메뉴 건너뛰기




Volumn 62, Issue 3, 2003, Pages 225-232

Molecular characterization of CD28 and cytotoxic T-lymphocyte-associated antigen 4 (CTLA-4) of woodchuck (Marmota monax)

Author keywords

Accessory molecules; CD28; Costimulation; CTLA 4; Woodchuck

Indexed keywords

ANTIBODY; CD28 ANTIGEN; COMPLEMENTARY DNA; CYTOTOXIC T LYMPHOCYTE ANTIGEN 4; HEXAPEPTIDE; METHIONYLTYROSYLPROLYLPROLYLPROLYLTYROSINE; UNCLASSIFIED DRUG;

EID: 0141613171     PISSN: 00012815     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1399-0039.2003.00086.x     Document Type: Article
Times cited : (10)

References (54)
  • 1
    • 0002899954 scopus 로고
    • The woodchuck model of hepatitis B virus infection
    • Arias IM, et al., eds, Raven Press, New York, NY
    • Tennant BC, Gerin JL. The woodchuck model of hepatitis B virus infection. In: Arias IM, et al., eds. The Liver: Biology, Pathobiology, Raven Press, New York, NY, 1994: 1455-66.
    • (1994) The Liver: Biology, Pathobiology , pp. 1455-1466
    • Tennant, B.C.1    Gerin, J.L.2
  • 2
    • 0028809476 scopus 로고
    • The woodchuck: An animal model for hepatitis B virus infection in man
    • Roggendorf M, Tolle TK. The woodchuck: an animal model for hepatitis B virus infection in man. Intervirology 1995: 38: 100-2.
    • (1995) Intervirology , vol.38 , pp. 100-102
    • Roggendorf, M.1    Tolle, T.K.2
  • 3
    • 0030001099 scopus 로고    scopus 로고
    • The woodchuck as a model of hepadnavirus infection, pathogenesis and therapy
    • Cote PJ, Gerin JL. The woodchuck as a model of hepadnavirus infection, pathogenesis and therapy. Forum Trends Exp Clin Med 1996: 6: 6131-59.
    • (1996) Forum Trends Exp Clin Med , vol.6 , pp. 6131-6159
    • Cote, P.J.1    Gerin, J.L.2
  • 4
    • 0034880621 scopus 로고    scopus 로고
    • Evaluation of new approaches of prophylactic and therapeutic vaccinations to hepatitis B viruses in the woodchuck model
    • Lu M, Roggendorf M. Evaluation of new approaches of prophylactic and therapeutic vaccinations to hepatitis B viruses in the woodchuck model. Intervirology 2001: 44: 214-23.
    • (2001) Intervirology , vol.44 , pp. 214-223
    • Lu, M.1    Roggendorf, M.2
  • 5
    • 0029112180 scopus 로고
    • In vitro activation of woodchuck lymphocytes measured by radiopurine incorporation and interleukin-2 production: Implications for modeling immunity and therapy in hepatitis B virus infection
    • Cote PJ, Gerin JL. In vitro activation of woodchuck lymphocytes measured by radiopurine incorporation and interleukin-2 production: implications for modeling immunity and therapy in hepatitis B virus infection. Hepatology 1995: 22: 687-99.
    • (1995) Hepatology , vol.22 , pp. 687-699
    • Cote, P.J.1    Gerin, J.L.2
  • 6
    • 0031747582 scopus 로고    scopus 로고
    • T-cell response to woodchuck hepatitis virus. WHV, antigens during acute self-limited WHV infection and convalescence and after viral challenge
    • Menne S, Maschke J, Lu M, Grosse-Wilde H, Roggendorf M. T-cell response to woodchuck hepatitis virus. WHV, antigens during acute self-limited WHV infection and convalescence and after viral challenge. J Virol 1998: 72: 6083-91.
    • (1998) J Virol , vol.72 , pp. 6083-6091
    • Menne, S.1    Maschke, J.2    Lu, M.3    Grosse-Wilde, H.4    Roggendorf, M.5
  • 7
    • 0031060105 scopus 로고    scopus 로고
    • Characterization of T-cell response to woodchuck hepatitis virus core protein and protection of woodchucks from infection by immunization with peptides containing a T-cell epitope
    • Menne S, Maschke J, Tolle TK, Lu M, Roggendorf M. Characterization of T-cell response to woodchuck hepatitis virus core protein and protection of woodchucks from infection by immunization with peptides containing a T-cell epitope. J Virol 1997: 71: 65-74.
    • (1997) J Virol , vol.71 , pp. 65-74
    • Menne, S.1    Maschke, J.2    Tolle, T.K.3    Lu, M.4    Roggendorf, M.5
  • 8
    • 0036147894 scopus 로고    scopus 로고
    • Deficiencies in the acute-phase cell-mediated immune response to viral antigens are associated with development of chronic woodchuck hepatitis virus infection following neonatal inoculation
    • Menne S, Roneker CA, Roggendorf M, Gerin JL, Cote PJ, Tennant BC. Deficiencies in the acute-phase cell-mediated immune response to viral antigens are associated with development of chronic woodchuck hepatitis virus infection following neonatal inoculation. J Virol 2003: 76: 1769-80.
    • (2003) J Virol , vol.76 , pp. 1769-1780
    • Menne, S.1    Roneker, C.A.2    Roggendorf, M.3    Gerin, J.L.4    Cote, P.J.5    Tennant, B.C.6
  • 9
    • 0030782959 scopus 로고    scopus 로고
    • Cloning and characterization of partial cDNAs for woodchuck cytokines and CD3epsilon with applications for the detection of RNA expression in tissues by RT-PCR assay
    • Nakamura I, Nupp JT, Rao BS et al. Cloning and characterization of partial cDNAs for woodchuck cytokines and CD3epsilon with applications for the detection of RNA expression in tissues by RT-PCR assay. J Med Virol 1997: 53: 85-95.
    • (1997) J Med Virol , vol.53 , pp. 85-95
    • Nakamura, I.1    Nupp, J.T.2    Rao, B.S.3
  • 10
    • 0141794854 scopus 로고    scopus 로고
    • Molecular characterization of woodchuck cytokines tumor necrosis factor alpha, interferon gamma and interleukin 6
    • Lohrengel B, Lu M, Roggendorf M. Molecular characterization of woodchuck cytokines tumor necrosis factor alpha, interferon gamma and interleukin 6. Immunogenetics 1998: 43: 332-5.
    • (1998) Immunogenetics , vol.43 , pp. 332-335
    • Lohrengel, B.1    Lu, M.2    Roggendorf, M.3
  • 11
    • 0034086066 scopus 로고    scopus 로고
    • Molecular cloning and characterization of major histocompatibility complex class I cDNAs from woodchuck Woodchuck MHC class I
    • Yang D, Lu M, Hao L, Roggendorf M. Molecular cloning and characterization of major histocompatibility complex class I cDNAs from woodchuck Woodchuck MHC class I. Tissue Antigens 2000: 55: 548-57.
    • (2000) Tissue Antigens , vol.55 , pp. 548-557
    • Yang, D.1    Lu, M.2    Hao, L.3    Roggendorf, M.4
  • 12
    • 0034003174 scopus 로고    scopus 로고
    • Posttranscriptional inhibition of class I major histocompatibility complex presentation on hepatocytess and lymphoid cells in chronic woodchuck hepatitis virus infection
    • Michalak TI, Hodgson PD, Churchill ND. Posttranscriptional inhibition of class I major histocompatibility complex presentation on hepatocytess and lymphoid cells in chronic woodchuck hepatitis virus infection. J Virol 2000: 74: 4483-94.
    • (2000) J Virol , vol.74 , pp. 4483-4494
    • Michalak, T.I.1    Hodgson, P.D.2    Churchill, N.D.3
  • 13
    • 0037518061 scopus 로고    scopus 로고
    • Molecular genetic and biochemical analysis of woodchuck (Marmota monax) MHC Class I polymorphism
    • Zhou J, Ferencik S, Rebmann V et al. Molecular genetic and biochemical analysis of woodchuck (Marmota monax) MHC Class I polymorphism Tissue Antigens 2003: 61: 240-8.
    • (2003) Tissue Antigens , vol.61 , pp. 240-248
    • Zhou, J.1    Ferencik, S.2    Rebmann, V.3
  • 14
    • 0027087331 scopus 로고
    • Costimulation of T lymphocytes: The role of CD28, CTLA-4, and B7/BB1 in interleukin-2 production and immunotherapy
    • Schwartz RH. Costimulation of T lymphocytes: the role of CD28, CTLA-4, and B7/BB1 in interleukin-2 production and immunotherapy. Cell 1992: 71: 1065-8.
    • (1992) Cell , vol.71 , pp. 1065-1068
    • Schwartz, R.H.1
  • 15
    • 0027403299 scopus 로고
    • The role of the CD28 receptor during T cell responses to antigen
    • Linsley PS, Ledbetter JA. The role of the CD28 receptor during T cell responses to antigen. Annu Rev Immunol 1993: 11: 191-212.
    • (1993) Annu Rev Immunol , vol.11 , pp. 191-212
    • Linsley, P.S.1    Ledbetter, J.A.2
  • 18
    • 0031091743 scopus 로고    scopus 로고
    • Is CTLA-4 a master switch for peripheral T cell tolerance?
    • Bluestone JA. Is CTLA-4 a master switch for peripheral T cell tolerance? J Immunol 1997: 158: 1989-93.
    • (1997) J Immunol , vol.158 , pp. 1989-1993
    • Bluestone, J.A.1
  • 20
    • 0028237348 scopus 로고
    • CD28-B7 interactions in T-cell activation
    • Allison JP. CD28-B7 interactions in T-cell activation. Curr Opin Immunol 1994: 6: 414-9.
    • (1994) Curr Opin Immunol , vol.6 , pp. 414-419
    • Allison, J.P.1
  • 21
    • 0023270567 scopus 로고
    • A new member of the immunoglobulin superfamily - CTLA-4
    • Brunet JF, Denizot F, Luciani MF et al. A new member of the immunoglobulin superfamily - CTLA-4. Nature 1987: 328: 267-70.
    • (1987) Nature , vol.328 , pp. 267-270
    • Brunet, J.F.1    Denizot, F.2    Luciani, M.F.3
  • 22
    • 0026486220 scopus 로고
    • Coexpression and functional cooperation of CTLA-4 and CD28 on activated T lymphocytes
    • Linsley PS, Greene JL, Tan P et al. Coexpression and functional cooperation of CTLA-4 and CD28 on activated T lymphocytes. J Exp Med 1992: 176: 1595-604.
    • (1992) J Exp Med , vol.176 , pp. 1595-1604
    • Linsley, P.S.1    Greene, J.L.2    Tan, P.3
  • 23
    • 15844380367 scopus 로고    scopus 로고
    • Regulation of CTLA-4 expression during T-cell activation
    • Perkins D, Wang Z, Donovan C et al. Regulation of CTLA-4 expression during T-cell activation. J Immunol 1996: 156: 4154-9.
    • (1996) J Immunol , vol.156 , pp. 4154-4159
    • Perkins, D.1    Wang, Z.2    Donovan, C.3
  • 25
    • 0029953858 scopus 로고    scopus 로고
    • CTLA-4 ligation blocks CD28-dependent T-cell activation
    • Walunas TL, Bakker CY, Bluestone JA. CTLA-4 ligation blocks CD28-dependent T-cell activation. J Exp Med 1996: 183: 2541-50.
    • (1996) J Exp Med , vol.183 , pp. 2541-2550
    • Walunas, T.L.1    Bakker, C.Y.2    Bluestone, J.A.3
  • 26
    • 0028484545 scopus 로고
    • CTLA-4 can function as a negative regulator of T-cell activation
    • Walunas TL, Lenschow DJ, Bakker CY et al. CTLA-4 can function as a negative regulator of T-cell activation. Immunity 1994: 1: 405-13.
    • (1994) Immunity , vol.1 , pp. 405-413
    • Walunas, T.L.1    Lenschow, D.J.2    Bakker, C.Y.3
  • 27
    • 0028841784 scopus 로고
    • The Yin and Yang of T cell costimulation
    • Allison JP, Krummel MF. The Yin and Yang of T cell costimulation. Science 1995: 270: 932-3.
    • (1995) Science , vol.270 , pp. 932-933
    • Allison, J.P.1    Krummel, M.F.2
  • 28
    • 0028791059 scopus 로고
    • Lymphoproliferative disorders with early lethality in mice deficient in Ctla-4
    • Waterhouse P, Penninger JM, Timms E et al. Lymphoproliferative disorders with early lethality in mice deficient in Ctla-4. Science 1995: 270: 985-8.
    • (1995) Science , vol.270 , pp. 985-988
    • Waterhouse, P.1    Penninger, J.M.2    Timms, E.3
  • 29
    • 0028867420 scopus 로고
    • Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4
    • Tivol EA, Borriello F, Schweitzer AN, Lynch WP, Bluestone JA, Sharpe AH. Loss of CTLA-4 leads to massive lymphoproliferation and fatal multiorgan tissue destruction, revealing a critical negative regulatory role of CTLA-4. Immunity 1995: 3: 541-7.
    • (1995) Immunity , vol.3 , pp. 541-547
    • Tivol, E.A.1    Borriello, F.2    Schweitzer, A.N.3    Lynch, W.P.4    Bluestone, J.A.5    Sharpe, A.H.6
  • 30
    • 0029120245 scopus 로고
    • CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation
    • Krummel MF, Allison JP. CD28 and CTLA-4 have opposing effects on the response of T cells to stimulation. J Exp Med 1995: 182: 459-65.
    • (1995) J Exp Med , vol.182 , pp. 459-465
    • Krummel, M.F.1    Allison, J.P.2
  • 31
    • 0030300139 scopus 로고    scopus 로고
    • The role of CTLA-4 in the regulation and initiation of T-cell responses
    • Chambers CA, Krummel MF, Boitel B et al. The role of CTLA-4 in the regulation and initiation of T-cell responses. Immunol Rev 1996: 153: 27-46.
    • (1996) Immunol Rev , vol.153 , pp. 27-46
    • Chambers, C.A.1    Krummel, M.F.2    Boitel, B.3
  • 32
    • 0029931976 scopus 로고    scopus 로고
    • Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphatidylinositol 3-kinase association
    • Pages F, Ragueneau M, Klasen S et al. Two distinct intracytoplasmic regions of the T-cell adhesion molecule CD28 participate in phosphatidylinositol 3-kinase association. J Biol Chem 1996: 271: 9403-9.
    • (1996) J Biol Chem , vol.271 , pp. 9403-9409
    • Pages, F.1    Ragueneau, M.2    Klasen, S.3
  • 33
    • 0028182749 scopus 로고
    • Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T- cell
    • Pages F, Ragueneau M, Rottapel R et al. Binding of phosphatidylinositol-3-OH kinase to CD28 is required for T- cell. Nature 1994: 369: 327-9.
    • (1994) Nature , vol.369 , pp. 327-329
    • Pages, F.1    Ragueneau, M.2    Rottapel, R.3
  • 34
    • 0028118512 scopus 로고
    • Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat T cells
    • Truitt KE, Hicks CM, Imboden JB. Stimulation of CD28 triggers an association between CD28 and phosphatidylinositol 3-kinase in Jurkat T cells. J Exp Med 1994: 179: 1071-6.
    • (1994) J Exp Med , vol.179 , pp. 1071-1076
    • Truitt, K.E.1    Hicks, C.M.2    Imboden, J.B.3
  • 35
    • 0028211126 scopus 로고
    • The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 3′-kinase
    • Stein PH, Fraser JD, Weiss A. The cytoplasmic domain of CD28 is both necessary and sufficient for costimulation of interleukin-2 secretion and association with phosphatidylinositol 3′-kinase. Mol Cell Biol 1994: 14: 3392-402.
    • (1994) Mol Cell Biol , vol.14 , pp. 3392-3402
    • Stein, P.H.1    Fraser, J.D.2    Weiss, A.3
  • 36
    • 0028221022 scopus 로고
    • T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr (P: Met-Xaa-Met motif
    • Prasad KV, Cai YC, Raab M et al. T-cell antigen CD28 interacts with the lipid kinase phosphatidylinositol 3-kinase by a cytoplasmic Tyr (P: Met-Xaa-Met motif. Proc Natl Acad Sci U S A 1994: 91: 2834-8.
    • (1994) Proc Natl Acad Sci U S A , vol.91 , pp. 2834-2838
    • Prasad, K.V.1    Cai, Y.C.2    Raab, M.3
  • 37
    • 0027940531 scopus 로고
    • CD28 signal transduction: Tyrosine phosphorylation and receptor association of phosphoinositide-3 kinase correlate with Ca (2+: Independent costimulatory activity
    • Lu Y, Phillips CA, Bjorndahl JM, Trevillyan JM. CD28 signal transduction: tyrosine phosphorylation and receptor association of phosphoinositide-3 kinase correlate with Ca (2+: independent costimulatory activity. Eur J Immunol 1994: 24: 2732-9.
    • (1994) Eur J Immunol , vol.24 , pp. 2732-2739
    • Lu, Y.1    Phillips, C.A.2    Bjorndahl, J.M.3    Trevillyan, J.M.4
  • 38
    • 0028910221 scopus 로고
    • CTLA-4 binding to the lipid kinase phosphatidylinositol 3-kinase in T cells
    • Schneider H, Prasad KV, Shoelson SE, Rudd CE. CTLA-4 binding to the lipid kinase phosphatidylinositol 3-kinase in T cells. J Exp Med 1995: 181: 351-5.
    • (1995) J Exp Med , vol.181 , pp. 351-355
    • Schneider, H.1    Prasad, K.V.2    Shoelson, S.E.3    Rudd, C.E.4
  • 39
    • 0030010956 scopus 로고    scopus 로고
    • Signaling through CD28/CTLA-4 family receptors, puzzling participation of phosphatidylinositol-3 kinase
    • Hutchcroft JE, Bierer BE. Signaling through CD28/CTLA-4 family receptors, puzzling participation of phosphatidylinositol-3 kinase. J Immunol 1996: 156: 4071-4.
    • (1996) J Immunol , vol.156 , pp. 4071-4074
    • Hutchcroft, J.E.1    Bierer, B.E.2
  • 40
    • 0023514599 scopus 로고
    • Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system
    • Aruffo A, Seed B. Molecular cloning of a CD28 cDNA by a high-efficiency COS cell expression system. Proc Natl Acad Sci U S A 1987: 84: 8573-7.
    • (1987) Proc Natl Acad Sci U S A , vol.84 , pp. 8573-8577
    • Aruffo, A.1    Seed, B.2
  • 41
    • 0029031518 scopus 로고
    • Binding stoichiometry of the cytotoxic T lymphocyte-associated molecule-4. CTLA-4: A disulfide-linked homodimer binds two CD86 molecules
    • Linsley PS, Nadler SG, Bajorath J et al. Binding stoichiometry of the cytotoxic T lymphocyte-associated molecule-4. CTLA-4: a disulfide-linked homodimer binds two CD86 molecules. J Biol Chem 1995: 270: 15417-24.
    • (1995) J Biol Chem , vol.270 , pp. 15417-15424
    • Linsley, P.S.1    Nadler, S.G.2    Bajorath, J.3
  • 42
    • 0029914089 scopus 로고    scopus 로고
    • Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell costimulatory interactions
    • Greene JL, Leytze GM, Emswiler J et al. Covalent dimerization of CD28/CTLA-4 and oligomerization of CD80/CD86 regulate T cell costimulatory interactions. J Biol Chem 1996: 271: 26762-71.
    • (1996) J Biol Chem , vol.271 , pp. 26762-26771
    • Greene, J.L.1    Leytze, G.M.2    Emswiler, J.3
  • 43
    • 0032568415 scopus 로고    scopus 로고
    • Enhanced responses to a DNA vaccine encoding a fusion antigen that is directed to sites of immune induction
    • Boyle JS, Brady JL, Lew AM. Enhanced responses to a DNA vaccine encoding a fusion antigen that is directed to sites of immune induction. Nature 1998: 392: 408-11.
    • (1998) Nature , vol.392 , pp. 408-411
    • Boyle, J.S.1    Brady, J.L.2    Lew, A.M.3
  • 44
    • 0026409881 scopus 로고
    • Identification of a cDNA encoding the rat CD28 homologue
    • Clark GJ, Dallman MJ. Identification of a cDNA encoding the rat CD28 homologue. Immunogenetics 1992: 35: 54-7.
    • (1992) Immunogenetics , vol.35 , pp. 54-57
    • Clark, G.J.1    Dallman, M.J.2
  • 45
    • 0024205313 scopus 로고
    • Human Ig superfamily CTLA-4 gene: Chromosomal localization and identity of protein sequence between murine and human CTLA-4 cytoplasmic domains
    • Dariavach P, Mattei MG, Golstein P, Lefranc MP. Human Ig superfamily CTLA-4 gene: chromosomal localization and identity of protein sequence between murine and human CTLA-4 cytoplasmic domains. Eur J Immunol 1988: 18: 1901-5.
    • (1988) Eur J Immunol , vol.18 , pp. 1901-1905
    • Dariavach, P.1    Mattei, M.G.2    Golstein, P.3    Lefranc, M.P.4
  • 46
    • 0025273486 scopus 로고
    • The murine homologue of the T lymphocyte antigen CD28. Molecular cloning and cell surface expression
    • Gross JA, St. John T, Allison JP. The murine homologue of the T lymphocyte antigen CD28. Molecular cloning and cell surface expression. J Immunol 1990: 144: 3201-10.
    • (1990) J Immunol , vol.144 , pp. 3201-3210
    • Gross, J.A.1    St. John, T.2    Allison, J.P.3
  • 47
    • 0025735829 scopus 로고
    • CTLA-4 and CD28 activated lymphocyte molecules are closely related in both mouse and human as to sequence, message expression, gene structure, and chromosomal location
    • Harper K, Balzano C, Rouvier E, Mattei MG, Luciani MF, Golstein P. CTLA-4 and CD28 activated lymphocyte molecules are closely related in both mouse and human as to sequence, message expression, gene structure, and chromosomal location. J Immunol 1991: 147: 1037-4.4.
    • (1991) J Immunol , vol.147 , pp. 1037-1044
    • Harper, K.1    Balzano, C.2    Rouvier, E.3    Mattei, M.G.4    Luciani, M.F.5    Golstein, P.6
  • 48
    • 0029079389 scopus 로고
    • Cloning and sequencing of the rabbit gene encoding T-cell costimulatory molecules
    • Isono T, Seto A. Cloning and sequencing of the rabbit gene encoding T-cell costimulatory molecules. Immunogenetics 1995: 42: 217-20.
    • (1995) Immunogenetics , vol.42 , pp. 217-220
    • Isono, T.1    Seto, A.2
  • 49
    • 0029586620 scopus 로고    scopus 로고
    • Nucleotide sequence of the ACI rat CTLA-4 molecule
    • Oaks MK, Penwell RT, Tector AJ. Nucleotide sequence of the ACI rat CTLA-4 molecule. Immunogenetics 1996: 43: 173-4.
    • (1996) Immunogenetics , vol.43 , pp. 173-174
    • Oaks, M.K.1    Penwell, R.T.2    Tector, A.J.3
  • 50
    • 0029922383 scopus 로고    scopus 로고
    • Cattle CTLA-4, CD28 and chicken CD28 bind CD86: MYPPPY is not conserved in cattle CD28
    • Parsons KR, Young JR, Collins BA, Howard CJ. Cattle CTLA-4, CD28 and chicken CD28 bind CD86: MYPPPY is not conserved in cattle CD28. Immunogenetics 1996: 43: 388-91.
    • (1996) Immunogenetics , vol.43 , pp. 388-391
    • Parsons, K.R.1    Young, J.R.2    Collins, B.A.3    Howard, C.J.4
  • 52
    • 0034665298 scopus 로고    scopus 로고
    • Porcine CTLA4-Ig lacks a MYPPPY motif, binds inefficiently to human B7 and specifically suppresses human CD4+ T-cell responses costimulated by pig but not human B7
    • Vaughan AN, Malde P, Rogers NJ, Jackson IM, Lechler RI, Dorling A. Porcine CTLA4-Ig lacks a MYPPPY motif, binds inefficiently to human B7 and specifically suppresses human CD4+ T-cell responses costimulated by pig but not human B7. J Immunol 2000: 165: 3175-81.
    • (2000) J Immunol , vol.165 , pp. 3175-3181
    • Vaughan, A.N.1    Malde, P.2    Rogers, N.J.3    Jackson, I.M.4    Lechler, R.I.5    Dorling, A.6
  • 53
    • 0035087860 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of canine T-cell costiulatory molecule (CD28)
    • Khatlani TS, Ma Z, Okuda M, Onishi T. Molecular cloning and sequencing of canine T-cell costiulatory molecule (CD28). Vet Immunol Immunopathol 2001: 78: 341-8.
    • (2001) Vet Immunol Immunopathol , vol.78 , pp. 341-348
    • Khatlani, T.S.1    Ma, Z.2    Okuda, M.3    Onishi, T.4
  • 54
    • 0034922907 scopus 로고    scopus 로고
    • Cloning, sequencing and homology analysis of nonhuman primate Fas/Fas-ligand and co-stimulatory molecules
    • Villinger F, Bostik P, Mayne A et al. Cloning, sequencing and homology analysis of nonhuman primate Fas/Fas-ligand and co-stimulatory molecules. Immunogenetics 2001: 53: 315-28.
    • (2001) Immunogenetics , vol.53 , pp. 315-328
    • Villinger, F.1    Bostik, P.2    Mayne, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.