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Volumn 180, Issue , 2001, Pages 35-48

Structure and biology of complement protein C3, a connecting link between innate and acquired immunity

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT COMPONENT C3;

EID: 0035006284     PISSN: 01052896     EISSN: None     Source Type: Journal    
DOI: 10.1034/j.1600-065X.2001.1800103.x     Document Type: Review
Times cited : (449)

References (120)
  • 1
    • 0002431025 scopus 로고    scopus 로고
    • The chemistry and biology of C3,C4, and C5
    • Volanakis JE, Frank M, eds. New York: Marcel Dekker Inc
    • 1. Lambris JD, Sahu A, Wetsel R. The chemistry and biology of C3,C4, and C5. In: Volanakis JE, Frank M, eds. The human complement system in health and disease. New York: Marcel Dekker Inc; 1998. p. 83-118.
    • (1998) The Human Complement System in Health and Disease , pp. 83-118
    • Lambris, J.D.1    Sahu, A.2    Wetsel, R.3
  • 2
    • 0032521276 scopus 로고    scopus 로고
    • Sea urchin coelomocytes specifically express a homologue of the complement component C3
    • 2. Al-Sharif WZ, Sunyer JO, Lambris JD, Smith LC. Sea urchin coelomocytes specifically express a homologue of the complement component C3. J Immunol 1997;160:2983-2997.
    • (1997) J Immunol , vol.160 , pp. 2983-2997
    • Al-Sharif, W.Z.1    Sunyer, J.O.2    Lambris, J.D.3    Smith, L.C.4
  • 3
    • 0001653504 scopus 로고    scopus 로고
    • Phylogeny of the complement system
    • Volanakis JE, Frank MM, eds. New York: Marcel Dekker Inc
    • 3. Nonaka M, Phylogeny of the complement system. In: Volanakis JE, Frank MM, eds. The human complement system in health and disease. New York: Marcel Dekker Inc; 1998. p. 203-215.
    • (1998) The Human Complement System in Health and Disease , pp. 203-215
    • Nonaka, M.1
  • 4
    • 0004940281 scopus 로고
    • 1,4,2 to E*
    • 1,4,2 to E* Science 1958;127:234-236.
    • (1958) Science , vol.127 , pp. 234-236
    • Rapp, H.J.1
  • 5
    • 0016165221 scopus 로고
    • Role of complement in induction of antibody production in vivo. Effect of cobra factor and other C3-reactive agents on thymus-dependent and thymus-independent antibody responses
    • 5. Pepys MB. Role of complement in induction of antibody production in vivo. Effect of cobra factor and other C3-reactive agents on thymus-dependent and thymus-independent antibody responses. J Exp Med 1974;140:126-145.
    • (1974) J Exp Med , vol.140 , pp. 126-145
    • Pepys, M.B.1
  • 7
    • 0013141948 scopus 로고
    • Human complement component C3: cDNA coding sequence and derived primary structure
    • 7. De Bruijn MHL, Fey GH. Human complement component C3: cDNA coding sequence and derived primary structure. Proc Natl Acad Sci USA 1985;82:708-712.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 708-712
    • De Bruijn, M.H.L.1    Fey, G.H.2
  • 8
    • 0026095523 scopus 로고
    • Functional expression of furin demonstrating its intracellular localization and endoprotease activity for processing of proalbumin and complement pro-C3
    • 8. Misumi Y, Oda K, Fujiwara T, Takami N, Tashiro K, Ikehara Y. Functional expression of furin demonstrating its intracellular localization and endoprotease activity for processing of proalbumin and complement pro-C3. J Biol Chem 1991;266:16954-16959.
    • (1991) J Biol Chem , vol.266 , pp. 16954-16959
    • Misumi, Y.1    Oda, K.2    Fujiwara, T.3    Takami, N.4    Tashiro, K.5    Ikehara, Y.6
  • 9
    • 0022411349 scopus 로고
    • Structures of sugar chains of the third component of human complement
    • 9. Hase S, Kikuchi N, Ikenaka T, Inoue K. Structures of sugar chains of the third component of human complement. J Biochem (Tokyo) 1985;98:863-874.
    • (1985) J Biochem (Tokyo) , vol.98 , pp. 863-874
    • Hase, S.1    Kikuchi, N.2    Ikenaka, T.3    Inoue, K.4
  • 10
    • 0022629028 scopus 로고
    • Structural analysis of the asparagine-linked oligosaccharides of human complement component C3
    • 10. Hirani S, Lambris JD, Müller-Eberhard HJ. Structural analysis of the asparagine-linked oligosaccharides of human complement component C3. Biochem J 1986;233:613-616.
    • (1986) Biochem J , vol.233 , pp. 613-616
    • Hirani, S.1    Lambris, J.D.2    Müller-Eberhard, H.J.3
  • 11
    • 0019141474 scopus 로고
    • Crystal structure analysis and molecular model of human C3a anaphylatoxin. Hoppe Seylers
    • 11. Huber R, Scholze H, Paques EP, Deisenhofer J. Crystal structure analysis and molecular model of human C3a anaphylatoxin. Hoppe Seylers Z Physiol Chem 1980;361:1389-1399.
    • (1980) Z Physiol Chem , vol.361 , pp. 1389-1399
    • Huber, R.1    Scholze, H.2    Paques, E.P.3    Deisenhofer, J.4
  • 12
    • 0027390920 scopus 로고
    • Bisulfide bridges in human complement component C3b
    • 12. Dolmer K, Sottrup-Jensen L. Bisulfide bridges in human complement component C3b. FEBS Lett 1993;315:85-90.
    • (1993) FEBS Lett , vol.315 , pp. 85-90
    • Dolmer, K.1    Sottrup-Jensen, L.2
  • 13
    • 0032557324 scopus 로고    scopus 로고
    • X-ray crystal structure of C3d: A C3 fragment and ligand for complement receptor 2
    • 13. Nagar B, Jones RG, Diefenbach RJ, Isenman DE, Rini JM. X-ray crystal structure of C3d: a C3 fragment and ligand for complement receptor 2. Science 1998;280:1277-1281.
    • (1998) Science , vol.280 , pp. 1277-1281
    • Nagar, B.1    Jones, R.G.2    Diefenbach, R.J.3    Isenman, D.E.4    Rini, J.M.5
  • 15
    • 0013863229 scopus 로고
    • The reaction mechanism of β1c-Globulin (C′3) in immune hemolysis
    • 15. Müller-Eberhard HJ, Dalmasso AP, Calcott MA. The reaction mechanism of β1c-Globulin (C′3) in immune hemolysis. J Exp Med 1966;123:33-54.
    • (1966) J Exp Med , vol.123 , pp. 33-54
    • Müller-Eberhard, H.J.1    Dalmasso, A.P.2    Calcott, M.A.3
  • 16
    • 0031043135 scopus 로고    scopus 로고
    • The internal thioester and the covalent binding properties of the complement proteins C3 and C4
    • 16. Law SKA, Dodds AW. The internal thioester and the covalent binding properties of the complement proteins C3 and C4. Protein Sci 1997;6:263-274.
    • (1997) Protein Sci , vol.6 , pp. 263-274
    • Law, S.K.A.1    Dodds, A.W.2
  • 17
    • 0345176684 scopus 로고
    • Evidence for presence of an internal thiolester bond in third component of human complement
    • 17. Tack BF, Harrison RA, Janatova J, Thomas ML, Prahl JW. Evidence for presence of an internal thiolester bond in third component of human complement. Proc Natl Acad Sci USA 1980;77:5764-5768.
    • (1980) Proc Natl Acad Sci USA , vol.77 , pp. 5764-5768
    • Tack, B.F.1    Harrison, R.A.2    Janatova, J.3    Thomas, M.L.4    Prahl, J.W.5
  • 18
    • 0025023871 scopus 로고
    • Genomic organization of human complement component C3
    • 18. Fong KY, Botto M, Walport MJ, So AK. Genomic organization of human complement component C3. Genomics 1990;7:579-586.
    • (1990) Genomics , vol.7 , pp. 579-586
    • Fong, K.Y.1    Botto, M.2    Walport, M.J.3    So, A.K.4
  • 19
    • 0019501478 scopus 로고
    • Formation of the initial C3 convertase of the alternative pathway: Acquisition of C3b-like activities by spontaneous hydrolysis of the putative thioester in native C3
    • 19. Pangburn MK, Schreiber RD, Müller-Eberhard HJ. Formation of the initial C3 convertase of the alternative pathway: acquisition of C3b-like activities by spontaneous hydrolysis of the putative thioester in native C3. J Exp Med 1981;154:856-867.
    • (1981) J Exp Med , vol.154 , pp. 856-867
    • Pangburn, M.K.1    Schreiber, R.D.2    Müller-Eberhard, H.J.3
  • 20
    • 0025291095 scopus 로고
    • Demonstration in human plasma of a form of C3 that has the conformation of "C3b-like C3"
    • 20. Hack CE, Paardekooper J, Van Milligen F. Demonstration in human plasma of a form of C3 that has the conformation of "C3b-like C3". J Immunol 1990;144:4249-4255.
    • (1990) J Immunol , vol.144 , pp. 4249-4255
    • Hack, C.E.1    Paardekooper, J.2    Van Milligen, F.3
  • 21
    • 0028124668 scopus 로고
    • Specificity of the thioester-containing reactive site of human C3 and its significance to complement activation
    • 21. Sahu A, Kozel TR, Pangburn MK. Specificity of the thioester-containing reactive site of human C3 and its significance to complement activation. Biochem J 1994;302:429-436.
    • (1994) Biochem J , vol.302 , pp. 429-436
    • Sahu, A.1    Kozel, T.R.2    Pangburn, M.K.3
  • 22
    • 0027988132 scopus 로고
    • Covalent attachment of human complement C3 to IgG: Identification of the amino acid residue involved in ester linkage formation
    • 22. Sahu A, Pangburn MK. Covalent attachment of human complement C3 to IgG: identification of the amino acid residue involved in ester linkage formation. J Biol Chem 1994;269:28997-29002.
    • (1994) J Biol Chem , vol.269 , pp. 28997-29002
    • Sahu, A.1    Pangburn, M.K.2
  • 23
    • 0029119566 scopus 로고
    • Tyrosine is a potential site for covalent attachment of activated complement component C3
    • 23. Sahu A, Pangburn MK. Tyrosine is a potential site for covalent attachment of activated complement component C3. Mol Immunol 1995;32:711-716.
    • (1995) Mol Immunol , vol.32 , pp. 711-716
    • Sahu, A.1    Pangburn, M.K.2
  • 24
    • 0029865548 scopus 로고    scopus 로고
    • Investigation of mechanism-based inhibitors of complement targeting the activated thioester of human C3
    • 24. Sahu A, Pangburn MK. Investigation of mechanism-based inhibitors of complement targeting the activated thioester of human C3. Biochem Pharmacol 1996;51:797-804.
    • (1996) Biochem Pharmacol , vol.51 , pp. 797-804
    • Sahu, A.1    Pangburn, M.K.2
  • 25
    • 0026768697 scopus 로고
    • Covalent binding of C3b to C4b within the classical complement pathway C5 convertase: Determination of amino acid residues involved in ester linkage formation
    • 25. Kim YU, et al. Covalent binding of C3b to C4b within the classical complement pathway C5 convertase: determination of amino acid residues involved in ester linkage formation. J Biol Chem 1992;267:4171-4176.
    • (1992) J Biol Chem , vol.267 , pp. 4171-4176
    • Kim, Y.U.1
  • 26
    • 0024159572 scopus 로고
    • C5 convertase of the alternative complement pathway: Covalent linkage between two C3b molecules within the trimolecular complex enzyme
    • 26. Kinoshita T, Takata Y, Kozono H, Takeda J, Hong K, Inoue K. C5 convertase of the alternative complement pathway: covalent linkage between two C3b molecules within the trimolecular complex enzyme. J Immunol 1988;141:3895-3901.
    • (1988) J Immunol , vol.141 , pp. 3895-3901
    • Kinoshita, T.1    Takata, Y.2    Kozono, H.3    Takeda, J.4    Hong, K.5    Inoue, K.6
  • 27
    • 0031921084 scopus 로고    scopus 로고
    • The role of complement and complement receptors in induction and regulation of immunity
    • 27. Carroll MC. The role of complement and complement receptors in induction and regulation of immunity. Annu Rev Immunol 1998;16:545-568.
    • (1998) Annu Rev Immunol , vol.16 , pp. 545-568
    • Carroll, M.C.1
  • 28
    • 0023796341 scopus 로고
    • The multifunctional role of C3, the third component of complement
    • 28. Lambris JD. The multifunctional role of C3, the third component of complement. Immunol Today 1988;9:387-393.
    • (1988) Immunol Today , vol.9 , pp. 387-393
    • Lambris, J.D.1
  • 29
    • 0030004710 scopus 로고    scopus 로고
    • Dissection of CR1, factor H, MCP, and factor B binding and functional sites in third complement component
    • 29. Lambris JD, Lao Z, Oglesby TJ, Atkinson JP, Hack E, Becherer JD. Dissection of CR1, factor H, MCP, and factor B binding and functional sites in third complement component. J Immunol 1996;156:4821-4832.
    • (1996) J Immunol , vol.156 , pp. 4821-4832
    • Lambris, J.D.1    Lao, Z.2    Oglesby, T.J.3    Atkinson, J.P.4    Hack, E.5    Becherer, J.D.6
  • 30
    • 0019922677 scopus 로고
    • Generation of three different fragments of bound C3 with purified factor I or serum. I. Requirements for factor H vs CR1 cofactor activity
    • 30. Ross GD, Lambris JD, Cain JA, Newman SL. Generation of three different fragments of bound C3 with purified factor I or serum. I. Requirements for factor H vs CR1 cofactor activity. J Immunol 1982;129:2051-2060.
    • (1982) J Immunol , vol.129 , pp. 2051-2060
    • Ross, G.D.1    Lambris, J.D.2    Cain, J.A.3    Newman, S.L.4
  • 31
    • 0020576585 scopus 로고
    • Role of human factor I and C3b receptor in the cleavage of surface-bound C3b
    • 31. Medicus RG, Melamed J, Arnaout MA. Role of human factor I and C3b receptor in the cleavage of surface-bound C3b. Eur J Immunol 1983;13:465-470.
    • (1983) Eur J Immunol , vol.13 , pp. 465-470
    • Medicus, R.G.1    Melamed, J.2    Arnaout, M.A.3
  • 32
    • 0020362094 scopus 로고
    • Structural characterization of factor I mediated cleavage of the third component of complement
    • 32. Davis AEI, Harrison RA. Structural characterization of factor I mediated cleavage of the third component of complement. Biochemistry 1982;21:5745-5749.
    • (1982) Biochemistry , vol.21 , pp. 5745-5749
    • Davis, A.E.I.1    Harrison, R.A.2
  • 34
    • 0026572304 scopus 로고
    • Conformational differences between surface-bound and fluid-phase complement-component-C3 fragments. Epitope mapping by cDNA expression
    • 34. Nilsson B, Grossberger D, Nilsson Ekdahl K, Riegert P, Becherer D, Lambris JD. Conformational differences between surface-bound and fluid-phase complement-component-C3 fragments. Epitope mapping by cDNA expression. Biochem J 1992;282:715-721.
    • (1992) Biochem J , vol.282 , pp. 715-721
    • Nilsson, B.1    Grossberger, D.2    Nilsson Ekdahl, K.3    Riegert, P.4    Becherer, D.5    Lambris, J.D.6
  • 35
    • 0033151988 scopus 로고    scopus 로고
    • Active sites in complement components C5 and C3 identified by proximity to indels in the C3/4/5 protein family
    • 35. Low PJ, Ai R, Ogata RT. Active sites in complement components C5 and C3 identified by proximity to indels in the C3/4/5 protein family. J Immunol 1999;162:6580-6588.
    • (1999) J Immunol , vol.162 , pp. 6580-6588
    • Low, P.J.1    Ai, R.2    Ogata, R.T.3
  • 36
    • 0032212249 scopus 로고    scopus 로고
    • Active sites in complement component C3 mapped by mutations at indels
    • 36. Ogata RT, Ai R, Low PJ. Active sites in complement component C3 mapped by mutations at indels. J Immunol 1998;161:4785-4794.
    • (1998) J Immunol , vol.161 , pp. 4785-4794
    • Ogata, R.T.1    Ai, R.2    Low, P.J.3
  • 37
    • 0023929209 scopus 로고
    • A 34-amino acid peptide of the third component of complement mediates properdin binding
    • published erratum appears in J Immunol 1988;141:1788
    • 37. Daoudaki ME, Becherer JD, Lambris JD. A 34-amino acid peptide of the third component of complement mediates properdin binding [published erratum appears in J Immunol 1988;141:1788]. J Immunol 1988;140:1577-1580.
    • (1988) J Immunol , vol.140 , pp. 1577-1580
    • Daoudaki, M.E.1    Becherer, J.D.2    Lambris, J.D.3
  • 38
    • 0021950144 scopus 로고
    • Localization of the conglutinin binding site on the third component of human complement
    • 38. Hirani S, Lambris JD, Müller-Eberhard HJ. Localization of the conglutinin binding site on the third component of human complement. J Immunol 1985;134:1105-1109.
    • (1985) J Immunol , vol.134 , pp. 1105-1109
    • Hirani, S.1    Lambris, J.D.2    Müller-Eberhard, H.J.3
  • 39
    • 0023708278 scopus 로고
    • A discontinuous factor H binding site in the third component of complement as delineated by synthetic peptides
    • 39. Lambris JD, Avila D, Becherer JD, Müller-Eberhard HJ. A discontinuous factor H binding site in the third component of complement as delineated by synthetic peptides. J Biol Chem 1988;263:12147-12150.
    • (1988) J Biol Chem , vol.263 , pp. 12147-12150
    • Lambris, J.D.1    Avila, D.2    Becherer, J.D.3    Müller-Eberhard, H.J.4
  • 40
    • 0023785189 scopus 로고
    • Identification of the C3b receptor-binding domain in third component of complement
    • 40. Becherer JD, Lambris JD. Identification of the C3b receptor-binding domain in third component of complement. J Biol Chem 1988;263:14586-14591.
    • (1988) J Biol Chem , vol.263 , pp. 14586-14591
    • Becherer, J.D.1    Lambris, J.D.2
  • 41
    • 0009247302 scopus 로고
    • Mapping of the C3d receptor (CR2)-binding site and a neoantigenic site in the C3d domain of the third component of complement
    • 41. Lambris JD, Ganu VS, Hirani S, Müller-Eberhard HJ. Mapping of the C3d receptor (CR2)-binding site and a neoantigenic site in the C3d domain of the third component of complement. Proc Natl Acad Sci USA 1985;82:4235-1239.
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 4235-11239
    • Lambris, J.D.1    Ganu, V.S.2    Hirani, S.3    Müller-Eberhard, H.J.4
  • 42
    • 0017236603 scopus 로고
    • Multiple sedimenting species of properdin in human and interaction of purified properdin with the third component of complement
    • 42. Chapitis J, Lepow IH. Multiple sedimenting species of properdin in human and interaction of purified properdin with the third component of complement. J Exp Med 1976;143:241-257.
    • (1976) J Exp Med , vol.143 , pp. 241-257
    • Chapitis, J.1    Lepow, I.H.2
  • 43
    • 0021365642 scopus 로고
    • Mapping of the properdin-binding site in the third component of complement
    • 43. Lambris JD, Alsenz J, Schulz TF, Dierich MP. Mapping of the properdin-binding site in the third component of complement. Biochem J 1984;217:323-326.
    • (1984) Biochem J , vol.217 , pp. 323-326
    • Lambris, J.D.1    Alsenz, J.2    Schulz, T.F.3    Dierich, M.P.4
  • 44
    • 0021041583 scopus 로고
    • Fulminant meningococcal infections in a family with inherited deficiency of properdin
    • 44. Braconier JH, Sjoholm AG, Soderstrom C. Fulminant meningococcal infections in a family with inherited deficiency of properdin. Scand J Infect Dis 1983;15:339-344.
    • (1983) Scand J Infect Dis , vol.15 , pp. 339-344
    • Braconier, J.H.1    Sjoholm, A.G.2    Soderstrom, C.3
  • 45
    • 0025872447 scopus 로고
    • Complement-C3 - A molecular mosaic of binding sites
    • 45. Fishelson Z. Complement-C3 - a molecular mosaic of binding sites. Mol Immunol 1991;28:545-552.
    • (1991) Mol Immunol , vol.28 , pp. 545-552
    • Fishelson, Z.1
  • 46
    • 0028006579 scopus 로고
    • Interactions of human complement component C3 with factor B and with complement receptors type 1 (CR1, CD35) and type 3 (CR3, CD11b/CD18) involve an acidic sequence at the N-terminus of C3 α-chain
    • 46. Taniguchi-Sidle A, Isenman DE. Interactions of human complement component C3 with factor B and with complement receptors type 1 (CR1, CD35) and type 3 (CR3, CD11b/CD18) involve an acidic sequence at the N-terminus of C3 α-chain. J Immunol 1994;153:5285-5302.
    • (1994) J Immunol , vol.153 , pp. 5285-5302
    • Taniguchi-Sidle, A.1    Isenman, D.E.2
  • 47
    • 0034623118 scopus 로고    scopus 로고
    • Each of the three binding sites on complement factor H interacts with a distinct site on C3b
    • 47. Jokiranta TS, Hellwage J, Koistinen V, Zipfel PF, Meri S. Each of the three binding sites on complement factor H interacts with a distinct site on C3b. J Biol Chem 2000;275:27657-27662.
    • (2000) J Biol Chem , vol.275 , pp. 27657-27662
    • Jokiranta, T.S.1    Hellwage, J.2    Koistinen, V.3    Zipfel, P.F.4    Meri, S.5
  • 48
    • 0033582520 scopus 로고    scopus 로고
    • Identification of residues within the 727-767 segment of human complement component C3 important for its interaction with factor H and with complement receptor 1 (CR1, CD35)
    • 48. Oran AE, Isenman DE. Identification of residues within the 727-767 segment of human complement component C3 important for its interaction with factor H and with complement receptor 1 (CR1, CD35). J Biol Chem 1999;274:5120-5130.
    • (1999) J Biol Chem , vol.274 , pp. 5120-5130
    • Oran, A.E.1    Isenman, D.E.2
  • 49
    • 0016681070 scopus 로고
    • Specificity of human lymphocyte complement receptors
    • 49. Ross GD, Polley MJ. Specificity of human lymphocyte complement receptors. J Exp Med 1975;141:1163-1180.
    • (1975) J Exp Med , vol.141 , pp. 1163-1180
    • Ross, G.D.1    Polley, M.J.2
  • 50
    • 0022405823 scopus 로고
    • Human follicular dendritic cells express CR1, CR2, and CR3 complement receptor antigens
    • 50. Reynes M, et al. Human follicular dendritic cells express CR1, CR2, and CR3 complement receptor antigens. J Immunol 1985;135:2687-2694.
    • (1985) J Immunol , vol.135 , pp. 2687-2694
    • Reynes, M.1
  • 51
    • 0025971707 scopus 로고
    • Expression of CR2 (the C3dg/EBV receptor, CD21) on normal human peripheral blood T lymphocytes
    • 51. Fischer E, Delibrias C, Kazatchkine MD. Expression of CR2 (the C3dg/EBV receptor, CD21) on normal human peripheral blood T lymphocytes. J Immunol 1991;146:865-869.
    • (1991) J Immunol , vol.146 , pp. 865-869
    • Fischer, E.1    Delibrias, C.2    Kazatchkine, M.D.3
  • 52
    • 8944232100 scopus 로고    scopus 로고
    • Regulation of the B cell response to T-dependent antigens by classical pathway complement
    • 52. Fischer MB, et al. Regulation of the B cell response to T-dependent antigens by classical pathway complement. J Immunol 1996;157:549-556.
    • (1996) J Immunol , vol.157 , pp. 549-556
    • Fischer, M.B.1
  • 53
    • 15844412034 scopus 로고    scopus 로고
    • Disruption of the Cr2 locus results in a reduction in B-1a cells and in an impaired B cell response to T-dependent antigen
    • 53. Ahearn JM, et al. Disruption of the Cr2 locus results in a reduction in B-1a cells and in an impaired B cell response to T-dependent antigen. Immunity 1996;4:251-262.
    • (1996) Immunity , vol.4 , pp. 251-262
    • Ahearn, J.M.1
  • 54
    • 0029926153 scopus 로고    scopus 로고
    • Markedly impaired humoral immune response in mice deficient in complement receptors 1 and 2
    • 54. Molina H, et al. Markedly impaired humoral immune response in mice deficient in complement receptors 1 and 2. Proc Natl Acad Sci USA 1996;93:3357-3361.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 3357-3361
    • Molina, H.1
  • 55
    • 0025127325 scopus 로고
    • In vivo inhibition of the antibody response by a complement receptor-specific monoclonal antibody
    • 55. Heyman B, Wiersma EJ, Kinoshita T. In vivo inhibition of the antibody response by a complement receptor-specific monoclonal antibody. J Exp Med 1990;172:665-668.
    • (1990) J Exp Med , vol.172 , pp. 665-668
    • Heyman, B.1    Wiersma, E.J.2    Kinoshita, T.3
  • 56
    • 0025991505 scopus 로고
    • Suppression of the immune response by a soluble complement receptor of B lymphocytes
    • 56. Hebell T, Ahearn JM, Fearon DT. Suppression of the immune response by a soluble complement receptor of B lymphocytes. Science 1991;254:102-105.
    • (1991) Science , vol.254 , pp. 102-105
    • Hebell, T.1    Ahearn, J.M.2    Fearon, D.T.3
  • 57
    • 0025299101 scopus 로고
    • Characterization of murine complement receptor type 2 and its immunological cross-reactivity with type 1 receptor
    • 57. Kinoshita T, et al. Characterization of murine complement receptor type 2 and its immunological cross-reactivity with type 1 receptor. Int Immunol 1990;2:651-659.
    • (1990) Int Immunol , vol.2 , pp. 651-659
    • Kinoshita, T.1
  • 58
    • 0030593030 scopus 로고    scopus 로고
    • C3d of complement as a molecular adjuvant: Bridging innate and acquired immunity
    • 58. Dempsey PW, Allison MED, Akkaraju S, Goodnow CC, Fearon DT. C3d of complement as a molecular adjuvant: bridging innate and acquired immunity. Science 1996;271:348-350.
    • (1996) Science , vol.271 , pp. 348-350
    • Dempsey, P.W.1    Allison, M.E.D.2    Akkaraju, S.3    Goodnow, C.C.4    Fearon, D.T.5
  • 59
    • 0031954004 scopus 로고    scopus 로고
    • Enhanced molecular mimicry of CEA using photoaffinity crosslinked C3d peptide
    • 59. Lou D, Kohler H. Enhanced molecular mimicry of CEA using photoaffinity crosslinked C3d peptide. Nat Biotechnol 1998;16:458-462.
    • (1998) Nat Biotechnol , vol.16 , pp. 458-462
    • Lou, D.1    Kohler, H.2
  • 60
    • 0034252626 scopus 로고    scopus 로고
    • C3d enhancement of antibodies to hemagglutinin accelerates protection against influenza virus
    • 60. Ross TM, Bright RA, Robinson HL. C3d enhancement of antibodies to hemagglutinin accelerates protection against influenza virus. Nat Immunol 2000;1:127-131.
    • (2000) Nat Immunol , vol.1 , pp. 127-131
    • Ross, T.M.1    Bright, R.A.2    Robinson, H.L.3
  • 61
    • 0024266413 scopus 로고
    • Soluble gp350/220 and deletion mutant glycoprotein block Epstein-Barr virus adsorption to lymphocytes
    • 61. Tanner J, Whang Y, Sample J, Sears A, Kieff E. Soluble gp350/220 and deletion mutant glycoprotein block Epstein-Barr virus adsorption to lymphocytes. J Virol 1988;62:4452-4464.
    • (1988) J Virol , vol.62 , pp. 4452-4464
    • Tanner, J.1    Whang, Y.2    Sample, J.3    Sears, A.4    Kieff, E.5
  • 62
    • 0028898528 scopus 로고
    • Mutation of residues in the C3dg region of human complement component C3 corresponding to a proposed binding site for complement receptor type 2 (CR2, CD21) does not abolish binding of iC3b or C3dg to CR2
    • 62. Diefenbach RJ, Isenman DE. Mutation of residues in the C3dg region of human complement component C3 corresponding to a proposed binding site for complement receptor type 2 (CR2, CD21) does not abolish binding of iC3b or C3dg to CR2. J Immunol 1995;154:2303-2320.
    • (1995) J Immunol , vol.154 , pp. 2303-2320
    • Diefenbach, R.J.1    Isenman, D.E.2
  • 63
    • 4243269149 scopus 로고    scopus 로고
    • Studies on the interaction of C3dg with CR2
    • 63. Irani VR, Lambris JD. Studies on the interaction of C3dg with CR2. FASEB J 1999;13:A282-A282.
    • (1999) FASEB J , vol.13
    • Irani, V.R.1    Lambris, J.D.2
  • 64
    • 0034292433 scopus 로고    scopus 로고
    • Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21)
    • 64. Clemenza L, Isenman DE. Structure-guided identification of C3d residues essential for its binding to complement receptor 2 (CD21). J Immunol 2000;165:3839-3848.
    • (2000) J Immunol , vol.165 , pp. 3839-3848
    • Clemenza, L.1    Isenman, D.E.2
  • 65
    • 0026092213 scopus 로고
    • Structural features of the human C3-gene - Intron/exon organization, transcriptional start site, and promoter region sequence
    • 65. Vik DP, et al. Structural features of the human C3-gene - intron/exon organization, transcriptional start site, and promoter region sequence. Biochemistry 1991;30:1080-1085.
    • (1991) Biochemistry , vol.30 , pp. 1080-1085
    • Vik, D.P.1
  • 66
    • 0026052694 scopus 로고
    • Structural aspects of the human C5-gene - Intron/exon organization, 5′-flanking region features, and characterization of two truncated cDNA clones
    • 66. Carney DF, Haviland DL, Noack D, Wetsel RA, Vik DP, Tack BF. Structural aspects of the human C5-gene - intron/exon organization, 5′-flanking region features, and characterization of two truncated cDNA clones. J Biol Chem 1991;266:18786-18791.
    • (1991) J Biol Chem , vol.266 , pp. 18786-18791
    • Carney, D.F.1    Haviland, D.L.2    Noack, D.3    Wetsel, R.A.4    Vik, D.P.5    Tack, B.F.6
  • 67
    • 0024438880 scopus 로고
    • Sequence of the gene for murine complement component C4
    • 67. Ogata RT, Rosa PA, Zepf NE. Sequence of the gene for murine complement component C4. J Biol Chem 1989;264:16565-16572.
    • (1989) J Biol Chem , vol.264 , pp. 16565-16572
    • Ogata, R.T.1    Rosa, P.A.2    Zepf, N.E.3
  • 68
    • 0032213195 scopus 로고    scopus 로고
    • Complement diversity: A mechanism for generating immune diversity?
    • 68. Sunyer JO, Zarkadis IK, Lambris JD. Complement diversity: a mechanism for generating immune diversity? Immunol Today 1998;19:519-523.
    • (1998) Immunol Today , vol.19 , pp. 519-523
    • Sunyer, J.O.1    Zarkadis, I.K.2    Lambris, J.D.3
  • 70
    • 0028920683 scopus 로고
    • The third component of Xenopus complement. cDNA cloning, structural and functional analysis, and evidence for an alternate C3 transcript
    • 70. Lambris JD, et al. The third component of Xenopus complement. cDNA cloning, structural and functional analysis, and evidence for an alternate C3 transcript. Eur J Immunol 1995;25:572-578.
    • (1995) Eur J Immunol , vol.25 , pp. 572-578
    • Lambris, J.D.1
  • 71
    • 0035239213 scopus 로고    scopus 로고
    • Cloning and structure of three rainbow trout C3 molecules: A plausible explanation for their functional diversity
    • 71. Zarkadis IK, Sarrias MR, Sfyroera G, Sunyer JO, Lambris JD. Cloning and structure of three rainbow trout C3 molecules: a plausible explanation for their functional diversity. Dev Comp Immunol 2001;25:11-24.
    • (2001) Dev Comp Immunol , vol.25 , pp. 11-24
    • Zarkadis, I.K.1    Sarrias, M.R.2    Sfyroera, G.3    Sunyer, J.O.4    Lambris, J.D.5
  • 72
    • 0029775627 scopus 로고    scopus 로고
    • Multiple forms of complement C3 in trout, that differ in binding to complement activators
    • 72. Sunyer JO, Zarkadis IK, Sahu A, Lambris JD. Multiple forms of complement C3 in trout, that differ in binding to complement activators. Proc Natl Acad Sci USA 1996;93:8546-8551.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 8546-8551
    • Sunyer, J.O.1    Zarkadis, I.K.2    Sahu, A.3    Lambris, J.D.4
  • 73
    • 0021993882 scopus 로고
    • Identification and characterization of a variant of the third component of complement (C3) in rainbow trout (Salmo gairdneri) serum
    • 73. Nonaka M, Irie M, Tanabe K, Kaidoh T, Natsuume-Sakai S, Takahashi M. Identification and characterization of a variant of the third component of complement (C3) in rainbow trout (Salmo gairdneri) serum. J Biol Chem 1985;260:809-814.
    • (1985) J Biol Chem , vol.260 , pp. 809-814
    • Nonaka, M.1    Irie, M.2    Tanabe, K.3    Kaidoh, T.4    Natsuume-Sakai, S.5    Takahashi, M.6
  • 74
    • 0001652502 scopus 로고    scopus 로고
    • Sequence diversity of cDNA encoding the third component (C3) of carp (Cyprinus carpio)
    • 74. Nakao K, Obo R, Mutsuro J, Yano T. Sequence diversity of cDNA encoding the third component (C3) of carp (Cyprinus carpio). Dev Comp Immunol 1997;21:144.
    • (1997) Dev Comp Immunol , vol.21 , pp. 144
    • Nakao, K.1    Obo, R.2    Mutsuro, J.3    Yano, T.4
  • 76
    • 0031569091 scopus 로고    scopus 로고
    • Structural C3 diversity in fish - Characterization of five forms of C3 in the diploid fish Sparus aurata
    • 76. Sunyer JO, Tort L, Lambris JD. Structural C3 diversity in fish - characterization of five forms of C3 in the diploid fish Sparus aurata. J Immunol 1997;158:2813-2821.
    • (1997) J Immunol , vol.158 , pp. 2813-2821
    • Sunyer, J.O.1    Tort, L.2    Lambris, J.D.3
  • 77
    • 0021259318 scopus 로고
    • The molecular basis for the difference in immune hemolysis activity of the Chido and Rodgers isotypes of human complement component C4
    • 77. Isenman DE, Young JR. The molecular basis for the difference in immune hemolysis activity of the Chido and Rodgers isotypes of human complement component C4. J Immunol 1984;132:3019-3027.
    • (1984) J Immunol , vol.132 , pp. 3019-3027
    • Isenman, D.E.1    Young, J.R.2
  • 78
    • 0021472477 scopus 로고
    • A comparison of the properties of two classes, C4A and C4B, of the human complement component C4
    • 78. Law SKA, Dodds AW, Porter RR. A comparison of the properties of two classes, C4A and C4B, of the human complement component C4. EMBO J 1984;3:1819-1823.
    • (1984) EMBO J , vol.3 , pp. 1819-1823
    • Law, S.K.A.1    Dodds, A.W.2    Porter, R.R.3
  • 80
    • 0027377047 scopus 로고
    • Antibody dependent haemolysin, complement and opsonin in sera of a major carp, Cirrhina mrigala and catfish, Clarias batrachus and Heteropneustes fossilis
    • 80. Saha K, Dash K, Sahu A, Antibody dependent haemolysin, complement and opsonin in sera of a major carp, Cirrhina mrigala and catfish, Clarias batrachus and Heteropneustes fossilis. Comp Immunol Microbiol Infect Dis 1993;16:323-330.
    • (1993) Comp Immunol Microbiol Infect Dis , vol.16 , pp. 323-330
    • Saha, K.1    Dash, K.2    Sahu, A.3
  • 81
    • 0031941775 scopus 로고    scopus 로고
    • Structure, functions, and evolution of the third complement component and viral molecular mimicry
    • 81. Sahu A, Sunyer JO, Moore WT, Sarrias MR, Soulika AM, Lambris JD. Structure, functions, and evolution of the third complement component and viral molecular mimicry. Immunol Res 1998;17:109-121.
    • (1998) Immunol Res , vol.17 , pp. 109-121
    • Sahu, A.1    Sunyer, J.O.2    Moore, W.T.3    Sarrias, M.R.4    Soulika, A.M.5    Lambris, J.D.6
  • 82
    • 0023718738 scopus 로고
    • Vaccinia virus encodes a secretory polypeptide structurally related to complement control proteins
    • 82. Kotwal GJ, Moss B. Vaccinia virus encodes a secretory polypeptide structurally related to complement control proteins. Nature 1988;335:176-178.
    • (1988) Nature , vol.335 , pp. 176-178
    • Kotwal, G.J.1    Moss, B.2
  • 83
    • 0025203480 scopus 로고
    • Inhibition of the complement cascade by the major secretory protein of vaccinia virus
    • 83. Kotwal GJ, Isaacs SN, Mckenzie R, Frank MM, Moss B. Inhibition of the complement cascade by the major secretory protein of vaccinia virus. Science 1990;250:827-830.
    • (1990) Science , vol.250 , pp. 827-830
    • Kotwal, G.J.1    Isaacs, S.N.2    McKenzie, R.3    Frank, M.M.4    Moss, B.5
  • 84
    • 0026544083 scopus 로고
    • Vaccinia virus complement-control protein prevents antibody-dependent complement-enhanced neutralization of infectivity and contributes to virulence
    • 84. Isaacs SN, Kotwal GJ, Moss B. Vaccinia virus complement-control protein prevents antibody-dependent complement-enhanced neutralization of infectivity and contributes to virulence. Proc Natl Acad Sci USA 1992;89:628-632.
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 628-632
    • Isaacs, S.N.1    Kotwal, G.J.2    Moss, B.3
  • 85
    • 0026478547 scopus 로고
    • Regulation of complement activity by vaccinia virus complement-control protein
    • 85. Mckenzie R, Kotwal GJ, Moss B, Hammer CH, Frank MM. Regulation of complement activity by vaccinia virus complement-control protein. J Infect Dis 1992;166:1245-1250.
    • (1992) J Infect Dis , vol.166 , pp. 1245-1250
    • Mckenzie, R.1    Kotwal, G.J.2    Moss, B.3    Hammer, C.H.4    Frank, M.M.5
  • 86
    • 0032560578 scopus 로고    scopus 로고
    • Extracellular enveloped vaccinia virus is resistant to complement because of incorporation of host complement control proteins into its envelope
    • 86. Vanderplasschen A, Mathew E, Hollinshead M, Sim RB, Smith GL. Extracellular enveloped vaccinia virus is resistant to complement because of incorporation of host complement control proteins into its envelope. Proc Natl Acad Sci USA 1998;95:7544-7549.
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 7544-7549
    • Vanderplasschen, A.1    Mathew, E.2    Hollinshead, M.3    Sim, R.B.4    Smith, G.L.5
  • 87
    • 0027765716 scopus 로고
    • Potential virulence determinants in terminal regions of variola smallpox virus genome
    • 87. Massung RF, et al. Potential virulence determinants in terminal regions of variola smallpox virus genome. Nature 1993;366:748-751.
    • (1993) Nature , vol.366 , pp. 748-751
    • Massung, R.F.1
  • 88
    • 21144461583 scopus 로고
    • Structural-functional organization of the smallpox virus genome. 1. Cloning of viral-DNA HINDIII and XHOI fragments and sequencing of HINDIII fragment-M, fragment-L, and fragment-I
    • 88. Shchelkunov SN, et al. Structural-functional organization of the smallpox virus genome. 1. Cloning of viral-DNA HINDIII and XHOI fragments and sequencing of HINDIII fragment-M, fragment-L, and fragment-I. Mol Biol 1992;26:731-744.
    • (1992) Mol Biol , vol.26 , pp. 731-744
    • Shchelkunov, S.N.1
  • 89
    • 0026764619 scopus 로고
    • New member of the multigene family of complement control proteins in herpesvirus saimiri
    • 89. Albrecht JC, Fleckenstein B. New member of the multigene family of complement control proteins in herpesvirus saimiri. J Virol 1992;66:3937-3940.
    • (1992) J Virol , vol.66 , pp. 3937-3940
    • Albrecht, J.C.1    Fleckenstein, B.2
  • 90
    • 0029069871 scopus 로고
    • The complement control protein homolog of herpesvirus saimiri regulates serum complement by inhibiting C3 convertase activity
    • 90. Fodor WL, et al. The complement control protein homolog of herpesvirus saimiri regulates serum complement by inhibiting C3 convertase activity. J Virol 1995;69:3889-3892.
    • (1995) J Virol , vol.69 , pp. 3889-3892
    • Fodor, W.L.1
  • 91
    • 0000842916 scopus 로고    scopus 로고
    • Nucleotide sequence of the Kaposi sarcoma-associated herpesvirus (HHV8)
    • 91. Russo JJ, et al. Nucleotide sequence of the Kaposi sarcoma-associated herpesvirus (HHV8). Proc Natl Acad Sci USA 1996;93:14862-14867.
    • (1996) Proc Natl Acad Sci USA , vol.93 , pp. 14862-14867
    • Russo, J.J.1
  • 92
    • 0030738667 scopus 로고    scopus 로고
    • Complete sequence and genomic analysis of murine gammaherpesvirus 68
    • 92. Virgin HW, et al. Complete sequence and genomic analysis of murine gammaherpesvirus 68. J Virol 1997;71:5894-5904.
    • (1997) J Virol , vol.71 , pp. 5894-5904
    • Virgin, H.W.1
  • 93
    • 0021246307 scopus 로고
    • Glycoprotein C of herpes simplex virus 1 acts as a receptor for the C3b complement component on infected cells
    • 93. Friedman HM, Cohen GH, Eisenberg RJ, Seidel CA, Cines DB. Glycoprotein C of herpes simplex virus 1 acts as a receptor for the C3b complement component on infected cells. Nature 1984;309:633-635.
    • (1984) Nature , vol.309 , pp. 633-635
    • Friedman, H.M.1    Cohen, G.H.2    Eisenberg, R.J.3    Seidel, C.A.4    Cines, D.B.5
  • 94
    • 0002124576 scopus 로고
    • Antigenic structure of herpes simplex viruses
    • van Regenmortel MVH, Neurath AR, eds. Amsterdam: Elsevier Science Publishers
    • 94. Spear PG, Antigenic structure of herpes simplex viruses. In: van Regenmortel MVH, Neurath AR, eds. Immunochemistry of viruses. The basis for serodiagnosis and vaccines. Amsterdam: Elsevier Science Publishers; 1985. p. 425-446.
    • (1985) Immunochemistry of Viruses. The Basis for Serodiagnosis and Vaccines , pp. 425-446
    • Spear, P.G.1
  • 95
    • 0023624346 scopus 로고
    • Herpes simplex virus glycoproteins gC-1 and gC-2 bind to the third component of complement and provide protection against complement mediated neutralization of viral infectivity
    • 95. McNearney TA, Odell C, Holers VM, Spear PG, Atkinson JP. Herpes simplex virus glycoproteins gC-1 and gC-2 bind to the third component of complement and provide protection against complement mediated neutralization of viral infectivity. J Exp Med 1987;166:1525-1535.
    • (1987) J Exp Med , vol.166 , pp. 1525-1535
    • McNearney, T.A.1    Odell, C.2    Holers, V.M.3    Spear, P.G.4    Atkinson, J.P.5
  • 96
    • 0029888982 scopus 로고    scopus 로고
    • Immune evasion properties of herpes simplex virus type 1 glycoprotein gC
    • 96. Friedman HM, et al. Immune evasion properties of herpes simplex virus type 1 glycoprotein gC. J Virol 1996;70:4253-4260.
    • (1996) J Virol , vol.70 , pp. 4253-4260
    • Friedman, H.M.1
  • 97
    • 0020727366 scopus 로고
    • O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus
    • 97. Johnson DC, Spear PG. O-linked oligosaccharides are acquired by herpes simplex virus glycoproteins in the Golgi apparatus. Cell 1983;32:987-997.
    • (1983) Cell , vol.32 , pp. 987-997
    • Johnson, D.C.1    Spear, P.G.2
  • 98
    • 0029018333 scopus 로고
    • Interaction of herpes simplex virus glycoprotein gC with mammalian cell surface molecules
    • 98. Tal-Singer R, et al. Interaction of herpes simplex virus glycoprotein gC with mammalian cell surface molecules. J Virol 1995;69:4471-4483.
    • (1995) J Virol , vol.69 , pp. 4471-4483
    • Tal-Singer, R.1
  • 101
    • 0028100351 scopus 로고
    • The interaction of glycoprotein C of herpes simplex virus types 1 and 2 with the alternative complement pathway
    • 101. Hung SL, et al. The interaction of glycoprotein C of herpes simplex virus types 1 and 2 with the alternative complement pathway. Virology 1994;203:299-312.
    • (1994) Virology , vol.203 , pp. 299-312
    • Hung, S.L.1
  • 102
    • 0033430228 scopus 로고    scopus 로고
    • In vivo role of complement-interacting domains of herpes simplex virus type I glycoprotein gC
    • 102. Lubinski J, Wang L, Mastellos D, Sahu A, Lambris JD, Friedman HM. In vivo role of complement-interacting domains of herpes simplex virus type I glycoprotein gC. J Exp Med 1999;190:1637-1646.
    • (1999) J Exp Med , vol.190 , pp. 1637-1646
    • Lubinski, J.1    Wang, L.2    Mastellos, D.3    Sahu, A.4    Lambris, J.D.5    Friedman, H.M.6
  • 103
    • 0025820146 scopus 로고
    • Complement evasion strategies of microorganisms
    • 103. Cooper NR. Complement evasion strategies of microorganisms. Immunol Today 1991;12:327-331.
    • (1991) Immunol Today , vol.12 , pp. 327-331
    • Cooper, N.R.1
  • 104
    • 0024965987 scopus 로고
    • Identification of an epitope in the major envelope protein of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2)
    • 104. Nemerow GR, Houghten RA, Moore MD, Cooper NR. Identification of an epitope in the major envelope protein of Epstein-Barr virus that mediates viral binding to the B lymphocyte EBV receptor (CR2). Cell 1989;56:369-377.
    • (1989) Cell , vol.56 , pp. 369-377
    • Nemerow, G.R.1    Houghten, R.A.2    Moore, M.D.3    Cooper, N.R.4
  • 105
    • 0025883254 scopus 로고
    • Analysis of Epstein-Barr virus-binding sites on complement receptor 2 (CR2/CD21) using human-mouse chimeras and peptides. At least two distinct sites are necessary for ligand-receptor interaction
    • 105. Molina H, et al. Analysis of Epstein-Barr virus-binding sites on complement receptor 2 (CR2/CD21) using human-mouse chimeras and peptides. At least two distinct sites are necessary for ligand-receptor interaction. J Biol Chem 1991;266:12173-12179.
    • (1991) J Biol Chem , vol.266 , pp. 12173-12179
    • Molina, H.1
  • 106
    • 0028278231 scopus 로고
    • Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses
    • 106. Bergelson JM, Chan M, Solomon KR, Stjohn NF, Lin HM, Finberg RW. Decay-accelerating factor (CD55), a glycosylphosphatidylinositol-anchored complement regulatory protein, is a receptor for several echoviruses. Proc Natl Acad Sci USA 1994;91:6245-6249.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6245-6249
    • Bergelson, J.M.1    Chan, M.2    Solomon, K.R.3    Stjohn, N.F.4    Lin, H.M.5    Finberg, R.W.6
  • 107
    • 0028325229 scopus 로고
    • Multiple isoforms of CD46 (membrane cofactor protein) serve as receptors for measles virus
    • 107. Manchester M, Liszewski MK, Atkinson JP, Oldstone MB. Multiple isoforms of CD46 (membrane cofactor protein) serve as receptors for measles virus. Proc Natl Acad Sci USA 1994;91:2161-2165.
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 2161-2165
    • Manchester, M.1    Liszewski, M.K.2    Atkinson, J.P.3    Oldstone, M.B.4
  • 109
    • 0033921989 scopus 로고    scopus 로고
    • Complement inhibitors: A resurgent concept in anti-inflammatory therapeutics
    • 109. Sahu A, Lambris JD, Complement inhibitors: a resurgent concept in anti-inflammatory therapeutics. Immunopharmacology 2000;49:133-148.
    • (2000) Immunopharmacology , vol.49 , pp. 133-148
    • Sahu, A.1    Lambris, J.D.2
  • 110
    • 0003131305 scopus 로고    scopus 로고
    • Complement inhibitors targeting C3, C4, and, C5
    • Lambris JD, Holers VM, eds. Totowa: Humana Press Inc
    • 110. Sahu A, Morikis D, Lambris JD. Complement inhibitors targeting C3, C4, and, C5. In: Lambris JD, Holers VM, eds. Therapeutic interventions in the complement system. Totowa: Humana Press Inc; 2000. p. 75-112.
    • (2000) Therapeutic Interventions in the Complement System , pp. 75-112
    • Sahu, A.1    Morikis, D.2    Lambris, J.D.3
  • 111
    • 0030013492 scopus 로고    scopus 로고
    • Inhibition of human complement by a C3-binding peptide isolated from a phage displayed random peptide library
    • 111. Sahu A, Kay BK, Lambris JD. Inhibition of human complement by a C3-binding peptide isolated from a phage displayed random peptide library. J Immunol 1996;157:884-891.
    • (1996) J Immunol , vol.157 , pp. 884-891
    • Sahu, A.1    Kay, B.K.2    Lambris, J.D.3
  • 112
    • 0034691542 scopus 로고    scopus 로고
    • C3 activation is inhibited by analogs of compstatin but not by serine protease inhibitors or peptidyl α-ketoheterocycles
    • 112. Furlong ST, et al. C3 activation is inhibited by analogs of compstatin but not by serine protease inhibitors or peptidyl α-ketoheterocycles. Immunopharmacology 2000;48:199-212.
    • (2000) Immunopharmacology , vol.48 , pp. 199-212
    • Furlong, S.T.1
  • 113
    • 0034283672 scopus 로고    scopus 로고
    • Binding kinetics, structure-activity relationship, and biotransformation of the complement inhibitor compstatin
    • 113. Sahu A, Soulika AM, Morikis D, Spruce L, Moore WT, Lambris JD. Binding kinetics, structure-activity relationship, and biotransformation of the complement inhibitor compstatin. J Immunol 2000;165:2491-2499.
    • (2000) J Immunol , vol.165 , pp. 2491-2499
    • Sahu, A.1    Soulika, A.M.2    Morikis, D.3    Spruce, L.4    Moore, W.T.5    Lambris, J.D.6
  • 114
    • 0033042537 scopus 로고    scopus 로고
    • Compstatin, a peptide inhibitor of C3, prolongs survival of ex vivo perfused pig xenografts
    • 114. Fiane AE, et al. Compstatin, a peptide inhibitor of C3, prolongs survival of ex vivo perfused pig xenografts. Xenotransplantation 1999;6:52-65.
    • (1999) Xenotransplantation , vol.6 , pp. 52-65
    • Fiane, A.E.1
  • 115
    • 0033033170 scopus 로고    scopus 로고
    • Prolongation of ex vivo-perfused pig xenograft survival by the complement inhibitor compstatin
    • 115. Fiane AE, et al. Prolongation of ex vivo-perfused pig xenograft survival by the complement inhibitor compstatin. Transplant Proc 1999;31:934-935.
    • (1999) Transplant Proc , vol.31 , pp. 934-935
    • Fiane, A.E.1
  • 116
    • 0032170593 scopus 로고    scopus 로고
    • Compstatin inhibits complement and cellular activation in whole blood in two models of extracorporeal circulation
    • 116. Nilsson B, et al. Compstatin inhibits complement and cellular activation in whole blood in two models of extracorporeal circulation. Blood 1998;92:1661-1667.
    • (1998) Blood , vol.92 , pp. 1661-1667
    • Nilsson, B.1
  • 117
    • 0033839596 scopus 로고    scopus 로고
    • Inhibition of heparin/ protamine complex-induced complement activation by compstatin in baboons
    • 117. Soulika AM, et al. Inhibition of heparin/ protamine complex-induced complement activation by compstatin in baboons. Clin Immunol 2000;96:212-221.
    • (2000) Clin Immunol , vol.96 , pp. 212-221
    • Soulika, A.M.1
  • 118
    • 0031888668 scopus 로고    scopus 로고
    • Solution structure of compstatin, a potent complement inhibitor
    • 118. Morikis D, Assa-Munt N, Sahu A, Lambris JD. Solution structure of compstatin, a potent complement inhibitor. Protein Sci 1998;7:619-627.
    • (1998) Protein Sci , vol.7 , pp. 619-627
    • Morikis, D.1    Assa-Munt, N.2    Sahu, A.3    Lambris, J.D.4
  • 119
    • 0032534678 scopus 로고    scopus 로고
    • Expression of the third component of complement, C3, in regenerating limb blastema cells of urodeles
    • 119. Del Rio-Tsonis K, Tsonis PA, Zarkadis IK, Tsangas AG, Lambris JD. Expression of the third component of complement, C3, in regenerating limb blastema cells of urodeles. J Immunol 1998;161:6819-6814.
    • (1998) J Immunol , vol.161 , pp. 6819-16814
    • Del Rio-Tsonis, K.1    Tsonis, P.A.2    Zarkadis, I.K.3    Tsangas, A.G.4    Lambris, J.D.5
  • 120
    • 0035865055 scopus 로고    scopus 로고
    • A novel role of complement: Mice deficient in the fifth component of complement (C5) exhibit impaired liver regeneration
    • In press
    • 120. Mastellos D, Papadimitriou J, Franchini S, Tsonis PA, Lambris JD. A novel role of complement: mice deficient in the fifth component of complement (C5) exhibit impaired liver regeneration. J Immunol (In press).
    • J Immunol
    • Mastellos, D.1    Papadimitriou, J.2    Franchini, S.3    Tsonis, P.A.4    Lambris, J.D.5


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