrison, L.M.3    Chadderdon, R.C.4    Cappello, M.5
  • 23
    • 3042666256 scopus 로고    scopus 로고
    • MUSCLE: multiple sequence alignment with high accuracy and high throughput
    • Edgar R.C. MUSCLE: multiple sequence alignment with high accuracy and high throughput. Nucleic Acids Res 2004, 32:1792-1797.
    • (2004) Nucleic Acids Res , vol.32 , pp. 1792-1797
    • Edgar, R.C.1
  • 26
    • 84857853471 scopus 로고    scopus 로고
    • Schistosoma mansoni venom allergen like proteins present differential allergic responses in a murine model of airway inflammation
    • Farias L.P., Rodrigues D., Cunna V., Rofatto H.K., Faquim-Mauro E.L., Leite L.C. Schistosoma mansoni venom allergen like proteins present differential allergic responses in a murine model of airway inflammation. PLoS Negl Trop Dis 2012, 6:e1510.
    • (2012) PLoS Negl Trop Dis , vol.6
    • Farias, L.P.1    Rodrigues, D.2    Cunna, V.3    Rofatto, H.K.4    Faquim-Mauro, E.L.5    Leite, L.C.6
  • 28
    • 84858281092 scopus 로고    scopus 로고
    • Epigenetics: a key regulator of platyhelminth developmental biology?
    • Geyer K.K., Hoffmann K.F. Epigenetics: a key regulator of platyhelminth developmental biology?. Int J Parasitol 2012, 42:221-224.
    • (2012) Int J Parasitol , vol.42 , pp. 221-224
    • Geyer, K.K.1    Hoffmann, K.F.2
  • 30
    • 70350244564 scopus 로고    scopus 로고
    • Schistosoma genomics: new perspectives on schistosome biology and host-parasite interaction
    • Han Z.G., Brindley P.J., Wang S.Y., Chen Z. Schistosoma genomics: new perspectives on schistosome biology and host-parasite interaction. Annu Rev Genomics Hum Genet 2009, 10:211-240.
    • (2009) Annu Rev Genomics Hum Genet , vol.10 , pp. 211-240
    • Han, Z.G.1    Brindley, P.J.2    Wang, S.Y.3    Chen, Z.4
  • 31
    • 84863418993 scopus 로고    scopus 로고
    • Classically activated macrophages use stable microtubules for matrix metalloproteinase-9 (MMP-9) secretion
    • Hanania R., Sun H.S., Xu K., Pustylnik S., Jeganathan S., Harrison R.E. Classically activated macrophages use stable microtubules for matrix metalloproteinase-9 (MMP-9) secretion. J Biol Chem 2012, 287:8468-8483.
    • (2012) J Biol Chem , vol.287 , pp. 8468-8483
    • Hanania, R.1    Sun, H.S.2    Xu, K.3    Pustylnik, S.4    Jeganathan, S.5    Harrison, R.E.6
  • 33
    • 0029860140 scopus 로고    scopus 로고
    • Molecular identification of a Schistosoma mansoni tegumental protein with similarity to cytoplasmic dynein light chains
    • Hoffmann K.F., Strand M. Molecular identification of a Schistosoma mansoni tegumental protein with similarity to cytoplasmic dynein light chains. J Biol Chem 1996, 271:26117-26123.
    • (1996) J Biol Chem , vol.271 , pp. 26117-26123
    • Hoffmann, K.F.1    Strand, M.2
  • 34
    • 0036939339 scopus 로고    scopus 로고
    • Cytokine-mediated host responses during schistosome infections; walking the fine line between immunological control and immunopathology
    • Hoffmann K.F., Wynn T.A., Dunne D.W. Cytokine-mediated host responses during schistosome infections; walking the fine line between immunological control and immunopathology. Adv Parasitol 2002, 52:265-307.
    • (2002) Adv Parasitol , vol.52 , pp. 265-307
    • Hoffmann, K.F.1    Wynn, T.A.2    Dunne, D.W.3
  • 35
    • 0036702991 scopus 로고    scopus 로고
    • Schistosome glycoconjugates in host-parasite interplay
    • Hokke C.H., Deelder A.M. Schistosome glycoconjugates in host-parasite interplay. Glycoconj J 2001, 18:573-587.
    • (2001) Glycoconj J , vol.18 , pp. 573-587
    • Hokke, C.H.1    Deelder, A.M.2
  • 37
    • 0030743230 scopus 로고    scopus 로고
    • Structural mapping of the glycans from the egg glycoproteins of Schistosoma mansoni and Schistosoma japonicum: identification of novel core structures and terminal sequences
    • Khoo K.H., Chatterjee D., Caulfield J.P., Morris H.R., Dell A. Structural mapping of the glycans from the egg glycoproteins of Schistosoma mansoni and Schistosoma japonicum: identification of novel core structures and terminal sequences. Glycobiology 1997, 7:663-677.
    • (1997) Glycobiology , vol.7 , pp. 663-677
    • Khoo, K.H.1    Chatterjee, D.2    Caulfield, J.P.3    Morris, H.R.4    Dell, A.5
  • 40
    • 77950023643 scopus 로고    scopus 로고
    • A comparative proteomic study of the undeveloped and developed Schistosoma mansoni egg and its contents: the miracidium, hatch fluid and secretions
    • Mathieson W., Wilson R.A. A comparative proteomic study of the undeveloped and developed Schistosoma mansoni egg and its contents: the miracidium, hatch fluid and secretions. Int J Parasitol 2010, 40:617-628.
    • (2010) Int J Parasitol , vol.40 , pp. 617-628
    • Mathieson, W.1    Wilson, R.A.2
  • 43
    • 77952089075 scopus 로고    scopus 로고
    • Structural characterization of glycans on omega-1, a major Schistosoma mansoni egg glycoprotein that drives Th2 responses
    • Meevissen M.H., Wuhrer M., Doenhoff M.J., Schramm G., Haas H., Deelder A.M., Hokke C.H. Structural characterization of glycans on omega-1, a major Schistosoma mansoni egg glycoprotein that drives Th2 responses. J Proteome Res 2010, 9:2630-2642.
    • (2010) J Proteome Res , vol.9 , pp. 2630-2642
    • Meevissen, M.H.1    Wuhrer, M.2    Doenhoff, M.J.3    Schramm, G.4    Haas, H.5    Deelder, A.M.6    Hokke, C.H.7
  • 44
    • 78149278914 scopus 로고    scopus 로고
    • A large repertoire of parasite epitopes matched by a large repertoire of host immune receptors in an invertebrate host/parasite model
    • Mone Y., Gourbal B., Duval D., Du Pasquier L., Kieffer-Jaquinod S., Mitta G. A large repertoire of parasite epitopes matched by a large repertoire of host immune receptors in an invertebrate host/parasite model. PLoS Negl Trop Dis 2010, 4:e813.
    • (2010) PLoS Negl Trop Dis , vol.4
    • Mone, Y.1    Gourbal, B.2    Duval, D.3    Du Pasquier, L.4    Kieffer-Jaquinod, S.5    Mitta, G.6
  • 47
    • 84877823906 scopus 로고    scopus 로고
    • In silico analysis of the fucosylation-associated genome of the human blood fluke Schistosoma mansoni: cloning and characterization of the fucosyltransferase multigene family
    • Peterson N.A., Anderson T.K., Yoshino T.P. In silico analysis of the fucosylation-associated genome of the human blood fluke Schistosoma mansoni: cloning and characterization of the fucosyltransferase multigene family. PloS One 2013, 8:e63299.
    • (2013) PloS One , vol.8
    • Peterson, N.A.1    Anderson, T.K.2    Yoshino, T.P.3
  • 48
    • 68049137307 scopus 로고    scopus 로고
    • Glycotope analysis in miracidia and primary sporocysts of Schistosoma mansoni: differential expression during the miracidium-to-sporocyst transformation
    • Peterson N.A., Hokke C.H., Deelder A.M., Yoshino T.P. Glycotope analysis in miracidia and primary sporocysts of Schistosoma mansoni: differential expression during the miracidium-to-sporocyst transformation. Int J Parasitol 2009, 39:1331-1344.
    • (2009) Int J Parasitol , vol.39 , pp. 1331-1344
    • Peterson, N.A.1    Hokke, C.H.2    Deelder, A.M.3    Yoshino, T.P.4
  • 49
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl M.W. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 2001, 29:e45.
    • (2001) Nucleic Acids Res , vol.29
    • Pfaffl, M.W.1
  • 50
    • 33947654354 scopus 로고    scopus 로고
    • Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins
    • Piccard H., Van den Steen P.E., Opdenakker G. Hemopexin domains as multifunctional liganding modules in matrix metalloproteinases and other proteins. J Leukoc Biol 2007, 81:870-892.
    • (2007) J Leukoc Biol , vol.81 , pp. 870-892
    • Piccard, H.1    Van den Steen, P.E.2    Opdenakker, G.3
  • 54
    • 69249156451 scopus 로고    scopus 로고
    • Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion
    • Sabeh F., Li X.Y., Saunders T.L., Rowe R.G., Weiss S.J. Secreted versus membrane-anchored collagenases: relative roles in fibroblast-dependent collagenolysis and invasion. J Biol Chem 2009, 284:23001-23011.
    • (2009) J Biol Chem , vol.284 , pp. 23001-23011
    • Sabeh, F.1    Li, X.Y.2    Saunders, T.L.3    Rowe, R.G.4    Weiss, S.J.5
  • 55
    • 0141989767 scopus 로고    scopus 로고
    • Global gene expression profiles during acute pathogen-induced pulmonary inflammation reveal divergent roles for Th1 and Th2 responses in tissue repair
    • Sandler N.G., Mentink-Kane M.M., Cheever A.W., Wynn T.A. Global gene expression profiles during acute pathogen-induced pulmonary inflammation reveal divergent roles for Th1 and Th2 responses in tissue repair. J Immunol 2003, 171:3655-3667.
    • (2003) J Immunol , vol.171 , pp. 3655-3667
    • Sandler, N.G.1    Mentink-Kane, M.M.2    Cheever, A.W.3    Wynn, T.A.4
  • 57
    • 37348999017 scopus 로고    scopus 로고
    • Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis
    • Shi J., Son M.Y., Yamada S., Szabova L., Kahan S., Chrysovergis K., Wolf L., Surmak A., Holmbeck K. Membrane-type MMPs enable extracellular matrix permissiveness and mesenchymal cell proliferation during embryogenesis. Dev Biol 2008, 313:196-209.
    • (2008) Dev Biol , vol.313 , pp. 196-209
    • Shi, J.1    Son, M.Y.2    Yamada, S.3    Szabova, L.4    Kahan, S.5    Chrysovergis, K.6    Wolf, L.7    Surmak, A.8    Holmbeck, K.9
  • 58
    • 0038575443 scopus 로고    scopus 로고
    • Extracellular matrix remodelling: the role of matrix metalloproteinases
    • Stamenkovic I. Extracellular matrix remodelling: the role of matrix metalloproteinases. J Pathol 2003, 200:448-464.
    • (2003) J Pathol , vol.200 , pp. 448-464
    • Stamenkovic, I.1
  • 60
    • 0033848113 scopus 로고    scopus 로고
    • Angiogenic activity of Onchocerca volvulus recombinant proteins similar to vespid venom antigen 5
    • Tawe W., Pearlman E., Unnasch T.R., Lustigman S. Angiogenic activity of Onchocerca volvulus recombinant proteins similar to vespid venom antigen 5. Mol Biochem Parasitol 2000, 109:91-99.
    • (2000) Mol Biochem Parasitol , vol.109 , pp. 91-99
    • Tawe, W.1    Pearlman, E.2    Unnasch, T.R.3    Lustigman, S.4
  • 61
    • 84880771899 scopus 로고    scopus 로고
    • Cathelicidin-like Helminth Defence Molecules (HDMs): absence of cytotoxic, anti-microbial and anti-protozoan activities imply a specific adaptation to immune modulation
    • Thivierge K., Cotton S., Schaefer D.A., Riggs M.W., To J., Lund M.E., Robinson M.W., Dalton J.P., Donnelly S.M. Cathelicidin-like Helminth Defence Molecules (HDMs): absence of cytotoxic, anti-microbial and anti-protozoan activities imply a specific adaptation to immune modulation. PLoS Negl Trop Dis 2013, 7:e2307.
    • (2013) PLoS Negl Trop Dis , vol.7
    • Thivierge, K.1    Cotton, S.2    Schaefer, D.A.3    Riggs, M.W.4    To, J.5    Lund, M.E.6    Robinson, M.W.7    Dalton, J.P.8    Donnelly, S.M.9
  • 62
    • 0036259938 scopus 로고    scopus 로고
    • Hemopexin: structure, function, and regulation
    • Tolosano E., Altruda F. Hemopexin: structure, function, and regulation. DNA Cell Biol 2002, 21:297-306.
    • (2002) DNA Cell Biol , vol.21 , pp. 297-306
    • Tolosano, E.1    Altruda, F.2
  • 63
    • 84871867341 scopus 로고    scopus 로고
    • Schistosoma mansoni Hemozoin Modulates Alternative activation of macrophages via specific suppression of retnla expression and secretion
    • Truscott M., Evans D.A., Gunn M., Hoffmann K.F. Schistosoma mansoni Hemozoin Modulates Alternative activation of macrophages via specific suppression of retnla expression and secretion. Infect Immun 2013, 81:133-142.
    • (2013) Infect Immun , vol.81 , pp. 133-142
    • Truscott, M.1    Evans, D.A.2    Gunn, M.3    Hoffmann, K.F.4
  • 64
    • 0035892755 scopus 로고    scopus 로고
    • Regulation of hepatic fibrosis and extracellular matrix genes by the th response: new insight into the role of tissue inhibitors of matrix metalloproteinases
    • Vaillant B., Chiaramonte M.G., Cheever A.W., Soloway P.D., Wynn T.A. Regulation of hepatic fibrosis and extracellular matrix genes by the th response: new insight into the role of tissue inhibitors of matrix metalloproteinases. J Immunol 2001, 167:7017-7026.
    • (2001) J Immunol , vol.167 , pp. 7017-7026
    • Vaillant, B.1    Chiaramonte, M.G.2    Cheever, A.W.3    Soloway, P.D.4    Wynn, T.A.5
  • 66
    • 70849122823 scopus 로고    scopus 로고
    • Glycan gimmickry by parasitic helminths: a strategy for modulating the host immune response?
    • van Die I., Cummings R.D. Glycan gimmickry by parasitic helminths: a strategy for modulating the host immune response?. Glycobiology 2010, 20:2-12.
    • (2010) Glycobiology , vol.20 , pp. 2-12
    • van Die, I.1    Cummings, R.D.2
  • 67
    • 84881050928 scopus 로고    scopus 로고
    • Functional genomic characterization of neoblast-like stem cells in larval Schistosoma mansoni
    • Wang B., Collins J.J., Newmark P.A. Functional genomic characterization of neoblast-like stem cells in larval Schistosoma mansoni. Elife 2013, 2:e00768.
    • (2013) Elife , vol.2
    • Wang, B.1    Collins, J.J.2    Newmark, P.A.3
  • 68
    • 58549116678 scopus 로고    scopus 로고
    • Proteomic analysis of Schistosoma mansoni proteins released during in vitro miracidium-to-sporocyst transformation
    • Wu X.J., Sabat G., Brown J.F., Zhang M., Taft A., Peterson N., Harms A., Yoshino T.P. Proteomic analysis of Schistosoma mansoni proteins released during in vitro miracidium-to-sporocyst transformation. Mol Biochem Parasitol 2009, 164:32-44.
    • (2009) Mol Biochem Parasitol , vol.164 , pp. 32-44
    • Wu, X.J.1    Sabat, G.2    Brown, J.F.3    Zhang, M.4    Taft, A.5    Peterson, N.6    Harms, A.7    Yoshino, T.P.8
  • 69
  • 71
    • 33646927292 scopus 로고    scopus 로고
    • Mass spectrometry of proton adducts of fucosylated N-glycans: fucose transfer between antennae gives rise to misleading fragments
    • Wuhrer M., Koeleman C.A., Hokke C.H., Deelder A.M. Mass spectrometry of proton adducts of fucosylated N-glycans: fucose transfer between antennae gives rise to misleading fragments. Rapid Commun Mass Spectrom 2006, 20:1747-1754.
    • (2006) Rapid Commun Mass Spectrom , vol.20 , pp. 1747-1754
    • Wuhrer, M.1    Koeleman, C.A.2    Hokke, C.H.3    Deelder, A.M.4
  • 72
    • 0028840320 scopus 로고
    • Production of Schistosoma mansoni daughter sporocysts from mother sporocysts maintained in synxenic culture with Biomphalaria glabrata embryonic (Bge) cells
    • Yoshino T.P., Laursen J.R. Production of Schistosoma mansoni daughter sporocysts from mother sporocysts maintained in synxenic culture with Biomphalaria glabrata embryonic (Bge) cells. J Parasitol 1995, 81:714-722.
    • (1995) J Parasitol , vol.81 , pp. 714-722
    • Yoshino, T.P.1    Laursen, J.R.2
  • 73
    • 84859201461 scopus 로고    scopus 로고
    • Glycotope sharing between snail hemolymph and larval schistosomes: larval transformation products alter shared glycan patterns of plasma proteins
    • Yoshino T.P., Wu X.J., Liu H., Gonzalez L.A., Deelder A.M., Hokke C.H. Glycotope sharing between snail hemolymph and larval schistosomes: larval transformation products alter shared glycan patterns of plasma proteins. PLoS Negl Trop Dis 2012, 6:e1569.
    • (2012) PLoS Negl Trop Dis , vol.6
    • Yoshino, T.P.1    Wu, X.J.2    Liu, H.3    Gonzalez, L.A.4    Deelder, A.M.5    Hokke, C.H.6


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