메뉴 건너뛰기




Volumn 80, Issue , 2014, Pages 83-116

Structural biology of the membrane attack complex

Author keywords

Complememt system; Lipid membrane pore; Membrane attack complex; Pore forming proteins; Structural biology

Indexed keywords

COMPLEMENT; COMPLEMENT MEMBRANE ATTACK COMPLEX; PORE FORMING CYTOTOXIC PROTEIN;

EID: 84906317003     PISSN: 03060225     EISSN: None     Source Type: Journal    
DOI: 10.1007/978-94-017-8881-6_6     Document Type: Article
Times cited : (23)

References (187)
  • 1
    • 84861721290 scopus 로고    scopus 로고
    • Crystal structure of C5b-6 suggests structural basis for priming assembly of the membrane attack complex
    • Aleshin AE, DiScipio RG, Stec B, Liddington RC (2012) Crystal structure of C5b-6 suggests structural basis for priming assembly of the membrane attack complex. J Biol Chem 287:19642–19652
    • (2012) J Biol Chem , vol.287 , pp. 19642-19652
    • Aleshin, A.E.1    Discipio, R.G.2    Stec, B.3    Liddington, R.C.4
  • 2
    • 84858967104 scopus 로고    scopus 로고
    • Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC)
    • Aleshin AE, Schraufstatter IU, Stec B, Bankston LA, Liddington RC, DiScipio RG (2012) Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC). J Biol Chem 287:10210–10222
    • (2012) J Biol Chem , vol.287 , pp. 10210-10222
    • Aleshin, A.E.1    Schraufstatter, I.U.2    Stec, B.3    Bankston, L.A.4    Liddington, R.C.5    Discipio, R.G.6
  • 3
    • 0034467504 scopus 로고    scopus 로고
    • Pore-forming bacterial protein toxins: An overview
    • Alouf JE (2001) Pore-forming bacterial protein toxins: an overview. Curr Top Microbiol Immunol 257:1–14
    • (2001) Curr Top Microbiol Immunol , vol.257 , pp. 1-14
    • Alouf, J.E.1
  • 4
    • 0022397877 scopus 로고
    • The membrane attack complex of complement: Lipid insertion of tubular and nontubular polymerized C9
    • Amiguet P, Brunner J, Tschopp J (1985) The membrane attack complex of complement: lipid insertion of tubular and nontubular polymerized C9. Biochemistry 24:7328–7334
    • (1985) Biochemistry , vol.24 , pp. 7328-7334
    • Amiguet, P.1    Brunner, J.2    Tschopp, J.3
  • 6
    • 52949087550 scopus 로고    scopus 로고
    • Disparate proteins use similar architectures to damage membranes
    • Anderluh G, Lakey JH (2008) Disparate proteins use similar architectures to damage membranes. Trends Biochem Sci 33:482–490
    • (2008) Trends Biochem Sci , vol.33 , pp. 482-490
    • Anderluh, G.1    Lakey, J.H.2
  • 9
    • 0024505599 scopus 로고
    • Immunohistochemical study of complement S protein (Vitronectin) in normal and diseased human kidneys: Relationship to neoantigens of the C5b-9 terminal complex
    • Bariety J, Hinglais N, Bhakdi S, Mandet C, Rouchon M, Kazatchkine MD (1989) Immunohistochemical study of complement S protein (vitronectin) in normal and diseased human kidneys: relationship to neoantigens of the C5b-9 terminal complex. Clin Exp Immunol 75:76–81
    • (1989) Clin Exp Immunol , vol.75 , pp. 76-81
    • Bariety, J.1    Hinglais, N.2    Bhakdi, S.3    Mandet, C.4    Rouchon, M.5    Kazatchkine, M.D.6
  • 10
    • 0022881696 scopus 로고
    • Single-channel analysis of the conductance fluctuations induced in lipid bilayer membranes by complement proteins C5b-9
    • Benz R, Schmid A, Wiedmer T, Sims PJ (1986) Single-channel analysis of the conductance fluctuations induced in lipid bilayer membranes by complement proteins C5b-9. J Membr Biol 94:37–45
    • (1986) J Membr Biol , vol.94 , pp. 37-45
    • Benz, R.1    Schmid, A.2    Wiedmer, T.3    Sims, P.J.4
  • 11
    • 0018319887 scopus 로고
    • Proteolytic transformation of SC5b-9 into an amphiphilic macromolecule resembling the C5b-9 membrane attack complex of complement
    • Bhakdi S, Bhakdi-Lehnen B, Tranum-Jensen J (1979) Proteolytic transformation of SC5b-9 into an amphiphilic macromolecule resembling the C5b-9 membrane attack complex of complement. Immunology 37:901–912
    • (1979) Immunology , vol.37 , pp. 901-912
    • Bhakdi, S.1    Bhakdi-Lehnen, B.2    Tranum-Jensen, J.3
  • 12
  • 13
    • 0021160732 scopus 로고
    • On the cause and nature of C9-related heterogeneity of terminal complement complexes generated on target erythrocytes through the action of whole serum
    • Bhakdi S, Tranum-Jensen J (1984) On the cause and nature of C9-related heterogeneity of terminal complement complexes generated on target erythrocytes through the action of whole serum. J Immunol 133:1453–1463
    • (1984) J Immunol , vol.133 , pp. 1453-1463
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 14
    • 0022624819 scopus 로고
    • C5b-9 assembly: Average binding of one C9 molecule to C5b-8 without poly-C9 formation generates a stable transmembrane pore
    • Bhakdi S, Tranum-Jensen J (1986) C5b-9 assembly: average binding of one C9 molecule to C5b-8 without poly-C9 formation generates a stable transmembrane pore. J Immunol 136:2999–3005
    • (1986) J Immunol , vol.136 , pp. 2999-3005
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 15
    • 0025896269 scopus 로고
    • Complement lysis: A hole is a hole
    • (discussion 321)
    • Bhakdi S, Tranum-Jensen J (1991) Complement lysis: a hole is a hole. Immunol Today 12:318–320 (discussion 321)
    • (1991) Immunol Today , vol.12 , pp. 318-320
    • Bhakdi, S.1    Tranum-Jensen, J.2
  • 16
    • 0018887801 scopus 로고
    • The terminal membrane C5b-9 complex of human complement. Evidence for the existence of multiple protease-resistant polypeptides that form the trans-membrane complement channel
    • Bhakdi S, Tranum-Jensen J, Klump O (1980) The terminal membrane C5b-9 complex of human complement. Evidence for the existence of multiple protease-resistant polypeptides that form the trans-membrane complement channel. J Immunol 124:2451–2457
    • (1980) J Immunol , vol.124 , pp. 2451-2457
    • Bhakdi, S.1    Tranum-Jensen, J.2    Klump, O.3
  • 19
    • 0031041068 scopus 로고    scopus 로고
    • Mutational analysis of the active site and antibody epitopes of the complement-inhibitory glycoprotein, CD59
    • Bodian DL, Davis SJ, Morgan BP, Rushmere NK (1997) Mutational analysis of the active site and antibody epitopes of the complement-inhibitory glycoprotein, CD59. J Exp Med 185:507–516
    • (1997) J Exp Med , vol.185 , pp. 507-516
    • Bodian, D.L.1    Davis, S.J.2    Morgan, B.P.3    Rushmere, N.K.4
  • 20
    • 0027190974 scopus 로고
    • The CUB domain. A widespread module in developmentally regulated proteins
    • Bork P, Beckmann G (1993) The CUB domain. A widespread module in developmentally regulated proteins. J Mol Biol 231:539–545
    • (1993) J Mol Biol , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 21
    • 37049050492 scopus 로고
    • Lesions in erythrocyte membranes caused by immune haemolysis
    • Boros T, Dourmashkin RR, Humphrey JH (1964) Lesions in erythrocyte membranes caused by immune haemolysis. Nature 202:251–252
    • (1964) Nature , vol.202 , pp. 251-252
    • Boros, T.1    Dourmashkin, R.R.2    Humphrey, J.H.3
  • 22
    • 15444371872 scopus 로고    scopus 로고
    • Functional insights from the structure of the multifunctional C345C domain of C5 of complement
    • Bramham J, Thai CT, Soares DC, Uhrin D, Ogata RT, Barlow PN (2005) Functional insights from the structure of the multifunctional C345C domain of C5 of complement. J Biol Chem 280:10636–10645
    • (2005) J Biol Chem , vol.280 , pp. 10636-10645
    • Bramham, J.1    Thai, C.T.2    Soares, D.C.3    Uhrin, D.4    Ogata, R.T.5    Barlow, P.N.6
  • 23
    • 33748771463 scopus 로고    scopus 로고
    • Incorporation of human complement C8 into the membrane attack complex is mediated by a binding site located within the C8beta MACPF domain
    • Brannen CL, Sodetz JM (2007) Incorporation of human complement C8 into the membrane attack complex is mediated by a binding site located within the C8beta MACPF domain. Mol Immunol 44:960–965
    • (2007) Mol Immunol , vol.44 , pp. 960-965
    • Brannen, C.L.1    Sodetz, J.M.2
  • 26
    • 34247611993 scopus 로고    scopus 로고
    • Structural features of the ligand binding site on human complement protein C8gamma: A member of the lipocalin family
    • Chiswell B, Lovelace LL, Brannen C, Ortlund EA, Lebioda L, Sodetz JM (2007) Structural features of the ligand binding site on human complement protein C8gamma: a member of the lipocalin family. Biochim Biophys Acta 1774:637–644
    • (2007) Biochim Biophys Acta , vol.1774 , pp. 637-644
    • Chiswell, B.1    Lovelace, L.L.2    Brannen, C.3    Ortlund, E.A.4    Lebioda, L.5    Sodetz, J.M.6
  • 27
    • 4444291857 scopus 로고    scopus 로고
    • Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane
    • Czajkowsky DM, Hotze EM, Shao Z, Tweten RK (2004) Vertical collapse of a cytolysin prepore moves its transmembrane beta-hairpins to the membrane. EMBO J 23:3206–3215
    • (2004) EMBO J , vol.23 , pp. 3206-3215
    • Czajkowsky, D.M.1    Hotze, E.M.2    Shao, Z.3    Tweten, R.K.4
  • 28
    • 0021828626 scopus 로고
    • Proteolytic modification of human complement protein C9: Loss of poly(C9) and circular lesion formation without impairment of function
    • Dankert JR, Esser AF (1985) Proteolytic modification of human complement protein C9: loss of poly(C9) and circular lesion formation without impairment of function. Proc Natl Acad Sci USA 82:2128–2132
    • (1985) Proc Natl Acad Sci USA , vol.82 , pp. 2128-2132
    • Dankert, J.R.1    Esser, A.F.2
  • 29
    • 0021810223 scopus 로고
    • Ninth component of complement: Self-aggregation and interaction with lipids
    • Dankert JR, Shiver JW, Esser AF (1985) Ninth component of complement: self-aggregation and interaction with lipids. Biochemistry 24:2754–2762
    • (1985) Biochemistry , vol.24 , pp. 2754-2762
    • Dankert, J.R.1    Shiver, J.W.2    Esser, A.F.3
  • 30
    • 0019785378 scopus 로고
    • The conversion of human complement component C5 into fragment C5b by the alternative-pathway C5 convertase
    • DiScipio RG (1981) The conversion of human complement component C5 into fragment C5b by the alternative-pathway C5 convertase. Biochem J 199:497–504
    • (1981) Biochem J , vol.199 , pp. 497-504
    • Discipio, R.G.1
  • 31
    • 0026785372 scopus 로고
    • Formation and structure of the C5b-7 complex of the lytic pathway of complement
    • DiScipio RG (1992) Formation and structure of the C5b-7 complex of the lytic pathway of complement. J Biol Chem 267:17087–17094
    • (1992) J Biol Chem , vol.267 , pp. 17087-17094
    • Discipio, R.G.1
  • 34
    • 0022270784 scopus 로고
    • The architecture of complement component C9 and poly(C9)
    • DiScipio RG, Hugli TE (1985) The architecture of complement component C9 and poly(C9). J Biol Chem 260:14802–14809
    • (1985) J Biol Chem , vol.260 , pp. 14802-14809
    • Discipio, R.G.1    Hugli, T.E.2
  • 35
    • 0024421491 scopus 로고
    • The molecular architecture of human complement component C6
    • DiScipio RG, Hugli TE (1989) The molecular architecture of human complement component C6. J Biol Chem 264:16197–16206
    • (1989) J Biol Chem , vol.264 , pp. 16197-16206
    • Discipio, R.G.1    Hugli, T.E.2
  • 36
    • 0033527540 scopus 로고    scopus 로고
    • Function of the factor I modules (FIMS) of human complement component C6
    • DiScipio RG, Linton SM, Rushmere NK (1999) Function of the factor I modules (FIMS) of human complement component C6. J Biol Chem 274:31811–31818
    • (1999) J Biol Chem , vol.274 , pp. 31811-31818
    • Discipio, R.G.1    Linton, S.M.2    Rushmere, N.K.3
  • 37
    • 0021036761 scopus 로고
    • The activation of human complement component C5 by a fluid phase C5 convertase
    • DiScipio RG, Smith CA, Müller-Eberhard HJ, Hugli TE (1983) The activation of human complement component C5 by a fluid phase C5 convertase. J Biol Chem 258:10629–10636
    • (1983) J Biol Chem , vol.258 , pp. 10629-10636
    • Discipio, R.G.1    Smith, C.A.2    Müller-Eberhard, H.J.3    Hugli, T.E.4
  • 38
    • 84864593970 scopus 로고    scopus 로고
    • The cholesterol-dependent cytolysin signature motif: A critical element in the allosteric pathway that couples membrane binding to pore assembly
    • Dowd KJ, Tweten RK (2012) The cholesterol-dependent cytolysin signature motif: a critical element in the allosteric pathway that couples membrane binding to pore assembly. PLoS Pathog 8:e1002787
    • (2012) Plos Pathog , vol.8
    • Dowd, K.J.1    Tweten, R.K.2
  • 39
    • 0038780809 scopus 로고    scopus 로고
    • Listeriolysin O-mediated calcium influx potentiates entry of Listeria monocytogenes into the human Hep-2 epithelial cell line
    • Dramsi S, Cossart P (2003) Listeriolysin O-mediated calcium influx potentiates entry of Listeria monocytogenes into the human Hep-2 epithelial cell line. Infect Immun 71:3614–3618
    • (2003) Infect Immun , vol.71 , pp. 3614-3618
    • Dramsi, S.1    Cossart, P.2
  • 40
    • 84862605391 scopus 로고    scopus 로고
    • Packing a punch: The mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins
    • Dunstone MA, Tweten RK (2012) Packing a punch: the mechanism of pore formation by cholesterol dependent cytolysins and membrane attack complex/perforin-like proteins. Curr Opin Struct Biol 22:342–349
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 342-349
    • Dunstone, M.A.1    Tweten, R.K.2
  • 41
    • 0023949611 scopus 로고
    • Astrotactin: A novel neuronal cell surface antigen that mediates neuron-astroglial interactions in cerebellar microcultures
    • Edmondson JC, Liem RK, Kuster JE, Hatten ME (1988) Astrotactin: a novel neuronal cell surface antigen that mediates neuron-astroglial interactions in cerebellar microcultures. J Cell Biol 106:505–517
    • (1988) J Cell Biol , vol.106 , pp. 505-517
    • Edmondson, J.C.1    Liem, R.K.2    Kuster, J.E.3    Hatten, M.E.4
  • 42
    • 84869237413 scopus 로고    scopus 로고
    • Innate immune recognition and inflammasome activation in listeria monocytogenes infection
    • Eitel J, Suttorp N, Opitz B (2010) Innate immune recognition and inflammasome activation in listeria monocytogenes infection. Front Microbiol 1:149
    • (2010) Front Microbiol , vol.1
    • Eitel, J.1    Suttorp, N.2    Opitz, B.3
  • 43
    • 0017366069 scopus 로고
    • Cytochrome b5 and cytochrome b5 reductasephospholipid vesicles. Intervesicle protein transfer and oreintation factors in protein-protein interactions
    • Enoch HG, Fleming PJ, Strittmatter P (1977) Cytochrome b5 and cytochrome b5 reductasephospholipid vesicles. Intervesicle protein transfer and oreintation factors in protein-protein interactions. J Biol Chem 252:5656–5660
    • (1977) J Biol Chem , vol.252 , pp. 5656-5660
    • Enoch, H.G.1    Fleming, P.J.2    Strittmatter, P.3
  • 44
    • 0025827387 scopus 로고
    • Big MAC attack: Complement proteins cause leaky patches
    • (discussion 321)
    • Esser AF (1991) Big MAC attack: complement proteins cause leaky patches. Immunol Today 12:316–318 (discussion 321)
    • (1991) Immunol Today , vol.12 , pp. 316-318
    • Esser, A.F.1
  • 45
    • 84862628488 scopus 로고    scopus 로고
    • The modular serine proteases of the complement cascade
    • Forneris F, Wu J, Gros P (2012) The modular serine proteases of the complement cascade. Curr Opin Struct Biol 22:333–341
    • (2012) Curr Opin Struct Biol , vol.22 , pp. 333-341
    • Forneris, F.1    Wu, J.2    Gros, P.3
  • 46
    • 33745899624 scopus 로고    scopus 로고
    • The structure of bovine complement component three reveals the basis for thioester function
    • Fredslund F, Jenner L, Husted LB, Nyborg J, Andersen GR, Sottrup-Jensen L (2006) The structure of bovine complement component three reveals the basis for thioester function. J Mol Biol 361:115–127
    • (2006) J Mol Biol , vol.361 , pp. 115-127
    • Fredslund, F.1    Jenner, L.2    Husted, L.B.3    Nyborg, J.4    Ersen, G.R.5    Sottrup-Jensen, L.6
  • 48
    • 0033977538 scopus 로고    scopus 로고
    • Role of listeriolysin O in cell-tocell spread of Listeria monocytogenes
    • Gedde MM, Higgins DE, Tilney LG, Portnoy DA (2000) Role of listeriolysin O in cell-tocell spread of Listeria monocytogenes. Infect Immun 68:999–1003
    • (2000) Infect Immun , vol.68 , pp. 999-1003
    • Gedde, M.M.1    Higgins, D.E.2    Tilney, L.G.3    Portnoy, D.A.4
  • 49
    • 0028201342 scopus 로고
    • C5A anaphylatoxin and its seven transmembrane-segment receptor
    • Gerard C, Gerard NP (1994) C5A anaphylatoxin and its seven transmembrane-segment receptor. Annu Rev Immunol 12:775–808
    • (1994) Annu Rev Immunol , vol.12 , pp. 775-808
    • Gerard, C.1    Gerard, N.P.2
  • 50
    • 0026078539 scopus 로고
    • The chemotactic receptor for human C5a anaphylatoxin
    • Gerard NP, Gerard C (1991) The chemotactic receptor for human C5a anaphylatoxin. Nature 349:614–617
    • (1991) Nature , vol.349 , pp. 614-617
    • Gerard, N.P.1    Gerard, C.2
  • 51
    • 23444457403 scopus 로고    scopus 로고
    • Inactivation and activity of cholesterol-dependent cytolysins: What structural studies tell us
    • Gilbert RJ (2005) Inactivation and activity of cholesterol-dependent cytolysins: what structural studies tell us. Structure 13:1097–1106
    • (2005) Structure , vol.13 , pp. 1097-1106
    • Gilbert, R.J.1
  • 52
    • 0033612389 scopus 로고    scopus 로고
    • Two structural transitions in membrane pore formation by pneumolysin, the poreforming toxin of streptococcus pneumoniae
    • Gilbert RJ, Jiménez JL, Chen S, Tickle IJ, Rossjohn J, Parker M, Andrew PW, Saibil HR (1999) Two structural transitions in membrane pore formation by pneumolysin, the poreforming toxin of streptococcus pneumoniae. Cell 97:647–655
    • (1999) Cell , vol.97 , pp. 647-655
    • Gilbert, R.J.1    Jiménez, J.L.2    Chen, S.3    Tickle, I.J.4    Rossjohn, J.5    Parker, M.6    Rew, P.W.7    Saibil, H.R.8
  • 53
    • 77955973704 scopus 로고    scopus 로고
    • Cholesterol-dependent cytolysins
    • Gilbert RJC (2010) Cholesterol-dependent cytolysins. Adv Exp Med Biol 677:56–66
    • (2010) Adv Exp Med Biol , vol.677 , pp. 56-66
    • Gilbert, R.1
  • 55
    • 34548670476 scopus 로고    scopus 로고
    • Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense
    • Hadders MA, Beringer DX, Gros P (2007) Structure of C8alpha-MACPF reveals mechanism of membrane attack in complement immune defense. Science 317:1552–1554
    • (2007) Science , vol.317 , pp. 1552-1554
    • Hadders, M.A.1    Beringer, D.X.2    Gros, P.3
  • 57
    • 0014529344 scopus 로고
    • The ninth component of human complement: Isolation, description and mode of action
    • Hadding U, Muller-Eberhard HJ (1969) The ninth component of human complement: isolation, description and mode of action. Immunology 16:719–735
    • (1969) Immunology , vol.16 , pp. 719-735
    • Hadding, U.1    Muller-Eberhard, H.J.2
  • 58
    • 0024448568 scopus 로고
    • Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6
    • Haefliger JA, Tschopp J, Vial N, Jenne DE (1989) Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6. J Biol Chem 264:18041–18051
    • (1989) J Biol Chem , vol.264 , pp. 18041-18051
    • Haefliger, J.A.1    Tschopp, J.2    Vial, N.3    Jenne, D.E.4
  • 59
    • 0027528974 scopus 로고
    • Interaction between apolipoproteins A-I and A-II and the membrane attack complex of complement. Affinity of the apoproteins for polymeric C9
    • Hamilton KK, Zhao J, Sims PJ (1993) Interaction between apolipoproteins A-I and A-II and the membrane attack complex of complement. Affinity of the apoproteins for polymeric C9. J Biol Chem 268:3632–3638
    • (1993) J Biol Chem , vol.268 , pp. 3632-3638
    • Hamilton, K.K.1    Zhao, J.2    Sims, P.J.3
  • 60
    • 0016644255 scopus 로고
    • On the mechanism of cytolysis by complement: Evidence on insertion of C5b and C7 subunits of the C5b, 6, 7 complex into phospholipid bilayers of erythrocyte membranes
    • Hammer CH, Nicholson A, Mayer MM (1975) On the mechanism of cytolysis by complement: evidence on insertion of C5b and C7 subunits of the C5b, 6, 7 complex into phospholipid bilayers of erythrocyte membranes. Proc Natl Acad Sci USA 72:5076–5080
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 5076-5080
    • Hammer, C.H.1    Nicholson, A.2    Mayer, M.M.3
  • 61
    • 0029060839 scopus 로고
    • Structure of the human C7 gene and comparison with the C6, C8A, C8B, and C9 genes
    • Hobart MJ, Fernie BA, DiScipio RG (1995) Structure of the human C7 gene and comparison with the C6, C8A, C8B, and C9 genes. J Immunol 154:5188–5194
    • (1995) J Immunol , vol.154 , pp. 5188-5194
    • Hobart, M.J.1    Fernie, B.A.2    Discipio, R.G.3
  • 62
    • 84857650341 scopus 로고    scopus 로고
    • Membrane assembly of the cholesterol-dependent cytolysin pore complex
    • Hotze EM, Tweten RK (2012) Membrane assembly of the cholesterol-dependent cytolysin pore complex. Biochim Biophys Acta 1818:1028–1038
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1028-1038
    • Hotze, E.M.1    Tweten, R.K.2
  • 64
    • 26644444355 scopus 로고    scopus 로고
    • Insights into the human CD59 complement binding interface toward engineering new therapeutics
    • Huang Y, Smith CA, Song H, Morgan BP, Abagyan R, Tomlinson S (2005) Insights into the human CD59 complement binding interface toward engineering new therapeutics. J Biol Chem 280:34073–34079
    • (2005) J Biol Chem , vol.280 , pp. 34073-34079
    • Huang, Y.1    Smith, C.A.2    Song, H.3    Morgan, B.P.4    Abagyan, R.5    Tomlinson, S.6
  • 67
    • 0026600180 scopus 로고
    • Clusterin: The intriguing guises of a widely expressed glycoprotein
    • Jenne DE, Tschopp J (1992) Clusterin: the intriguing guises of a widely expressed glycoprotein. Trends Biochem Sci 17:154–159
    • (1992) Trends Biochem Sci , vol.17 , pp. 154-159
    • Jenne, D.E.1    Tschopp, J.2
  • 68
    • 84878591801 scopus 로고    scopus 로고
    • Structural basis for recognition of the pore-forming toxin intermedilysin by human complement receptor CD59
    • Johnson S, Brooks NJ, Smith RAG, Lea SM, Bubeck D (2013) Structural basis for recognition of the pore-forming toxin intermedilysin by human complement receptor CD59. Cell Rep 3:1369–1377
    • (2013) Cell Rep , vol.3 , pp. 1369-1377
    • Johnson, S.1    Brooks, N.J.2    Smith, R.3    Lea, S.M.4    Bubeck, D.5
  • 70
    • 58849087549 scopus 로고    scopus 로고
    • Rapid membrane disruption by a perforin-like protein facilitates parasite exit from host cells
    • Kafsack BF, Pena JD, Coppens I, Ravindran S, Boothroyd JC, Carruthers VB (2009) Rapid membrane disruption by a perforin-like protein facilitates parasite exit from host cells. Science 323:530–533
    • (2009) Science , vol.323 , pp. 530-533
    • Kafsack, B.F.1    Pena, J.D.2    Coppens, I.3    Ravindran, S.4    Boothroyd, J.C.5    Carruthers, V.B.6
  • 72
    • 0015827924 scopus 로고
    • The membrane attack mechanism of complement. Reversible interactions among the five native components in free solution
    • Kolb WP, Haxby JA, Arroyave CM, Müller-Eberhard HJ (1973) The membrane attack mechanism of complement. Reversible interactions among the five native components in free solution. J Exp Med 138:428–437
    • (1973) J Exp Med , vol.138 , pp. 428-437
    • Kolb, W.P.1    Haxby, J.A.2    Arroyave, C.M.3    Müller-Eberhard, H.J.4
  • 73
    • 0016221719 scopus 로고
    • Mode of action of human C9: Adsorption of multiple C9 molecules to cell-bound C8
    • Kolb WP, Müller-Eberhard HJ (1974) Mode of action of human C9: adsorption of multiple C9 molecules to cell-bound C8. J Immunol 113:479–488
    • (1974) J Immunol , vol.113 , pp. 479-488
    • Kolb, W.P.1    Müller-Eberhard, H.J.2
  • 75
    • 0024816497 scopus 로고
    • N-deglycosylation of human complement component C9 reduces its hemolytic activity
    • Kontermann R, Rauterberg EW (1989) N-deglycosylation of human complement component C9 reduces its hemolytic activity. Mol Immunol 26:1125–1132
    • (1989) Mol Immunol , vol.26 , pp. 1125-1132
    • Kontermann, R.1    Rauterberg, E.W.2
  • 76
    • 67649819389 scopus 로고    scopus 로고
    • Intermedilysin-receptor interactions during assembly of the pore complex: Assembly intermediates increase host cell susceptibility to complement-mediated lysis
    • LaChapelle S, Tweten RK, Hotze EM (2009) Intermedilysin-receptor interactions during assembly of the pore complex: assembly intermediates increase host cell susceptibility to complement-mediated lysis. J Biol Chem 284:12719–12726
    • (2009) J Biol Chem , vol.284 , pp. 12719-12726
    • Lachapelle, S.1    Tweten, R.K.2    Hotze, E.M.3
  • 77
    • 0014772363 scopus 로고
    • Reactive lysis: The complement-mediated lysis of unsensitized cells. II. The characterization of activated reactor as C56 and the participation of C8 and C9
    • Lachmann PJ, Thompson RA (1970) Reactive lysis: the complement-mediated lysis of unsensitized cells. II. The characterization of activated reactor as C56 and the participation of C8 and C9. J Exp Med 131:643–657
    • (1970) J Exp Med , vol.131 , pp. 643-657
    • Lachmann, P.J.1    Thompson, R.A.2
  • 78
    • 0024395615 scopus 로고
    • Identification of the discontinuous epitope in human complement protein C9 recognized by anti-melittin antibodies
    • Laine RO, Esser AF (1989) Identification of the discontinuous epitope in human complement protein C9 recognized by anti-melittin antibodies. J Immunol 143:553–557
    • (1989) J Immunol , vol.143 , pp. 553-557
    • Laine, R.O.1    Esser, A.F.2
  • 80
    • 79551581253 scopus 로고    scopus 로고
    • Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex
    • Laursen NS, Andersen KR, Braren I, Spillner E, Sottrup-Jensen L, Andersen GR (2011) Substrate recognition by complement convertases revealed in the C5-cobra venom factor complex. EMBO J 30:606–616
    • (2011) EMBO J , vol.30 , pp. 606-616
    • Laursen, N.S.1    Ersen, K.R.2    Braren, I.3    Spillner, E.4    Sottrup-Jensen, L.5    Ersen, G.R.6
  • 83
    • 0019335148 scopus 로고
    • Mechanism of exchange of cytochrome b5 between phosphatidylcholine vesicles
    • Leto TL, Roseman MA, Holloway PW (1980) Mechanism of exchange of cytochrome b5 between phosphatidylcholine vesicles. Biochemistry 19:1911–1916
    • (1980) Biochemistry , vol.19 , pp. 1911-1916
    • Leto, T.L.1    Roseman, M.A.2    Holloway, P.W.3
  • 84
    • 84862221167 scopus 로고    scopus 로고
    • SMART 7: Recent updates to the protein domain annotation resource
    • (Database issue)
    • Letunic I, Doerks T, Bork P (2012) SMART 7: recent updates to the protein domain annotation resource. Nucleic Acids Res 40:D302–D305 (Database issue)
    • (2012) Nucleic Acids Res , vol.40 , pp. D302-D305
    • Letunic, I.1    Doerks, T.2    Bork, P.3
  • 85
    • 74449088938 scopus 로고    scopus 로고
    • The membrane attack complex of complement drives the progression of atherosclerosis in apolipoprotein
    • Lewis RD, Jackson CL, Morgan BP, Hughes TR (2010) The membrane attack complex of complement drives the progression of atherosclerosis in apolipoprotein E knockout mice. Mol Immunol 47:1098–1105
    • (2010) E Knockout Mice. Mol Immunol , vol.47 , pp. 1098-1105
    • Lewis, R.D.1    Jackson, C.L.2    Morgan, B.P.3    Hughes, T.R.4
  • 87
    • 0011278883 scopus 로고
    • Components of Guinea pig complement. Ii. Separation of serum fractions essential for immune hemolysis
    • Linscott WD, Nishioka K (1963) Components of Guinea pig complement. Ii. Separation of serum fractions essential for immune hemolysis. J Exp Med 118:795–815
    • (1963) J Exp Med , vol.118 , pp. 795-815
    • Linscott, W.D.1    Nishioka, K.2
  • 88
    • 0029095712 scopus 로고
    • Identity of the segment of human complement C8 recognized by complement regulatory protein CD59
    • Lockert DH, Kaufman KM, Chang CP, Husler T, Sodetz JM, Sims PJ (1995) Identity of the segment of human complement C8 recognized by complement regulatory protein CD59. J Biol Chem 270:19723–19728
    • (1995) J Biol Chem , vol.270 , pp. 19723-19728
    • Lockert, D.H.1    Kaufman, K.M.2    Chang, C.P.3    Husler, T.4    Sodetz, J.M.5    Sims, P.J.6
  • 89
    • 34848895087 scopus 로고    scopus 로고
    • Crystal structure of complement protein C8gamma in complex with a peptide containing the C8gamma binding site on C8alpha: Implications for C8gamma ligand binding
    • Lovelace LL, Chiswell B, Slade DJ, Sodetz JM, Lebioda L (2008) Crystal structure of complement protein C8gamma in complex with a peptide containing the C8gamma binding site on C8alpha: implications for C8gamma ligand binding. Mol Immunol 45:750–756
    • (2008) Mol Immunol , vol.45 , pp. 750-756
    • Lovelace, L.L.1    Chiswell, B.2    Slade, D.J.3    Sodetz, J.M.4    Lebioda, L.5
  • 90
    • 79955953166 scopus 로고    scopus 로고
    • Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement
    • Lovelace LL, Cooper CL, Sodetz JM, Lebioda L (2011) Structure of human C8 protein provides mechanistic insight into membrane pore formation by complement. J Biol Chem 286:17585–17592
    • (2011) J Biol Chem , vol.286 , pp. 17585-17592
    • Lovelace, L.L.1    Cooper, C.L.2    Sodetz, J.M.3    Lebioda, L.4
  • 91
    • 38749123992 scopus 로고    scopus 로고
    • Friend or foe: The same fold for attack and defense
    • Lukoyanova N, Saibil HR (2008) Friend or foe: the same fold for attack and defense. Trends Immunol 29:51–53
    • (2008) Trends Immunol , vol.29 , pp. 51-53
    • Lukoyanova, N.1    Saibil, H.R.2
  • 92
    • 0024585009 scopus 로고
    • Membrane permeability to macromolecules mediated by the membrane attack complex
    • Malinski JA, Nelsestuen GL (1989) Membrane permeability to macromolecules mediated by the membrane attack complex. Biochemistry 28:61–70
    • (1989) Biochemistry , vol.28 , pp. 61-70
    • Malinski, J.A.1    Nelsestuen, G.L.2
  • 94
    • 34548849117 scopus 로고    scopus 로고
    • The role of complement in inflammatory diseases from behind the scenes into the spotlight
    • Markiewski MM, Lambris JD (2007) The role of complement in inflammatory diseases from behind the scenes into the spotlight. Am J Pathol 171:715–727
    • (2007) Am J Pathol , vol.171 , pp. 715-727
    • Markiewski, M.M.1    Lambris, J.D.2
  • 96
    • 0023263548 scopus 로고
    • Killing of human melanoma cells by the membrane attack complex of human complement as a function of its molecular composition
    • Martin DE, Chiu FJ, Gigli I, Muller-Eberhard HJ (1987) Killing of human melanoma cells by the membrane attack complex of human complement as a function of its molecular composition. J Clin Invest 80:226–233
    • (1987) J Clin Invest , vol.80 , pp. 226-233
    • Martin, D.E.1    Chiu, F.J.2    Gigli, I.3    Muller-Eberhard, H.J.4
  • 97
    • 0022253052 scopus 로고
    • Isolation of a lytic, pore-forming protein (Perforin) from cytolytic T-lymphocytes
    • Masson D, Tschopp J (1985) Isolation of a lytic, pore-forming protein (perforin) from cytolytic T-lymphocytes. J Biol Chem 260:9069–9072
    • (1985) J Biol Chem , vol.260 , pp. 9069-9072
    • Masson, D.1    Tschopp, J.2
  • 98
    • 0015410094 scopus 로고
    • Mechanism of cytolysis by complement
    • Mayer MM (1972) Mechanism of cytolysis by complement. Proc Natl Acad Sci USA 69:2954–2958
    • (1972) Proc Natl Acad Sci USA , vol.69 , pp. 2954-2958
    • Mayer, M.M.1
  • 100
    • 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
    • Meri S, Morgan BP, Davies A, Daniels RH, Olavesen MG, Waldmann H, Lachmann PJ (1990) 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) Immunology , vol.71 , pp. 1-9
    • Meri, S.1    Morgan, B.P.2    Davies, A.3    Daniels, R.H.4    Olavesen, M.G.5    Waldmann, H.6    Lachmann, P.J.7
  • 101
    • 0025368397 scopus 로고
    • Human protectin (CD59), an 18-20-kD homologous complement restriction factor, does not restrict perforin-mediated lysis
    • Meri S, Morgan BP, Wing M, Jones J, Davies A, Podack E, Lachmann PJ (1990) Human protectin (CD59), an 18-20-kD homologous complement restriction factor, does not restrict perforin-mediated lysis. J Exp Med 172:367–370
    • (1990) J Exp Med , vol.172 , pp. 367-370
    • Meri, S.1    Morgan, B.P.2    Wing, M.3    Jones, J.4    Davies, A.5    Podack, E.6    Lachmann, P.J.7
  • 102
    • 0024410923 scopus 로고
    • Activation-dependent epitopes in the terminal complement pathway
    • Mollnes TE, Lea T, Tschopp J (1989) Activation-dependent epitopes in the terminal complement pathway. Complement Inflamm 6:223–235
    • (1989) Complement Inflamm , vol.6 , pp. 223-235
    • Mollnes, T.E.1    Lea, T.2    Tschopp, J.3
  • 103
    • 0028062876 scopus 로고
    • Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form
    • Morgan PJ, Hyman SC, Byron O, Andrew PW, Mitchell TJ, Rowe AJ (1994) Modeling the bacterial protein toxin, pneumolysin, in its monomeric and oligomeric form. J Biol Chem 269:25315–25320
    • (1994) J Biol Chem , vol.269 , pp. 25315-25320
    • Morgan, P.J.1    Hyman, S.C.2    Byron, O.3    Rew, P.W.4    Mitchell, T.J.5    Rowe, A.J.6
  • 104
    • 35649022765 scopus 로고    scopus 로고
    • Live cell imaging of outward and inward vesiculation induced by the complement c5b-9 complex
    • Moskovich O, Fishelson Z (2007) Live cell imaging of outward and inward vesiculation induced by the complement c5b-9 complex. J Biol Chem 282(41):29977–29986
    • (2007) J Biol Chem , vol.282 , Issue.41 , pp. 29977-29986
    • Moskovich, O.1    Fishelson, Z.2
  • 105
    • 0022567063 scopus 로고
    • The membrane attack complex of complement
    • Müller-Eberhard HJ (1986) The membrane attack complex of complement. Ann Rev Immunol 4:503–528
    • (1986) Ann Rev Immunol , vol.4 , pp. 503-528
    • Müller-Eberhard, H.J.1
  • 106
    • 0018814543 scopus 로고
    • Molecular biology and chemistry of the alternative pathway of complement
    • Müller-Eberhard HJ, Schreiber RD (1980) Molecular biology and chemistry of the alternative pathway of complement. Adv Immunol 29:1–53
    • (1980) Adv Immunol , vol.29 , pp. 1-53
    • Müller-Eberhard, H.J.1    Schreiber, R.D.2
  • 107
    • 0024614958 scopus 로고
    • CTL-mediated cytolysis: Perforin and alternative pathways?
    • Nabholz M, Tschopp J (1989) CTL-mediated cytolysis: perforin and alternative pathways? Immunol Lett 20:179–180
    • (1989) Immunol Lett , vol.20 , pp. 179-180
    • Nabholz, M.1    Tschopp, J.2
  • 108
    • 0023664828 scopus 로고
    • The eighth component of human complement: Evidence that it is an oligomeric serum protein assembled from products of three different genes
    • Ng SC, Rao AG, Howard OM, Sodetz JM (1987) The eighth component of human complement: evidence that it is an oligomeric serum protein assembled from products of three different genes. Biochemistry 26:5229–5233
    • (1987) Biochemistry , vol.26 , pp. 5229-5233
    • Ng, S.C.1    Rao, A.G.2    Howard, O.M.3    Sodetz, J.M.4
  • 109
    • 0026643467 scopus 로고
    • The human complement regulatory protein CD59 binds to the alpha-chain of C8 and to the ‘‘b’’domain of C9
    • Ninomiya H, Sims PJ (1992) The human complement regulatory protein CD59 binds to the alpha-chain of C8 and to the ‘‘b’’domain of C9. J Biol Chem 267:13675–13680
    • (1992) J Biol Chem , vol.267 , pp. 13675-13680
    • Ninomiya, H.1    Sims, P.J.2
  • 110
    • 0037018929 scopus 로고    scopus 로고
    • Crystal structure of human complement protein C8gamma at 1.2 Å resolution reveals a lipocalin fold and a distinct ligand binding site
    • Ortlund E, Parker CL, Schreck SF, Ginell S, Minor W, Sodetz JM, Lebioda L (2002) Crystal structure of human complement protein C8gamma at 1.2 Å resolution reveals a lipocalin fold and a distinct ligand binding site. Biochemistry 41:7030–7037
    • (2002) Biochemistry , vol.41 , pp. 7030-7037
    • Ortlund, E.1    Parker, C.L.2    Schreck, S.F.3    Ginell, S.4    Minor, W.5    Sodetz, J.M.6    Lebioda, L.7
  • 111
    • 0032536856 scopus 로고    scopus 로고
    • Assembly mechanism of the oligomeric streptolysin O pore: The early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization
    • Palmer M, Harris R, Freytag C, Kehoe M, Tranum-Jensen J, Bhakdi S (1998) Assembly mechanism of the oligomeric streptolysin O pore: the early membrane lesion is lined by a free edge of the lipid membrane and is extended gradually during oligomerization. EMBO J 17:1598–1605
    • (1998) EMBO J , vol.17 , pp. 1598-1605
    • Palmer, M.1    Harris, R.2    Freytag, C.3    Kehoe, M.4    Tranum-Jensen, J.5    Bhakdi, S.6
  • 112
    • 0036843632 scopus 로고    scopus 로고
    • Role of the human C8 subunits in complement-mediated bacterial killing: Evidence that C8 gamma is not essential
    • Parker CL, Sodetz JM (2002) Role of the human C8 subunits in complement-mediated bacterial killing: evidence that C8 gamma is not essential. Mol Immunol 39:453–458
    • (2002) Mol Immunol , vol.39 , pp. 453-458
    • Parker, C.L.1    Sodetz, J.M.2
  • 113
    • 0024995537 scopus 로고
    • Localization and molecular modelling of the membrane-inserted domain of the ninth component of human complement and perforin
    • Peitsch MC, Amiguet P, Guy R, Brunner J, Maizel JV, Tschopp J (1990) Localization and molecular modelling of the membrane-inserted domain of the ninth component of human complement and perforin. Mol Immunol 27:589–602
    • (1990) Mol Immunol , vol.27 , pp. 589-602
    • Peitsch, M.C.1    Amiguet, P.2    Guy, R.3    Brunner, J.4    Maizel, J.V.5    Tschopp, J.6
  • 114
    • 0025044561 scopus 로고
    • Structural homologies of component C5 of human complement with components C3 and C4 by neutron scattering
    • Perkins SJ, Smith KF, Nealis AS, Lachmann PJ, Harrison RA (1990) Structural homologies of component C5 of human complement with components C3 and C4 by neutron scattering. Biochemistry 29:175–180
    • (1990) Biochemistry , vol.29 , pp. 175-180
    • Perkins, S.J.1    Smith, K.F.2    Nealis, A.S.3    Lachmann, P.J.4    Harrison, R.A.5
  • 115
    • 0018319183 scopus 로고
    • Neisseria meningitidis and Neisseria gonorrhoeae bacteremia associated with C6, C7, or C8 deficiency
    • Petersen BH, Lee TJ, Snyderman R, Brooks GF (1979) Neisseria meningitidis and Neisseria gonorrhoeae bacteremia associated with C6, C7, or C8 deficiency. Ann Intern Med 90:917–920
    • (1979) Ann Intern Med , vol.90 , pp. 917-920
    • Petersen, B.H.1    Lee, T.J.2    Snyderman, R.3    Brooks, G.F.4
  • 116
    • 65649135090 scopus 로고    scopus 로고
    • Bramham J (2009) 1H, 15 N and 13C resonance assignment of the pair of Factor-I like modules of the complement protein C7
    • Phelan MM, Thai C-T, Herbert AP, Bella J, Uhrín D, Ogata RT, Barlow PN, Bramham J (2009) 1H, 15 N and 13C resonance assignment of the pair of Factor-I like modules of the complement protein C7. Biomol NMR Assign 3:49–52
    • Biomol NMR Assign , vol.3 , pp. 49-52
    • Phelan, M.M.1    Thai, C.-T.2    Herbert, A.P.3    Bella, J.4    Uhrín, D.5    Ogata, R.T.6    Barlow, P.N.7
  • 117
    • 67749099821 scopus 로고    scopus 로고
    • Solution structure of factor I-like modules from complement C7 reveals a pair of follistatin domains in compact pseudosymmetric arrangement
    • Phelan MM, Thai C-T, Soares DC, Ogata RT, Barlow PN, Bramham J (2009) Solution structure of factor I-like modules from complement C7 reveals a pair of follistatin domains in compact pseudosymmetric arrangement. J Biol Chem 284:19637–19649
    • (2009) J Biol Chem , vol.284 , pp. 19637-19649
    • Phelan, M.M.1    Thai, C.-T.2    Soares, D.C.3    Ogata, R.T.4    Barlow, P.N.5    Bramham, J.6
  • 118
    • 0021252925 scopus 로고
    • Molecular composition of the tubular structure of the membrane attack complex of complement
    • Podack ER (1984) Molecular composition of the tubular structure of the membrane attack complex of complement. J Biol Chem 259:8641–8647
    • (1984) J Biol Chem , vol.259 , pp. 8641-8647
    • Podack, E.R.1
  • 119
    • 0020679842 scopus 로고
    • Assembly of two types of tubules with putative cytolytic function by cloned natural killer cells
    • Podack ER, Dennert G (1983) Assembly of two types of tubules with putative cytolytic function by cloned natural killer cells. Nature 302:442–445
    • (1983) Nature , vol.302 , pp. 442-445
    • Podack, E.R.1    Dennert, G.2
  • 120
    • 0018834867 scopus 로고
    • Membrane attack complex of complement: A structural analysis of its assembly
    • Podack ER, Esser AF, Biesecker G, Müller-Eberhard HJ (1980) Membrane attack complex of complement: a structural analysis of its assembly. J Exp Med 151:301–313
    • (1980) J Exp Med , vol.151 , pp. 301-313
    • Podack, E.R.1    Esser, A.F.2    Biesecker, G.3    Müller-Eberhard, H.J.4
  • 121
  • 122
    • 0017691877 scopus 로고
    • The SC5b-7 complex: Formation, isolation, properties, and subunit composition
    • Podack ER, Kolb WP, Muller-Eberhard HJ (1977) The SC5b-7 complex: formation, isolation, properties, and subunit composition. J Immunol 119:2024–2029
    • (1977) J Immunol , vol.119 , pp. 2024-2029
    • Podack, E.R.1    Kolb, W.P.2    Muller-Eberhard, H.J.3
  • 123
    • 0018904579 scopus 로고
    • SC5b-9 complex of complement: Formation of the dimeric membrane attack complex by removal of S-protein
    • Podack ER, Müller-Eberhard HJ (1980) SC5b-9 complex of complement: formation of the dimeric membrane attack complex by removal of S-protein. J Immunol 124:1779–1783
    • (1980) J Immunol , vol.124 , pp. 1779-1783
    • Podack, E.R.1    Müller-Eberhard, H.J.2
  • 124
    • 0020002246 scopus 로고
    • Membrane attach complex of complement (MAC): Three-dimensional analysis of MAC-phospholipid vesicle recombinants
    • Podack ER, Müller-Eberhard HJ, Horst H, Hoppe W (1982) Membrane attach complex of complement (MAC): three-dimensional analysis of MAC-phospholipid vesicle recombinants. J Immunol 128:2353–2357
    • (1982) J Immunol , vol.128 , pp. 2353-2357
    • Podack, E.R.1    Müller-Eberhard, H.J.2    Horst, H.3    Hoppe, W.4
  • 126
    • 0019992685 scopus 로고
    • Molecular organization of C9 within the membrane attack complex of complement. Induction of circular C9 polymerization by the C5b-8 assembly
    • Podack ER, Tschoop J, Müller-Eberhard HJ (1982) Molecular organization of C9 within the membrane attack complex of complement. Induction of circular C9 polymerization by the C5b-8 assembly. J Exp Med 156:268–282
    • (1982) J Exp Med , vol.156 , pp. 268-282
    • Podack, E.R.1    Tschoop, J.2    Müller-Eberhard, H.J.3
  • 127
    • 0020491521 scopus 로고
    • Circular polymerization of the ninth component of complement. Ring closure of the tubular complex confers resistance to detergent dissociation and to proteolytic degradation
    • Podack ER, Tschopp J (1982) Circular polymerization of the ninth component of complement. Ring closure of the tubular complex confers resistance to detergent dissociation and to proteolytic degradation. J Biol Chem 257:15204–15212
    • (1982) J Biol Chem , vol.257 , pp. 15204-15212
    • Podack, E.R.1    Tschopp, J.2
  • 128
    • 0020032614 scopus 로고
    • Polymerization of the ninth component of complement (C9): Formation of poly(C9) with a tubular ultrastructure resembling the membrane attack complex of complement
    • Podack ER, Tschopp J (1982) Polymerization of the ninth component of complement (C9): formation of poly(C9) with a tubular ultrastructure resembling the membrane attack complex of complement. Proc Natl Acad Sci USA 79:574–578
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 574-578
    • Podack, E.R.1    Tschopp, J.2
  • 129
    • 0021256194 scopus 로고
    • Membrane attack by complement
    • Podack ER, Tschopp J (1984) Membrane attack by complement. Mol Immunol 21:589–603
    • (1984) Mol Immunol , vol.21 , pp. 589-603
    • Podack, E.R.1    Tschopp, J.2
  • 131
    • 0033576666 scopus 로고    scopus 로고
    • Chlamydial homologues of the MACPF (MAC/perforin) domain
    • Ponting CP (1999) Chlamydial homologues of the MACPF (MAC/perforin) domain. Curr Biol 9:R911–R913
    • (1999) Curr Biol , vol.9 , pp. R911-R913
    • Ponting, C.P.1
  • 133
    • 0024594182 scopus 로고
    • SC5b-7, SC5b-8 and SC5b-9 complexes of complement: Ultrastructure and localization of the S-protein (vitronectin) within the macromolecules
    • Preissner KP, Podack ER, Müller-Eberhard HJ (1989) SC5b-7, SC5b-8 and SC5b-9 complexes of complement: ultrastructure and localization of the S-protein (vitronectin) within the macromolecules. Eur J Immunol 19:69–75
    • (1989) Eur J Immunol , vol.19 , pp. 69-75
    • Preissner, K.P.1    Podack, E.R.2    Müller-Eberhard, H.J.3
  • 134
    • 0025831155 scopus 로고
    • Structure and biological role of vitronectin
    • Preissner KT (1991) Structure and biological role of vitronectin. Annu Rev Cell Biol 7:275–310
    • (1991) Annu Rev Cell Biol , vol.7 , pp. 275-310
    • Preissner, K.T.1
  • 135
    • 0021885862 scopus 로고
    • The membrane attack complex of complement: Relation of C7 to the metastable membrane binding site of the intermediate complex C5b-7
    • Preissner KT, Podack ER, Müller-Eberhard HJ (1985) The membrane attack complex of complement: relation of C7 to the metastable membrane binding site of the intermediate complex C5b-7. J Immunol 135:445–451
    • (1985) J Immunol , vol.135 , pp. 445-451
    • Preissner, K.T.1    Podack, E.R.2    Müller-Eberhard, H.J.3
  • 136
    • 0021802859 scopus 로고
    • Self-association of the seventh component of human complement (C7): Dimerization and polymerization
    • Preissner KT, Podack ER, Müller-Eberhard HJ (1985) Self-association of the seventh component of human complement (C7): dimerization and polymerization. J Immunol 135:452–458
    • (1985) J Immunol , vol.135 , pp. 452-458
    • Preissner, K.T.1    Podack, E.R.2    Müller-Eberhard, H.J.3
  • 137
    • 3543016107 scopus 로고    scopus 로고
    • Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit betastrand alignment
    • Ramachandran R, Tweten RK, Johnson AE (2004) Membrane-dependent conformational changes initiate cholesterol-dependent cytolysin oligomerization and intersubunit betastrand alignment. Nat Struct Mol Biol 11:697–705
    • (2004) Nat Struct Mol Biol , vol.11 , pp. 697-705
    • Ramachandran, R.1    Tweten, R.K.2    Johnson, A.E.3
  • 138
    • 0020173803 scopus 로고
    • Transmembrane channel formation by complement: Functional analysis of the number of C5b6, C7, C8, and C9 molecules required for a single channel
    • Ramm LE, Whitlow MB, Mayer MM (1982) Transmembrane channel formation by complement: functional analysis of the number of C5b6, C7, C8, and C9 molecules required for a single channel. Proc Natl Acad Sci USA 79:4751–4755
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 4751-4755
    • Ramm, L.E.1    Whitlow, M.B.2    Mayer, M.M.3
  • 139
    • 0021925787 scopus 로고
    • The relationship between channel size and the number of C9 molecules in the C5b-9 complex
    • Ramm LE, Whitlow MB, Mayer MM (1985) The relationship between channel size and the number of C9 molecules in the C5b-9 complex. J Immunol 134:2594–2599
    • (1985) J Immunol , vol.134 , pp. 2594-2599
    • Ramm, L.E.1    Whitlow, M.B.2    Mayer, M.M.3
  • 140
    • 0035865060 scopus 로고    scopus 로고
    • Formation of high-affinity C5 convertases of the alternative pathway of complement
    • Rawal N, Pangburn M (2001) Formation of high-affinity C5 convertases of the alternative pathway of complement. J Immunol 166:2635–2642
    • (2001) J Immunol , vol.166 , pp. 2635-2642
    • Rawal, N.1    Pangburn, M.2
  • 141
    • 0141643292 scopus 로고    scopus 로고
    • Formation of high affinity C5 convertase of the classical pathway of complement
    • Rawal N, Pangburn MK (2003) Formation of high affinity C5 convertase of the classical pathway of complement. J Biol Chem 278:38476–38483
    • (2003) J Biol Chem , vol.278 , pp. 38476-38483
    • Rawal, N.1    Pangburn, M.K.2
  • 142
    • 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
    • Rollins SA, Zhao J, Ninomiya H, Sims PJ (1991) 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) J Immunol , vol.146 , pp. 2345-2351
    • Rollins, S.A.1    Zhao, J.2    Ninomiya, H.3    Sims, P.J.4
  • 145
    • 0030666371 scopus 로고    scopus 로고
    • Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form
    • Rossjohn J, Feil SC, McKinstry WJ, Tweten RK, Parker MW (1997) Structure of a cholesterol-binding, thiol-activated cytolysin and a model of its membrane form. Cell 89:685–692
    • (1997) Cell , vol.89 , pp. 685-692
    • Rossjohn, J.1    Feil, S.C.2    McKinstry, W.J.3    Tweten, R.K.4    Parker, M.W.5
  • 146
    • 35948959015 scopus 로고    scopus 로고
    • Discovery and development of the complement inhibitor eculizumab for the treatment of paroxysmal nocturnal hemoglobinuria
    • Rother RP, Rollins SA, Mojcik CF, Brodsky RA, Bell L (2007) Discovery and development of the complement inhibitor eculizumab for the treatment of paroxysmal nocturnal hemoglobinuria. Nat Biotechnol 25:1256–1264
    • (2007) Nat Biotechnol , vol.25 , pp. 1256-1264
    • Rother, R.P.1    Rollins, S.A.2    Mojcik, C.F.3    Brodsky, R.A.4    Bell, L.5
  • 148
    • 84879123070 scopus 로고    scopus 로고
    • Disulfide-bond scanning reveals assembly state and b-strand tilt angle of the PFO b-barrel
    • Sato TK, Tweten RK, Johnson AE (2013) Disulfide-bond scanning reveals assembly state and b-strand tilt angle of the PFO b-barrel. Nat Chem Biol 9:383–389
    • (2013) Nat Chem Biol , vol.9 , pp. 383-389
    • Sato, T.K.1    Tweten, R.K.2    Johnson, A.E.3
  • 149
    • 0031829918 scopus 로고    scopus 로고
    • Expression and characterization of recombinant subunits of human complement component C8: Further analysis of the function of C8 alpha and C8 gamma
    • Schreck SF, Plumb ME, Platteborze PL, Kaufman KM, Michelotti GA, Letson CS, Sodetz JM (1998) Expression and characterization of recombinant subunits of human complement component C8: further analysis of the function of C8 alpha and C8 gamma. J Immunol 161:311–318
    • (1998) J Immunol , vol.161 , pp. 311-318
    • Schreck, S.F.1    Plumb, M.E.2    Platteborze, P.L.3    Kaufman, K.M.4    Michelotti, G.A.5    Letson, C.S.6    Sodetz, J.M.7
  • 150
    • 0033615736 scopus 로고    scopus 로고
    • The mechanism of membrane insertion for a cholesterol-dependent cytolysin: A novel paradigm for pore-forming toxins
    • Shatursky O, Heuck AP, Shepard LA, Rossjohn J, Parker MW, Johnson AE, Tweten RK (1999) The mechanism of membrane insertion for a cholesterol-dependent cytolysin: a novel paradigm for pore-forming toxins. Cell 99:293–299
    • (1999) Cell , vol.99 , pp. 293-299
    • Shatursky, O.1    Heuck, A.P.2    Shepard, L.A.3    Rossjohn, J.4    Parker, M.W.5    Johnson, A.E.6    Tweten, R.K.7
  • 151
    • 0032514655 scopus 로고    scopus 로고
    • Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: An alpha-helical to beta-sheet transition identified by fluorescence spectroscopy
    • Shepard LA, Heuck AP, Hamman BD, Rossjohn J, Parker MW, Ryan KR, Johnson AE, Tweten RK (1998) Identification of a membrane-spanning domain of the thiol-activated pore-forming toxin Clostridium perfringens perfringolysin O: an alpha-helical to beta-sheet transition identified by fluorescence spectroscopy. Biochemistry 37:14563–14574
    • (1998) Biochemistry , vol.37 , pp. 14563-14574
    • Shepard, L.A.1    Heuck, A.P.2    Hamman, B.D.3    Rossjohn, J.4    Parker, M.W.5    Ryan, K.R.6    Johnson, A.E.7    Tweten, R.K.8
  • 152
    • 0023693490 scopus 로고
    • Homology of perforin to the ninth component of complement (C9)
    • Shinkai Y, Takio K, Okumura K (1988) Homology of perforin to the ninth component of complement (C9). Nature 334:525–527
    • (1988) Nature , vol.334 , pp. 525-527
    • Shinkai, Y.1    Takio, K.2    Okumura, K.3
  • 153
    • 0022826207 scopus 로고
    • Interaction of complement proteins C5b-6 and C5b-7 with phospholipid vesicles: Effects of phospholipid structural features
    • Silversmith RE, Nelsestuen GL (1986) Interaction of complement proteins C5b-6 and C5b-7 with phospholipid vesicles: effects of phospholipid structural features. Biochemistry 25:7717–7725
    • (1986) Biochemistry , vol.25 , pp. 7717-7725
    • Silversmith, R.E.1    Nelsestuen, G.L.2
  • 155
    • 0020963697 scopus 로고
    • Complement pores in erythrocyte membranes. Analysis of C8/C9 binding required for functional membrane damage
    • Sims PJ (1983) Complement pores in erythrocyte membranes. Analysis of C8/C9 binding required for functional membrane damage. Biochim Biophys Acta 732:541–552
    • (1983) Biochim Biophys Acta , vol.732 , pp. 541-552
    • Sims, P.J.1
  • 156
    • 0024253430 scopus 로고
    • Complement proteins C5b-9 cause release of membrane vesicles from the platelet surface that are enriched in the membrane receptor for coagulation factor Va and express prothrombinase activity
    • Sims PJ, Faioni EM, Wiedmer T, Shattil SJ (1988) Complement proteins C5b-9 cause release of membrane vesicles from the platelet surface that are enriched in the membrane receptor for coagulation factor Va and express prothrombinase activity. J Biol Chem 263:18205–18212
    • (1988) J Biol Chem , vol.263 , pp. 18205-18212
    • Sims, P.J.1    Faioni, E.M.2    Wiedmer, T.3    Shattil, S.J.4
  • 157
    • 0019186379 scopus 로고
    • Analysis of solute diffusion across the C5b-9 membrane lesion of complement: Evidence that individual C5b-9 complexes do not function as discrete, uniform pores
    • Sims PJ, Lauf PK (1980) Analysis of solute diffusion across the C5b-9 membrane lesion of complement: evidence that individual C5b-9 complexes do not function as discrete, uniform pores. J Immunol 125:2617–2625
    • (1980) J Immunol , vol.125 , pp. 2617-2625
    • Sims, P.J.1    Lauf, P.K.2
  • 158
    • 43049094015 scopus 로고    scopus 로고
    • Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit
    • Slade DJ, Lovelace LL, Chruszcz M, Minor W, Lebioda L, Sodetz JM (2008) Crystal structure of the MACPF domain of human complement protein C8 alpha in complex with the C8 gamma subunit. J Mol Biol 379:331–342
    • (2008) J Mol Biol , vol.379 , pp. 331-342
    • Slade, D.J.1    Lovelace, L.L.2    Chruszcz, M.3    Minor, W.4    Lebioda, L.5    Sodetz, J.M.6
  • 159
    • 0026512967 scopus 로고
    • Molecular modeling of the domain structure of C9 of human complement by neutron and X-ray solution scattering
    • Smith KF, Harrison RA, Perkins SJ (1992) Molecular modeling of the domain structure of C9 of human complement by neutron and X-ray solution scattering. Biochemistry 31:754–764
    • (1992) Biochemistry , vol.31 , pp. 754-764
    • Smith, K.F.1    Harrison, R.A.2    Perkins, S.J.3
  • 160
    • 84877955628 scopus 로고    scopus 로고
    • Role of pore-forming toxins in neonatal sepsis
    • Sonnen AF-P, Henneke P (2013) Role of pore-forming toxins in neonatal sepsis. Clin Dev Immunol 2013:608456
    • (2013) Clin Dev Immunol , vol.2013
    • Sonnen, A.-P.1    Henneke, P.2
  • 161
    • 0020623026 scopus 로고
    • Evidence of direct insertion of terminal complement proteins into cell membrane bilayers during cytolysis. Labeling by a photosensitive membrane probe reveals a major role for the eighth and ninth components
    • Steckel EW, Welbaum BE, Sodetz JM (1983) Evidence of direct insertion of terminal complement proteins into cell membrane bilayers during cytolysis. Labeling by a photosensitive membrane probe reveals a major role for the eighth and ninth components. J Biol Chem 258:4318–4324
    • (1983) J Biol Chem , vol.258 , pp. 4318-4324
    • Steckel, E.W.1    Welbaum, B.E.2    Sodetz, J.M.3
  • 162
    • 0025194986 scopus 로고
    • Localized requirement for torso-like expression in follicle cells for development of terminal anlagen of the Drosophila embryo
    • Stevens LM, Frohnhofer HG, Klingler M, Nusslein-Volhard C (1990) Localized requirement for torso-like expression in follicle cells for development of terminal anlagen of the Drosophila embryo. Nature 346:660–663
    • (1990) Nature , vol.346 , pp. 660-663
    • Stevens, L.M.1    Frohnhofer, H.G.2    Klingler, M.3    Nusslein-Volhard, C.4
  • 163
    • 0023280690 scopus 로고
    • Evidence that C5b recognizes and mediates C8 incorporation into the cytolytic complex of complement
    • Stewart JL, Kolb WP, Sodetz JM (1987) Evidence that C5b recognizes and mediates C8 incorporation into the cytolytic complex of complement. J Immunol 139:1960–1964
    • (1987) J Immunol , vol.139 , pp. 1960-1964
    • Stewart, J.L.1    Kolb, W.P.2    Sodetz, J.M.3
  • 164
    • 0021225135 scopus 로고
    • Measurement of the ratio of the eighth and ninth components of human complement on complement-lysed membranes
    • Stewart JL, Monahan JB, Brickner A, Sodetz JM (1984) Measurement of the ratio of the eighth and ninth components of human complement on complement-lysed membranes. Biochemistry 23:4016–4022
    • (1984) Biochemistry , vol.23 , pp. 4016-4022
    • Stewart, J.L.1    Monahan, J.B.2    Brickner, A.3    Sodetz, J.M.4
  • 165
    • 0014236839 scopus 로고
    • Immune lytic transformation: A state of irreversible damage generated as a result of the reaction of the eighth component in the guinea pig complement system
    • Stolfi RL (1968) Immune lytic transformation: a state of irreversible damage generated as a result of the reaction of the eighth component in the guinea pig complement system. J Immunol 100:46–54
    • (1968) J Immunol , vol.100 , pp. 46-54
    • Stolfi, R.L.1
  • 166
    • 0030907702 scopus 로고    scopus 로고
    • Mutation of recombinant complement component C9 reveals the significance of the N-terminal region for polymerization
    • Taylor KM, Trimby AR, Campbell AK (1997) Mutation of recombinant complement component C9 reveals the significance of the N-terminal region for polymerization. Immunology 91:20–27
    • (1997) Immunology , vol.91 , pp. 20-27
    • Taylor, K.M.1    Trimby, A.R.2    Campbell, A.K.3
  • 167
    • 4644327017 scopus 로고    scopus 로고
    • Complement components C5 and C7: Recombinant factor I modules of C7 bind to the C345C domain of C5
    • Thai C-T, Ogata RT (2004) Complement components C5 and C7: recombinant factor I modules of C7 bind to the C345C domain of C5. J Immunol 173:4547–4552
    • (2004) J Immunol , vol.173 , pp. 4547-4552
    • Thai, C.-T.1    Ogata, R.T.2
  • 168
    • 18644370595 scopus 로고    scopus 로고
    • Recombinant C345C and factor I modules of complement components C5 and C7 inhibit C7 incorporation into the complement membrane attack complex
    • Thai C-T, Ogata RT (2005) Recombinant C345C and factor I modules of complement components C5 and C7 inhibit C7 incorporation into the complement membrane attack complex. J Immunol 174:6227–6232
    • (2005) J Immunol , vol.174 , pp. 6227-6232
    • Thai, C.-T.1    Ogata, R.T.2
  • 169
    • 0014772091 scopus 로고
    • Reactive lysis: The complement-mediated lysis of unsensitized cells. I. The characterization of the indicator factor and its identification as C7
    • Thompson RA, Lachmann PJ (1970) Reactive lysis: the complement-mediated lysis of unsensitized cells. I. The characterization of the indicator factor and its identification as C7. J Exp Med 131:629–641
    • (1970) J Exp Med , vol.131 , pp. 629-641
    • Thompson, R.A.1    Lachmann, P.J.2
  • 170
    • 17444405610 scopus 로고    scopus 로고
    • Structural basis of pore formation by the bacterial toxin pneumolysin
    • Tilley SJ, Orlova EV, Gilbert RJC, Andrew PW, Saibil HR (2005) Structural basis of pore formation by the bacterial toxin pneumolysin. Cell 121:247–256
    • (2005) Cell , vol.121 , pp. 247-256
    • Tilley, S.J.1    Orlova, E.V.2    Gilbert, R.3    Rew, P.W.4    Saibil, H.R.5
  • 171
    • 0022480649 scopus 로고
    • On the identity of vitronectin and S-protein: Immunological crossreactivity and functional studies
    • Tomasini BR, Mosher DF (1986) On the identity of vitronectin and S-protein: immunological crossreactivity and functional studies. Blood 68:737–742
    • (1986) Blood , vol.68 , pp. 737-742
    • Tomasini, B.R.1    Mosher, D.F.2
  • 173
    • 84894058854 scopus 로고    scopus 로고
    • Pyogenic brain and lung abscesses due to streptococcus intermedius
    • Trabue C, Pearman R, Doering T (2013) Pyogenic brain and lung abscesses due to streptococcus intermedius. J Gen Intern Med. doi:10.1007/s11606-013-2565-3
    • (2013) J Gen Intern Med
    • Trabue, C.1    Pearman, R.2    Doering, T.3
  • 174
    • 84880651157 scopus 로고    scopus 로고
    • The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation
    • Triantafilou K, Hughes TR, Triantafilou M, Morgan BP (2013) The complement membrane attack complex triggers intracellular Ca2+ fluxes leading to NLRP3 inflammasome activation. J Cell Sci 126:2903–2913
    • (2013) J Cell Sci , vol.126 , pp. 2903-2913
    • Triantafilou, K.1    Hughes, T.R.2    Triantafilou, M.3    Morgan, B.P.4
  • 175
    • 0021264462 scopus 로고
    • Ultrastructure of the membrane attack complex of complement. Heterogeneity of the complex caused by different degree of C9 polymerization
    • Tschopp J (1984) Ultrastructure of the membrane attack complex of complement. Heterogeneity of the complex caused by different degree of C9 polymerization. J Biol Chem 259:7857–7863
    • (1984) J Biol Chem , vol.259 , pp. 7857-7863
    • Tschopp, J.1
  • 176
    • 0021320278 scopus 로고
    • Molecular weight of poly(C9). 12 to 18 C9 molecules form the transmembrane channel of complement
    • Tschopp J, Engel A, Podack ER (1984) Molecular weight of poly(C9). 12 to 18 C9 molecules form the transmembrane channel of complement. J Biol Chem 259:1922–1928
    • (1984) J Biol Chem , vol.259 , pp. 1922-1928
    • Tschopp, J.1    Engel, A.2    Podack, E.R.3
  • 177
    • 0022466507 scopus 로고
    • Structural/functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis
    • Tschopp J, Masson D, Stanley KK (1986) Structural/functional similarity between proteins involved in complement- and cytotoxic T-lymphocyte-mediated cytolysis. Nature 322:831–834
    • (1986) Nature , vol.322 , pp. 831-834
    • Tschopp, J.1    Masson, D.2    Stanley, K.K.3
  • 178
    • 0019831621 scopus 로고
    • Membranolysis by the ninth component of human complement
    • Tschopp J, Podack ER (1981) Membranolysis by the ninth component of human complement. Biochem Biophys Res Commun 100:1409–1414
    • (1981) Biochem Biophys Res Commun , vol.100 , pp. 1409-1414
    • Tschopp, J.1    Podack, E.R.2
  • 179
    • 4143136022 scopus 로고
    • Ultrastructure of the membrane attack complex of complement: Detection of the tetramolecular C9-polymerizing complex C5b-8
    • Tschopp J, Podack ER, Müller-Eberhard HJ (1982) Ultrastructure of the membrane attack complex of complement: detection of the tetramolecular C9-polymerizing complex C5b-8. Proc Natl Acad Sci USA 79:7474–7478
    • (1982) Proc Natl Acad Sci USA , vol.79 , pp. 7474-7478
    • Tschopp, J.1    Podack, E.R.2    Müller-Eberhard, H.J.3
  • 180
    • 33845199637 scopus 로고    scopus 로고
    • Perforin-mediated target-cell death and immune homeostasis
    • Voskoboinik I, Smyth MJ, Trapani JA (2006) Perforin-mediated target-cell death and immune homeostasis. Nat Rev Immunol 6:940–952
    • (2006) Nat Rev Immunol , vol.6 , pp. 940-952
    • Voskoboinik, I.1    Smyth, M.J.2    Trapani, J.A.3
  • 181
    • 79957978193 scopus 로고    scopus 로고
    • Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9
    • Wickham SE, Hotze EM, Farrand AJ, Polekhina G, Nero TL, Tomlinson S, Parker MW, Tweten RK (2011) Mapping the intermedilysin-human CD59 receptor interface reveals a deep correspondence with the binding site on CD59 for complement binding proteins C8alpha and C9. J Biol Chem 286:20952–20962
    • (2011) J Biol Chem , vol.286 , pp. 20952-20962
    • Wickham, S.E.1    Hotze, E.M.2    Farrand, A.J.3    Polekhina, G.4    Nero, T.L.5    Tomlinson, S.6    Parker, M.W.7    Tweten, R.K.8
  • 184
    • 0022497854 scopus 로고
    • Purification and characterization of a cytolytic pore-forming protein from granules of cloned lymphocytes with natural killer activity
    • Young JD, Hengartner H, Podack ER, Cohn ZA (1986) Purification and characterization of a cytolytic pore-forming protein from granules of cloned lymphocytes with natural killer activity. Cell 44:849–859
    • (1986) Cell , vol.44 , pp. 849-859
    • Young, J.D.1    Hengartner, H.2    Podack, E.R.3    Cohn, Z.A.4
  • 186
    • 0025376488 scopus 로고
    • Comparison of channels formed by poly C9, C5b-8 and the membrane attack complex of complement
    • Zalman LS, Muller-Eberhard HJ (1990) Comparison of channels formed by poly C9, C5b-8 and the membrane attack complex of complement. Mol Immunol 27:533–537
    • (1990) Mol Immunol , vol.27 , pp. 533-537
    • Zalman, L.S.1    Muller-Eberhard, H.J.2
  • 187
    • 0030999525 scopus 로고    scopus 로고
    • Structural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopy
    • Zhang X, Boyar W, Toth MJ, Wennogle L, Gonnella NC (1997) Structural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopy. Proteins 28:261–267
    • (1997) Proteins , vol.28 , pp. 261-267
    • Zhang, X.1    Boyar, W.2    Toth, M.J.3    Wennogle, L.4    Gonnella, N.C.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.