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Volumn 6, Issue 10, 2007, Pages 1905-1912

Internal and surface-localized major surface proteases of Leishmania spp. and their differential release from promastigotes

Author keywords

[No Author keywords available]

Indexed keywords

BETA CYCLODEXTRIN DERIVATIVE; COLLAGEN; ISOENZYME; LAMININ; MATRIGEL; METHYL BETA CYCLODEXTRIN; METHYL-BETA-CYCLODEXTRIN; PEPTIDE HYDROLASE; PROTEOGLYCAN; UNCLASSIFIED DRUG;

EID: 35348923020     PISSN: 15359778     EISSN: None     Source Type: Journal    
DOI: 10.1128/EC.00073-07     Document Type: Article
Times cited : (24)

References (49)
  • 1
    • 0027509513 scopus 로고
    • Expression of lipophosphoglycan, high-molecular-weight phosphoglycan and glycoprotein 63 in promastigotes and amastigotes of Leishmania mexicana
    • Bahr, V., Y. D. Stierhof, T. Ilg, M. Demar, M. Quinten, and P. Overath. 1993. Expression of lipophosphoglycan, high-molecular-weight phosphoglycan and glycoprotein 63 in promastigotes and amastigotes of Leishmania mexicana. Mol. Biochem. Parasitol. 58:107-121.
    • (1993) Mol. Biochem. Parasitol , vol.58 , pp. 107-121
    • Bahr, V.1    Stierhof, Y.D.2    Ilg, T.3    Demar, M.4    Quinten, M.5    Overath, P.6
  • 2
    • 34249819334 scopus 로고    scopus 로고
    • Plasmodium yoelii: Combinatorial expression of variants of the 235-kDa rhoptry antigen during infection
    • Bayele, H. K., and K. N. Brown. 2007. Plasmodium yoelii: combinatorial expression of variants of the 235-kDa rhoptry antigen during infection. Exp. Parasitol. 116:354-360.
    • (2007) Exp. Parasitol , vol.116 , pp. 354-360
    • Bayele, H.K.1    Brown, K.N.2
  • 3
    • 35348909001 scopus 로고    scopus 로고
    • Bonifacino, J. S. 1998. Metabolic labeling with amino acids, p. 10.18.11-10.18.10. In F. M. Ausubel, R. Brent, R. E. Knigston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, 2. John Wiley & Sons, Inc., New York, NY.
    • Bonifacino, J. S. 1998. Metabolic labeling with amino acids, p. 10.18.11-10.18.10. In F. M. Ausubel, R. Brent, R. E. Knigston, D. D. Moore, J. G. Seidman, J. A. Smith, and K. Struhl (ed.), Current protocols in molecular biology, vol. 2. John Wiley & Sons, Inc., New York, NY.
  • 4
    • 0019887744 scopus 로고
    • Phase separation of integral membrane proteins in Triton X-114 solution
    • Bordier, C. 1981. Phase separation of integral membrane proteins in Triton X-114 solution. J. Biol. Chem. 256:1604-1607.
    • (1981) J. Biol. Chem , vol.256 , pp. 1604-1607
    • Bordier, C.1
  • 5
  • 6
    • 0035862695 scopus 로고    scopus 로고
    • Regulation of GP63 mRNA stability in promastigotes of virulent and attenuated Leishmania chagasi
    • Brittingham, A., M. A. Miller, J. E. Donelson, and M. E. Wilson. 2001. Regulation of GP63 mRNA stability in promastigotes of virulent and attenuated Leishmania chagasi. Mol. Biochem. Parasitol. 112:51-59.
    • (2001) Mol. Biochem. Parasitol , vol.112 , pp. 51-59
    • Brittingham, A.1    Miller, M.A.2    Donelson, J.E.3    Wilson, M.E.4
  • 7
    • 32444441225 scopus 로고    scopus 로고
    • A zymographic study of metalloprotease activities in extracts and extracellular secretions of Leishmania (Viannia) braziliensis strains
    • Cuervo, P., L. Saboia-Vahia, F. Costa Silva-Filho, O. Fernandes, E. Cupolillo, and J. B. de Jesus. 2006. A zymographic study of metalloprotease activities in extracts and extracellular secretions of Leishmania (Viannia) braziliensis strains. Parasitology 132:177-185.
    • (2006) Parasitology , vol.132 , pp. 177-185
    • Cuervo, P.1    Saboia-Vahia, L.2    Costa Silva-Filho, F.3    Fernandes, O.4    Cupolillo, E.5    de Jesus, J.B.6
  • 8
    • 0026592139 scopus 로고
    • Human leishmaniases: Epidemiology and public health aspects
    • Desjeux, P. 1992. Human leishmaniases: epidemiology and public health aspects. World Health Stat. Q. 45:267-275.
    • (1992) World Health Stat. Q , vol.45 , pp. 267-275
    • Desjeux, P.1
  • 9
    • 3042555141 scopus 로고    scopus 로고
    • Leishmaniasis: Current situation and new perspectives
    • Desjeux, P. 2004. Leishmaniasis: current situation and new perspectives. Comp. Immunol. Microbiol. Infect. Dis. 27:305-318.
    • (2004) Comp. Immunol. Microbiol. Infect. Dis , vol.27 , pp. 305-318
    • Desjeux, P.1
  • 10
    • 30144438749 scopus 로고    scopus 로고
    • Leishmanolysin (gp63 metallopeptidase)-like activity extracellularly released by Herpetomonas samuelpessoai
    • Elias, C. G., F. M. Pereira, B. A. Silva, C. S. Alviano, R. M. Soares, and A. L. Santos. 2006. Leishmanolysin (gp63 metallopeptidase)-like activity extracellularly released by Herpetomonas samuelpessoai. Parasitology 132:37-47.
    • (2006) Parasitology , vol.132 , pp. 37-47
    • Elias, C.G.1    Pereira, F.M.2    Silva, B.A.3    Alviano, C.S.4    Soares, R.M.5    Santos, A.L.6
  • 11
    • 0030664774 scopus 로고    scopus 로고
    • African trypanosomes have differentially expressed genes encoding homologues of the Leishmania GP63 surface protease
    • El-Sayed, N. M., and J. E. Donelson. 1997. African trypanosomes have differentially expressed genes encoding homologues of the Leishmania GP63 surface protease. J. Biol. Chem. 272:26742-26748.
    • (1997) J. Biol. Chem , vol.272 , pp. 26742-26748
    • El-Sayed, N.M.1    Donelson, J.E.2
  • 12
    • 22244453726 scopus 로고    scopus 로고
    • El-Sayed, N. M, P. J. Myler, D. C. Bartholomew D. Nilsson, G. Aggarwal, A. N. Tran, E. Ghedin, E. A. Worthey, A. L. Delcher, G. Blandin, S. J. Westenberger, E. Caler, G. C. Cerqueira, C. Branche, B. Haas, A. Anupama, E. Arner, L. Aslund, P. Attipoe, E. Bontempi, F. Bringaud, P. Burton, E. Cadag, D. A. Campbell, M. Carrington, J. Crabtree, H. Darban, J. F. da Silveira, P. de Jong, K. Edwards, P. T. Englund, G. Fazelina, T. Feldblyum, M. Ferella, A. C. Frasch, K. Gull, D. Horn, L. Hou, Y. Huang, E. Kindlund, M. Klingbeil, S. Kluge, H. Koo, D. Lacerda, M. J. Levin, H. Lorenzi, T. Louie, C. R. Machado, R. McCulloch, A. McKenna, Y. Mizuno, J. C. Mottram, S. Nelson, S. Ochaya, K. Osoegawa, G. Pai, M. Parsons, M. Pentony, U. Pettersson, M. Pop, J. L. Ramirez, J. Rinta, L. Robertson, S. L. Salzberg, D. O. Sanchez, A. Seyler, R. Sharma, J. Shetty, A. J. Simpson, E. Sisk, M. T. Tammi, R. Tarleton, S. Teixeira, S. Van Aken, C. Vogt, P. N. Ward, B. Wickstead, J. Wortman, O. White, C. M. Fraser
    • El-Sayed, N. M., P. J. Myler, D. C. Bartholomew D. Nilsson, G. Aggarwal, A. N. Tran, E. Ghedin, E. A. Worthey, A. L. Delcher, G. Blandin, S. J. Westenberger, E. Caler, G. C. Cerqueira, C. Branche, B. Haas, A. Anupama, E. Arner, L. Aslund, P. Attipoe, E. Bontempi, F. Bringaud, P. Burton, E. Cadag, D. A. Campbell, M. Carrington, J. Crabtree, H. Darban, J. F. da Silveira, P. de Jong, K. Edwards, P. T. Englund, G. Fazelina, T. Feldblyum, M. Ferella, A. C. Frasch, K. Gull, D. Horn, L. Hou, Y. Huang, E. Kindlund, M. Klingbeil, S. Kluge, H. Koo, D. Lacerda, M. J. Levin, H. Lorenzi, T. Louie, C. R. Machado, R. McCulloch, A. McKenna, Y. Mizuno, J. C. Mottram, S. Nelson, S. Ochaya, K. Osoegawa, G. Pai, M. Parsons, M. Pentony, U. Pettersson, M. Pop, J. L. Ramirez, J. Rinta, L. Robertson, S. L. Salzberg, D. O. Sanchez, A. Seyler, R. Sharma, J. Shetty, A. J. Simpson, E. Sisk, M. T. Tammi, R. Tarleton, S. Teixeira, S. Van Aken, C. Vogt, P. N. Ward, B. Wickstead, J. Wortman, O. White, C. M. Fraser, K. D. Stuart, and B. Andersson. 2005. The genome sequence of Trypanosoma cruzi, etiologic agent of Chagas disease. Science 309:409-415.
  • 13
    • 0026516594 scopus 로고
    • Identification of a surface metalloproteinase on 13 species of Leishmania isolated from humans, Cnthidia fasciculata, and Herpetomonas samuelpessoai
    • Etges, R. 1992. Identification of a surface metalloproteinase on 13 species of Leishmania isolated from humans, Cnthidia fasciculata, and Herpetomonas samuelpessoai. Acta Trop. 50:205-217.
    • (1992) Acta Trop , vol.50 , pp. 205-217
    • Etges, R.1
  • 14
    • 0037947831 scopus 로고    scopus 로고
    • Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors
    • Foster, L. J., C. L. De Hoog, and M. Mann. 2003. Unbiased quantitative proteomics of lipid rafts reveals high specificity for signaling factors. Proc. Natl. Acad. Sci. USA 100:5813-5818.
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5813-5818
    • Foster, L.J.1    De Hoog, C.L.2    Mann, M.3
  • 15
    • 4043075522 scopus 로고    scopus 로고
    • The Py235 proteins: Glimpses into the versatility of a malaria multigene family
    • Gruner, A. C., G. Snounou, K. Fuller, W. Jarra, L. Renia, and P. R. Preiser. 2004. The Py235 proteins: glimpses into the versatility of a malaria multigene family. Microbes Infect. 6:864-873.
    • (2004) Microbes Infect , vol.6 , pp. 864-873
    • Gruner, A.C.1    Snounou, G.2    Fuller, K.3    Jarra, W.4    Renia, L.5    Preiser, P.R.6
  • 16
    • 2442649946 scopus 로고    scopus 로고
    • Down-regulation of gp63 in Leishmania amazonensis reduces its early development in Lutzomyia longipalpis
    • Hajmova, M., K. P. Chang, B. Kolli, and P. Volf. 2004. Down-regulation of gp63 in Leishmania amazonensis reduces its early development in Lutzomyia longipalpis. Microbes Infect. 6:646-649.
    • (2004) Microbes Infect , vol.6 , pp. 646-649
    • Hajmova, M.1    Chang, K.P.2    Kolli, B.3    Volf, P.4
  • 17
    • 0035818530 scopus 로고    scopus 로고
    • Cholesterol depletion induces large scale domain segregation in living cell membranes
    • Hao, M., S. Mukherjee, and F. R. Maxfield. 2001. Cholesterol depletion induces large scale domain segregation in living cell membranes. Proc. Natl. Acad. Sci. USA 98:13072-13077.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 13072-13077
    • Hao, M.1    Mukherjee, S.2    Maxfield, F.R.3
  • 18
    • 0141991014 scopus 로고    scopus 로고
    • Extracellular release of the surface metalloprotease, gp63, from Leishmania and insect trypanosomatids
    • Jaffe, C. L., and D. M. Dwyer. 2003. Extracellular release of the surface metalloprotease, gp63, from Leishmania and insect trypanosomatids. Parasitol. Res. 91:229-237.
    • (2003) Parasitol. Res , vol.91 , pp. 229-237
    • Jaffe, C.L.1    Dwyer, D.M.2
  • 19
    • 0025122367 scopus 로고
    • Stable transfection of the human parasite Leishmania major delineates a 30-kilobase region sufficient for extrachromosomal replication and expression
    • Kapler, G. M., C. M. Coburn, and S. M. Beverley. 1990. Stable transfection of the human parasite Leishmania major delineates a 30-kilobase region sufficient for extrachromosomal replication and expression. Mol. Cell. Biol. 10:1084-1094.
    • (1990) Mol. Cell. Biol , vol.10 , pp. 1084-1094
    • Kapler, G.M.1    Coburn, C.M.2    Beverley, S.M.3
  • 20
    • 0034853629 scopus 로고    scopus 로고
    • The 235-kDa rhoptry protein of Plasmodium (yoelii) yoelii: Function at the junction
    • Khan, S. M., W. Jarra, and P. R. Preiser. 2001. The 235-kDa rhoptry protein of Plasmodium (yoelii) yoelii: function at the junction. Mol. Biochem. Parasitol. 117:1-10.
    • (2001) Mol. Biochem. Parasitol , vol.117 , pp. 1-10
    • Khan, S.M.1    Jarra, W.2    Preiser, P.R.3
  • 21
    • 0035826909 scopus 로고    scopus 로고
    • Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretasc; ADAM 10
    • Kojro, E., G. Gimpl, S. Lammich, W. Marz, and F. Fahrenholz. 2001. Low cholesterol stimulates the nonamyloidogenic pathway by its effect on the alpha-secretasc; ADAM 10. Proc. Natl. Acad. Sci. USA 98:5815-5820.
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 5815-5820
    • Kojro, E.1    Gimpl, G.2    Lammich, S.3    Marz, W.4    Fahrenholz, F.5
  • 22
    • 0027975364 scopus 로고
    • Identification by extrachromosomal amplification and overexpression of a zeta-ciystallin/NADPH-oxidoreductase homologue constitutively expressed in Leishmania spp
    • Liu, X., and K. P. Chang. 1994. Identification by extrachromosomal amplification and overexpression of a zeta-ciystallin/NADPH-oxidoreductase homologue constitutively expressed in Leishmania spp. Mol. Biochem. Parasitol. 66:201-210.
    • (1994) Mol. Biochem. Parasitol , vol.66 , pp. 201-210
    • Liu, X.1    Chang, K.P.2
  • 23
    • 0028972393 scopus 로고
    • Analysis of the active site and activation mechanism of the Leishmania surface metalloproteinase GP63
    • Macdonald, M. H., C. J. Morrison, and W. R. McMaster. 1995. Analysis of the active site and activation mechanism of the Leishmania surface metalloproteinase GP63. Biochim. Biophys. Acta 1253:199-207.
    • (1995) Biochim. Biophys. Acta , vol.1253 , pp. 199-207
    • Macdonald, M.H.1    Morrison, C.J.2    McMaster, W.R.3
  • 24
    • 0038644451 scopus 로고    scopus 로고
    • Membrane cholesterol regulates LFA-1 function and lipid raft heterogeneity
    • Marwali, M. R., J. Rey-Ladino, L. Dreolini, D. Shaw, and F. Takei. 2003. Membrane cholesterol regulates LFA-1 function and lipid raft heterogeneity. Blood 102:215-222.
    • (2003) Blood , vol.102 , pp. 215-222
    • Marwali, M.R.1    Rey-Ladino, J.2    Dreolini, L.3    Shaw, D.4    Takei, F.5
  • 25
    • 0037305054 scopus 로고    scopus 로고
    • Migration through the extracellular matrix by the parasitic protozoan Leishmania is enhanced by surface metalloprotease gp63
    • McGwire, B. S., K. P. Chang, and D. M. Engman. 2003. Migration through the extracellular matrix by the parasitic protozoan Leishmania is enhanced by surface metalloprotease gp63. Infect. Immun. 71:1008-1010.
    • (2003) Infect. Immun , vol.71 , pp. 1008-1010
    • McGwire, B.S.1    Chang, K.P.2    Engman, D.M.3
  • 26
    • 0037088686 scopus 로고    scopus 로고
    • Extracellular release of the glycosylphosphatidylinositol (GPI)-linked Leishmania surface metalloprotease, Gp63, is independent of GPI phospholipolysis: Implications for parasite virulence
    • McGwire, B. S., W. A. O'Connell, K. P. Chang, and D. M. Engman. 2002. Extracellular release of the glycosylphosphatidylinositol (GPI)-linked Leishmania surface metalloprotease, Gp63, is independent of GPI phospholipolysis: implications for parasite virulence. J. Biol. Chem. 277:8802-8809.
    • (2002) J. Biol. Chem , vol.277 , pp. 8802-8809
    • McGwire, B.S.1    O'Connell, W.A.2    Chang, K.P.3    Engman, D.M.4
  • 28
    • 34347339518 scopus 로고    scopus 로고
    • Peacock, C. S., K. Seeger, D. Harris, L. Murphy, J. C. Ruiz, M. A. Quail, N. Peters, E. Adlem, A. Tivey, M. Aslett, A. Kerhornou, A. Ivens, A. Fraser, M. A. Rajandream, T. Carver, H. Norbertczak, T. Chillingworth, Z. Hance, K. Jagels, S. Moule, D. Ormond, S. Rutter, R. Squares, S. Whitehead, E. Rabbinowitsch, C. Arrowsmith, B. White, S. Thurston, F. Bringaud, S. L. Baldauf, A. Faulconbridge, D. Jeffares, D. P. Depledge, S. O. Oyola, J. D. Hilley, L. O. Brito, L. R. Tosi, B. Barrell, A. K. Cruz, J. C. Mottram, D. F. Smith, and M. Berriman. 2007. Comparative genomic analysis of three Leishmania species that cause diverse human disease. Nat. Genet. 39:839-847.
    • Peacock, C. S., K. Seeger, D. Harris, L. Murphy, J. C. Ruiz, M. A. Quail, N. Peters, E. Adlem, A. Tivey, M. Aslett, A. Kerhornou, A. Ivens, A. Fraser, M. A. Rajandream, T. Carver, H. Norbertczak, T. Chillingworth, Z. Hance, K. Jagels, S. Moule, D. Ormond, S. Rutter, R. Squares, S. Whitehead, E. Rabbinowitsch, C. Arrowsmith, B. White, S. Thurston, F. Bringaud, S. L. Baldauf, A. Faulconbridge, D. Jeffares, D. P. Depledge, S. O. Oyola, J. D. Hilley, L. O. Brito, L. R. Tosi, B. Barrell, A. K. Cruz, J. C. Mottram, D. F. Smith, and M. Berriman. 2007. Comparative genomic analysis of three Leishmania species that cause diverse human disease. Nat. Genet. 39:839-847.
  • 29
    • 8644255077 scopus 로고    scopus 로고
    • Tumor necrosis factor alpha induces human atrial myofibroblast proliferation, invasion and MMP-9 secretion: Inhibition by simvastatin
    • Porter, K. E., N. A. Turner, D. J. O'Regan, and S. G. Ball. 2004. Tumor necrosis factor alpha induces human atrial myofibroblast proliferation, invasion and MMP-9 secretion: inhibition by simvastatin. Cardiovasc. Res. 64:507-515.
    • (2004) Cardiovasc. Res , vol.64 , pp. 507-515
    • Porter, K.E.1    Turner, N.A.2    O'Regan, D.J.3    Ball, S.G.4
  • 30
    • 0033561460 scopus 로고    scopus 로고
    • A rhoptryprotein-associated mechanism of clonal phenotypic variation in rodent malaria
    • Preiser, P. R., W. Jarra, T. Capiod, and G. Snounou. 1999. A rhoptryprotein-associated mechanism of clonal phenotypic variation in rodent malaria. Nature 398:618-622.
    • (1999) Nature , vol.398 , pp. 618-622
    • Preiser, P.R.1    Jarra, W.2    Capiod, T.3    Snounou, G.4
  • 31
    • 0346787814 scopus 로고    scopus 로고
    • Cholesterol is required for Leishmania donovani infection: Implications in leishmaniasis
    • Pucadyil, T. J., P. Tewary, R. Madhubala, and A. Chattopadhyay. 2004. Cholesterol is required for Leishmania donovani infection: implications in leishmaniasis. Mol. Biochem. Parasitol. 133:145-152.
    • (2004) Mol. Biochem. Parasitol , vol.133 , pp. 145-152
    • Pucadyil, T.J.1    Tewary, P.2    Madhubala, R.3    Chattopadhyay, A.4
  • 32
    • 19344371567 scopus 로고    scopus 로고
    • Regulation of genes encoding the major surface protease of Leishmania chagasi via mRNA stability
    • Purdy, J. E., J. E. Donelson, and M. E. Wilson. 2005. Regulation of genes encoding the major surface protease of Leishmania chagasi via mRNA stability. Mol. Biochem. Parasitol. 142:88-97.
    • (2005) Mol. Biochem. Parasitol , vol.142 , pp. 88-97
    • Purdy, J.E.1    Donelson, J.E.2    Wilson, M.E.3
  • 33
    • 0026598731 scopus 로고
    • Three distinct RNAs for the surface protease gp63 are differentially expressed during development of Leishmania donovani chagasi promastigotes to an infectious form
    • Ramamoorthy, R., J. E. Donelson, K. E. Paetz, M. Maybodi, S. C. Roberts, and M. E. Wilson. 1992. Three distinct RNAs for the surface protease gp63 are differentially expressed during development of Leishmania donovani chagasi promastigotes to an infectious form. J. Biol. Chem. 267:1888-1895.
    • (1992) J. Biol. Chem , vol.267 , pp. 1888-1895
    • Ramamoorthy, R.1    Donelson, J.E.2    Paetz, K.E.3    Maybodi, M.4    Roberts, S.C.5    Wilson, M.E.6
  • 34
    • 10844291804 scopus 로고    scopus 로고
    • Cysteine cathepsins are central contributors of invasion by cultured adenosylmethionine decarboxylase-transformed rodent fibroblasts
    • Ravanko, K., K. Jarvinen, J. Helin, N. Kalkkinen, and E. Holtta. 2004. Cysteine cathepsins are central contributors of invasion by cultured adenosylmethionine decarboxylase-transformed rodent fibroblasts. Cancer Res. 64:8831-8838.
    • (2004) Cancer Res , vol.64 , pp. 8831-8838
    • Ravanko, K.1    Jarvinen, K.2    Helin, J.3    Kalkkinen, N.4    Holtta, E.5
  • 36
    • 0024390249 scopus 로고
    • Metacyclogenesis in Leishmania promastigotes
    • Sacks, D. L. 1989. Metacyclogenesis in Leishmania promastigotes. Exp. Parasitol. 69:100-103.
    • (1989) Exp. Parasitol , vol.69 , pp. 100-103
    • Sacks, D.L.1
  • 37
    • 33845428139 scopus 로고    scopus 로고
    • The ubiquitous gp63-like metalloprotease from lower tiypanosomatids: In the search for a function
    • Santos, A. L., M. H. Branquinha, and C. M. D'Avila-Levy. 2006. The ubiquitous gp63-like metalloprotease from lower tiypanosomatids: in the search for a function. An. Acad. Bras. Cienc. 78:687-714.
    • (2006) An. Acad. Bras. Cienc , vol.78 , pp. 687-714
    • Santos, A.L.1    Branquinha, M.H.2    D'Avila-Levy, C.M.3
  • 38
    • 0033953643 scopus 로고    scopus 로고
    • Malaria multigene families: The price of chronicity
    • Snounou, G., W. Jarra, and P. R. Preiser. 2000. Malaria multigene families: the price of chronicity. Parasitol. Today 16:28-30.
    • (2000) Parasitol. Today , vol.16 , pp. 28-30
    • Snounou, G.1    Jarra, W.2    Preiser, P.R.3
  • 39
    • 23944499321 scopus 로고    scopus 로고
    • Complexity of the major surface protease (msp) gene organization in Leishmania (Viannia) braziliensis: Evolutionary and functional implications
    • Victoir, K., J. Arevalo, S. De Doncker, D. C. Barker, T. Laurent, E. Godfroid, A. Bollen, D. Le Ray, and J. C. Dujardin. 2005. Complexity of the major surface protease (msp) gene organization in Leishmania (Viannia) braziliensis: evolutionary and functional implications. Parasitology 131:207-214.
    • (2005) Parasitology , vol.131 , pp. 207-214
    • Victoir, K.1    Arevalo, J.2    De Doncker, S.3    Barker, D.C.4    Laurent, T.5    Godfroid, E.6    Bollen, A.7    Le Ray, D.8    Dujardin, J.C.9
  • 41
    • 0032523872 scopus 로고    scopus 로고
    • Differentially expressed Leishmania major gp63 genes encode cell surface leishmanolysin with distinct signals for glycosylphosphatidylinositol attachment
    • Voth, B. R., B. L. Kelly, P. B. Joshi, A. C. Ivens, and W. R. McMaster. 1998. Differentially expressed Leishmania major gp63 genes encode cell surface leishmanolysin with distinct signals for glycosylphosphatidylinositol attachment. Mol. Biochem. Parasitol. 93:31-41.
    • (1998) Mol. Biochem. Parasitol , vol.93 , pp. 31-41
    • Voth, B.R.1    Kelly, B.L.2    Joshi, P.B.3    Ivens, A.C.4    McMaster, W.R.5
  • 42
    • 0034496239 scopus 로고    scopus 로고
    • Distribution of GPI-anchored proteins in the protozoan parasite Leishmania, based on an improved ultrastructural description using high-pressure frozen cells
    • Weise, F., Y. D. Stierhof, C. Kuhn, M. Wiese, and P. Overath. 2000. Distribution of GPI-anchored proteins in the protozoan parasite Leishmania, based on an improved ultrastructural description using high-pressure frozen cells. J. Cell Sci. 113(Pt. 24):4587-4603.
    • (2000) J. Cell Sci , vol.113 , Issue.PART. 24 , pp. 4587-4603
    • Weise, F.1    Stierhof, Y.D.2    Kuhn, C.3    Wiese, M.4    Overath, P.5
  • 43
    • 0024395616 scopus 로고
    • Expression of the major surface glycoprotein of Leishmania donovani chagasi in virulent and attenuated promastigotes
    • Wilson, M. E., K. K. Hardin, and J. E. Donelson. 1989. Expression of the major surface glycoprotein of Leishmania donovani chagasi in virulent and attenuated promastigotes. J. Immunol. 143:678-684.
    • (1989) J. Immunol , vol.143 , pp. 678-684
    • Wilson, M.E.1    Hardin, K.K.2    Donelson, J.E.3
  • 44
    • 0027306112 scopus 로고
    • The effect of ongoing protein synthesis on the steady-state levels of Gp63 RNAs in Leishmania chagasi
    • Wilson, M. E., K. E. Paetz, R. Ramamoorthy, and J. E. Donelson. 1993. The effect of ongoing protein synthesis on the steady-state levels of Gp63 RNAs in Leishmania chagasi. J. Biol. Chem. 268:15731-15736.
    • (1993) J. Biol. Chem , vol.268 , pp. 15731-15736
    • Wilson, M.E.1    Paetz, K.E.2    Ramamoorthy, R.3    Donelson, J.E.4
  • 45
    • 0141888314 scopus 로고    scopus 로고
    • The major surface protease (MSP or GP63) of Leishmania sp. Biosynthesis, regulation of expression, and function
    • Yao, C., J. E. Donelson, and M. E. Wilson. 2003. The major surface protease (MSP or GP63) of Leishmania sp. Biosynthesis, regulation of expression, and function. Mol. Biochem. Parasitol. 132:1-16.
    • (2003) Mol. Biochem. Parasitol , vol.132 , pp. 1-16
    • Yao, C.1    Donelson, J.E.2    Wilson, M.E.3
  • 47
    • 12344252118 scopus 로고    scopus 로고
    • Internal and surface subpopulations of the major surface protease (MSP) of Leishmania chagasi
    • Yao, C., J. Luo, C. Hsiao, J. E. Donelson, and M. E. Wilson. 2005. Internal and surface subpopulations of the major surface protease (MSP) of Leishmania chagasi. Mol. Biochem. Parasitol. 139:173-183.
    • (2005) Mol. Biochem. Parasitol , vol.139 , pp. 173-183
    • Yao, C.1    Luo, J.2    Hsiao, C.3    Donelson, J.E.4    Wilson, M.E.5
  • 48
    • 1942542161 scopus 로고    scopus 로고
    • Multiple products of the Leishmania chagasi major surface protease (MSP or GP63) gene family
    • Yao, C., J. Luo, P. Storlie, J. E. Donelson, and M. E. Wilson. 2004. Multiple products of the Leishmania chagasi major surface protease (MSP or GP63) gene family. Mol. Biochem. Parasitol. 135:171-183.
    • (2004) Mol. Biochem. Parasitol , vol.135 , pp. 171-183
    • Yao, C.1    Luo, J.2    Storlie, P.3    Donelson, J.E.4    Wilson, M.E.5
  • 49
    • 0025887577 scopus 로고
    • Hydrogen peroxide-mediated toxicity for Leishmania donovani chagasi promastigotes. Role of hydroxyl radical and protection by heat shock
    • Zarley, J. H., B. E. Britigan, and M. E. Wilson. 1991. Hydrogen peroxide-mediated toxicity for Leishmania donovani chagasi promastigotes. Role of hydroxyl radical and protection by heat shock. J. Clin. Investig. 88:1511-1521.
    • (1991) J. Clin. Investig , vol.88 , pp. 1511-1521
    • Zarley, J.H.1    Britigan, B.E.2    Wilson, M.E.3


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