메뉴 건너뛰기




Volumn 7, Issue 11, 1995, Pages 1839-1849

Ligand binding kinetics of IL-2 and IL-15 to heteromers formed by extracellular domains of the three IL-2 receptor subunits

Author keywords

Cytokine; IL 15; IL 2; IL 2R; Kinetics; Ligand; Surface plasmon resonance

Indexed keywords

CYTOKINE; INTERLEUKIN 15; INTERLEUKIN 2; INTERLEUKIN 2 RECEPTOR; RECEPTOR SUBUNIT;

EID: 0028832725     PISSN: 09538178     EISSN: None     Source Type: Journal    
DOI: 10.1093/intimm/7.11.1839     Document Type: Article
Times cited : (33)

References (52)
  • 1
    • 0027405991 scopus 로고
    • The IL-2 receptor complex: Its structure, function, and target genes
    • Minami, Y., Kono, T., Miyazaki, T. and Taniguchi, T. 1993. The IL-2 receptor complex: its structure, function, and target genes. Annu. Rev. Immunol. 11:245.
    • (1993) Annu. Rev. Immunol , vol.11 , pp. 245
    • Minami, Y.1    Kono, T.2    Miyazaki, T.3    Taniguchi, T.4
  • 2
    • 0024441816 scopus 로고
    • The interleukin 2 receptor
    • Smith, K. A. 1989. The interleukin 2 receptor. Annu. Rev. Cell. Biol. 5:397.
    • (1989) Annu. Rev. Cell. Biol , vol.5 , pp. 397
    • Smith, K.A.1
  • 3
    • 0024349603 scopus 로고
    • The multi-subunit interleukin-2 receptor
    • Waldmann, T. A. 1989. The multi-subunit interleukin-2 receptor. Annu. Rev. Biochem. 58:875.
    • (1989) Annu. Rev. Biochem , vol.58 , pp. 875
    • Waldmann, T.A.1
  • 4
    • 0027394657 scopus 로고
    • The IL-2/IL-2 receptor system: A current overview
    • Taniguchi, T. and Minami, Y. 1993. The IL-2/IL-2 receptor system: a current overview. Cell 73:5.
    • (1993) Cell , vol.73 , pp. 5
    • Taniguchi, T.1    Minami, Y.2
  • 5
    • 0023601839 scopus 로고
    • The interleukin 2 receptor. Functional consequences of its bimolecular structure
    • Wang, H. M. and Smith, K. A. 1987. The interleukin 2 receptor. Functional consequences of its bimolecular structure. J. Exp. Med. 166:1055.
    • (1987) J. Exp. Med , vol.166 , pp. 1055
    • Wang, H.M.1    Smith, K.A.2
  • 6
    • 0023549884 scopus 로고
    • Contrasting interleukin binding properties of the alpha (p55) and beta (p70) protein subunits of the human high-affinity interleukin 2 receptor
    • Lowenthal, J. W. and Greene, W. C. 1987. Contrasting interleukin binding properties of the alpha (p55) and beta (p70) protein subunits of the human high-affinity interleukin 2 receptor. J. Exp. Med. 166:1156.
    • (1987) J. Exp. Med , vol.166 , pp. 1156
    • Lowenthal, J.W.1    Greene, W.C.2
  • 7
    • 0025912847 scopus 로고
    • Quantitative characterization of the intrinsic ligand-binding affinity of the interleukin 2 receptor beta chain and its modulation by the alpha chain and a second affinity-modulating element
    • Ringheim, G. E., Freimark, B. D. and Robb, R. J. 1991. Quantitative characterization of the intrinsic ligand-binding affinity of the interleukin 2 receptor beta chain and its modulation by the alpha chain and a second affinity-modulating element. Lymph. Cyt. Res. 10:219.
    • (1991) Lymph. Cyt. Res , vol.10 , pp. 219
    • Ringheim, G.E.1    Freimark, B.D.2    Robb, R.J.3
  • 8
    • 0024403321 scopus 로고
    • Interleukin-2 receptor beta chain gene: Generation of three receptor forms by cloned human alpha and beta chain cDNA’s
    • Hatakeyama, M., Tsudo, M., Minamoto, S., Kono, T., Doi, T., Miyata, T., Miyasaka, M. and Taniguchi, T. 1989. Interleukin-2 receptor beta chain gene: generation of three receptor forms by cloned human alpha and beta chain cDNA’s. Science 244:551.
    • (1989) Science , vol.244 , pp. 551
    • Hatakeyama, M.1    Tsudo, M.2    Minamoto, S.3    Kono, T.4    Doi, T.5    Miyata, T.6    Miyasaka, M.7    Taniguchi, T.8
  • 9
    • 0026521321 scopus 로고
    • An associated molecule, p64, with IL-2 receptor beta chain. Its possible involvement in the formation of the functional intermediate-affinity IL-2 receptor complex
    • Takeshita, T., Ohtani, K., Asao, H., Kumaki, S., Nakamura, M. and Sugamura, K. 1992. An associated molecule, p64, with IL-2 receptor beta chain. Its possible involvement in the formation of the functional intermediate-affinity IL-2 receptor complex. J. Immunol. 148:2154.
    • (1992) J. Immunol , vol.148 , pp. 2154
    • Takeshita, T.1    Ohtani, K.2    Asao, H.3    Kumaki, S.4    Nakamura, M.5    Sugamura, K.6
  • 10
    • 0026734981 scopus 로고
    • Characterization of the interleukin 2 receptors (IL-2R) expressed on human natural killer cells activated In vivo by IL-2: Association of the p64 IL-2R gamma chain with the IL-2R beta chain in functional intermediate-affinity IL-2R
    • Vtoss, S. D., Sondel, P. M. and Robb, R. J. 1992. Characterization of the interleukin 2 receptors (IL-2R) expressed on human natural killer cells activated In vivo by IL-2: association of the p64 IL-2R gamma chain with the IL-2R beta chain in functional intermediate-affinity IL-2R. J. Exp. Med. 176:531.
    • (1992) J. Exp. Med , vol.176 , pp. 531
    • Vtoss, S.D.1    Sondel, P.M.2    Robb, R.J.3
  • 11
    • 0025162844 scopus 로고
    • Structural design and molecular evolution of a cytokine receptor superfamily
    • Bazan, J. F. 1990. Structural design and molecular evolution of a cytokine receptor superfamily. Proc. Natl Acad. Sci. USA 87:6934.
    • (1990) Proc. Natl Acad. Sci. USA , vol.87 , pp. 6934
    • Bazan, J.F.1
  • 12
    • 0025767165 scopus 로고
    • WKS motifs and the cytokine receptor framework of tissue factor
    • Bazan, J. F. 1991. WKS motifs and the cytokine receptor framework of tissue factor. Trends Biochem. Sci. 16:10.
    • (1991) Trends Biochem. Sci , vol.16 , pp. 10
    • Bazan, J.F.1
  • 13
    • 0025043519 scopus 로고
    • Partial agonist/antagonist mouse interleukin-2 proteins indicate that a third component of the receptor complex functions in signal transduction
    • Zurawski, S. M., Imler, J. L. and Zurawski, G. 1990. Partial agonist/antagonist mouse interleukin-2 proteins indicate that a third component of the receptor complex functions in signal transduction. EMBO J. 9:3899.
    • (1990) EMBO J , vol.9 , pp. 3899
    • Zurawski, S.M.1    Imler, J.L.2    Zurawski, G.3
  • 14
    • 0025975005 scopus 로고
    • Signal transduction by interleukin 2 receptor beta chain: Importance of the structural integrity as revealed by site-directed mutagenesis and generation of chimeric receptors
    • Mori, H., Barsoumian, E. L., Hatakeyama, M. and Taniguchi, T. 1991. Signal transduction by interleukin 2 receptor beta chain: importance of the structural integrity as revealed by site-directed mutagenesis and generation of chimeric receptors. Int. Immunol. 3:149.
    • (1991) Int. Immunol , vol.3 , pp. 149
    • Mori, H.1    Barsoumian, E.L.2    Hatakeyama, M.3    Taniguchi, T.4
  • 15
    • 0027672155 scopus 로고
    • The interleukin-2 receptor complex and signal transduction: Role of the beta-chain
    • Kono, T., Minami, Y. and Taniguchi, T. 1993. The interleukin-2 receptor complex and signal transduction: role of the beta-chain. Semin. Immunol. 5:299.
    • (1993) Semin. Immunol , vol.5 , pp. 299
    • Kono, T.1    Minami, Y.2    Taniguchi, T.3
  • 16
    • 0024836051 scopus 로고
    • A restricted cytoplasmic region of IL-2 receptor beta chain is essential for growth signal transduction but not for ligand binding and internalization
    • Hatakeyama, M., Mori, H., Doi, T. and Taniguchi, T. 1989. A restricted cytoplasmic region of IL-2 receptor beta chain is essential for growth signal transduction but not for ligand binding and internalization. Cell 59:837.
    • (1989) Cell , vol.59 , pp. 837
    • Hatakeyama, M.1    Mori, H.2    Doi, T.3    Taniguchi, T.4
  • 18
    • 0028363377 scopus 로고
    • The interleukin (IL) 2 receptor beta chain is shared by IL-2 and a cytokine, provisionally designated IL-T, that stimulates T-cell proliferation and the induction of lymphokine-activated killer cells
    • Bamford, R. N., Grant, A. J., Burton, J. D., Peters, C., Kurys, G., Goldman, C. K., Brennan, J., Roessler, E. and Waldmann, T. A. 1994. The interleukin (IL) 2 receptor beta chain is shared by IL-2 and a cytokine, provisionally designated IL-T, that stimulates T-cell proliferation and the induction of lymphokine-activated killer cells. Proc. Natl Acad. Sci. USA 91:4940.
    • (1994) Proc. Natl Acad. Sci. USA , vol.91 , pp. 4940
    • Bamford, R.N.1    Grant, A.J.2    Burton, J.D.3    Peters, C.4    Kurys, G.5    Goldman, C.K.6    Brennan, J.7    Roessler, E.8    Waldmann, T.A.9
  • 19
    • 0025876152 scopus 로고
    • Kinetic analysis of monoclonal antibody-antigen Interactions with a new biosensor based analytical system
    • Karlsson, R., Michaelsson, A. and Mattsson, L. 1991. Kinetic analysis of monoclonal antibody-antigen Interactions with a new biosensor based analytical system. J. Immunol. Methods 145:229.
    • (1991) J. Immunol. Methods , vol.145 , pp. 229
    • Karlsson, R.1    Michaelsson, A.2    Mattsson, L.3
  • 21
    • 0027373282 scopus 로고
    • Definition and spatial location of mouse interleukin-2 residues that interact with its heterotrimeric receptor
    • Zurawski, S. M., Vfega, F., Jr, Doyle, E. L., Huyghe, B., Raherty, K., McKay, D. B. and Zurawski, G. 1993. Definition and spatial location of mouse interleukin-2 residues that interact with its heterotrimeric receptor. EMBOJ. 12:5113.
    • (1993) EMBOJ , vol.12 , pp. 5113
    • Zurawski, S.M.1    Vfega, F.2    Doyle, E.L.3    Huyghe, B.4    Raherty, K.5    McKay, D.B.6    Zurawski, G.7
  • 22
    • 0023991402 scopus 로고
    • Identification of three critical regions within mouse interleukin 2 by fine structural deletion analysis
    • Zurawski, S. M. and Zurawski, G. 1988. Identification of three critical regions within mouse interleukin 2 by fine structural deletion analysis. EMBOJ. 7:1061.
    • (1988) EMBOJ , vol.7 , pp. 1061
    • Zurawski, S.M.1    Zurawski, G.2
  • 23
    • 0027500841 scopus 로고
    • Affinity and kinetic analysis of the interaction of the cell adhesion molecules rat cd2 and cd48
    • Van der Merwe, A. P. A., Brown, M. H., Davis, S. J. and Barclay, A. N. 1993. Affinity and kinetic analysis of the interaction of the cell adhesion molecules rat cd2 and cd48. EMBO J. 12:4945.
    • (1993) EMBO J , vol.12 , pp. 4945
    • van der Merwe, A.P.A.1    Brown, M.H.2    Davis, S.J.3    Barclay, A.N.4
  • 24
    • 0027293351 scopus 로고
    • Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: Use of nonlinear least squares analysis methods
    • O’Shannessy, D. J., Brighma, B. M., Soneson, K. K., Hensley, P. and Brooks, I. 1993. Determination of rate and equilibrium binding constants for macromolecular interactions using surface plasmon resonance: use of nonlinear least squares analysis methods. Anal. Biochem. 212:457.
    • (1993) Anal. Biochem , vol.212 , pp. 457
    • O’Shannessy, D.J.1    Brighma, B.M.2    Soneson, K.K.3    Hensley, P.4    Brooks, I.5
  • 25
    • 0026645486 scopus 로고
    • Determination of kinetic constants for the interaction between a monoclonal antibody and peptides using surface plasmon resonance
    • Altschuh, D., Dubs, M. C., Weiss, E., Zeder-Lutz, G. and Van Regenmortel, M. H. V. 1992. Determination of kinetic constants for the interaction between a monoclonal antibody and peptides using surface plasmon resonance. Biochemistry 31:6298.
    • (1992) Biochemistry , vol.31 , pp. 6298
    • Altschuh, D.1    Dubs, M.C.2    Weiss, E.3    Zeder-Lutz, G.4    Van Regenmortel, M.H.V.5
  • 27
    • 0024453717 scopus 로고
    • Mouse interleukin-2 structure-function studies: Substitutions in the first alpha-helix can specifically inactivate p70 receptor binding and mutations in the fifth alpha-helix can specifically inactivate p55 receptor binding
    • Zurawski, S. M. and Zurawski, G. 1989. Mouse interleukin-2 structure-function studies: substitutions in the first alpha-helix can specifically inactivate p70 receptor binding and mutations in the fifth alpha-helix can specifically inactivate p55 receptor binding. EMBO J. 8:2583.
    • (1989) EMBO J , vol.8 , pp. 2583
    • Zurawski, S.M.1    Zurawski, G.2
  • 28
    • 0024448768 scopus 로고
    • Structure of the functional interleukin-2 receptor. Evidence for the association of human p55 and murine p75 molecules in a mouse T cell line
    • Yamaguchi, A., Ide, T., Hatakeyama, M., Doi, T., Kono, T., Uchiyama, T., Kikuchi, K., Taniguchi, T. and Uede, T. 1989. Structure of the functional interleukin-2 receptor. Evidence for the association of human p55 and murine p75 molecules in a mouse T cell line. Int. Immunol. 1:160.
    • (1989) Int. Immunol , vol.1 , pp. 160
    • Yamaguchi, A.1    Ide, T.2    Hatakeyama, M.3    Doi, T.4    Kono, T.5    Uchiyama, T.6    Kikuchi, K.7    Taniguchi, T.8    Uede, T.9
  • 29
    • 0025609656 scopus 로고
    • Stepwise formation of the high-affinity complex of the interleukin 2 receptor
    • Saito, Y., Ogura, T., Kamio, M., Sabe, H., Uchiyama, T. and Honjo, T. 1990. Stepwise formation of the high-affinity complex of the interleukin 2 receptor. Int. Immunol. 2:1167.
    • (1990) Int. Immunol , vol.2 , pp. 1167
    • Saito, Y.1    Ogura, T.2    Kamio, M.3    Sabe, H.4    Uchiyama, T.5    Honjo, T.6
  • 30
    • 0027371839 scopus 로고
    • Pseudo-high-affinity IL-2 receptor and growth signal transduction in lymphocytes
    • Saito, Y., Nazarea, M. and Honjo, T. 1993. Pseudo-high-affinity IL-2 receptor and growth signal transduction in lymphocytes. Int. Immunol. 5:1211.
    • (1993) Int. Immunol , vol.5 , pp. 1211
    • Saito, Y.1    Nazarea, M.2    Honjo, T.3
  • 31
    • 0023231404 scopus 로고
    • The murine interleukin 2 receptor. Irreversible cross-linking of radiolabeled interleukin 2 to high affinity interleukin 2 receptors reveals a noncovalently associated subunit
    • Saragovi, H. and Malek, T. R. 1987. The murine interleukin 2 receptor. Irreversible cross-linking of radiolabeled interleukin 2 to high affinity interleukin 2 receptors reveals a noncovalently associated subunit. J. Immunol. 139:1918.
    • (1987) J. Immunol , vol.139 , pp. 1918
    • Saragovi, H.1    Malek, T.R.2
  • 32
    • 0027245994 scopus 로고
    • Unexpected effects of the IL-2 receptor alpha subunit on high affinity IL-2 receptor assembly and function detected with a mutant IL-2 analog [published erratum appears in J. Immunol. 150:5731]
    • Kuziel, W. A., Ju, G., Grdina, T. A. and Greene, W. C. 1993. Unexpected effects of the IL-2 receptor alpha subunit on high affinity IL-2 receptor assembly and function detected with a mutant IL-2 analog [published erratum appears in J. Immunol. 150:5731], J. Immunol. 150:3357.
    • (1993) J. Immunol , vol.150 , pp. 3357
    • Kuziel, W.A.1    Ju, G.2    Grdina, T.A.3    Greene, W.C.4
  • 34
    • 0026577201 scopus 로고
    • The interleukin 2 receptor (IL-2R): The IL-2R alpha subunit alters the function of the IL-2R beta subunit to enhance IL-2 binding and signaling by mechanisms that do not require binding of IL-2 to IL-2R alpha subunit
    • Grant, A. J., Roessler, E., Ju, G., Tsudo, M., Sugamura, K. and Waldmann, T. A. 1992. The interleukin 2 receptor (IL-2R): the IL-2R alpha subunit alters the function of the IL-2R beta subunit to enhance IL-2 binding and signaling by mechanisms that do not require binding of IL-2 to IL-2R alpha subunit. Proc. Natl Acad. Sci. USA 89:2165.
    • (1992) Proc. Natl Acad. Sci. USA , vol.89 , pp. 2165
    • Grant, A.J.1    Roessler, E.2    Ju, G.3    Tsudo, M.4    Sugamura, K.5    Waldmann, T.A.6
  • 37
    • 0028117163 scopus 로고
    • Cytokine signal transduction
    • Kishimoto, T., Taga, T. and Akira, S. 1994. Cytokine signal transduction. Cell 76:253.
    • (1994) Cell , vol.76 , pp. 253
    • Kishimoto, T.1    Taga, T.2    Akira, S.3
  • 38
    • 0027731604 scopus 로고
    • Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors for IL-2 and IL-4
    • Kodo, M., Takeshita, T., Ishii, N., Nakamura, M., Watanabe, S., Arai, K. and Sugamura, K. 1993. Sharing of the interleukin-2 (IL-2) receptor gamma chain between receptors for IL-2 and IL-4. Science 262:1874.
    • (1993) Science , vol.262 , pp. 1874
    • Kodo, M.1    Takeshita, T.2    Ishii, N.3    Nakamura, M.4    Watanabe, S.5    Arai, K.6    Sugamura, K.7
  • 39
  • 40
    • 0027751556 scopus 로고
    • Interleukin-2 receptor gamma chain: A functional component of the interleukin-7 receptor
    • Noguchi, M., Nakamura, Y., Russell, S. M., Ziegler, S. F., Tsang, M., Cao, X. and Leonard, W. J. 1993. Interleukin-2 receptor gamma chain: a functional component of the interleukin-7 receptor. Science 262:1877.
    • (1993) Science , vol.262 , pp. 1877
    • Noguchi, M.1    Nakamura, Y.2    Russell, S.M.3    Ziegler, S.F.4    Tsang, M.5    Cao, X.6    Leonard, W.J.7
  • 41
    • 0027274890 scopus 로고
    • Receptors for interleukin-13 and interleukin-4 are complex and share a novel component that functions in signal transduction
    • Zurawski, S. M., Vaga, F., Jr, Huyghe, B. and Zurawski, G. 1993. Receptors for interleukin-13 and interleukin-4 are complex and share a novel component that functions in signal transduction. EMBOJ. 12:2663.
    • (1993) EMBOJ , vol.12 , pp. 2663
    • Zurawski, S.M.1    Vaga, F.2    Huyghe, B.3    Zurawski, G.4
  • 43
    • 0025339533 scopus 로고
    • Role of alpha chain-IL-2 complex in the formation of the ternary complex of IL-2 and high-affinity IL-2 receptor
    • Kamio, M., Uchiyama, T., Arima, N., Itoh, K., Ishikawa, T., Hori, T. and Uchino, H. 1990. Role of alpha chain-IL-2 complex in the formation of the ternary complex of IL-2 and high-affinity IL-2 receptor. Int. Immunol. 2:521.
    • (1990) Int. Immunol , vol.2 , pp. 521
    • Kamio, M.1    Uchiyama, T.2    Arima, N.3    Itoh, K.4    Ishikawa, T.5    Hori, T.6    Uchino, H.7
  • 44
    • 0025342187 scopus 로고
    • Natural killer cells activated by interleukin 2 treatment In vivo respond to interleukin 2 primarily through the p75 receptor and maintain the p55 (TAC) negative phenotype
    • Weil-Hillman, G., Vass, S. D., Fisch, P., Schell, K., Hank, J. A., Sosman, J. A., Sugamura, K. and Sondel, P. M. 1990. Natural killer cells activated by interleukin 2 treatment In vivo respond to interleukin 2 primarily through the p75 receptor and maintain the p55 (TAC) negative phenotype. Cancer Res. 50:2683.
    • (1990) Cancer Res , vol.50 , pp. 2683
    • Weil-Hillman, G.1    Vass, S.D.2    Fisch, P.3    Schell, K.4    Hank, J.A.5    Sosman, J.A.6    Sugamura, K.7    Sondel, P.M.8
  • 45
    • 0023200925 scopus 로고
    • Direct activation of human resting T cells by IL 2: The role of an IL 2 receptor distinct from the Tac protein
    • Bich-Thuy, L. T., Dukovich, M., Peffer, N. J., Fauci, A. S., Kehrl, J. H. and Greene, W. C. 1987. Direct activation of human resting T cells by IL 2: the role of an IL 2 receptor distinct from the Tac protein. J. Immunol. 139:1550.
    • (1987) J. Immunol , vol.139 , pp. 1550
    • Bich-Thuy, L.T.1    Dukovich, M.2    Peffer, N.J.3    Fauci, A.S.4    Kehrl, J.H.5    Greene, W.C.6
  • 46
    • 0027405858 scopus 로고
    • Purification of interferon gamma-interferon gamma receptor complexes by preparative electrophoresis on native gels
    • Fountoulakis, M., Takacs-Di Lorenzo, E., Juranville, J. F. and Manneberg, M. 1993. Purification of interferon gamma-interferon gamma receptor complexes by preparative electrophoresis on native gels. Anal. Biochem. 208:270.
    • (1993) Anal. Biochem , vol.208 , pp. 270
    • Fountoulakis, M.1    Takacs-Di Lorenzo, E.2    Juranville, J.F.3    Manneberg, M.4
  • 47
    • 0026008653 scopus 로고
    • Structural analyses of proteins electroblotted from native polyacrylamide gels onto polyvinyldiene difluoride membranes: A method for determining the stoichiometry of protein-protein interaction in solution
    • Wang, F. and Pan, Y. C. E. 1991. Structural analyses of proteins electroblotted from native polyacrylamide gels onto polyvinyldiene difluoride membranes: a method for determining the stoichiometry of protein-protein interaction in solution. Anal. Biochem. 198:285.
    • (1991) Anal. Biochem , vol.198 , pp. 285
    • Wang, F.1    Pan, Y.C.E.2
  • 48
    • 0028235211 scopus 로고
    • Expression and ligand characterization of the beta-subunit
    • Sana, T. R., Wu, Z., Smith, K. A. and Ciardelli, T. L. 1994. Expression and ligand characterization of the beta-subunit. Biochemistry 33:5838.
    • (1994) Biochemistry , vol.33 , pp. 5838
    • Sana, T.R.1    Wu, Z.2    Smith, K.A.3    Ciardelli, T.L.4
  • 49
    • 0028064835 scopus 로고
    • High affinity interleukin-6 receptor is a hexameric complex consisting of two molecules each of interleukin-6, interleukin-6 receptor and gp-130
    • Ward, L. D., Howlett, G. J., Discolo, G. and Yasukaw 1994. High affinity interleukin-6 receptor is a hexameric complex consisting of two molecules each of interleukin-6, interleukin-6 receptor and gp-130. J. Bid. Chem. 269:23286.
    • (1994) J. Bid. Chem , vol.269 , pp. 23286
    • Ward, L.D.1    Howlett, G.J.2    Discolo, G.3    Yasukaw, G.4
  • 50
    • 0028362141 scopus 로고
    • Monomerdimer equilibria of interleukin-8 and neutrophil-activating peptide: 2. Evidence of IL-8 binding as a dimer and oligomer to IL-8 receptor B
    • Schnitzel, W., Monschein, U. and Besemer, J. 1994. Monomerdimer equilibria of interleukin-8 and neutrophil-activating peptide: 2. Evidence of IL-8 binding as a dimer and oligomer to IL-8 receptor B. J. Leukocyte Biol. 55:763.
    • (1994) J. Leukocyte Biol , vol.55 , pp. 763
    • Schnitzel, W.1    Monschein, U.2    Besemer, J.3
  • 52
    • 0023785459 scopus 로고
    • Structural analysis of recombinant soluble human interleukin-2 receptor: Primary structure, assignment of disulfide bonds and core IL-2 binding structure
    • Miedel, M. C., Hulmes, J. D., Weber, D. V., Bailon, P. and Pan, Y. C. E. 1988. Structural analysis of recombinant soluble human interleukin-2 receptor: primary structure, assignment of disulfide bonds and core IL-2 binding structure. Biochem. Biophys. Res. Commun. 154:372.
    • (1988) Biochem. Biophys. Res. Commun , vol.154 , pp. 372
    • Miedel, M.C.1    Hulmes, J.D.2    Weber, D.V.3    Bailon, P.4    Pan, Y.C.E.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.