메뉴 건너뛰기




Volumn 6, Issue 9, 2010, Pages

Steric shielding of surface epitopes and impaired immune recognition induced by the Ebola virus glycoprotein

Author keywords

[No Author keywords available]

Indexed keywords

BETA1 INTEGRIN; CELL SURFACE PROTEIN; EPITOPE; GLYCAN; PROTEIN SUBUNIT; VIRUS GLYCOPROTEIN;

EID: 78149348506     PISSN: 15537366     EISSN: 15537374     Source Type: Journal    
DOI: 10.1371/journal.ppat.1001098     Document Type: Article
Times cited : (119)

References (52)
  • 1
    • 0002858305 scopus 로고    scopus 로고
    • Filoviridae: Marburg and Eboila Viruses
    • In: Knipe DM, Howley PM, Griggen DE, Lamb RA, Martin MA, et al., eds., Lippincott, Williams & Wilkins
    • Sanchez A, Khan AS, Zaki SR, Nabel GJ, Ksiazek TG, et al. (2001) Filoviridae: Marburg and Eboila Viruses. In: Knipe DM, Howley PM, Griggen DE, Lamb RA, Martin MA, et al., eds. Fields Virology: Lippincott, Williams & Wilkins. pp 1279-1304.
    • (2001) Fields Virology , pp. 1279-1304
    • Sanchez, A.1    Khan, A.S.2    Zaki, S.R.3    Nabel, G.J.4    Ksiazek, T.G.5
  • 2
    • 4043053773 scopus 로고    scopus 로고
    • Pathogenesis of filoviral haemorrhagic fevers
    • Mahanty S, Bray M (2004) Pathogenesis of filoviral haemorrhagic fevers. The Lancet Infectious Diseases 4: 487-498.
    • (2004) The Lancet Infectious Diseases , vol.4 , pp. 487-498
    • Mahanty, S.1    Bray, M.2
  • 3
    • 33646156412 scopus 로고    scopus 로고
    • Ebola virus glycoprotein GP is not cytotoxic when expressed constitutively at a moderate level
    • Alazard-Dany N, Volchkova V, Reynard O, Carbonnelle C, Dolnik O, et al. (2006) Ebola virus glycoprotein GP is not cytotoxic when expressed constitutively at a moderate level. J Gen Virol 87: 1247-1257.
    • (2006) J Gen Virol , vol.87 , pp. 1247-1257
    • Alazard-Dany, N.1    Volchkova, V.2    Reynard, O.3    Carbonnelle, C.4    Dolnik, O.5
  • 5
    • 0032566901 scopus 로고    scopus 로고
    • The nonstructural small glycoprotein sGP of Ebola virus is secreted as an antiparallel-orientated homodimer
    • Volchkova VA, Feldmann H, Klenk HD, Volchkov VE (1998) The nonstructural small glycoprotein sGP of Ebola virus is secreted as an antiparallel-orientated homodimer. Virology 250: 408-414.
    • (1998) Virology , vol.250 , pp. 408-414
    • Volchkova, V.A.1    Feldmann, H.2    Klenk, H.D.3    Volchkov, V.E.4
  • 7
    • 0036893140 scopus 로고    scopus 로고
    • Covalent modifications of the ebola virus glycoprotein
    • Jeffers SA, Sanders DA, Sanchez A (2002) Covalent modifications of the ebola virus glycoprotein. J Virol 76: 12463-12472.
    • (2002) J Virol , vol.76 , pp. 12463-12472
    • Jeffers, S.A.1    Sanders, D.A.2    Sanchez, A.3
  • 8
    • 0033831191 scopus 로고    scopus 로고
    • Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury
    • Yang ZY, Duckers HJ, Sullivan NJ, Sanchez A, Nabel EG, et al. (2000) Identification of the Ebola virus glycoprotein as the main viral determinant of vascular cell cytotoxicity and injury. Nat Med 6: 886-889.
    • (2000) Nat Med , vol.6 , pp. 886-889
    • Yang, Z.Y.1    Duckers, H.J.2    Sullivan, N.J.3    Sanchez, A.4    Nabel, E.G.5
  • 9
    • 0033835531 scopus 로고    scopus 로고
    • Differential induction of cellular detachment by envelope glycoproteins of Marburg and Ebola (Zaire) viruses
    • Chan SY, Ma MC, Goldsmith MA (2000) Differential induction of cellular detachment by envelope glycoproteins of Marburg and Ebola (Zaire) viruses. J Gen Virol 81: 2155-2159.
    • (2000) J Gen Virol , vol.81 , pp. 2155-2159
    • Chan, S.Y.1    Ma, M.C.2    Goldsmith, M.A.3
  • 10
    • 0034610176 scopus 로고    scopus 로고
    • Downregulation of beta1 integrins by Ebola virus glycoprotein: Implication for virus entry
    • Takada A, Watanabe S, Ito H, Okazaki K, Kida H, et al. (2000) Downregulation of beta1 integrins by Ebola virus glycoprotein: implication for virus entry. Virology 278: 20-26.
    • (2000) Virology , vol.278 , pp. 20-26
    • Takada, A.1    Watanabe, S.2    Ito, H.3    Okazaki, K.4    Kida, H.5
  • 11
    • 0035831317 scopus 로고    scopus 로고
    • Recovery of infectious Ebola virus from complementary DNA: RNA editing of the GP gene and viral cytotoxicity
    • Volchkov VE, Volchkova VA, Muhlberger E, Kolesnikova LV, Weik M, et al. (2001) Recovery of infectious Ebola virus from complementary DNA: RNA editing of the GP gene and viral cytotoxicity. Science 291: 1965-1969.
    • (2001) Science , vol.291 , pp. 1965-1969
    • Volchkov, V.E.1    Volchkova, V.A.2    Muhlberger, E.3    Kolesnikova, L.V.4    Weik, M.5
  • 12
    • 0036171135 scopus 로고    scopus 로고
    • Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence
    • Simmons G, Wool-Lewis RJ, Baribaud F, Netter RC, Bates P (2002) Ebola virus glycoproteins induce global surface protein down-modulation and loss of cell adherence. J Virol 76: 2518-2528.
    • (2002) J Virol , vol.76 , pp. 2518-2528
    • Simmons, G.1    Wool-Lewis, R.J.2    Baribaud, F.3    Netter, R.C.4    Bates, P.5
  • 13
    • 1642446620 scopus 로고    scopus 로고
    • Ebola virus glycoprotein-mediated anoikis of primary human cardiac microvascular endothelial cells
    • Ray RB, Basu A, Steele R, Beyene A, McHowat J, et al. (2004) Ebola virus glycoprotein-mediated anoikis of primary human cardiac microvascular endothelial cells. Virology 321: 181-188.
    • (2004) Virology , vol.321 , pp. 181-188
    • Ray, R.B.1    Basu, A.2    Steele, R.3    Beyene, A.4    McHowat, J.5
  • 14
    • 10644277846 scopus 로고    scopus 로고
    • Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent proteintrafficking pathway
    • Sullivan NJ, Peterson M, Yang ZY, Kong WP, Duckers H, et al. (2005) Ebola virus glycoprotein toxicity is mediated by a dynamin-dependent proteintrafficking pathway. J Virol 79: 547-553.
    • (2005) J Virol , vol.79 , pp. 547-553
    • Sullivan, N.J.1    Peterson, M.2    Yang, Z.Y.3    Kong, W.P.4    Duckers, H.5
  • 15
    • 58149109098 scopus 로고    scopus 로고
    • Requirements for cell rounding and surface protein down-regulation by Ebola virus glycoprotein
    • Francica JR, Matukonis MK, Bates P (2009) Requirements for cell rounding and surface protein down-regulation by Ebola virus glycoprotein. Virology 383: 237-247.
    • (2009) Virology , vol.383 , pp. 237-247
    • Francica, J.R.1    Matukonis, M.K.2    Bates, P.3
  • 16
    • 33846557891 scopus 로고    scopus 로고
    • The ERK mitogenactivated protein kinase pathway contributes to Ebola virus glycoproteininduced cytotoxicity
    • Zampieri CA, Fortin JF, Nolan GP, Nabel GJ (2007) The ERK mitogenactivated protein kinase pathway contributes to Ebola virus glycoproteininduced cytotoxicity. J Virol 81: 1230-1240.
    • (2007) J Virol , vol.81 , pp. 1230-1240
    • Zampieri, C.A.1    Fortin, J.F.2    Nolan, G.P.3    Nabel, G.J.4
  • 17
    • 0037018099 scopus 로고    scopus 로고
    • Lipid raft microdomains: A gateway for compartmentalized trafficking of Ebola and Marburg viruses
    • Bavari S, Bosio CM, Wiegand E, Ruthel G, Will AB, et al. (2002) Lipid raft microdomains: a gateway for compartmentalized trafficking of Ebola and Marburg viruses. J Exp Med 195: 593-602.
    • (2002) J Exp Med , vol.195 , pp. 593-602
    • Bavari, S.1    Bosio, C.M.2    Wiegand, E.3    Ruthel, G.4    Will, A.B.5
  • 18
    • 47049107589 scopus 로고    scopus 로고
    • Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor
    • Lee JE, Fusco ML, Hessell AJ, Oswald WB, Burton DR, et al. (2008) Structure of the Ebola virus glycoprotein bound to an antibody from a human survivor. Nature 454: 177-182.
    • (2008) Nature , vol.454 , pp. 177-182
    • Lee, J.E.1    Fusco, M.L.2    Hessell, A.J.3    Oswald, W.B.4    Burton, D.R.5
  • 19
    • 0025297888 scopus 로고
    • Why are proteins O-glycosylated?
    • Jentoft N (1990) Why are proteins O-glycosylated? Trends Biochem Sci 15: 291-294.
    • (1990) Trends Biochem Sci , vol.15 , pp. 291-294
    • Jentoft, N.1
  • 20
    • 0032949982 scopus 로고    scopus 로고
    • Endoproteolytic processing of the ebola virus envelope glycoprotein: Cleavage is not required for function
    • Wool-Lewis RJ, Bates P (1999) Endoproteolytic processing of the ebola virus envelope glycoprotein: cleavage is not required for function. J Virol 73: 1419-1426.
    • (1999) J Virol , vol.73 , pp. 1419-1426
    • Wool-Lewis, R.J.1    Bates, P.2
  • 21
    • 0036133094 scopus 로고    scopus 로고
    • Reverse genetics demonstrates that proteolytic processing of the Ebola virus glycoprotein is not essential for replication in cell culture
    • Neumann G, Feldmann H, Watanabe S, Lukashevich I, Kawaoka Y (2002) Reverse genetics demonstrates that proteolytic processing of the Ebola virus glycoprotein is not essential for replication in cell culture. J Virol 76: 406-410.
    • (2002) J Virol , vol.76 , pp. 406-410
    • Neumann, G.1    Feldmann, H.2    Watanabe, S.3    Lukashevich, I.4    Kawaoka, Y.5
  • 22
    • 2942526839 scopus 로고    scopus 로고
    • Ectodomain shedding of the glycoprotein GP of Ebola virus
    • Dolnik O, Volchkova V, Garten W, Carbonnelle C, Becker S, et al. (2004) Ectodomain shedding of the glycoprotein GP of Ebola virus. Embo J 23: 2175-2184.
    • (2004) Embo J , vol.23 , pp. 2175-2184
    • Dolnik, O.1    Volchkova, V.2    Garten, W.3    Carbonnelle, C.4    Becker, S.5
  • 23
    • 0024795060 scopus 로고
    • Inhibition of mucin glycosylation by aryl-N-acetyl-alpha-galactosaminides in human colon cancer cells
    • Kuan SF, Byrd JC, Basbaum C, Kim YS (1989) Inhibition of mucin glycosylation by aryl-N-acetyl-alpha-galactosaminides in human colon cancer cells. J Biol Chem 264: 19271-19277.
    • (1989) J Biol Chem , vol.264 , pp. 19271-19277
    • Kuan, S.F.1    Byrd, J.C.2    Basbaum, C.3    Kim, Y.S.4
  • 24
    • 0026986665 scopus 로고
    • Effect of benzyl-alpha-GalNAc, an inhibitor of mucin glycosylation, on cancer-associated antigens in human colon cancer cells
    • Huang J, Byrd JC, Yoon WH, Kim YS (1992) Effect of benzyl-alpha-GalNAc, an inhibitor of mucin glycosylation, on cancer-associated antigens in human colon cancer cells. Oncol Res 4: 507-515.
    • (1992) Oncol Res , vol.4 , pp. 507-515
    • Huang, J.1    Byrd, J.C.2    Yoon, W.H.3    Kim, Y.S.4
  • 25
    • 0032526691 scopus 로고    scopus 로고
    • GalNAc-alpha-O-benzyl inhibits NeuAcalpha2-3 glycosylation and blocks the intracellular transport of apical glycoproteins and mucus in differentiated HT-29 cells
    • Huet G, Hennebicq-Reig S, de Bolos C, Ulloa F, Lesuffleur T, et al. (1998) GalNAc-alpha-O-benzyl inhibits NeuAcalpha2-3 glycosylation and blocks the intracellular transport of apical glycoproteins and mucus in differentiated HT-29 cells. J Cell Biol 141: 1311-1322.
    • (1998) J Cell Biol , vol.141 , pp. 1311-1322
    • Huet, G.1    Hennebicq-Reig, S.2    de Bolos, C.3    Ulloa, F.4    Lesuffleur, T.5
  • 26
    • 33646686040 scopus 로고    scopus 로고
    • HIV nonprogressors preferentially maintain highly functional HIV-specific CD8+ T cells
    • Betts MR, Nason MC, West SM, De Rosa SC, Migueles SA, et al. (2006) HIV nonprogressors preferentially maintain highly functional HIV-specific CD8+ T cells. Blood 107: 4781-4789.
    • (2006) Blood , vol.107 , pp. 4781-4789
    • Betts, M.R.1    Nason, M.C.2    West, S.M.3    de Rosa, S.C.4    Migueles, S.A.5
  • 27
    • 69449090610 scopus 로고    scopus 로고
    • Ebolavirus glycoprotein GP masks both its own epitopes and the presence of cellular surface proteins
    • Reynard O, Borowiak M, Volchkova VA, Delpeut S, Mateo M, et al. (2009) Ebolavirus glycoprotein GP masks both its own epitopes and the presence of cellular surface proteins. J Virol 83: 9596-9601.
    • (2009) J Virol , vol.83 , pp. 9596-9601
    • Reynard, O.1    Borowiak, M.2    Volchkova, V.A.3    Delpeut, S.4    Mateo, M.5
  • 28
    • 0026452726 scopus 로고
    • Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4
    • Willey RL, Maldarelli F, Martin MA, Strebel K (1992) Human immunodeficiency virus type 1 Vpu protein induces rapid degradation of CD4. J Virol 66: 7193-7200.
    • (1992) J Virol , vol.66 , pp. 7193-7200
    • Willey, R.L.1    Maldarelli, F.2    Martin, M.A.3    Strebel, K.4
  • 30
    • 0029875421 scopus 로고    scopus 로고
    • Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein
    • Schwartz O, Marechal V, Le Gall S, Lemonnier F, Heard JM (1996) Endocytosis of major histocompatibility complex class I molecules is induced by the HIV-1 Nef protein. Nat Med 2: 338-342.
    • (1996) Nat Med , vol.2 , pp. 338-342
    • Schwartz, O.1    Marechal, V.2    Le Gall, S.3    Lemonnier, F.4    Heard, J.M.5
  • 31
    • 0022403592 scopus 로고
    • Impaired intracellular transport of class I MHC antigens as a possible means for adenoviruses to evade immune surveillance
    • Andersson M, Paabo S, Nilsson T, Peterson PA (1985) Impaired intracellular transport of class I MHC antigens as a possible means for adenoviruses to evade immune surveillance. Cell 43: 215-222.
    • (1985) Cell , vol.43 , pp. 215-222
    • Andersson, M.1    Paabo, S.2    Nilsson, T.3    Peterson, P.A.4
  • 32
    • 0034068631 scopus 로고    scopus 로고
    • Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins
    • Ishido S, Wang C, Lee BS, Cohen GB, Jung JU (2000) Downregulation of major histocompatibility complex class I molecules by Kaposi's sarcoma-associated herpesvirus K3 and K5 proteins. J Virol 74: 5300-5309.
    • (2000) J Virol , vol.74 , pp. 5300-5309
    • Ishido, S.1    Wang, C.2    Lee, B.S.3    Cohen, G.B.4    Jung, J.U.5
  • 33
    • 62449282065 scopus 로고    scopus 로고
    • Hepatitis C virus infection downregulates the ligands of the activating receptor NKG2D
    • Wen C, He X, Ma H, Hou N, Wei C, et al. (2008) Hepatitis C virus infection downregulates the ligands of the activating receptor NKG2D. Cell Mol Immunol 5: 475-478.
    • (2008) Cell Mol Immunol , vol.5 , pp. 475-478
    • Wen, C.1    He, X.2    Ma, H.3    Hou, N.4    Wei, C.5
  • 34
    • 40349108461 scopus 로고    scopus 로고
    • Downregulation of NKG2D and NKp80 ligands by Kaposi's sarcoma-associated herpesvirus K5 protects against NK cell cytotoxicity
    • Thomas M, Boname JM, Field S, Nejentsev S, Salio M, et al. (2008) Downregulation of NKG2D and NKp80 ligands by Kaposi's sarcoma-associated herpesvirus K5 protects against NK cell cytotoxicity. Proc Natl Acad Sci U S A 105: 1656-1661.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 1656-1661
    • Thomas, M.1    Boname, J.M.2    Field, S.3    Nejentsev, S.4    Salio, M.5
  • 35
    • 0141992093 scopus 로고    scopus 로고
    • The MHC class I antigen presentation pathway: Strategies for viral immune evasion
    • Hewitt EW (2003) The MHC class I antigen presentation pathway: strategies for viral immune evasion. Immunology 110: 163-169.
    • (2003) Immunology , vol.110 , pp. 163-169
    • Hewitt, E.W.1
  • 36
    • 13744260155 scopus 로고    scopus 로고
    • Glc1.8 from Microplitis demolitor bracovirus induces a loss of adhesion and phagocytosis in insect high five and S2 cells
    • Beck M, Strand MR (2005) Glc1.8 from Microplitis demolitor bracovirus induces a loss of adhesion and phagocytosis in insect high five and S2 cells. J Virol 79: 1861-1870.
    • (2005) J Virol , vol.79 , pp. 1861-1870
    • Beck, M.1    Strand, M.R.2
  • 37
    • 0028950808 scopus 로고
    • Episialin (MUC1) overexpression inhibits integrin-mediated cell adhesion to extracellular matrix components
    • Wesseling J, van der Valk SW, Vos HL, Sonnenberg A, Hilkens J (1995) Episialin (MUC1) overexpression inhibits integrin-mediated cell adhesion to extracellular matrix components. J Cell Biol 129: 255-265.
    • (1995) J Cell Biol , vol.129 , pp. 255-265
    • Wesseling, J.1    van der Valk, S.W.2    Vos, H.L.3    Sonnenberg, A.4    Hilkens, J.5
  • 38
    • 0033135026 scopus 로고    scopus 로고
    • Overexpression of sialomucin complex, a rat homologue of MUC4, inhibits tumor killing by lymphokineactivated killer cells
    • Komatsu M, Yee L, Carraway KL (1999) Overexpression of sialomucin complex, a rat homologue of MUC4, inhibits tumor killing by lymphokineactivated killer cells. Cancer Res 59: 2229-2236.
    • (1999) Cancer Res , vol.59 , pp. 2229-2236
    • Komatsu, M.1    Yee, L.2    Carraway, K.L.3
  • 39
    • 33749424145 scopus 로고    scopus 로고
    • Membrane mucin Muc4 induces density-dependent changes in ERK activation in mammary epithelial and tumor cells: Role in reversal of contact inhibition
    • Pino V, Ramsauer VP, Salas P, Carothers Carraway CA, Carraway KL (2006) Membrane mucin Muc4 induces density-dependent changes in ERK activation in mammary epithelial and tumor cells: role in reversal of contact inhibition. J Biol Chem 281: 29411-29420.
    • (2006) J Biol Chem , vol.281 , pp. 29411-29420
    • Pino, V.1    Ramsauer, V.P.2    Salas, P.3    Carothers Carraway, C.A.4    Carraway, K.L.5
  • 40
    • 0347123435 scopus 로고    scopus 로고
    • Mucins in cancer: Protection and control of the cell surface
    • Hollingsworth MA, Swanson BJ (2004) Mucins in cancer: protection and control of the cell surface. Nat Rev Cancer 4: 45-60.
    • (2004) Nat Rev Cancer , vol.4 , pp. 45-60
    • Hollingsworth, M.A.1    Swanson, B.J.2
  • 41
    • 0029937975 scopus 로고    scopus 로고
    • A mechanism for inhibition of Ecadherin-mediated cell-cell adhesion by the membrane-associated mucin episialin/MUC1
    • Wesseling J, van der Valk SW, Hilkens J (1996) A mechanism for inhibition of Ecadherin-mediated cell-cell adhesion by the membrane-associated mucin episialin/MUC1. Mol Biol Cell 7: 565-577.
    • (1996) Mol Biol Cell , vol.7 , pp. 565-577
    • Wesseling, J.1    van der Valk, S.W.2    Hilkens, J.3
  • 42
    • 0037137491 scopus 로고    scopus 로고
    • Roles of mucin-type O-glycans in cell adhesion
    • Fukuda M (2002) Roles of mucin-type O-glycans in cell adhesion. Biochim Biophys Acta 1573: 394-405.
    • (2002) Biochim Biophys Acta , vol.1573 , pp. 394-405
    • Fukuda, M.1
  • 43
    • 0037456827 scopus 로고    scopus 로고
    • Antibody neutralization and escape by HIV-1
    • Wei X, Decker JM, Wang S, Hui H, Kappes JC, et al. (2003) Antibody neutralization and escape by HIV-1. Nature 422: 307-312.
    • (2003) Nature , vol.422 , pp. 307-312
    • Wei, X.1    Decker, J.M.2    Wang, S.3    Hui, H.4    Kappes, J.C.5
  • 45
    • 0033039502 scopus 로고    scopus 로고
    • Ebola virus can be effectively neutralized by antibody produced in natural human infection
    • Maruyama T, Rodriguez LL, Jahrling PB, Sanchez A, Khan AS, et al. (1999) Ebola virus can be effectively neutralized by antibody produced in natural human infection. J Virol 73: 6024-6030.
    • (1999) J Virol , vol.73 , pp. 6024-6030
    • Maruyama, T.1    Rodriguez, L.L.2    Jahrling, P.B.3    Sanchez, A.4    Khan, A.S.5
  • 46
    • 0028957721 scopus 로고
    • Prognostic significance of MUC1 epithelial mucin expression in breast cancer
    • McGuckin MA, Walsh MD, Hohn BG, Ward BG, Wright RG (1995) Prognostic significance of MUC1 epithelial mucin expression in breast cancer. Hum Pathol 26: 432-439.
    • (1995) Hum Pathol , vol.26 , pp. 432-439
    • McGuckin, M.A.1    Walsh, M.D.2    Hohn, B.G.3    Ward, B.G.4    Wright, R.G.5
  • 47
    • 0022531183 scopus 로고
    • Cell surface sialomucin and resistance to natural cell-mediated cytotoxicity of rat mammary tumor ascites cells
    • Sherblom AP, Moody CE (1986) Cell surface sialomucin and resistance to natural cell-mediated cytotoxicity of rat mammary tumor ascites cells. Cancer Res 46: 4543-4546.
    • (1986) Cancer Res , vol.46 , pp. 4543-4546
    • Sherblom, A.P.1    Moody, C.E.2
  • 48
    • 33747587237 scopus 로고    scopus 로고
    • Multiple initial culture conditions enhance the establishment of cell lines from primary ovarian cancer specimens
    • Bertozzi CC, Chang CY, Jairaj S, Shan X, Huang J, et al. (2006) Multiple initial culture conditions enhance the establishment of cell lines from primary ovarian cancer specimens. In Vitro Cell Dev Biol Anim 42: 58-62.
    • (2006) In Vitro Cell Dev Biol Anim , vol.42 , pp. 58-62
    • Bertozzi, C.C.1    Chang, C.Y.2    Jairaj, S.3    Shan, X.4    Huang, J.5
  • 49
    • 34247212403 scopus 로고    scopus 로고
    • Engineering artificial antigen-presenting cells to express a diverse array of costimulatory molecules
    • Suhoski MM, Golovina TN, Aqui NA, Tai VC, Varela-Rohena A, et al. (2007) Engineering artificial antigen-presenting cells to express a diverse array of costimulatory molecules. Mol Ther 15: 981-988.
    • (2007) Mol Ther , vol.15 , pp. 981-988
    • Suhoski, M.M.1    Golovina, T.N.2    Aqui, N.A.3    Tai, V.C.4    Varela-Rohena, A.5
  • 50
    • 0038545370 scopus 로고    scopus 로고
    • CD28 and inducible costimulatory protein Src homology 2 binding domains show distinct regulation of phosphatidylinositol 3-kinase, Bcl-xL, and IL-2 expression in primary human CD4 T lymphocytes
    • Parry RV, Rumbley CA, Vandenberghe LH, June CH, Riley JL (2003) CD28 and inducible costimulatory protein Src homology 2 binding domains show distinct regulation of phosphatidylinositol 3-kinase, Bcl-xL, and IL-2 expression in primary human CD4 T lymphocytes. J Immunol 171: 166-174.
    • (2003) J Immunol , vol.171 , pp. 166-174
    • Parry, R.V.1    Rumbley, C.A.2    Vandenberghe, L.H.3    June, C.H.4    Riley, J.L.5
  • 51
    • 57349118383 scopus 로고    scopus 로고
    • Control of HIV-1 immune escape by CD8 T cells expressing enhanced T-cell receptor
    • Varela-Rohena A, Molloy PE, Dunn SM, Li Y, Suhoski MM, et al. (2008) Control of HIV-1 immune escape by CD8 T cells expressing enhanced T-cell receptor. Nat Med 14: 1390-1395.
    • (2008) Nat Med , vol.14 , pp. 1390-1395
    • Varela-Rohena, A.1    Molloy, P.E.2    Dunn, S.M.3    Li, Y.4    Suhoski, M.M.5
  • 52
    • 0037227929 scopus 로고    scopus 로고
    • Differential Nlinked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR
    • Lin G, Simmons G, Pohlmann S, Baribaud F, Ni H, et al. (2003) Differential Nlinked glycosylation of human immunodeficiency virus and Ebola virus envelope glycoproteins modulates interactions with DC-SIGN and DC-SIGNR. J Virol 77: 1337-1346.
    • (2003) J Virol , vol.77 , pp. 1337-1346
    • Lin, G.1    Simmons, G.2    Pohlmann, S.3    Baribaud, F.4    Ni, H.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.