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Volumn 188, Issue 4, 2012, Pages 1942-1952

Trypanosoma cruzi immune evasion mediated by host cell-derived microvesicles

Author keywords

[No Author keywords available]

Indexed keywords

CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; TRANSFORMING GROWTH FACTOR BETA;

EID: 84856887544     PISSN: 00221767     EISSN: 15506606     Source Type: Journal    
DOI: 10.4049/jimmunol.1102053     Document Type: Article
Times cited : (132)

References (58)
  • 3
    • 0023240026 scopus 로고
    • Trypanolytic activity and antibodies to metacyclic trypomastigotes of Trypanosoma cruzi in non-Chagasic human sera
    • Yoshida, N., and M. F. Araguth. 1987. Trypanolytic activity and antibodies to metacyclic trypomastigotes of Trypanosoma cruzi in non-Chagasic human sera. Parasite Immunol. 9: 389-393. (Pubitemid 17074204)
    • (1987) Parasite Immunology , vol.9 , Issue.3 , pp. 389-393
    • Yoshida, N.1    Araguth, M.F.2
  • 4
    • 0025803681 scopus 로고
    • Complement-mediated lysis of Trypanosoma cruzi trypomastigotes by human anti-alpha-galactosyl antibodies
    • Almeida, I. C., S. R. Milani, P. A. Gorin, and L. R. Travassos. 1991. Complement-mediated lysis of Trypanosoma cruzi trypomastigotes by human anti-alpha-galactosyl antibodies. J. Immunol. 146: 2394-2400.
    • (1991) J. Immunol. , vol.146 , pp. 2394-2400
    • Almeida, I.C.1    Milani, S.R.2    Gorin, P.A.3    Travassos, L.R.4
  • 5
    • 0018407794 scopus 로고
    • Membrane-bound antibodies to bloodstream Trypanosoma cruzi in mice: Strain differences in susceptibility to complement-mediated lysis
    • Krettli, A. U., P. Weisz-Carrington, and R. S. Nussenzweig. 1979. Membrane-bound antibodies to bloodstream Trypanosoma cruzi in mice: strain differences in susceptibility to complement-mediated lysis. Clin. Exp. Immunol. 37: 416-423. (Pubitemid 9238280)
    • (1979) Clinical and Experimental Immunology , vol.37 , Issue.3 , pp. 416-423
    • Krettli, A.U.1    Weisz-Carrington, P.2    Nussenzweig, R.S.3
  • 6
    • 0033963255 scopus 로고    scopus 로고
    • The targets of the lytic antibody response against Trypanosoma cruzi
    • Krautz, G. M., J. C. Kissinger, and A. U. Krettli. 2000. The targets of the lytic antibody response against Trypanosoma cruzi. Parasitol. Today (Regul.Ed.) 16: 31-34.
    • (2000) Parasitol. Today (Regul.Ed.) , vol.16 , pp. 31-34
    • Krautz, G.M.1    Kissinger, J.C.2    Krettli, A.U.3
  • 7
    • 79952118301 scopus 로고    scopus 로고
    • Inefficient complement system clearance of Trypanosoma cruzi metacyclic trypomastigotes enables resistant strains to invade eukaryotic cells
    • Cestari, I., and M. I. Ramirez. 2010. Inefficient complement system clearance of Trypanosoma cruzi metacyclic trypomastigotes enables resistant strains to invade eukaryotic cells. PLoS One 5: e9721.
    • (2010) PLoS One , vol.5
    • Cestari, I.1    Ramirez, M.I.2
  • 8
    • 33644981279 scopus 로고    scopus 로고
    • Molecular basis of mammalian cell invasion by Trypanosoma cruzi
    • Yoshida, N. 2006. Molecular basis of mammalian cell invasion by Trypanosoma cruzi. An. Acad. Bras. Cienc. 78: 87-111.
    • (2006) An. Acad. Bras. Cienc. , vol.78 , pp. 87-111
    • Yoshida, N.1
  • 9
    • 0028923312 scopus 로고
    • Lysosome recruitment during host cell invasion by Trypanosoma cruzi
    • Andrews, N. W. 1995. Lysosome recruitment during host cell invasion by Trypanosoma cruzi. Trends Cell Biol. 5: 133-137.
    • (1995) Trends Cell Biol. , vol.5 , pp. 133-137
    • Andrews, N.W.1
  • 10
    • 43049139913 scopus 로고    scopus 로고
    • Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from tumour cells
    • DOI 10.1038/ncb1725, PII NCB1725
    • Al-Nedawi, K., B. Meehan, J. Micallef, V. Lhotak, L. May, A. Guha, and J. Rak. 2008. Intercellular transfer of the oncogenic receptor EGFRvIII by microvesicles derived from tumour cells. Nat. Cell Biol. 10: 619-624. (Pubitemid 351627382)
    • (2008) Nature Cell Biology , vol.10 , Issue.5 , pp. 619-624
    • Al-Nedawi, K.1    Meehan, B.2    Micallef, J.3    Lhotak, V.4    May, L.5    Guha, A.6    Rak, J.7
  • 11
    • 0033929004 scopus 로고    scopus 로고
    • Transfer of the chemokine receptor CCR5 between cells by membrane- derived microparticles: A mechanism for cellular human immunodeficiency virus 1 infection
    • DOI 10.1038/77498
    • Mack, M., A. Kleinschmidt, H. Brühl, C. Klier, P. J. Nelson, J. Cihak, J. Plachý, M. Stangassinger, V. Erfle, and D. Schlöndorff. 2000. Transfer of the chemokine receptor CCR5 between cells by membrane-derived microparticles: a mechanism for cellular human immunodeficiency virus 1 infection. Nat. Med. 6: 769-775. (Pubitemid 30469425)
    • (2000) Nature Medicine , vol.6 , Issue.7 , pp. 769-775
    • Mack, M.1    Kleinschmidt, A.2    Bruhl, H.3    Klier, C.4    Nelson, P.J.5    Cihak, J.6    Plachy, J.7    Stangassinger, M.8    Erfle, V.9    Schlondorff, D.10
  • 12
    • 0037402527 scopus 로고    scopus 로고
    • Characterisation and properties of ectosomes released by human polymorphonuclear neutrophils
    • DOI 10.1016/S0014-4827(03)00055-7
    • Gasser, O., C. Hess, S. Miot, C. Deon, J. C. Sanchez, and J. A. Schifferli. 2003. Characterisation and properties of ectosomes released by human polymorphonuclear neutrophils. Exp. Cell Res. 285: 243-257. (Pubitemid 36432112)
    • (2003) Experimental Cell Research , vol.285 , Issue.2 , pp. 243-257
    • Gasser, O.1    Hess, C.2    Miot, S.3    Deon, C.4    Sanchez, J.-C.5    Schifferli, J.A.6
  • 13
    • 70349306861 scopus 로고    scopus 로고
    • Membrane microparticles mediate transfer of P-glycoprotein to drug sensitive cancer cells
    • Bebawy, M., V. Combes, E. Lee, R. Jaiswal, J. Gong, A. Bonhoure, and G. E. Grau. 2009. Membrane microparticles mediate transfer of P-glycoprotein to drug sensitive cancer cells. Leukemia 23: 1643-1649.
    • (2009) Leukemia , vol.23 , pp. 1643-1649
    • Bebawy, M.1    Combes, V.2    Lee, E.3    Jaiswal, R.4    Gong, J.5    Bonhoure, A.6    Grau, G.E.7
  • 17
    • 78149475085 scopus 로고    scopus 로고
    • Human plasma membrane-derived vesicles halt proliferation and induce differentiation of THP-1 acute monocytic leukemia cells
    • Ansa-Addo, E. A., S. Lange, D. Stratton, S. Antwi-Baffour, I. Cestari, M. I. Ramirez, M. V. McCrossan, and J. M. Inal. 2010. Human plasma membrane-derived vesicles halt proliferation and induce differentiation of THP-1 acute monocytic leukemia cells. J. Immunol. 185: 5236-5246.
    • (2010) J. Immunol. , vol.185 , pp. 5236-5246
    • Ansa-Addo, E.A.1    Lange, S.2    Stratton, D.3    Antwi-Baffour, S.4    Cestari, I.5    Ramirez, M.I.6    McCrossan, M.V.7    Inal, J.M.8
  • 18
    • 27844531030 scopus 로고    scopus 로고
    • Emission of membrane vesicles: Roles in complement resistance, immunity and cancer
    • DOI 10.1007/s00281-005-0004-1
    • Pilzer, D., O. Gasser, O. Moskovich, J. A. Schifferli, and Z. Fishelson. 2005. Emission of membrane vesicles: roles in complement resistance, immunity and cancer. Springer Semin. Immunopathol. 27: 375-387. (Pubitemid 41639888)
    • (2005) Springer Seminars in Immunopathology , vol.27 , Issue.3 , pp. 375-387
    • Pilzer, D.1    Gasser, O.2    Moskovich, O.3    Schifferli, J.A.4    Fishelson, Z.5
  • 21
    • 33748305634 scopus 로고    scopus 로고
    • Cell vesiculation and immunopathology: implications in cerebral malaria
    • DOI 10.1016/j.micinf.2006.04.006, PII S1286457906001687
    • Coltel, N., V. Combes, S. C. Wassmer, G. Chimini, and G. E. Grau. 2006. Cell vesiculation and immunopathology: implications in cerebral malaria. Microbes Infect. 8: 2305-2316. (Pubitemid 44322058)
    • (2006) Microbes and Infection , vol.8 , Issue.8 , pp. 2305-2316
    • Coltel, N.1    Combes, V.2    Wassmer, S.C.3    Chimini, G.4    Grau, G.E.5
  • 23
    • 70450223706 scopus 로고    scopus 로고
    • Role of early lectin pathway activation in the complement-mediated killing of Trypanosoma cruzi
    • Cestari, I. d. S., A. Krarup, R. B. Sim, J. M. Inal, and M. I. Ramirez. 2009. Role of early lectin pathway activation in the complement-mediated killing of Trypanosoma cruzi. Mol. Immunol. 47: 426-437.
    • (2009) Mol. Immunol. , vol.47 , pp. 426-437
    • Cestari, I.D.S.1    Krarup, A.2    Sim, R.B.3    Inal, J.M.4    Ramirez, M.I.5
  • 24
    • 0022178612 scopus 로고
    • In vitro differentiation of Trypanosoma cruzi under chemically defined conditions
    • DOI 10.1016/0166-6851(85)90073-8
    • Contreras, V. T., J. M. Salles, N. Thomas, C. M. Morel, and S. Goldenberg. 1985. In vitro differentiation of Trypanosoma cruzi under chemically defined conditions. Mol. Biochem. Parasitol. 16: 315-327. (Pubitemid 16248528)
    • (1985) Molecular and Biochemical Parasitology , vol.16 , Issue.3 , pp. 315-327
    • Contreras, V.T.1    Salles, J.M.2    Thomas, N.3
  • 25
    • 0021895138 scopus 로고
    • 2+ indicators with greatly improved fluorescence properties
    • Grynkiewicz, G., M. Poenie, and R. Y. Tsien. 1985. A new generation of Ca2+ indicators with greatly improved fluorescence properties. J. Biol. Chem. 260: 3440-3450. (Pubitemid 15114340)
    • (1985) Journal of Biological Chemistry , vol.260 , Issue.6 , pp. 3440-3450
    • Grynkiewicz, G.1    Poenie, M.2    Tsien, R.Y.3
  • 27
    • 54249162286 scopus 로고    scopus 로고
    • Complement C2 receptor inhibitor trispanning confers an increased ability to resist complement-mediated lysis in Trypanosoma cruzi
    • Cestari, I. d. S., I. Evans-Osses, J. C. Freitas, J. M. Inal, and M. I. Ramirez. 2008. Complement C2 receptor inhibitor trispanning confers an increased ability to resist complement-mediated lysis in Trypanosoma cruzi. J. Infect. Dis. 198: 1276-1283.
    • (2008) J. Infect. Dis. , vol.198 , pp. 1276-1283
    • Cestari, I.D.S.1    Evans-Osses, I.2    Freitas, J.C.3    Inal, J.M.4    Ramirez, M.I.5
  • 28
    • 0027380363 scopus 로고
    • Small-scale preparation of complement components C3 and C4
    • DOI 10.1016/0076-6879(93)23037-N
    • Dodds, A. W. 1993. Small-scale preparation of complement components C3 and C4. Methods Enzymol. 223: 46-61. (Pubitemid 23321179)
    • (1993) Methods in Enzymology , vol.223 , pp. 46-61
    • Dodds, A.W.1
  • 29
    • 0035655395 scopus 로고    scopus 로고
    • Rapid secretion of interleukin-1beta by microvesicle shedding
    • DOI 10.1016/S1074-7613(01)00229-1
    • MacKenzie, A., H. L. Wilson, E. Kiss-Toth, S. K. Dower, R. A. North, and A. Surprenant. 2001. Rapid secretion of interleukin-1beta by microvesicle shedding. Immunity 15: 825-835. (Pubitemid 34008509)
    • (2001) Immunity , vol.15 , Issue.5 , pp. 825-835
    • MacKenzie, A.1    Wilson, H.L.2    Kiss-Toth, E.3    Dower, S.K.4    North, R.A.5    Surprenant, A.6
  • 31
    • 0346101755 scopus 로고    scopus 로고
    • A Corresponding Tyrosine Residue in the C2/Factor B Type A Domain Is a Hot Spot in the Decay Acceleration of the Complement C3 Convertases
    • DOI 10.1074/jbc.M304620200
    • Kuttner-Kondo, L. A., M. P. Dybvig, L. M. Mitchell, N. Muqim, J. P. Atkinson, M. E. Medof, and D. E. Hourcade. 2003. A corresponding tyrosine residue in the C2/factor B type A domain is a hot spot in the decay acceleration of the complement C3 convertases. J. Biol. Chem. 278: 52386-52391. (Pubitemid 38035829)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.52 , pp. 52386-52391
    • Kuttner-Kondo, L.A.1    Dybvig, M.P.2    Mitchell, L.M.3    Muqim, N.4    Atkinson, J.P.5    Medof, M.E.6    Hourcade, D.E.7
  • 32
    • 0029131548 scopus 로고
    • Trypanosome invasion of mammalian cells requires activation of the TGF beta signaling pathway
    • Ming, M., M. E. Ewen, and M. E. Pereira. 1995. Trypanosome invasion of mammalian cells requires activation of the TGF beta signaling pathway. Cell 82: 287-296.
    • (1995) Cell , vol.82 , pp. 287-296
    • Ming, M.1    Ewen, M.E.2    Pereira, M.E.3
  • 33
    • 0034101539 scopus 로고    scopus 로고
    • Dual role for transforming growth factor beta-dependent signaling in Trypanosoma cruzi infection of mammalian cells
    • DOI 10.1128/IAI.68.4.2077-2081.2000
    • Hall, B. S., and M. A. Pereira. 2000. Dual role for transforming growth factor beta-dependent signaling in Trypanosoma cruzi infection of mammalian cells. Infect. Immun. 68: 2077-2081. (Pubitemid 30164839)
    • (2000) Infection and Immunity , vol.68 , Issue.4 , pp. 2077-2081
    • Hall, B.S.1    Pereira, M.A.2
  • 34
  • 35
    • 0027980104 scopus 로고
    • Role in host cell invasion of Trypanosoma cruzi-induced cytosolic-free Ca2+ transients
    • Tardieux, I., M. H. Nathanson, and N. W. Andrews. 1994. Role in host cell invasion of Trypanosoma cruzi-induced cytosolic-free Ca2+ transients. J. Exp. Med. 179: 1017-1022.
    • (1994) J. Exp. Med. , vol.179 , pp. 1017-1022
    • Tardieux, I.1    Nathanson, M.H.2    Andrews, N.W.3
  • 37
    • 0027237566 scopus 로고
    • Involvement of the stage-specific 82-kilodalton adhesion molecule of Trypanosoma cruzi metacyclic trypomastigotes in host cell invasion
    • Ramirez, M. I., Rde. C. Ruiz, J. E. Araya, J. F. Da Silveira, and N. Yoshida. 1993. Involvement of the stage-specific 82-kilodalton adhesion molecule of Trypanosoma cruzi metacyclic trypomastigotes in host cell invasion. Infect. Immun. 61: 3636-3641.
    • (1993) Infect. Immun. , vol.61 , pp. 3636-3641
    • Ramirez, M.I.1    Ruiz, R.D.C.2    Araya, J.E.3    Da Silveira, J.F.4    Yoshida, N.5
  • 38
    • 0344352478 scopus 로고    scopus 로고
    • Oligopeptidase B-dependent signaling mediates host cell invasion by Trypanosoma cruzi
    • DOI 10.1093/emboj/17.17.4975
    • Caler, E. V., S. Vaena de Avalos, P. A. Haynes, N. W. Andrews, and B. A. Burleigh. 1998. Oligopeptidase B-dependent signaling mediates host cell invasion by Trypanosoma cruzi. EMBO J. 17: 4975-4986. (Pubitemid 28408464)
    • (1998) EMBO Journal , vol.17 , Issue.17 , pp. 4975-4986
    • Caler, E.V.1    De Avalos, S.V.2    Haynes, P.A.3    Andrews, N.W.4    Burleigh, B.A.5
  • 39
    • 0037332590 scopus 로고    scopus 로고
    • 2+ signaling activity in stably transfected Trypanosoma cruzi epimastigotes expressing the metacyclic stage-specific surface molecule gp82
    • DOI 10.1128/IAI.71.3.1561-1565.2003
    • Manque, P. M., I. Neira, V. D. Atayde, E. Cordero, A. T. Ferreira, J. F. da Silveira, M. Ramirez, and N. Yoshida. 2003. Cell adhesion and Ca2+ signaling activity in stably transfected Trypanosoma cruzi epimastigotes expressing the metacyclic stage-specific surface molecule gp82. Infect. Immun. 71: 1561-1565. (Pubitemid 36254346)
    • (2003) Infection and Immunity , vol.71 , Issue.3 , pp. 1561-1565
    • Manque, P.M.1    Neira, I.2    Atayde, V.D.3    Cordero, E.4    Ferreira, A.T.5    Da, S.J.F.6    Ramirez, M.7    Yoshida, N.8
  • 40
    • 40849094253 scopus 로고    scopus 로고
    • Circulating microparticles in normal pregnancy and pre-eclampsia
    • Redman, C. W., and I. L. Sargent. 2008. Circulating microparticles in normal pregnancy and pre-eclampsia. Placenta 29 (Suppl. A): S73-S77.
    • (2008) Placenta , vol.29 , Issue.SUPPL. A
    • Redman, C.W.1    Sargent, I.L.2
  • 41
    • 27744571140 scopus 로고    scopus 로고
    • Microparticles as regulators of inflammation: Novel players of cellular crosstalk in the rheumatic diseases
    • DOI 10.1002/art.21350
    • Distler, J. H., D. S. Pisetsky, L. C. Huber, J. R. Kalden, S. Gay, and O. Distler. 2005. Microparticles as regulators of inflammation: novel players of cellular crosstalk in the rheumatic diseases. Arthritis Rheum. 52: 3337-3348. (Pubitemid 41612200)
    • (2005) Arthritis and Rheumatism , vol.52 , Issue.11 , pp. 3337-3348
    • Distler, J.H.W.1    Pisetsky, D.S.2    Huber, L.C.3    Kalden, J.R.4    Gay, S.5    Distler, O.6
  • 42
    • 20444417857 scopus 로고    scopus 로고
    • Microparticles released by human neutrophils adhere to erythrocytes in the presence of complement
    • DOI 10.1016/j.yexcr.2005.03.011, PII S0014482705001187
    • Gasser, O., and J. A. Schifferli. 2005. Microparticles released by human neutrophils adhere to erythrocytes in the presence of complement. Exp. Cell Res. 307: 381-387. (Pubitemid 40799363)
    • (2005) Experimental Cell Research , vol.307 , Issue.2 , pp. 381-387
    • Gasser, O.1    Schifferli, J.A.2
  • 43
    • 1342303386 scopus 로고    scopus 로고
    • The Classical Activation Pathway of the Human Complement System Is Specifically Inhibited by Calreticulin from Trypanosoma cruzi
    • Ferreira, V., C. Valck, G. Sánchez, A. Gingras, S. Tzima, M. C. Molina, R. Sim, W. Schwaeble, and A. Ferreira. 2004. The classical activation pathway of the human complement system is specifically inhibited by calreticulin from Trypanosoma cruzi. J. Immunol. 172: 3042-3050. (Pubitemid 38263693)
    • (2004) Journal of Immunology , vol.172 , Issue.5 , pp. 3042-3050
    • Ferreira, V.1    Valck, C.2    Sanchez, G.3    Gingras, A.4    Tzima, S.5    Molina, M.C.6    Sim, R.7    Schwaeble, W.8    Ferreira, A.9
  • 44
    • 0022538997 scopus 로고
    • Mechanism of resistance to lysis by the alternative complement pathway in Trypanosoma cruzi trypomastigotes: Effect of specific monoclonal antibody
    • Schenkman, S., M. L. Güther, and N. Yoshida. 1986. Mechanism of resistance to lysis by the alternative complement pathway in Trypanosoma cruzi trypomastigotes: effect of specific monoclonal antibody. J. Immunol. 137: 1623-1628. (Pubitemid 16014816)
    • (1986) Journal of Immunology , vol.137 , Issue.5 , pp. 1623-1628
    • Schenkman, S.1    Guther, M.L.S.2    Yoshida, N.3
  • 46
    • 0027930729 scopus 로고
    • Role of sialic acid in the resistance of Trypanosoma cruzi trypomastigotes to complement
    • Tomlinson, S., L. C. Pontes de Carvalho, F. Vandekerckhove, and V. Nussenzweig. 1994. Role of sialic acid in the resistance of Trypanosoma cruzi trypomastigotes to complement. J. Immunol. 153: 3141-3147. (Pubitemid 24292539)
    • (1994) Journal of Immunology , vol.153 , Issue.7 , pp. 3141-3147
    • Tomlinson, S.1    Pontes, D.C.L.C.2    Vandekerckhove, F.3    Nussenzweig, V.4
  • 48
    • 0037128162 scopus 로고    scopus 로고
    • Complement interaction with trypanosomatid promastigotes in normal human serum
    • DOI 10.1084/jem.20011319
    • Domínguez, M., I. Moreno, M. López-Trascasa, and A. Toraño. 2002. Complement interaction with trypanosomatid promastigotes in normal human serum. J. Exp. Med. 195: 451-459. (Pubitemid 34461298)
    • (2002) Journal of Experimental Medicine , vol.195 , Issue.4 , pp. 451-459
    • Dominguez, M.1    Moreno, I.2    Lopez-Trascasa, M.3    Torano, A.4
  • 49
    • 5144222255 scopus 로고    scopus 로고
    • Complement: A unique innate immune sensor for danger signals
    • DOI 10.1016/j.molimm.2004.06.011, PII S0161589004002184
    • Gasque, P. 2004. Complement: a unique innate immune sensor for danger signals. Mol. Immunol. 41: 1089-1098. (Pubitemid 39345390)
    • (2004) Molecular Immunology , vol.41 , Issue.11 SPEC. ISS. , pp. 1089-1098
    • Gasque, P.1
  • 51
    • 0022550078 scopus 로고
    • Inhibition of serum complement haemolytic activity by lipid vesicles containing phosphatidylserine
    • DOI 10.1016/0014-5793(86)80350-7
    • Comis, A., and S. B. Easterbrook-Smith. 1986. Inhibition of serum complement haemolytic activity by lipid vesicles containing phosphatidylserine. FEBS Lett. 197: 321-327. (Pubitemid 16037943)
    • (1986) FEBS Letters , vol.197 , Issue.1-2 , pp. 321-327
    • Comis, A.1    Easterbrook-Smith, S.B.2
  • 53
    • 33749488765 scopus 로고    scopus 로고
    • Human tumor-released microvesicles promote the differentiation of myeloid cells with transforming growth factor-beta-mediated suppressive activity on T lymphocytes
    • DOI 10.1158/0008-5472.CAN-06-1819
    • Valenti, R., V. Huber, P. Filipazzi, L. Pilla, G. Sovena, A. Villa, A. Corbelli, S. Fais, G. Parmiani, and L. Rivoltini. 2006. Human tumor-released microvesicles promote the differentiation of myeloid cells with transforming growth factor-beta-mediated suppressive activity on T lymphocytes. Cancer Res. 66: 9290-9298. (Pubitemid 44521151)
    • (2006) Cancer Research , vol.66 , Issue.18 , pp. 9290-9298
    • Valenti, R.1    Huber, V.2    Filipazzi, P.3    Pilla, L.4    Sovena, G.5    Villa, A.6    Corbelli, A.7    Fais, S.8    Parmiani, G.9    Rivoltini, L.10
  • 57
    • 0025741792 scopus 로고
    • Regulation of Trypanosoma cruzi infections in vitro and in vivo by transforming growth factor beta (TGF-beta)
    • Silva, J. S., D. R. Twardzik, and S. G. Reed. 1991. Regulation of Trypanosoma cruzi infections in vitro and in vivo by transforming growth factor beta (TGF-beta). J. Exp. Med. 174: 539-545.
    • (1991) J. Exp. Med. , vol.174 , pp. 539-545
    • Silva, J.S.1    Twardzik, D.R.2    Reed, S.G.3
  • 58
    • 15944408359 scopus 로고    scopus 로고
    • Activation of transforming growth factor beta by Trypanosoma cruzi
    • DOI 10.1111/j.1462-5822.2004.00481.x
    • Waghabi, M. C., M. Keramidas, J. J. Feige, T. C. Araujo-Jorge, and S. Bailly. 2005. Activation of transforming growth factor beta by Trypanosoma cruzi. Cell. Microbiol. 7: 511-517. (Pubitemid 40439450)
    • (2005) Cellular Microbiology , vol.7 , Issue.4 , pp. 511-517
    • Waghabi, M.C.1    Keramidas, M.2    Feige, J.-J.3    Araujo-Jorge, T.C.4    Bailly, S.5


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