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Volumn 162, Issue 1, 1999, Pages 195-202

Immunosuppressive activities of recombinant glycosylation - Inhibiting factor mutants

Author keywords

[No Author keywords available]

Indexed keywords

CYTOKINE; GLYCOSYLATION INHIBITING FACTOR; IMMUNOGLOBULIN E; IMMUNOGLOBULIN G1; UNCLASSIFIED DRUG;

EID: 0032933557     PISSN: 00221767     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article
Times cited : (21)

References (33)
  • 1
    • 0021559729 scopus 로고
    • Regulation of IgE synthesis
    • Ishizaka, K. 1984. Regulation of IgE synthesis. Annu. Rev. Immunol. 2:159.
    • (1984) Annu. Rev. Immunol. , vol.2 , pp. 159
    • Ishizaka, K.1
  • 2
    • 0021722306 scopus 로고
    • IgE-binding factors from mouse T lymphocytes. III. Role of antigen-specific suppressor T cells in the formation of IgE-suppressive factor
    • Jardieu, P., T. Uede, and K. Ishizaka. 1984. IgE-binding factors from mouse T lymphocytes. III. Role of antigen-specific suppressor T cells in the formation of IgE-suppressive factor. J. Immunol. 133:3266.
    • (1984) J. Immunol. , vol.133 , pp. 3266
    • Jardieu, P.1    Uede, T.2    Ishizaka, K.3
  • 3
    • 0022626127 scopus 로고
    • Immunosuppressive effects of glycosylation inhibiting factor on the IgE and IgG response
    • Akasaki, M., P. Jardieu, and K. Ishizaka. 1986. Immunosuppressive effects of glycosylation inhibiting factor on the IgE and IgG response. J. Immunol. 136: 3172.
    • (1986) J. Immunol. , vol.136 , pp. 3172
    • Akasaki, M.1    Jardieu, P.2    Ishizaka, K.3
  • 4
    • 0030050101 scopus 로고    scopus 로고
    • Biochemical characterization of antigen-specific glycosylation-inhibiting factor from antigen-specific suppressor T cells. I. Identification of a 55-kilodalton glycosylation-inhibiting factor peptide with TCR α-chain determinant
    • Nakano, T., Y. Ishii, and K. Ishizaka. 1996. Biochemical characterization of antigen-specific glycosylation-inhibiting factor from antigen-specific suppressor T cells. I. Identification of a 55-kilodalton glycosylation-inhibiting factor peptide with TCR α-chain determinant. J. Immunol. 156:1728.
    • (1996) J. Immunol. , vol.156 , pp. 1728
    • Nakano, T.1    Ishii, Y.2    Ishizaka, K.3
  • 5
    • 0030069936 scopus 로고    scopus 로고
    • Biochemical characterization of antigen-specific glycosylation-inhibiting factor from antigen-specific suppressor T cells. II. The 55-kDa glycosylation-inhibiting factor peptide is a derivative of TCR α-chain and a subunit of antigen-specific glycosylation-inhibiting factor
    • Ishii, Y., T. Nakano, and K. Ishizaka. 1996. Biochemical characterization of antigen-specific glycosylation-inhibiting factor from antigen-specific suppressor T cells. II. The 55-kDa glycosylation-inhibiting factor peptide is a derivative of TCR α-chain and a subunit of antigen-specific glycosylation-inhibiting factor. J. Immunol. 156:1735.
    • (1996) J. Immunol. , vol.156 , pp. 1735
    • Ishii, Y.1    Nakano, T.2    Ishizaka, K.3
  • 7
    • 0027994720 scopus 로고
    • Requirement of posttranslational modifications for the generation of biologic activity of glycosylation-inhibiting factor
    • Liu, Y.-C., T. Nakano, C. Elly, and K. Ishizaka. 1994. Requirement of posttranslational modifications for the generation of biologic activity of glycosylation-inhibiting factor. Proc. Natl. Acad. Sci. USA 91:11227.
    • (1994) Proc. Natl. Acad. Sci. USA , vol.91 , pp. 11227
    • Liu, Y.-C.1    Nakano, T.2    Elly, C.3    Ishizaka, K.4
  • 8
    • 0031013144 scopus 로고    scopus 로고
    • Conversion of inactive glycosylation inhibiting factor to bioactive derivatives by modification of a SH group
    • Nakano, T., H. Watarai, Y. C. Liu, Y. Oyama, T. Mikayama, and K. Ishizaka. 1997. Conversion of inactive glycosylation inhibiting factor to bioactive derivatives by modification of a SH group. Proc. Natl. Acad. Sci. USA 94:202.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 202
    • Nakano, T.1    Watarai, H.2    Liu, Y.C.3    Oyama, Y.4    Mikayama, T.5    Ishizaka, K.6
  • 9
    • 0023990358 scopus 로고
    • Tat protein from human immunodeficiency virus forms a metal-linked dimer
    • Frankel, A. D., D. S. Bredt, and C. O. Pabo. 1988. Tat protein from human immunodeficiency virus forms a metal-linked dimer. Science 240:70.
    • (1988) Science , vol.240 , pp. 70
    • Frankel, A.D.1    Bredt, D.S.2    Pabo, C.O.3
  • 10
    • 0023254634 scopus 로고
    • Oestradiol induction of a glucocorticoid-responsive gene by a chimeric receptor
    • Green, S., and P. Chambon. 1987. Oestradiol induction of a glucocorticoid-responsive gene by a chimeric receptor. Nature 325:75.
    • (1987) Nature , vol.325 , pp. 75
    • Green, S.1    Chambon, P.2
  • 11
    • 0023927676 scopus 로고
    • Antigen-specific T cells that form IgE-potentiating factor. IgG-potentiating factor and antigen-specific glycosylation enhancing factor on antigen stimulation
    • Iwata, M., M. Adachi, and K. Ishizaka. 1988. Antigen-specific T cells that form IgE-potentiating factor. IgG-potentiating factor and antigen-specific glycosylation enhancing factor on antigen stimulation. J. Immunol. 140:2534.
    • (1988) J. Immunol. , vol.140 , pp. 2534
    • Iwata, M.1    Adachi, M.2    Ishizaka, K.3
  • 12
    • 0023151317 scopus 로고
    • Carrier-specific suppression of antibody responses by antigen-specific glycosylation inhibiting factor
    • Jardieu, P., M. Akasaki, and K. Ishizaka. 1987. Carrier-specific suppression of antibody responses by antigen-specific glycosylation inhibiting factor. J. Immunol. 138:1494.
    • (1987) J. Immunol. , vol.138 , pp. 1494
    • Jardieu, P.1    Akasaki, M.2    Ishizaka, K.3
  • 13
    • 0020601431 scopus 로고
    • Antigen recognition by H-2 restricted T cells. I. Cell-free antigen processing
    • Shimonkevitz, R., J. Kappler, P. Marrach, and H. Grey. 1981. Antigen recognition by H-2 restricted T cells. I. Cell-free antigen processing. J. Exp. Med. 158: 303.
    • (1981) J. Exp. Med. , vol.158 , pp. 303
    • Shimonkevitz, R.1    Kappler, J.2    Marrach, P.3    Grey, H.4
  • 14
    • 0016596278 scopus 로고
    • Reaginic antibody formation in the mouse. IV. Suppression of IgE and IgG antibody responses to ovalbumin following the administration of high dose urea-denatured antigen
    • Takatsu, K., and K. Ishizaka. 1975. Reaginic antibody formation in the mouse. IV. Suppression of IgE and IgG antibody responses to ovalbumin following the administration of high dose urea-denatured antigen. Cell. Immunol. 20:276.
    • (1975) Cell. Immunol. , vol.20 , pp. 276
    • Takatsu, K.1    Ishizaka, K.2
  • 16
    • 0019958714 scopus 로고
    • Lymphocytes bearing Fc receptors for IgE VIII: Affinity of mouse IgE for FcR on mouse B lymphocytes
    • Vander-Mallie, R., T. Ishizaka, and K. Ishizaka. 1982. Lymphocytes bearing Fc receptors for IgE VIII: affinity of mouse IgE for FcR on mouse B lymphocytes. J. Immunol. 128:2306.
    • (1982) J. Immunol. , vol.128 , pp. 2306
    • Vander-Mallie, R.1    Ishizaka, T.2    Ishizaka, K.3
  • 18
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during the assembly of the head of bacteriophage T4
    • Laemmli, U. K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227:680.
    • (1970) Nature , vol.227 , pp. 680
    • Laemmli, U.K.1
  • 19
    • 0029056925 scopus 로고
    • Association of the "major histocompatibility complex subregion" I-J determinant with bioactive glycosylation-inhibiting factor
    • Nakano, T., Y. C. Liu, T. Mikayama, H. Watarai, M. Taniguchi, and K. Ishizaka. 1995. Association of the "major histocompatibility complex subregion" I-J determinant with bioactive glycosylation-inhibiting factor. Proc. Natl. Acad. Sci. USA 92:9196.
    • (1995) Proc. Natl. Acad. Sci. USA , vol.92 , pp. 9196
    • Nakano, T.1    Liu, Y.C.2    Mikayama, T.3    Watarai, H.4    Taniguchi, M.5    Ishizaka, K.6
  • 20
    • 0023816153 scopus 로고
    • Construction of antigen-specific suppressor T cell hybridomas from spleen cells of mice primed for the persistent IgE antibody formation
    • Iwata, M., and K. Ishizaka. 1988. Construction of antigen-specific suppressor T cell hybridomas from spleen cells of mice primed for the persistent IgE antibody formation. J. Immunol. 141:3270.
    • (1988) J. Immunol. , vol.141 , pp. 3270
    • Iwata, M.1    Ishizaka, K.2
  • 21
    • 0027972744 scopus 로고
    • Cloning the human gene for macrophage migration inhibitory factor (MIF)
    • Paralkar, V., and G. Wistow. 1994. Cloning the human gene for macrophage migration inhibitory factor (MIF). Genomics 19:48.
    • (1994) Genomics , vol.19 , pp. 48
    • Paralkar, V.1    Wistow, G.2
  • 22
    • 0025345415 scopus 로고
    • Intermediates in the folding reactions of small proteins
    • Kim, P. S., and R. L. Balswin. 1990. Intermediates in the folding reactions of small proteins. Annu. Rev. Biochem. 59:631.
    • (1990) Annu. Rev. Biochem. , vol.59 , pp. 631
    • Kim, P.S.1    Balswin, R.L.2
  • 24
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. 1991. MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24:946.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946
    • Kraulis, P.J.1
  • 25
    • 0027166062 scopus 로고
    • Amino acid exchange and covalent modification by cysteme and glutathione explain isoforms of fatty acid-binding protein occurring in bovine liver
    • Dörmann, P., T. Börchers, U. Korf, P. Højrup, P. Roepstorff, and F. Spener. 1993. Amino acid exchange and covalent modification by cysteme and glutathione explain isoforms of fatty acid-binding protein occurring in bovine liver. J. Biol. Chem. 268:16286.
    • (1993) J. Biol. Chem. , vol.268 , pp. 16286
    • Dörmann, P.1    Börchers, T.2    Korf, U.3    Højrup, P.4    Roepstorff, P.5    Spener, F.6
  • 26
    • 0025998536 scopus 로고
    • Biochemical characterization of murine glycosylation-inhibiting factor
    • Tagaya, Y., A. Mori, and K. Ishizaka. 1991. Biochemical characterization of murine glycosylation-inhibiting factor. Proc. Natl. Acad. Sci. USA 88:9117.
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 9117
    • Tagaya, Y.1    Mori, A.2    Ishizaka, K.3
  • 27
    • 0026546810 scopus 로고
    • Glycosylation-inhibiting factor from human T cell hybridomas constructed from peripheral blood lymphocytes of a bee venom-sensitive allergic patient
    • Thomas, P., H. Gomi, T. Takeuchi, C. Carini, Y. Tagaya, and K. Ishizaka. 1992. Glycosylation-inhibiting factor from human T cell hybridomas constructed from peripheral blood lymphocytes of a bee venom-sensitive allergic patient. J. Immunol. 148:729.
    • (1992) J. Immunol. , vol.148 , pp. 729
    • Thomas, P.1    Gomi, H.2    Takeuchi, T.3    Carini, C.4    Tagaya, Y.5    Ishizaka, K.6
  • 28
    • 0030958703 scopus 로고    scopus 로고
    • High-affinity binding of bioactive glycosylation-inhibiting factor to antigen-primed T cells and natural killer cells
    • Sugie, K., T. Nakano, T. Tomura, K. Takakura, T. Mikayama, and K. Ishizaka. 1997. High-affinity binding of bioactive glycosylation-inhibiting factor to antigen-primed T cells and natural killer cells. Proc. Natl. Acad. Sci. USA 94:5278.
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 5278
    • Sugie, K.1    Nakano, T.2    Tomura, T.3    Takakura, K.4    Mikayama, T.5    Ishizaka, K.6
  • 30
    • 0027154672 scopus 로고
    • Mechanistic differences between migration inhibitory factor (MIF) and IFN-γ synergize with lipid A to mediate migration inhibition but only IFN-γ induces production of TNF-α and nitric oxide
    • Herriott, M. J., H. Jiang, C. A. Stewart, D. J. Fast, and R. W. Leu. 1993. Mechanistic differences between migration inhibitory factor (MIF) and IFN-γ synergize with lipid A to mediate migration inhibition but only IFN-γ induces production of TNF-α and nitric oxide. J. Immunol. 150:4524.
    • (1993) J. Immunol. , vol.150 , pp. 4524
    • Herriott, M.J.1    Jiang, H.2    Stewart, C.A.3    Fast, D.J.4    Leu, R.W.5
  • 31
    • 0027997701 scopus 로고
    • Purification, bioactivity, and secondary structure analysis of mouse and human macrophage migration inhibitory factor (MIF)
    • Bernhagen, J., R. A. Mitchell, T. Calandra, W. Voelter, A. Cerami, and R. Bucala. 1994. Purification, bioactivity, and secondary structure analysis of mouse and human macrophage migration inhibitory factor (MIF). Biochemistry 33:14144.
    • (1994) Biochemistry , vol.33 , pp. 14144
    • Bernhagen, J.1    Mitchell, R.A.2    Calandra, T.3    Voelter, W.4    Cerami, A.5    Bucala, R.6
  • 32
    • 0028305693 scopus 로고
    • The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor
    • Calandra, T., J. Bernhagen, R. A. Mitchell, and R. Bucala. 1994. The macrophage is an important and previously unrecognized source of macrophage migration inhibitory factor. J. Exp. Med. 179:1895.
    • (1994) J. Exp. Med. , vol.179 , pp. 1895
    • Calandra, T.1    Bernhagen, J.2    Mitchell, R.A.3    Bucala, R.4
  • 33
    • 0029959442 scopus 로고    scopus 로고
    • Cellular mechanisms for the formation of a soluble form derivative of T-cell receptor α chain by suppressor T cells
    • Ishii, Y., T. Nakano, and K. Ishizaka. 1996. Cellular mechanisms for the formation of a soluble form derivative of T-cell receptor α chain by suppressor T cells. Proc. Natl. Acad. Sci. USA 93:7207.
    • (1996) Proc. Natl. Acad. Sci. USA , vol.93 , pp. 7207
    • Ishii, Y.1    Nakano, T.2    Ishizaka, K.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.