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Volumn 22, Issue 3, 1996, Pages 281-296

Structure-function relationships of the complement regulatory protein, CD59

Author keywords

CD59; Function; Mutation; Structure

Indexed keywords

CD59 ANTIGEN; SNAKE VENOM;

EID: 0030391598     PISSN: 10799796     EISSN: None     Source Type: Journal    
DOI: 10.1006/bcmd.1996.0111     Document Type: Article
Times cited : (43)

References (47)
  • 1
    • 0027373017 scopus 로고
    • Membrane defense against complement lysis: The structure and biological properties of CD59
    • 1. Davies A, Lachmann PJ. Membrane defense against complement lysis: the structure and biological properties of CD59. Immunol Res. 12:258-275, 1993.
    • (1993) Immunol Res. , vol.12 , pp. 258-275
    • Davies, A.1    Lachmann, P.J.2
  • 2
    • 0025857372 scopus 로고
    • Inhibition of homologous complement by CD59 is mediated by a species-selective recognition conferred through binding to C8 within C5b-8 or C9 within C5b-9
    • 2. Rollins SA, Zhao J, Ninomiya H, Sims PJ. Inhibition of homologous complement by CD59 is mediated by a species-selective recognition conferred through binding to C8 within C5b-8 or C9 within C5b-9. J Immunol 146:2345-2351, 1991.
    • (1991) J Immunol , vol.146 , pp. 2345-2351
    • Rollins, S.A.1    Zhao, J.2    Ninomiya, H.3    Sims, P.J.4
  • 3
    • 0025179976 scopus 로고
    • Human protectin (CD59), an 18,000-20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 into lipid bilayers
    • 3. Meri S, Morgan BP, Davies A, et al. Human protectin (CD59), an 18,000-20,000 MW complement lysis restricting factor, inhibits C5b-8 catalysed insertion of C9 into lipid bilayers. Immunology. 71:1-9, 1990.
    • (1990) Immunology , vol.71 , pp. 1-9
    • Meri, S.1    Morgan, B.P.2    Davies, A.3
  • 4
    • 0026079656 scopus 로고
    • CD59 functions as a signal-transducing molecule for human T cell activation
    • 4. Korty PE, Brando C, Shevach EM. CD59 functions as a signal-transducing molecule for human T cell activation. J Immunol 146:4092-4098, 1991.
    • (1991) J Immunol , vol.146 , pp. 4092-4098
    • Korty, P.E.1    Brando, C.2    Shevach, E.M.3
  • 5
    • 0026489919 scopus 로고
    • CD59 molecule: A second ligand for CD2 in T cell adhesion
    • 5. Deckert M, Kubar J, Zoccola D, et al. CD59 molecule: a second ligand for CD2 in T cell adhesion. Eur J Immunol 22:2943-2947, 1992.
    • (1992) Eur J Immunol , vol.22 , pp. 2943-2947
    • Deckert, M.1    Kubar, J.2    Zoccola, D.3
  • 6
    • 0026704425 scopus 로고
    • Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59
    • 6. Hahn WC, Menu E, Bothwell AL, Sims PJ, Bierer BE. Overlapping but nonidentical binding sites on CD2 for CD58 and a second ligand CD59. Science 256:1805-1807, 1992.
    • (1992) Science , vol.256 , pp. 1805-1807
    • Hahn, W.C.1    Menu, E.2    Bothwell, A.L.3    Sims, P.J.4    Bierer, B.E.5
  • 7
    • 0026643467 scopus 로고
    • The human complement regulatory protein CD59 binds to the α chain of C8 and to the "b" domain of C9
    • 7. Ninomiya H, Sims PJ. The human complement regulatory protein CD59 binds to the α chain of C8 and to the "b" domain of C9. J Biol Chem 267:13675-13680, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 13675-13680
    • Ninomiya, H.1    Sims, P.J.2
  • 8
    • 0025873527 scopus 로고
    • Amplified gene expression in CD59-transfected Chinese hamster ovary cells confers protection against the membrane attack complex of human complement
    • 8. Zhao J, Rollins SA, Maher SE, Bothwell AL, Sims PJ. Amplified gene expression in CD59-transfected Chinese hamster ovary cells confers protection against the membrane attack complex of human complement. J. Biol Chem. 266:13418-13422, 1991.
    • (1991) J. Biol Chem. , vol.266 , pp. 13418-13422
    • Zhao, J.1    Rollins, S.A.2    Maher, S.E.3    Bothwell, A.L.4    Sims, P.J.5
  • 9
    • 0024456866 scopus 로고
    • CD59, an Ly-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells
    • 9. Davies A, Simmons DL, Hale G, et al. CD59, an Ly-6-like protein expressed in human lymphoid cells, regulates the action of the complement membrane attack complex on homologous cells. J Exp Med 170:637-654, 1989.
    • (1989) J Exp Med , vol.170 , pp. 637-654
    • Davies, A.1    Simmons, D.L.2    Hale, G.3
  • 10
    • 0025318769 scopus 로고
    • Isolation and expression of the full-length cDNA encoding CD59 antigen of human lymphocytes
    • 10. Sawada R, Ohashi K, Anaguchi H, et al. Isolation and expression of the full-length cDNA encoding CD59 antigen of human lymphocytes. DNA Cell Biol 9:213-220, 1990.
    • (1990) DNA Cell Biol , vol.9 , pp. 213-220
    • Sawada, R.1    Ohashi, K.2    Anaguchi, H.3
  • 11
    • 0027495763 scopus 로고
    • Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein
    • 11. Sugita Y, Nakano Y, Oda E, et al. Determination of carboxyl-terminal residue and disulfide bonds of MACIF (CD59), a glycosyl-phosphatidylinositol-anchored membrane protein. J Biochem (Tokyo) 14:473-477, 1993.
    • (1993) J Biochem (Tokyo) , vol.14 , pp. 473-477
    • Sugita, Y.1    Nakano, Y.2    Oda, E.3
  • 12
    • 0025885101 scopus 로고
    • Induction of the paroxysmal nocturnal hemoglobinuria phenotype in normal human erythrocytes: Effects of 2-aminoethylisothiouronium bromide on membrane proteins that regulate complement
    • 12. Ezzell JL, Wilcox LA, Bernshaw NJ, Parker CJ. Induction of the paroxysmal nocturnal hemoglobinuria phenotype in normal human erythrocytes: effects of 2-aminoethylisothiouronium bromide on membrane proteins that regulate complement. Blood 77:2764-2773, 1991.
    • (1991) Blood , vol.77 , pp. 2764-2773
    • Ezzell, J.L.1    Wilcox, L.A.2    Bernshaw, N.J.3    Parker, C.J.4
  • 13
    • 0011096388 scopus 로고
    • The action of two sulfhydryl compounds on normal human red cells: Relationship to red cells of paroxysmal nocturnal hemoglobinuria
    • 13. Sirchia G, Ferrone S, Mercuriali F. The action of two sulfhydryl compounds on normal human red cells: relationship to red cells of paroxysmal nocturnal hemoglobinuria. Blood 25:502-508, 1965.
    • (1965) Blood , vol.25 , pp. 502-508
    • Sirchia, G.1    Ferrone, S.2    Mercuriali, F.3
  • 14
    • 0015044811 scopus 로고
    • Quantitative studies on the sensitivity to complement lysis of red cells treated with thiol-reactive reagents
    • 14. Stead NW, Rosse WF. Quantitative studies on the sensitivity to complement lysis of red cells treated with thiol-reactive reagents. Blood 37:454-462, 1971.
    • (1971) Blood , vol.37 , pp. 454-462
    • Stead, N.W.1    Rosse, W.F.2
  • 15
    • 0026713676 scopus 로고
    • Contribution of the N-linked carbohydrate of erythrocyte antigen CD59 to its complement-inhibitory activity
    • 15. Ninomiya H, Stewart BH, Rollins SA, Zhao J, Bothwell AL, Sims PJ. Contribution of the N-linked carbohydrate of erythrocyte antigen CD59 to its complement-inhibitory activity. J Biol Chem 267:8404-8410, 1992.
    • (1992) J Biol Chem , vol.267 , pp. 8404-8410
    • Ninomiya, H.1    Stewart, B.H.2    Rollins, S.A.3    Zhao, J.4    Bothwell, A.L.5    Sims, P.J.6
  • 16
    • 0025176664 scopus 로고
    • Erythrocyte membrane inhibitor of reactive lysis: Effects of phosphatidylinositol-specificphospholipase C on the isolated and cell-associated protein
    • 16. Holguin MH, Wilcox LA, Bernshaw NJ, Rosse WF, Parker CJ. Erythrocyte membrane inhibitor of reactive lysis: effects of phosphatidylinositol-specificphospholipase C on the isolated and cell-associated protein. Blood 75:284-289, 1990.
    • (1990) Blood , vol.75 , pp. 284-289
    • Holguin, M.H.1    Wilcox, L.A.2    Bernshaw, N.J.3    Rosse, W.F.4    Parker, C.J.5
  • 18
    • 0026756484 scopus 로고
    • Structure of the CD59-encoding gene: Further evidence of a relationship to murine lymphocyte antigen Ly-6 protein
    • 18. Petranka JG, Fleenor DE, Sykes K, Kaufman RE, Rosse WF. Structure of the CD59-encoding gene: further evidence of a relationship to murine lymphocyte antigen Ly-6 protein. Proc Natl Acad Sci USA 89:7876-7879, 1992.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 7876-7879
    • Petranka, J.G.1    Fleenor, D.E.2    Sykes, K.3    Kaufman, R.E.4    Rosse, W.F.5
  • 19
    • 0025052018 scopus 로고
    • Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis
    • 19. Roldan AL, Cubellis MV, Masucci MT, et al. Cloning and expression of the receptor for human urokinase plasminogen activator, a central molecule in cell surface, plasmin dependent proteolysis. EMBO J 9:467-474, 1990.
    • (1990) EMBO J , vol.9 , pp. 467-474
    • Roldan, A.L.1    Cubellis, M.V.2    Masucci, M.T.3
  • 20
    • 0002233448 scopus 로고
    • The structure and pharmacology of elapid cytotoxins
    • Harvey AL, ed, New York, Pergamon Press
    • 20. Dufton MJ, Hider RC. The structure and pharmacology of elapid cytotoxins. In: Harvey AL, ed, Snake Toxins, New York, Pergamon Press, p. 259, 1993.
    • (1993) Snake Toxins , pp. 259
    • Dufton, M.J.1    Hider, R.C.2
  • 21
    • 0023841809 scopus 로고
    • Squid glycoproteins with structural similarities to Thy-1 and Ly-6 antigens
    • 21. Williams AF, Tse AG-D, Gagnon J. Squid glycoproteins with structural similarities to Thy-1 and Ly-6 antigens. Immunogenetics 27:265-272, 1988.
    • (1988) Immunogenetics , vol.27 , pp. 265-272
    • Williams, A.F.1    Tse, Ag.-D.2    Gagnon, J.3
  • 22
    • 0026793960 scopus 로고
    • Herpesvirus saimiri has a gene specifying a homologue of the cellular membrane glycoprotein CD59
    • 22. Albrecht JC, Nicholas J, Cameron KR, Newman C, Fleckenstein B, Honess RW. Herpesvirus saimiri has a gene specifying a homologue of the cellular membrane glycoprotein CD59. Virology 190:527-530, 1992.
    • (1992) Virology , vol.190 , pp. 527-530
    • Albrecht, J.C.1    Nicholas, J.2    Cameron, K.R.3    Newman, C.4    Fleckenstein, B.5    Honess, R.W.6
  • 23
    • 0025107412 scopus 로고
    • Structure of the snake short-chain neurotoxin, erabutoxin c, precursor gene
    • 23. Fuse N, Tsuchiya T, Nonomura Y, Menez A, Tamiya T. Structure of the snake short-chain neurotoxin, erabutoxin c, precursor gene. Eur J Biochem 193:629-633, 1990.
    • (1990) Eur J Biochem , vol.193 , pp. 629-633
    • Fuse, N.1    Tsuchiya, T.2    Nonomura, Y.3    Menez, A.4    Tamiya, T.5
  • 24
    • 0028136127 scopus 로고
    • The structure of the gene for the urokinase plasminogen activator receptor (UPAR)
    • 24. Casey J, Petranka J, Kottera J, Fleenor DE, Rosse WF. The structure of the gene for the urokinase plasminogen activator receptor (UPAR). Blood 84:1151-1156, 1994.
    • (1994) Blood , vol.84 , pp. 1151-1156
    • Casey, J.1    Petranka, J.2    Kottera, J.3    Fleenor, D.E.4    Rosse, W.F.5
  • 25
    • 0028773130 scopus 로고
    • Structure of a soluble, glycosylated form of the human complement regulatory protein CD59
    • 25. Fletcher CM, Harrison RA, Lachmann PJ, Neuhaus D. Structure of a soluble, glycosylated form of the human complement regulatory protein CD59. Structure 2:185-199, 1994.
    • (1994) Structure , vol.2 , pp. 185-199
    • Fletcher, C.M.1    Harrison, R.A.2    Lachmann, P.J.3    Neuhaus, D.4
  • 26
    • 0028205728 scopus 로고
    • Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins
    • 26. Kieffer B, Driscoll PC, Campbell ID, Willis AC, van der Merwe PA, Davis SJ. Three-dimensional solution structure of the extracellular region of the complement regulatory protein CD59, a new cell-surface protein domain related to snake venom neurotoxins. Biochemistry 33:4471-4482, 1994.
    • (1994) Biochemistry , vol.33 , pp. 4471-4482
    • Kieffer, B.1    Driscoll, P.C.2    Campbell, I.D.3    Willis, A.C.4    Van Der Merwe, P.A.5    Davis, S.J.6
  • 27
    • 0024962029 scopus 로고
    • The crystal structure of erabutoxin a at 2.0-A resolution
    • 27. Corfield PW, Lee TJ, Low BW The crystal structure of erabutoxin a at 2.0-A resolution. J Biol Chem 264:9239-9242, 1989.
    • (1989) J Biol Chem , vol.264 , pp. 9239-9242
    • Corfield, P.W.1    Lee, T.J.2    Low, B.W.3
  • 28
    • 0027461253 scopus 로고
    • Solution conformation of cobrotoxin: A nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study
    • 28. Yu C, Bhaskaran R, Chuang LC, Yang CC. Solution conformation of cobrotoxin: a nuclear magnetic resonance and hybrid distance geometry-dynamical simulated annealing study. Biochemistry 32:2131-2136, 1993.
    • (1993) Biochemistry , vol.32 , pp. 2131-2136
    • Yu, C.1    Bhaskaran, R.2    Chuang, L.C.3    Yang, C.C.4
  • 29
    • 0026472379 scopus 로고
    • Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: A proton NMR and molecular modeling study
    • 29. Zinn JS, Roumestand C, Gilquin B, Bontems F, Menez A, Toma F. Three-dimensional solution structure of a curaremimetic toxin from Naja nigricollis venom: a proton NMR and molecular modeling study. Biochemistry 31:11335-11347, 1992.
    • (1992) Biochemistry , vol.31 , pp. 11335-11347
    • Zinn, J.S.1    Roumestand, C.2    Gilquin, B.3    Bontems, F.4    Menez, A.5    Toma, F.6
  • 30
    • 0026538668 scopus 로고
    • Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: Calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics
    • 30. Sutcliffe MJ, Dobson CM, Oswald RE. Solution structure of neuronal bungarotoxin determined by two-dimensional NMR spectroscopy: calculation of tertiary structure using systematic homologous model building, dynamical simulated annealing, and restrained molecular dynamics. Biochemistry 31:2962-2970, 1992.
    • (1992) Biochemistry , vol.31 , pp. 2962-2970
    • Sutcliffe, M.J.1    Dobson, C.M.2    Oswald, R.E.3
  • 31
    • 0002447044 scopus 로고
    • Recombination and mutagenesis of DNA sequences using PCR
    • McPherson MJ ed, New York, IRL Press at Oxford Press
    • 31. Horton RM, Pease LR. Recombination and mutagenesis of DNA sequences using PCR. In: McPherson MJ ed, Directed Mutagenesis. A Practical Approach, New York, IRL Press at Oxford Press, 1991.
    • (1991) Directed Mutagenesis. A Practical Approach
    • Horton, R.M.1    Pease, L.R.2
  • 32
    • 0028109879 scopus 로고
    • Molecular cloning of the rat analogue of human CD59: Structural comparison with human CD59 and identification of a putative active site
    • 32. Rushmere NK, Harrison RA, van den Berg CW, Morgan BP. Molecular cloning of the rat analogue of human CD59: structural comparison with human CD59 and identification of a putative active site. Biochem J 304:595-601, 1994.
    • (1994) Biochem J , vol.304 , pp. 595-601
    • Rushmere, N.K.1    Harrison, R.A.2    Van Den Berg, C.W.3    Morgan, B.P.4
  • 33
    • 0022943266 scopus 로고
    • The crystal structure of alpha-bungarotoxin at 2.5 A resolution: Relation to solution structure and binding to acetylcholine receptor
    • 33. Love RA, Stroud RM. The crystal structure of alpha-bungarotoxin at 2.5 A resolution: relation to solution structure and binding to acetylcholine receptor. Protein Eng 1:37-46, 1986.
    • (1986) Protein Eng , vol.1 , pp. 37-46
    • Love, R.A.1    Stroud, R.M.2
  • 34
    • 0039996064 scopus 로고
    • Three-dimensional structure of the long neurotoxin from cobra venom
    • 34. Walkinshaw MD, Saenger W, Maelicke A. Three-dimensional structure of the long neurotoxin from cobra venom. Proc Natl Acad Sci USA 77:2400-2404, 1980.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 2400-2404
    • Walkinshaw, M.D.1    Saenger, W.2    Maelicke, A.3
  • 35
    • 0025195902 scopus 로고
    • Cardiotoxin V4/II from Naja mossambica mossambica: The refined crystal structure
    • 35. Rees B, Bilwes A, Samama JP, Moras D. Cardiotoxin V4/II from Naja mossambica mossambica: The refined crystal structure. J Mol Biol 214:281-297, 1990.
    • (1990) J Mol Biol , vol.214 , pp. 281-297
    • Rees, B.1    Bilwes, A.2    Samama, J.P.3    Moras, D.4
  • 36
    • 0027217194 scopus 로고
    • Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator. A domain structure belonging to a novel superfamily of glycolipid-anchored membrane proteins
    • 36. Ploug M, Kjalke M, Ronne E, Weidle U, Hoyer Hansen G, Dano K. Localization of the disulfide bonds in the NH2-terminal domain of the cellular receptor for human urokinase-type plasminogen activator. A domain structure belonging to a novel superfamily of glycolipid-anchored membrane proteins. J Biol Chem 268:17539-17546, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 17539-17546
    • Ploug, M.1    Kjalke, M.2    Ronne, E.3    Weidle, U.4    Hoyer Hansen, G.5    Dano, K.6
  • 37
    • 0028924871 scopus 로고
    • Identity of the segment of human complement C8 recognized by complement regulatory protein CD59
    • 37. Lockert DH, Kaufman KM, Chang C-P, Husler T, Sodetz JM, Sims PJ. Identity of the segment of human complement C8 recognized by complement regulatory protein CD59. J Biol Chem 270:3483-3486, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 3483-3486
    • Lockert, D.H.1    Kaufman, K.M.2    Chang, C.-P.3    Husler, T.4    Sodetz, J.M.5    Sims, P.J.6
  • 38
    • 0028924871 scopus 로고
    • Chimeras of human complement C9 reveal the site recognized by complement regulatory protein CD59
    • 38. Husler T, Lockert DH, Kaufman KM, Sodetz JM, Sims PJ. Chimeras of human complement C9 reveal the site recognized by complement regulatory protein CD59. J Biol Chem 270:3483-3486, 1995.
    • (1995) J Biol Chem , vol.270 , pp. 3483-3486
    • Husler, T.1    Lockert, D.H.2    Kaufman, K.M.3    Sodetz, J.M.4    Sims, P.J.5
  • 39
    • 0027999925 scopus 로고
    • Identity of a peptide domain of human C9 that is bound by the cell-surface inhibitor, CD59
    • 39. Chang C-P, Husler T, Zhao J, Wiedmer T, Sims PJ. Identity of a peptide domain of human C9 that is bound by the cell-surface inhibitor, CD59. J Biol Chem. 269:26424-26430, 1994.
    • (1994) J Biol Chem. , vol.269 , pp. 26424-26430
    • Chang, C.-P.1    Husler, T.2    Zhao, J.3    Wiedmer, T.4    Sims, P.J.5
  • 40
    • 0024284235 scopus 로고
    • Alpha-toxin binding to acetylcholine receptor alpha 179-191 peptides: Intrinsic fluorescence studies
    • 40. Radding W, Corfield PW, Levinson LS, Hashim GA, Low BW. Alpha-toxin binding to acetylcholine receptor alpha 179-191 peptides: intrinsic fluorescence studies. FEBS Lett 231:212-216, 1988.
    • (1988) FEBS Lett , vol.231 , pp. 212-216
    • Radding, W.1    Corfield, P.W.2    Levinson, L.S.3    Hashim, G.A.4    Low, B.W.5
  • 41
    • 0025182462 scopus 로고
    • Acetylcholine receptor-bungarotoxin interactions: Determination of the region-to-region contacts by peptide-peptide interactions and molecular modeling of the receptor cavity
    • 41. Ruan R-H, Spurling J, Quiocho FA, Atassi MZ. Acetylcholine receptor-bungarotoxin interactions: Determination of the region-to-region contacts by peptide-peptide interactions and molecular modeling of the receptor cavity. Proc Natl Acad Sci USA 87:6156-6160, 1990.
    • (1990) Proc Natl Acad Sci USA , vol.87 , pp. 6156-6160
    • Ruan, R.-H.1    Spurling, J.2    Quiocho, F.A.3    Atassi, M.Z.4
  • 42
    • 0026613082 scopus 로고
    • 1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom
    • 42. Le Du MH, Marchot P, Bougis PE, Fontecilla Camps JC. 1.9-A resolution structure of fasciculin 1, an anti-acetylcholinesterase toxin from green mamba snake venom. J Biol Chem. 267:22122-22130, 1992.
    • (1992) J Biol Chem. , vol.267 , pp. 22122-22130
    • Le Du, M.H.1    Marchot, P.2    Bougis, P.E.3    Fontecilla Camps, J.C.4
  • 43
    • 0026650803 scopus 로고
    • Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins
    • 43. McDowell RS, Dennis MS, Louie A, Shuster M, Mulkerrin MG, Lazarus RA. Mambin, a potent glycoprotein IIb-IIIa antagonist and platelet aggregation inhibitor structurally related to the short neurotoxins. Biochemistry. 31:4766-4772, 1992.
    • (1992) Biochemistry , vol.31 , pp. 4766-4772
    • McDowell, R.S.1    Dennis, M.S.2    Louie, A.3    Shuster, M.4    Mulkerrin, M.G.5    Lazarus, R.A.6
  • 44
    • 0027396750 scopus 로고
    • Genetic engineering of snake toxins. Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis
    • 44. Pillet L, Tremeau O, Ducancel F, et al. Genetic engineering of snake toxins. Role of invariant residues in the structural and functional properties of a curaremimetic toxin, as probed by site-directed mutagenesis. J Biol Chem 268:909-916, 1993.
    • (1993) J Biol Chem , vol.268 , pp. 909-916
    • Pillet, L.1    Tremeau, O.2    Ducancel, F.3
  • 45
    • 0029796957 scopus 로고    scopus 로고
    • Elimination of potential sites of glycosylation fails to abrogate complement regulatory function of cell surface CD59
    • 45. Rother RP, Zhao J, Zhou Q, Sims PJ. Elimination of potential sites of glycosylation fails to abrogate complement regulatory function of cell surface CD59. J Biol Chem 271:23842-23845, 1996.
    • (1996) J Biol Chem , vol.271 , pp. 23842-23845
    • Rother, R.P.1    Zhao, J.2    Zhou, Q.3    Sims, P.J.4
  • 46
    • 0028221373 scopus 로고
    • Enhancement of the complement regulatory function of CD59 by site-directed mutagenesis at the N-glycosylation site
    • 46. Akami T, Arakawa K, Okamoto M, et al. Enhancement of the complement regulatory function of CD59 by site-directed mutagenesis at the N-glycosylation site. Transplant Proc 26:1256-1258, 1994.
    • (1994) Transplant Proc , vol.26 , pp. 1256-1258
    • Akami, T.1    Arakawa, K.2    Okamoto, M.3
  • 47
    • 0027978350 scopus 로고
    • Cardiotoxin II from Taiwan cobra venom, Naja naja atra. Structure in solution and comparison among homologous cardiotoxins
    • 47. Bhkaskaran R, Huang C-C, Tsia Y-C, Jayaraman G, Chang D-K, Yu C. Cardiotoxin II from Taiwan cobra venom, Naja naja atra. Structure in solution and comparison among homologous cardiotoxins. J Biol Chem 269:23500-23508, 1994.
    • (1994) J Biol Chem , vol.269 , pp. 23500-23508
    • Bhkaskaran, R.1    Huang, C.-C.2    Tsia, Y.-C.3    Jayaraman, G.4    Chang, D.-K.5    Yu, C.6


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