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Volumn 266, Issue 3, 1999, Pages 798-810

Binding to human dipeptidyl peptidase IV by adenosine deaminase and antibodies that inhibit ligand binding involves overlapping, discontinuous sites on a predicted β propeller domain

Author keywords

propeller epitopes; Adenosine deaminase; CD26; Dipeptidyl peptidase IV; Ligand binding

Indexed keywords

ADENOSINE DEAMINASE; ARGININE; DIPEPTIDYL PEPTIDASE IV; EPITOPE; LEUCINE; MONOCLONAL ANTIBODY; THREONINE;

EID: 0000038304     PISSN: 00142956     EISSN: None     Source Type: Journal    
DOI: 10.1046/j.1432-1327.1999.00902.x     Document Type: Article
Times cited : (88)

References (81)
  • 1
    • 0024599588 scopus 로고
    • Dipeptidyl peptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma
    • 1. Frohman, L.A., Downs, T.R., Heimer, E.P. & Felix, A.M. (1989) Dipeptidyl peptidase IV and trypsin-like enzymatic degradation of human growth hormone-releasing hormone in plasma. J. Clin. Invest. 83, 1533-1540.
    • (1989) J. Clin. Invest. , vol.83 , pp. 1533-1540
    • Frohman, L.A.1    Downs, T.R.2    Heimer, E.P.3    Felix, A.M.4
  • 2
    • 0027494070 scopus 로고
    • Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV
    • 2. Mentlein, R., Dahms, P., Grandt, D. & Kruger, R. (1993) Proteolytic processing of neuropeptide Y and peptide YY by dipeptidyl peptidase IV. Regul. Pept. 49, 133-144.
    • (1993) Regul. Pept. , vol.49 , pp. 133-144
    • Mentlein, R.1    Dahms, P.2    Grandt, D.3    Kruger, R.4
  • 3
    • 0030819309 scopus 로고    scopus 로고
    • Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation normal T cell expressed and activated) by dipeptidyl peptidase IV (CD26)-mediated cleavage
    • 3. Oravecz, T., Pall, M., Roderiquez, G., Gorrell, M.D., Ditto, M., Nguyen, N.Y., Boykins, R., Unsworth, E. & Norcross, M.A. (1997) Regulation of the receptor specificity and function of the chemokine RANTES (regulated on activation normal T cell expressed and activated) by dipeptidyl peptidase IV (CD26)-mediated cleavage. J. Exp. Med. 186, 1865-1872.
    • (1997) J. Exp. Med. , vol.186 , pp. 1865-1872
    • Oravecz, T.1    Pall, M.2    Roderiquez, G.3    Gorrell, M.D.4    Ditto, M.5    Nguyen, N.Y.6    Boykins, R.7    Unsworth, E.8    Norcross, M.A.9
  • 4
    • 0032571360 scopus 로고    scopus 로고
    • Amino-terminal truncation of chemokines by CD26/ dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection
    • 4. Proost, P., De Meester, I., Schols, D., Struyf, S., Lambeir, A.M., Wuyts, A., Opdenakker, G., De Clercq, E., Scharpe, S. & Van Damme, J. (1998) Amino-terminal truncation of chemokines by CD26/ dipeptidyl-peptidase IV. Conversion of RANTES into a potent inhibitor of monocyte chemotaxis and HIV-1-infection. J. Biol. Chem. 273, 7222-7227.
    • (1998) J. Biol. Chem. , vol.273 , pp. 7222-7227
    • Proost, P.1    De Meester, I.2    Schols, D.3    Struyf, S.4    Lambeir, A.M.5    Wuyts, A.6    Opdenakker, G.7    De Clercq, E.8    Scharpe, S.9    Van Damme, J.10
  • 7
    • 0025851818 scopus 로고
    • Expression of the rat CD26 antigen (dipeptidyl peptidase IV) on subpopulations of rat lymphocytes
    • 7. Gorrell, M.D., Wickson, J. & McCaughan, G.W. (1991) Expression of the rat CD26 antigen (dipeptidyl peptidase IV) on subpopulations of rat lymphocytes. Cell. Immunol. 134, 205-215.
    • (1991) Cell. Immunol. , vol.134 , pp. 205-215
    • Gorrell, M.D.1    Wickson, J.2    McCaughan, G.W.3
  • 8
    • 0025318818 scopus 로고
    • The T cell triggering molecule Tp103 is associated with dipeptidyl aminopeptidase IV activity
    • 8. Hegen, M., Niedobitek, G., Klein, C.E., Stein, H. & Fleischer, B. (1990) The T cell triggering molecule Tp103 is associated with dipeptidyl aminopeptidase IV activity. J. Immunol. 144, 2908-2914.
    • (1990) J. Immunol. , vol.144 , pp. 2908-2914
    • Hegen, M.1    Niedobitek, G.2    Klein, C.E.3    Stein, H.4    Fleischer, B.5
  • 9
    • 0028952382 scopus 로고
    • The cytoplasmic tail of the T cell receptor zeta chain is required for signaling via CD26
    • 9. Mittrucker, H.W., Steeg, C., Malissen, B. & Fleischer, B. (1995) The cytoplasmic tail of the T cell receptor zeta chain is required for signaling via CD26. Eur. J. Immunol. 25, 295-297.
    • (1995) Eur. J. Immunol. , vol.25 , pp. 295-297
    • Mittrucker, H.W.1    Steeg, C.2    Malissen, B.3    Fleischer, B.4
  • 11
    • 0027401263 scopus 로고
    • A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase
    • 11. Morrison, M.E., Vijayasaradhi, S., Engelstein, D., Albino, A.P. & Houghton, A.N. (1993) A marker for neoplastic progression of human melanocytes is a cell surface ectopeptidase. J. Exp. Med. 177, 1135-1143.
    • (1993) J. Exp. Med. , vol.177 , pp. 1135-1143
    • Morrison, M.E.1    Vijayasaradhi, S.2    Engelstein, D.3    Albino, A.P.4    Houghton, A.N.5
  • 12
    • 0027201145 scopus 로고
    • Direct association of adenosine deaminase with a T cell activation antigen, CD26
    • 12. Kameoka, J., Tanaka, T., Nojima, Y., Schlossman, S.F. & Morimoto, C. (1993) Direct association of adenosine deaminase with a T cell activation antigen, CD26. Science 261, 466-469.
    • (1993) Science , vol.261 , pp. 466-469
    • Kameoka, J.1    Tanaka, T.2    Nojima, Y.3    Schlossman, S.F.4    Morimoto, C.5
  • 14
    • 0030045246 scopus 로고    scopus 로고
    • Characterization of adenosine deaminase binding to human CD26 on T cells and its biologic role in immune response
    • 14. Dong, R.P., Kameoka, J., Hegen, M., Tanaka, T., Xu, X.H., Schlossman, S.F. & Morimoto, C. (1996) Characterization of adenosine deaminase binding to human CD26 on T cells and its biologic role in immune response. J. Immunol. 156, 1349-1355.
    • (1996) J. Immunol. , vol.156 , pp. 1349-1355
    • Dong, R.P.1    Kameoka, J.2    Hegen, M.3    Tanaka, T.4    Xu, X.H.5    Schlossman, S.F.6    Morimoto, C.7
  • 15
    • 0025093094 scopus 로고
    • Characterization of the adenosine deaminase-adenosine deaminase complexing protein binding reaction
    • 15. Schrader, W.P., West, C.A., Miczek, A.D. & Norton, E.K. (1990) Characterization of the adenosine deaminase-adenosine deaminase complexing protein binding reaction. J. Biol. Chem. 265, 19312-19318.
    • (1990) J. Biol. Chem. , vol.265 , pp. 19312-19318
    • Schrader, W.P.1    West, C.A.2    Miczek, A.D.3    Norton, E.K.4
  • 16
    • 0029940265 scopus 로고    scopus 로고
    • Specific binding of adenosine deaminase but not HIV-1 transactivator protein Tat to human CD26
    • 16. Blanco, J., Marie, I., Callebaut, C., Jacotot, E., Krust, B. & Hovanessian, A.G. (1996) Specific binding of adenosine deaminase but not HIV-1 transactivator protein Tat to human CD26. Exp. Cell Res. 225, 102-111.
    • (1996) Exp. Cell Res. , vol.225 , pp. 102-111
    • Blanco, J.1    Marie, I.2    Callebaut, C.3    Jacotot, E.4    Krust, B.5    Hovanessian, A.G.6
  • 17
    • 0031908810 scopus 로고    scopus 로고
    • Enzymatic and extraenzymatic role of ecto-adenosine deaminase in lymphocytes
    • 17. Franco, R., Valenzuela, A., Lluis, C. & Blanco, J. (1998) Enzymatic and extraenzymatic role of ecto-adenosine deaminase in lymphocytes. Immunol. Rev. 161, 27-12.
    • (1998) Immunol. Rev. , vol.161 , pp. 27-112
    • Franco, R.1    Valenzuela, A.2    Lluis, C.3    Blanco, J.4
  • 18
    • 0031573556 scopus 로고    scopus 로고
    • Determination of adenosine deaminase binding domain on CD26 and its immunoregulatory effect on T cell activation
    • 18. Dong, R.P., Tachibana, K., Hegen, M., Munakata, Y., Cho, D., Schlossman, S.F. & Morimoto, C. (1997) Determination of adenosine deaminase binding domain on CD26 and its immunoregulatory effect on T cell activation. J. Immunol. 159, 6070-6076.
    • (1997) J. Immunol. , vol.159 , pp. 6070-6076
    • Dong, R.P.1    Tachibana, K.2    Hegen, M.3    Munakata, Y.4    Cho, D.5    Schlossman, S.F.6    Morimoto, C.7
  • 19
    • 0028790702 scopus 로고
    • Expression of ecto-adenosine deaminase and CD26 in human T Cells triggered by the TCR-CD3 complex - Possible role of adenosine deaminase as costimulatory molecule
    • 19. Martin, M., Huguet, J., Centelles, J.J. & Franco, R. (1995) Expression of ecto-adenosine deaminase and CD26 in human T Cells triggered by the TCR-CD3 complex - possible role of adenosine deaminase as costimulatory molecule. J. Immunol. 155, 4630-4643.
    • (1995) J. Immunol. , vol.155 , pp. 4630-4643
    • Martin, M.1    Huguet, J.2    Centelles, J.J.3    Franco, R.4
  • 20
    • 0031569543 scopus 로고    scopus 로고
    • Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles
    • 20. Valenzuela, A., Blanco, J., Callebaut, C., Jacotot, E., Lluis, C., Hovanessian, A.G. & Franco, R. (1997) Adenosine deaminase binding to human CD26 is inhibited by HIV-1 envelope glycoprotein gp120 and viral particles. J. Immunol. 158, 3721-3729.
    • (1997) J. Immunol. , vol.158 , pp. 3721-3729
    • Valenzuela, A.1    Blanco, J.2    Callebaut, C.3    Jacotot, E.4    Lluis, C.5    Hovanessian, A.G.6    Franco, R.7
  • 22
    • 0032472380 scopus 로고    scopus 로고
    • Structure of proline iminopeptidase from Xanthomonas campestris pv. citri - A prototype for the prolyl oligopeptidase family
    • 22. Medrano, F.J., Alonso, J., Garcia, J.L., Romero, A., Bode, W. & Gomis-Ruth, F.X. (1998) Structure of proline iminopeptidase from Xanthomonas campestris pv. citri - a prototype for the prolyl oligopeptidase family. EMBO J. 17, 1-9.
    • (1998) EMBO J. , vol.17 , pp. 1-9
    • Medrano, F.J.1    Alonso, J.2    Garcia, J.L.3    Romero, A.4    Bode, W.5    Gomis-Ruth, F.X.6
  • 23
    • 0032563162 scopus 로고    scopus 로고
    • Prolyl oligopeptidase - An unusual beta-propeller domain regulates proteolysis
    • 23. Fulop, V., Bocskei, Z. & Polgar, L. (1998) Prolyl oligopeptidase -an unusual beta-propeller domain regulates proteolysis. Cell 94, 161-170.
    • (1998) Cell , vol.94 , pp. 161-170
    • Fulop, V.1    Bocskei, Z.2    Polgar, L.3
  • 25
    • 0001541882 scopus 로고    scopus 로고
    • CD26: Adenosine deaminase binding, immunoblotting and species cross reactivity examined using recombinant proteins
    • Kishimoto, T., ed.. Garland Publishing Inc., New York
    • 25. Gorrell, M.D., Levy, M.T., Abbott, C.A., Washington, E.A. & McCaughan, G.W. (1997) CD26: Adenosine deaminase binding, immunoblotting and species cross reactivity examined using recombinant proteins. In Leucocyte Typing VI (Kishimoto, T., ed.) pp. 484-485. Garland Publishing Inc., New York.
    • (1997) Leucocyte Typing VI , pp. 484-485
    • Gorrell, M.D.1    Levy, M.T.2    Abbott, C.A.3    Washington, E.A.4    McCaughan, G.W.5
  • 26
    • 0025912444 scopus 로고
    • Triggering of the proteinase dipeptidyl peptidase IV (CD26) amplifies human T lymphocyte proliferation
    • 26. Bednarczyk, J.L., Carroll, S.M., Marin, C. & McIntyre, B.W. (1991) Triggering of the proteinase dipeptidyl peptidase IV (CD26) amplifies human T lymphocyte proliferation. J. Cell. Biochem. 46, 206-218.
    • (1991) J. Cell. Biochem. , vol.46 , pp. 206-218
    • Bednarczyk, J.L.1    Carroll, S.M.2    Marin, C.3    McIntyre, B.W.4
  • 28
    • 0032510678 scopus 로고    scopus 로고
    • The role of charged residues mediating low affinity protein-protein recognition at the cell surface by CD2
    • 28. Davis, S., Davies, E., Tucknott, M., Jones, E. & Merwe, P.V.D. (1998) The role of charged residues mediating low affinity protein-protein recognition at the cell surface by CD2. Proc. Natl Acad. Sci. USA 95, 5490-5494.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 5490-5494
    • Davis, S.1    Davies, E.2    Tucknott, M.3    Jones, E.4    Merwe, P.V.D.5
  • 29
    • 0030050701 scopus 로고    scopus 로고
    • Binding in the growth hormone receptor complex
    • 29. Wells, J. (1996) Binding in the growth hormone receptor complex. Proc. Natl Acad. Sci. USA 93, 1-6.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 1-6
    • Wells, J.1
  • 30
    • 0030022776 scopus 로고    scopus 로고
    • Use of immobilized adenosine deaminase (EC 3.5.4.4) for the rapid purification of native human CD26 dipeptidyl peptidase IV (EC 3.4.14.5)
    • 30. De Meester, I., Vanhoof, G., Lambeir, A.M. & Scharpe, S. (1996) Use of immobilized adenosine deaminase (EC 3.5.4.4) for the rapid purification of native human CD26 dipeptidyl peptidase IV (EC 3.4.14.5). J. Immunol. Methods 189, 99-105.
    • (1996) J. Immunol. Methods , vol.189 , pp. 99-105
    • De Meester, I.1    Vanhoof, G.2    Lambeir, A.M.3    Scharpe, S.4
  • 32
    • 0031570721 scopus 로고    scopus 로고
    • CD26/dipeptidyl peptidase IV does not work as an adenosine deaminase-binding protein in rat cells
    • 32. Iwaki-Egawa, S., Watanabe, Y. & Fujimoto, Y. (1997) CD26/dipeptidyl peptidase IV does not work as an adenosine deaminase-binding protein in rat cells. Cell. Immunol. 178, 180-186.
    • (1997) Cell. Immunol. , vol.178 , pp. 180-186
    • Iwaki-Egawa, S.1    Watanabe, Y.2    Fujimoto, Y.3
  • 33
    • 0031945149 scopus 로고    scopus 로고
    • The CP-I subunit of adenosine deaminase complexing protein from calf kidney is identical to human, mouse, and rat dipeptidyl peptidase IV
    • 33. Ben-Shooshan, I. & Parola, A.H. (1998) The CP-I subunit of adenosine deaminase complexing protein from calf kidney is identical to human, mouse, and rat dipeptidyl peptidase IV. Comp. Biochem. Physiol. B. Biochem. Mol. Biol. 119, 289-292.
    • (1998) Comp. Biochem. Physiol. B. Biochem. Mol. Biol. , vol.119 , pp. 289-292
    • Ben-Shooshan, I.1    Parola, A.H.2
  • 34
    • 0033034717 scopus 로고    scopus 로고
    • Fibroblast activation protein: A cell surface dipeptidyl peptidase and gelatinase expressed by stellate cells at the tissue remodelling interface in human cirrhosis
    • 34. Levy, M.T., McCaughan, G.W., Abbott, C.A., Park, J.E., Cunningham, A.M., Mueller, E., Rettig, W.J, & Gorrell, M.D. (1999) Fibroblast activation protein: a cell surface dipeptidyl peptidase and gelatinase expressed by stellate cells at the tissue remodelling interface in human cirrhosis. Hepatology 29, 1768-1778.
    • (1999) Hepatology , vol.29 , pp. 1768-1778
    • Levy, M.T.1    McCaughan, G.W.2    Abbott, C.A.3    Park, J.E.4    Cunningham, A.M.5    Mueller, E.6    Rettig, W.J.7    Gorrell, M.D.8
  • 35
    • 0023449851 scopus 로고
    • cDNA cloning for a bile canaliculus domain-specific membrane glycoprotein of rat hepatocytes
    • 35. Hong, W. & Doyle, D. (1987) cDNA cloning for a bile canaliculus domain-specific membrane glycoprotein of rat hepatocytes. Proc. Natl Acad. Sci. USA 84, 7962-7966.
    • (1987) Proc. Natl Acad. Sci. USA , vol.84 , pp. 7962-7966
    • Hong, W.1    Doyle, D.2
  • 36
    • 0025372845 scopus 로고
    • High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants
    • 36. Davis, S.J., Ward, H.A., Puklavec, M.J., Willis, A.C., Williams, A.F. & Barclay, A.N. (1990) High level expression in Chinese hamster ovary cells of soluble forms of CD4 T lymphocyte glycoprotein including glycosylation variants. J. Biol. Chem. 265, 10410-10418.
    • (1990) J. Biol. Chem. , vol.265 , pp. 10410-10418
    • Davis, S.J.1    Ward, H.A.2    Puklavec, M.J.3    Willis, A.C.4    Williams, A.F.5    Barclay, A.N.6
  • 39
    • 0024991898 scopus 로고
    • pEF-BOS, a powerful mammalian expression vector
    • 39. Mizushima, S. & Nagata, S. (1990) pEF-BOS, a powerful mammalian expression vector. Nucleic Acids Res. 18, 5322.
    • (1990) Nucleic Acids Res. , vol.18 , pp. 5322
    • Mizushima, S.1    Nagata, S.2
  • 40
    • 0026576817 scopus 로고
    • Ovine lentivirus is macrophagetropic and does not replicate productively in T lymphocytes
    • 40. Gorrell, M., Brandon, M., Sheffer, D., Adams, R. & Narayan, O. (1992) Ovine lentivirus is macrophagetropic and does not replicate productively in T lymphocytes. J. Virol. 66, 2679-2688.
    • (1992) J. Virol. , vol.66 , pp. 2679-2688
    • Gorrell, M.1    Brandon, M.2    Sheffer, D.3    Adams, R.4    Narayan, O.5
  • 41
    • 0032828216 scopus 로고    scopus 로고
    • Two highly conserved glutamic acid residues in the predicted beta propeller domain of dipeptidyl peptidase IV are required for its enzyme activity
    • 41. Abbott, C.A., McCaughan, G.W. & Gorrell, M.D. (1999) Two highly conserved glutamic acid residues in the predicted beta propeller domain of dipeptidyl peptidase IV are required for its enzyme activity. FEBS Lett. 458, 278-284.
    • (1999) FEBS Lett. , vol.458 , pp. 278-284
    • Abbott, C.A.1    McCaughan, G.W.2    Gorrell, M.D.3
  • 42
    • 0027982677 scopus 로고
    • Genomic organisation, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene
    • 42. Abbott, C.A., Baker, E., Sutherland, G.R. & McCaughan, G.W. (1994) Genomic organisation, exact localization, and tissue expression of the human CD26 (dipeptidyl peptidase IV) gene. Immunogenetics 40, 331-338.
    • (1994) Immunogenetics , vol.40 , pp. 331-338
    • Abbott, C.A.1    Baker, E.2    Sutherland, G.R.3    McCaughan, G.W.4
  • 43
    • 0026665626 scopus 로고
    • Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface
    • 43. Misumi, Y., Hayashi, Y., Arakawa, F. & Ikehara, Y. (1992) Molecular cloning and sequence analysis of human dipeptidyl peptidase IV, a serine proteinase on the cell surface. Biochim. Biophys. Acta 1131, 333-336.
    • (1992) Biochim. Biophys. Acta , vol.1131 , pp. 333-336
    • Misumi, Y.1    Hayashi, Y.2    Arakawa, F.3    Ikehara, Y.4
  • 45
    • 0026601838 scopus 로고
    • Biochemical characterization of CD26 (dipeptidyl peptidase IV): Functional comparison of distinct epitopes recognized by various anti-CD26 monoclonal antibodies
    • 45. Torimoto, Y., Dang, N.H., Tanaka, T., Prado, C., Schlossman, S.F. & Morimoto, C. (1992) Biochemical characterization of CD26 (dipeptidyl peptidase IV): functional comparison of distinct epitopes recognized by various anti-CD26 monoclonal antibodies. Mol. Immunol. 29, 183-192.
    • (1992) Mol. Immunol. , vol.29 , pp. 183-192
    • Torimoto, Y.1    Dang, N.H.2    Tanaka, T.3    Prado, C.4    Schlossman, S.F.5    Morimoto, C.6
  • 47
    • 0023092312 scopus 로고
    • A novel pathway of human T cell activation via a 103 kD T cell activation antigen
    • 47. Fleischer, B. (1987) A novel pathway of human T cell activation via a 103 kD T cell activation antigen. J. Immunol. 138, 1346-1350.
    • (1987) J. Immunol. , vol.138 , pp. 1346-1350
    • Fleischer, B.1
  • 49
    • 0343725700 scopus 로고    scopus 로고
    • Alterations in structure and cellular localization of molecular forms of DP IVCD26 during T cell activation
    • 49. Kähne, T., Kroning, H., Thiel, U., Ulmer, A.J., Flad, H.D. & Ansorge, S. (1996) Alterations in structure and cellular localization of molecular forms of DP IV/CD26 during T cell activation. Cell. Immunol. 170, 63-70.
    • (1996) Cell. Immunol. , vol.170 , pp. 63-70
    • Kähne, T.1    Kroning, H.2    Thiel, U.3    Ulmer, A.J.4    Flad, H.D.5    Ansorge, S.6
  • 50
    • 0021689608 scopus 로고
    • Dipeptidyl peptidase IV as a new surface marker for a subpopulation of human T-lymphocytes
    • 50. Mentlein, R., Heymann, E., Scholz, W., Feller, A.C. & Flad, H.D. (1984) Dipeptidyl peptidase IV as a new surface marker for a subpopulation of human T-lymphocytes. Cell. Immunol. 89, 11-19.
    • (1984) Cell. Immunol. , vol.89 , pp. 11-19
    • Mentlein, R.1    Heymann, E.2    Scholz, W.3    Feller, A.C.4    Flad, H.D.5
  • 53
    • 0025349737 scopus 로고
    • Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: An analysis by tissue distribution, purification and N-terminal amino acid sequence
    • 53. McCaughan, G.W., Wickson, J.E., Creswick, P.F. & Gorrell, M.D. (1990) Identification of the bile canalicular cell surface molecule GP110 as the ectopeptidase dipeptidyl peptidase IV: an analysis by tissue distribution, purification and N-terminal amino acid sequence. Hepatology 11, 534-544.
    • (1990) Hepatology , vol.11 , pp. 534-544
    • McCaughan, G.W.1    Wickson, J.E.2    Creswick, P.F.3    Gorrell, M.D.4
  • 54
    • 0026771057 scopus 로고
    • Thymocyte costimulating antigen is CD26 (dipeptidyl-peptidase IV). Costimulation of granulocyte, macrophage, and T lineage cell proliferation via CD26
    • 54. Bristol, L.A., Sakaguchi, K., Appella, E., Doyle, D. & Takacs, L. (1992) Thymocyte costimulating antigen is CD26 (dipeptidyl-peptidase IV). Costimulation of granulocyte, macrophage, and T lineage cell proliferation via CD26. J. Immunol. 149, 367-372.
    • (1992) J. Immunol. , vol.149 , pp. 367-372
    • Bristol, L.A.1    Sakaguchi, K.2    Appella, E.3    Doyle, D.4    Takacs, L.5
  • 55
    • 0026690571 scopus 로고
    • A new approach to protein fold recognition
    • 55. Jones, D.T., Taylor, W.R. & Thornton, J.M. (1992) A new approach to protein fold recognition. Nature 358, 86-89.
    • (1992) Nature , vol.358 , pp. 86-89
    • Jones, D.T.1    Taylor, W.R.2    Thornton, J.M.3
  • 56
    • 0028300741 scopus 로고
    • Combining evolutionary information and neural networks to predict protein secondary structure
    • 56. Rost, B. & Sander, C. (1994) Combining evolutionary information and neural networks to predict protein secondary structure. Proteins 19, 55-72.
    • (1994) Proteins , vol.19 , pp. 55-72
    • Rost, B.1    Sander, C.2
  • 57
    • 0027291015 scopus 로고
    • Prediction of protein secondary structure at better than 709% accuracy
    • 57. Rost, B. & Sander, C. (1993) Prediction of protein secondary structure at better than 709% accuracy. J. Mol. Biol. 232, 584-599.
    • (1993) J. Mol. Biol. , vol.232 , pp. 584-599
    • Rost, B.1    Sander, C.2
  • 59
    • 0026244229 scopus 로고
    • MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures
    • 59. Kraulis, P. (1991) MOLSCRIPT: a program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.1
  • 60
    • 0031473847 scopus 로고    scopus 로고
    • SWISS-MODEL and the Swiss-PdbViewer: An environment for comparative protein modelling
    • 60. Guex, N. & Peitsch, M.C. (1997) SWISS-MODEL and the Swiss-PdbViewer: an environment for comparative protein modelling. Electrophoresis 18, 2714-2723.
    • (1997) Electrophoresis , vol.18 , pp. 2714-2723
    • Guex, N.1    Peitsch, M.C.2
  • 62
    • 0024436374 scopus 로고
    • Evidence for a role of dipeptidyl peptidase IV in fibronectinmediated interactions of hepatocytes with extracellular matrix
    • 62. Piazza, G.A., Callanan, H.M., Mowery, J. & Hixson, D.C. (1989) Evidence for a role of dipeptidyl peptidase IV in fibronectinmediated interactions of hepatocytes with extracellular matrix. Biochem. J. 262, 327-334.
    • (1989) Biochem. J. , vol.262 , pp. 327-334
    • Piazza, G.A.1    Callanan, H.M.2    Mowery, J.3    Hixson, D.C.4
  • 64
    • 0030028728 scopus 로고    scopus 로고
    • Principles of protein-protein interactions
    • 64. Jones, S. & Thornton, J. (1996) Principles of protein-protein interactions. Proc. Natl Acad. Sci. USA 93, 13-20.
    • (1996) Proc. Natl Acad. Sci. USA , vol.93 , pp. 13-20
    • Jones, S.1    Thornton, J.2
  • 65
    • 0027674927 scopus 로고
    • N-terminal amino acid sequence of the 60-kDa protein of rat kidney dipeptidyl peptidase IV
    • 65. Iwaki-Egawa, S., Watanabe, Y. & Fujimoto, Y. (1993) N-terminal amino acid sequence of the 60-kDa protein of rat kidney dipeptidyl peptidase IV. Biol. Chem. Hoppe Seyler 374, 973-975.
    • (1993) Biol. Chem. Hoppe Seyler , vol.374 , pp. 973-975
    • Iwaki-Egawa, S.1    Watanabe, Y.2    Fujimoto, Y.3
  • 66
    • 0031566333 scopus 로고    scopus 로고
    • Cytochrome cd1 structure: Unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds
    • 66. Baker, S.C., Saunders, N.F., Willis, A.C., Ferguson, S.J., Hajdu, J. & Fulop, V. (1997) Cytochrome cd1 structure: unusual haem environments in a nitrite reductase and analysis of factors contributing to beta-propeller folds. J. Mol. Biol. 269, 440-455.
    • (1997) J. Mol. Biol. , vol.269 , pp. 440-455
    • Baker, S.C.1    Saunders, N.F.2    Willis, A.C.3    Ferguson, S.J.4    Hajdu, J.5    Fulop, V.6
  • 67
    • 0030034646 scopus 로고    scopus 로고
    • Crystal structure of a G-protein beta gamma dimer al 2.1A resolution
    • 67. Sondek, J., Bohm, A., Lambright, D.G., Hamm, H.E. & Sigler, P.B. (1996) Crystal structure of a G-protein beta gamma dimer al 2.1A resolution. Nature 379, 369-374.
    • (1996) Nature , vol.379 , pp. 369-374
    • Sondek, J.1    Bohm, A.2    Lambright, D.G.3    Hamm, H.E.4    Sigler, P.B.5
  • 71
    • 0032570814 scopus 로고    scopus 로고
    • Adenosine deaminase-deficient mice generated using a two-stage genetic engineering strategy exhibit a combined immunodeficiency
    • 71. Blackburn, M.R., Datta, S.K. & Kellems, R.E. (1998) Adenosine deaminase-deficient mice generated using a two-stage genetic engineering strategy exhibit a combined immunodeficiency. J. Biol. Chem. 273, 5093-5100.
    • (1998) J. Biol. Chem. , vol.273 , pp. 5093-5100
    • Blackburn, M.R.1    Datta, S.K.2    Kellems, R.E.3
  • 73
    • 0030437695 scopus 로고    scopus 로고
    • Extracellular purine metabolism
    • 73. Zimmerman, H. (1996) Extracellular purine metabolism. Drug Dev. Res. 39, 337-352.
    • (1996) Drug Dev. Res. , vol.39 , pp. 337-352
    • Zimmerman, H.1
  • 74
    • 0031025034 scopus 로고    scopus 로고
    • Insights into thymic purine metabolism and adenosine deaminase deficiency revealed by transgenic mice overexpressing ecto-5′-nucleotidase (CD73)
    • 74. Resta, R., Hooker, S.W., Laurent, A.B., Jamshedur Rahman, S.M., Franklin, M., Knudsen, T.B., Nadon, N.L. & Thompson, L.F. (1997) Insights into thymic purine metabolism and adenosine deaminase deficiency revealed by transgenic mice overexpressing ecto-5′-nucleotidase (CD73). J. Clin. Invest. 99, 676-683.
    • (1997) J. Clin. Invest. , vol.99 , pp. 676-683
    • Resta, R.1    Hooker, S.W.2    Laurent, A.B.3    Jamshedur Rahman, S.M.4    Franklin, M.5    Knudsen, T.B.6    Nadon, N.L.7    Thompson, L.F.8
  • 75
    • 0027132013 scopus 로고
    • Comparison of a structural and a functional epitope
    • 75. Cunningham, B.C. & Wells, J.A. (1993) Comparison of a structural and a functional epitope. J. Mol. Biol. 234, 554-563.
    • (1993) J. Mol. Biol. , vol.234 , pp. 554-563
    • Cunningham, B.C.1    Wells, J.A.2
  • 77
    • 0001962681 scopus 로고    scopus 로고
    • CD26 workshop panel report
    • Kishimoto, T., ed.. Garland Publishing Inc., New York
    • 77. Hegen, M. (1997) CD26 workshop panel report. In Leucocyte Typing VI (Kishimoto, T., ed.) pp. 478-481. Garland Publishing Inc., New York.
    • (1997) Leucocyte Typing VI , pp. 478-481
    • Hegen, M.1
  • 79
    • 0003378906 scopus 로고
    • Structural organization of the DP IV gene and its relationship with DPX and FAP-alpha transcripts
    • Fleischer, B., ed.. R. G. Landes Company, Georgetown, TX, USA
    • 79. Marguet, D., Bernard, A., David, F., Lazaro-Trueba, I. & Pierres, M. (1995) Structural organization of the DP IV gene and its relationship with DPX and FAP-alpha transcripts. In Dipeptidyl Peptidase IV (CD26) in Metabolism and the Immune Response (Fleischer, B., ed.) pp. 37-53. R. G. Landes Company, Georgetown, TX, USA.
    • (1995) Dipeptidyl Peptidase IV (CD26) in Metabolism and the Immune Response , pp. 37-53
    • Marguet, D.1    Bernard, A.2    David, F.3    Lazaro-Trueba, I.4    Pierres, M.5
  • 80
    • 0032574691 scopus 로고    scopus 로고
    • Experimental support for a beta-propeller domain in integrin alpha-subunits and a calcium binding site on its lower surface
    • 80. Oxvig, C. & Springer, T.A. (1998) Experimental support for a beta-propeller domain in integrin alpha-subunits and a calcium binding site on its lower surface. Proc. Natl Acad. Sci. USA 95, 4870-4875.
    • (1998) Proc. Natl Acad. Sci. USA , vol.95 , pp. 4870-4875
    • Oxvig, C.1    Springer, T.A.2
  • 81
    • 0028985576 scopus 로고
    • The gene for fibroblast activation protein alpha (FAP), a putative cell surface-bound serine protease expressed in cancer stroma and wound healing, maps to chromosome band 2q23
    • 81. Mathew, S., Scanlan, M.J., Mohan Raj, B.K., Murty, V.V., Garin-Chesa, P., Old, L.J., Rettig, W.J. & Chaganti, R.S. (1995) The gene for fibroblast activation protein alpha (FAP), a putative cell surface-bound serine protease expressed in cancer stroma and wound healing, maps to chromosome band 2q23. Genomics 25, 335-337.
    • (1995) Genomics , vol.25 , pp. 335-337
    • Mathew, S.1    Scanlan, M.J.2    Mohan Raj, B.K.3    Murty, V.V.4    Garin-Chesa, P.5    Old, L.J.6    Rettig, W.J.7    Chaganti, R.S.8


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