메뉴 건너뛰기




Volumn 274, Issue 1, 2016, Pages 59-73

Structural insight into proteolytic activation and regulation of the complement system

Author keywords

complement; immune disorders; proteolytic cascade; structural biology

Indexed keywords

CLASSICAL COMPLEMENT PATHWAY C3 C5 CONVERTASE; COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C1S; COMPLEMENT COMPONENT C3A; COMPLEMENT COMPONENT C3B; COMPLEMENT COMPONENT C3B RECEPTOR; COMPLEMENT COMPONENT C4; COMPLEMENT COMPONENT C4A; COMPLEMENT COMPONENT C4B; COMPLEMENT COMPONENT C5B; COMPLEMENT INHIBITOR; COMPLEMENT MEMBRANE ATTACK COMPLEX; ECULIZUMAB; FICOLIN; LECTIN; MANNAN BINDING LECTIN; MANNAN BINDING LECTIN ASSOCIATED SERINE PROTEINASE; PATHOGEN ASSOCIATED MOLECULAR PATTERN; PATTERN RECOGNITION RECEPTOR; PROPERDIN; COMPLEMENT; MULTIPROTEIN COMPLEX;

EID: 84992451593     PISSN: 01052896     EISSN: 1600065X     Source Type: Journal    
DOI: 10.1111/imr.12465     Document Type: Review
Times cited : (32)

References (136)
  • 1
    • 84949497174 scopus 로고    scopus 로고
    • Complement activation, regulation, and molecular basis for complement-related diseases
    • Bajic G, Degn SE, Thiel S, Andersen GR. Complement activation, regulation, and molecular basis for complement-related diseases. EMBO J. 2015;34:2735–2757.
    • (2015) EMBO J , vol.34 , pp. 2735-2757
    • Bajic, G.1    Degn, S.E.2    Thiel, S.3    Andersen, G.R.4
  • 2
    • 84896055730 scopus 로고    scopus 로고
    • Complement is activated by IgG hexamers assembled at the cell surface
    • Diebolder CA, Beurskens FJ, de Jong RN, et al. Complement is activated by IgG hexamers assembled at the cell surface. Science. 2014;343:1260–1263.
    • (2014) Science , vol.343 , pp. 1260-1263
    • Diebolder, C.A.1    Beurskens, F.J.2    de Jong, R.N.3
  • 3
    • 84956951205 scopus 로고    scopus 로고
    • Structural basis of complement membrane attack complex formation
    • Serna M, Giles JL, Morgan BP, Bubeck D. Structural basis of complement membrane attack complex formation. Nat Commun. 2016;7:10587.
    • (2016) Nat Commun , vol.7 , pp. 10587
    • Serna, M.1    Giles, J.L.2    Morgan, B.P.3    Bubeck, D.4
  • 4
    • 84963538105 scopus 로고    scopus 로고
    • Heterogeneous MAC initiator and pore structures in a lipid bilayer by phase-plate cryo-electron tomography
    • Sharp TH, Koster AJ, Gros P. Heterogeneous MAC initiator and pore structures in a lipid bilayer by phase-plate cryo-electron tomography. Cell Rep. 2016;15:1–8.
    • (2016) Cell Rep , vol.15 , pp. 1-8
    • Sharp, T.H.1    Koster, A.J.2    Gros, P.3
  • 5
    • 84907215709 scopus 로고    scopus 로고
    • Complement activation by ligand-driven juxtaposition of discrete pattern recognition complexes
    • Degn SE, Kjaer TR, Kidmose RT, et al. Complement activation by ligand-driven juxtaposition of discrete pattern recognition complexes. Proc Natl Acad Sci USA. 2014;111:13445–13450.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. 13445-13450
    • Degn, S.E.1    Kjaer, T.R.2    Kidmose, R.T.3
  • 6
    • 84880682970 scopus 로고    scopus 로고
    • Humoral pattern recognition and the complement system
    • Degn SE, Thiel S. Humoral pattern recognition and the complement system. Scand J Immunol. 2013;78:181–193.
    • (2013) Scand J Immunol , vol.78 , pp. 181-193
    • Degn, S.E.1    Thiel, S.2
  • 7
    • 84890381384 scopus 로고    scopus 로고
    • Heteromeric complexes of native collectin kidney 1 and collectin liver 1 are found in the circulation with MASPs and activate the complement system
    • Henriksen ML, Brandt J, Andrieu JP, et al. Heteromeric complexes of native collectin kidney 1 and collectin liver 1 are found in the circulation with MASPs and activate the complement system. J Immunol. 2013;191:6117–6127.
    • (2013) J Immunol , vol.191 , pp. 6117-6127
    • Henriksen, M.L.1    Brandt, J.2    Andrieu, J.P.3
  • 8
    • 84881117420 scopus 로고    scopus 로고
    • Toward a structure-based comprehension of the lectin pathway of complement
    • Kjaer TR, Thiel S, Andersen GR. Toward a structure-based comprehension of the lectin pathway of complement. Mol Immunol. 2013;56:222–231.
    • (2013) Mol Immunol , vol.56 , pp. 222-231
    • Kjaer, T.R.1    Thiel, S.2    Andersen, G.R.3
  • 9
    • 84867324414 scopus 로고    scopus 로고
    • Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function
    • Degn SE, Jensen L, Hansen AG, et al. Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function. J Immunol. 2012;189:3957–3969.
    • (2012) J Immunol , vol.189 , pp. 3957-3969
    • Degn, S.E.1    Jensen, L.2    Hansen, A.G.3
  • 10
    • 84863001154 scopus 로고    scopus 로고
    • Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2
    • Heja D, Kocsis A, Dobo J, et al. Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2. Proc Natl Acad Sci USA. 2012;109:10498–10503.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 10498-10503
    • Heja, D.1    Kocsis, A.2    Dobo, J.3
  • 11
    • 80855128787 scopus 로고    scopus 로고
    • Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: implications for complement activation
    • Gingras AR, Girija UV, Keeble AH, et al. Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: implications for complement activation. Structure. 2011;19:1635–1643.
    • (2011) Structure , vol.19 , pp. 1635-1643
    • Gingras, A.R.1    Girija, U.V.2    Keeble, A.H.3
  • 12
    • 59849111369 scopus 로고    scopus 로고
    • Residue Lys57 in the collagen-like region of human L-ficolin and its counterpart Lys47 in H-ficolin play a key role in the interaction with the mannan-binding lectin-associated serine proteases and the collectin receptor calreticulin
    • Lacroix M, Dumestre-Perard C, Schoehn G, et al. Residue Lys57 in the collagen-like region of human L-ficolin and its counterpart Lys47 in H-ficolin play a key role in the interaction with the mannan-binding lectin-associated serine proteases and the collectin receptor calreticulin. J Immunol. 2009;182:456–465.
    • (2009) J Immunol , vol.182 , pp. 456-465
    • Lacroix, M.1    Dumestre-Perard, C.2    Schoehn, G.3
  • 13
    • 34247631620 scopus 로고    scopus 로고
    • Identification of the site of human mannan-binding lectin involved in the interaction with its partner serine proteases: the essential role of Lys55
    • Teillet F, Lacroix M, Thiel S, et al. Identification of the site of human mannan-binding lectin involved in the interaction with its partner serine proteases: the essential role of Lys55. J Immunol. 2007;178:5710–5716.
    • (2007) J Immunol , vol.178 , pp. 5710-5716
    • Teillet, F.1    Lacroix, M.2    Thiel, S.3
  • 14
    • 25844471033 scopus 로고    scopus 로고
    • A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations
    • Gal P, Harmat V, Kocsis A, et al. A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations. J Biol Chem. 2005;280:33435–33444.
    • (2005) J Biol Chem , vol.280 , pp. 33435-33444
    • Gal, P.1    Harmat, V.2    Kocsis, A.3
  • 15
    • 84875987157 scopus 로고    scopus 로고
    • Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway
    • Megyeri M, Harmat V, Major B, et al. Quantitative characterization of the activation steps of mannan-binding lectin (MBL)-associated serine proteases (MASPs) points to the central role of MASP-1 in the initiation of the complement lectin pathway. J Biol Chem. 2013;288:8922–8934.
    • (2013) J Biol Chem , vol.288 , pp. 8922-8934
    • Megyeri, M.1    Harmat, V.2    Major, B.3
  • 16
    • 84878407764 scopus 로고    scopus 로고
    • A molecular switch governs the interaction between the human complement protease C1s and its substrate, complement C4
    • Perry AJ, Wijeyewickrema LC, Wilmann PG, et al. A molecular switch governs the interaction between the human complement protease C1s and its substrate, complement C4. J Biol Chem. 2013;288:15821–15829.
    • (2013) J Biol Chem , vol.288 , pp. 15821-15829
    • Perry, A.J.1    Wijeyewickrema, L.C.2    Wilmann, P.G.3
  • 17
    • 84866528696 scopus 로고    scopus 로고
    • Crystal structure and functional characterization of the complement regulator mannose-binding lectin (MBL)/ficolin-associated protein-1 (MAP-1)
    • Skjoedt MO, Roversi P, Hummelshoj T, et al. Crystal structure and functional characterization of the complement regulator mannose-binding lectin (MBL)/ficolin-associated protein-1 (MAP-1). J Biol Chem. 2012;287:32913–32921.
    • (2012) J Biol Chem , vol.287 , pp. 32913-32921
    • Skjoedt, M.O.1    Roversi, P.2    Hummelshoj, T.3
  • 18
    • 70350041296 scopus 로고    scopus 로고
    • Paths reunited: initiation of the classical and lectin pathways of complement activation
    • Wallis R, Mitchell DA, Schmid R, Schwaeble WJ, Keeble AH. Paths reunited: initiation of the classical and lectin pathways of complement activation. Immunobiology. 2010;215:1–11.
    • (2010) Immunobiology , vol.215 , pp. 1-11
    • Wallis, R.1    Mitchell, D.A.2    Schmid, R.3    Schwaeble, W.J.4    Keeble, A.H.5
  • 19
    • 54449087793 scopus 로고    scopus 로고
    • Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins
    • Teillet F, Gaboriaud C, Lacroix M, Martin L, Arlaud GJ, Thielens NM. Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins. J Biol Chem. 2008;283:25715–25724.
    • (2008) J Biol Chem , vol.283 , pp. 25715-25724
    • Teillet, F.1    Gaboriaud, C.2    Lacroix, M.3    Martin, L.4    Arlaud, G.J.5    Thielens, N.M.6
  • 20
    • 84930188804 scopus 로고    scopus 로고
    • Structural insights into the initiating complex of the lectin pathway of complement activation
    • Kjaer TR, Le le TM, Pedersen JS, et al. Structural insights into the initiating complex of the lectin pathway of complement activation. Structure. 2015;23:342–351.
    • (2015) Structure , vol.23 , pp. 342-351
    • Kjaer, T.R.1    Le le, T.M.2    Pedersen, J.S.3
  • 21
  • 22
    • 77954312095 scopus 로고    scopus 로고
    • New insights into the molecular mechanisms of classical complement activation
    • Kojouharova M, Reid K, Gadjeva M. New insights into the molecular mechanisms of classical complement activation. Mol Immunol. 2010;47:2154–2160.
    • (2010) Mol Immunol , vol.47 , pp. 2154-2160
    • Kojouharova, M.1    Reid, K.2    Gadjeva, M.3
  • 23
    • 84935085624 scopus 로고    scopus 로고
    • Emerging and novel functions of complement protein C1q
    • Kouser L, Madhukaran SP, Shastri A, et al. Emerging and novel functions of complement protein C1q. Front Immunol. 2015;6:317.
    • (2015) Front Immunol , vol.6 , pp. 317
    • Kouser, L.1    Madhukaran, S.P.2    Shastri, A.3
  • 24
    • 84963969178 scopus 로고    scopus 로고
    • Progranulin deficiency promotes circuit-specific synaptic pruning by microglia via complement activation
    • Lui H, Zhang J, Makinson SR, et al. Progranulin deficiency promotes circuit-specific synaptic pruning by microglia via complement activation. Cell. 2016;165:921–935.
    • (2016) Cell , vol.165 , pp. 921-935
    • Lui, H.1    Zhang, J.2    Makinson, S.R.3
  • 25
    • 84962418507 scopus 로고    scopus 로고
    • Complement and microglia mediate early synapse loss in Alzheimer mouse models
    • Hong S, Beja-Glasser VF, Nfonoyim BM, et al. Complement and microglia mediate early synapse loss in Alzheimer mouse models. Science. 2016;352:712–716.
    • (2016) Science , vol.352 , pp. 712-716
    • Hong, S.1    Beja-Glasser, V.F.2    Nfonoyim, B.M.3
  • 26
    • 84888348687 scopus 로고    scopus 로고
    • TGF-beta signaling regulates neuronal C1q expression and developmental synaptic refinement
    • Bialas AR, Stevens B. TGF-beta signaling regulates neuronal C1q expression and developmental synaptic refinement. Nat Neurosci. 2013;16:1773–1782.
    • (2013) Nat Neurosci , vol.16 , pp. 1773-1782
    • Bialas, A.R.1    Stevens, B.2
  • 27
    • 0022395838 scopus 로고
    • Structural model of the collagen-like region of C1q comprising the kink region and the fibre-like packing of the six triple helices
    • Kilchherr E, Hofmann H, Steigemann W, Engel J. Structural model of the collagen-like region of C1q comprising the kink region and the fibre-like packing of the six triple helices. J Mol Biol. 1985;186:403–415.
    • (1985) J Mol Biol , vol.186 , pp. 403-415
    • Kilchherr, E.1    Hofmann, H.2    Steigemann, W.3    Engel, J.4
  • 28
    • 0344012497 scopus 로고    scopus 로고
    • The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties
    • Gaboriaud C, Juanhuix J, Gruez A, et al. The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J Biol Chem. 2003;278:46974–46982.
    • (2003) J Biol Chem , vol.278 , pp. 46974-46982
    • Gaboriaud, C.1    Juanhuix, J.2    Gruez, A.3
  • 29
    • 84882786824 scopus 로고    scopus 로고
    • Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation
    • Venkatraman Girija U, Gingras AR, Marshall JE, et al. Structural basis of the C1q/C1s interaction and its central role in assembly of the C1 complex of complement activation. Proc Natl Acad Sci USA. 2013;110:13916–13920.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 13916-13920
    • Venkatraman Girija, U.1    Gingras, A.R.2    Marshall, J.E.3
  • 30
    • 77957789299 scopus 로고    scopus 로고
    • Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex
    • Brier S, Pflieger D, Le Mignon M, et al. Mapping surface accessibility of the C1r/C1s tetramer by chemical modification and mass spectrometry provides new insights into assembly of the human C1 complex. J Biol Chem. 2010;285:32251–32263.
    • (2010) J Biol Chem , vol.285 , pp. 32251-32263
    • Brier, S.1    Pflieger, D.2    Le, M.M.3
  • 31
    • 0036469280 scopus 로고    scopus 로고
    • The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex
    • Budayova-Spano M, Lacroix M, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C. The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex. EMBO J. 2002;21:231–239.
    • (2002) EMBO J , vol.21 , pp. 231-239
    • Budayova-Spano, M.1    Lacroix, M.2    Thielens, N.M.3    Arlaud, G.J.4    Fontecilla-Camps, J.C.5    Gaboriaud, C.6
  • 32
    • 84878163798 scopus 로고    scopus 로고
    • Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites
    • Bally I, Ancelet S, Moriscot C, et al. Expression of recombinant human complement C1q allows identification of the C1r/C1s-binding sites. Proc Natl Acad Sci USA. 2013;110:8650–8655.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 8650-8655
    • Bally, I.1    Ancelet, S.2    Moriscot, C.3
  • 33
    • 67749116467 scopus 로고    scopus 로고
    • Identification of the C1q-binding sites of human C1r and C1s: a refined three-dimensional model of the C1 complex of complement
    • Bally I, Rossi V, Lunardi T, Thielens NM, Gaboriaud C, Arlaud GJ. Identification of the C1q-binding sites of human C1r and C1s: a refined three-dimensional model of the C1 complex of complement. J Biol Chem. 2009;284:19340–19348.
    • (2009) J Biol Chem , vol.284 , pp. 19340-19348
    • Bally, I.1    Rossi, V.2    Lunardi, T.3    Thielens, N.M.4    Gaboriaud, C.5    Arlaud, G.J.6
  • 35
    • 38949188247 scopus 로고    scopus 로고
    • Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r
    • Kardos J, Harmat V, Pallo A, et al. Revisiting the mechanism of the autoactivation of the complement protease C1r in the C1 complex: structure of the active catalytic region of C1r. Mol Immunol. 2008;45:1752–1760.
    • (2008) Mol Immunol , vol.45 , pp. 1752-1760
    • Kardos, J.1    Harmat, V.2    Pallo, A.3
  • 36
    • 0030053692 scopus 로고    scopus 로고
    • The reaction mechanism of the internal thioester in the human complement component C4
    • Dodds AW, Ren XD, Willis AC, Law SK. The reaction mechanism of the internal thioester in the human complement component C4. Nature. 1996;379:177–179.
    • (1996) Nature , vol.379 , pp. 177-179
    • Dodds, A.W.1    Ren, X.D.2    Willis, A.C.3    Law, S.K.4
  • 37
    • 84958074030 scopus 로고    scopus 로고
    • Schizophrenia risk from complex variation of complement component 4
    • Sekar A, Bialas AR, deRivera H, et al. Schizophrenia risk from complex variation of complement component 4. Nature. 2016;530:177–183.
    • (2016) Nature , vol.530 , pp. 177-183
    • Sekar, A.1    Bialas, A.R.2    deRivera, H.3
  • 38
    • 84866558185 scopus 로고    scopus 로고
    • Structural basis for activation of the complement system by component C4 cleavage
    • Kidmose RT, Laursen NS, Dobo J, et al. Structural basis for activation of the complement system by component C4 cleavage. Proc Natl Acad Sci USA. 2012;109:15425–15430.
    • (2012) Proc Natl Acad Sci USA , vol.109 , pp. 15425-15430
    • Kidmose, R.T.1    Laursen, N.S.2    Dobo, J.3
  • 39
    • 84865419895 scopus 로고    scopus 로고
    • Identification of a catalytic exosite for complement component C4 on the serine protease domain of C1s
    • Duncan RC, Mohlin F, Taleski D, et al. Identification of a catalytic exosite for complement component C4 on the serine protease domain of C1s. J Immunol. 2012;189:2365–2373.
    • (2012) J Immunol , vol.189 , pp. 2365-2373
    • Duncan, R.C.1    Mohlin, F.2    Taleski, D.3
  • 40
    • 84921741805 scopus 로고    scopus 로고
    • A revised mechanism for the activation of complement C3 to C3b: a molecular explanation of a disease-associated polymorphism
    • Rodriguez E, Nan R, Li K, Gor J, Perkins SJ. A revised mechanism for the activation of complement C3 to C3b: a molecular explanation of a disease-associated polymorphism. J Biol Chem. 2015;290:2334–2350.
    • (2015) J Biol Chem , vol.290 , pp. 2334-2350
    • Rodriguez, E.1    Nan, R.2    Li, K.3    Gor, J.4    Perkins, S.J.5
  • 41
    • 84982860138 scopus 로고    scopus 로고
    • Solution structures of complement C2 and its C4 complexes propose pathway specific mechanisms for control and activation of the complement proconvertases
    • Mortensen S, Jensen JK, Andersen GR. Solution structures of complement C2 and its C4 complexes propose pathway specific mechanisms for control and activation of the complement proconvertases. J Biol Chem. 2016; pii: jbc.M116.722017.
    • (2016) J Biol Chem
    • Mortensen, S.1    Jensen, J.K.2    Andersen, G.R.3
  • 42
    • 70450223899 scopus 로고    scopus 로고
    • The down-stream effects of mannan-induced lectin complement pathway activation depend quantitatively on alternative pathway amplification
    • Harboe M, Garred P, Karlstrom E, Lindstad JK, Stahl GL, Mollnes TE. The down-stream effects of mannan-induced lectin complement pathway activation depend quantitatively on alternative pathway amplification. Mol Immunol. 2009;47:373–380.
    • (2009) Mol Immunol , vol.47 , pp. 373-380
    • Harboe, M.1    Garred, P.2    Karlstrom, E.3    Lindstad, J.K.4    Stahl, G.L.5    Mollnes, T.E.6
  • 43
    • 9644280856 scopus 로고    scopus 로고
    • The quantitative role of alternative pathway amplification in classical pathway induced terminal complement activation
    • Harboe M, Ulvund G, Vien L, Fung M, Mollnes TE. The quantitative role of alternative pathway amplification in classical pathway induced terminal complement activation. Clin Exp Immunol. 2004;138:439–446.
    • (2004) Clin Exp Immunol , vol.138 , pp. 439-446
    • Harboe, M.1    Ulvund, G.2    Vien, L.3    Fung, M.4    Mollnes, T.E.5
  • 44
    • 40149093101 scopus 로고    scopus 로고
    • The tick-over theory revisited: formation and regulation of the soluble alternative complement C3 convertase (C3 (H 2 O) Bb)
    • Bexborn F, Andersson PO, Chen H, Nilsson B, Ekdahl KN. The tick-over theory revisited: formation and regulation of the soluble alternative complement C3 convertase (C3 (H 2 O) Bb). Mol Immunol. 2008;45:2370–2379.
    • (2008) Mol Immunol , vol.45 , pp. 2370-2379
    • Bexborn, F.1    Andersson, P.O.2    Chen, H.3    Nilsson, B.4    Ekdahl, K.N.5
  • 45
    • 0020438716 scopus 로고
    • C3 convertase of human complement: enhanced formation and stability of the enzyme generated with nickel instead of magnesium
    • Fishelson Z, Muller-Eberhard HJ. C3 convertase of human complement: enhanced formation and stability of the enzyme generated with nickel instead of magnesium. J Immunol. 1982;129:2603–2607.
    • (1982) J Immunol , vol.129 , pp. 2603-2607
    • Fishelson, Z.1    Muller-Eberhard, H.J.2
  • 46
    • 0016703811 scopus 로고
    • Properdin: binding to C3b and stabilization of the C3b-dependent C3 convertase
    • Fearon DT, Austen KF. Properdin: binding to C3b and stabilization of the C3b-dependent C3 convertase. J Exp Med. 1975;142:856–863.
    • (1975) J Exp Med , vol.142 , pp. 856-863
    • Fearon, D.T.1    Austen, K.F.2
  • 48
    • 78650638514 scopus 로고    scopus 로고
    • Structures of C3b in complex with factors B and D give insight into complement convertase formation
    • Forneris F, Ricklin D, Wu J, et al. Structures of C3b in complex with factors B and D give insight into complement convertase formation. Science. 2010;330:1816–1820.
    • (2010) Science , vol.330 , pp. 1816-1820
    • Forneris, F.1    Ricklin, D.2    Wu, J.3
  • 49
    • 69249220131 scopus 로고    scopus 로고
    • Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex
    • Janssen BJ, Gomes L, Koning RI, et al. Insights into complement convertase formation based on the structure of the factor B-cobra venom factor complex. EMBO J. 2009;28:2469–2478.
    • (2009) EMBO J , vol.28 , pp. 2469-2478
    • Janssen, B.J.1    Gomes, L.2    Koning, R.I.3
  • 50
    • 0024205864 scopus 로고
    • A novel cleavage product of human complement component C3 with structural and functional properties of cobra venom factor
    • O'Keefe MC, Caporale LH, Vogel CW. A novel cleavage product of human complement component C3 with structural and functional properties of cobra venom factor. J Biol Chem. 1988;263:12690–12697.
    • (1988) J Biol Chem , vol.263 , pp. 12690-12697
    • O'Keefe, M.C.1    Caporale, L.H.2    Vogel, C.W.3
  • 51
    • 0034284191 scopus 로고    scopus 로고
    • Two clusters of acidic amino acids near the NH2 terminus of complement component C4 alpha′-chain are important for C2 binding
    • Pan Q, Ebanks RO, Isenman DE. Two clusters of acidic amino acids near the NH2 terminus of complement component C4 alpha′-chain are important for C2 binding. J Immunol. 2000;165:2518–2527.
    • (2000) J Immunol , vol.165 , pp. 2518-2527
    • Pan, Q.1    Ebanks, R.O.2    Isenman, D.E.3
  • 52
    • 33847651701 scopus 로고    scopus 로고
    • Factor B structure provides insights into activation of the central protease of the complement system
    • Milder FJ, Gomes L, Schouten A, et al. Factor B structure provides insights into activation of the central protease of the complement system. Nat Struct Mol Biol. 2007;14:224–228.
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 224-228
    • Milder, F.J.1    Gomes, L.2    Schouten, A.3
  • 53
    • 34247262583 scopus 로고    scopus 로고
    • Molecular interactions between MASP-2, C4, and C2 and their activation fragments leading to complement activation via the lectin pathway
    • Wallis R, Dodds AW, Mitchell DA, Sim RB, Reid KB, Schwaeble WJ. Molecular interactions between MASP-2, C4, and C2 and their activation fragments leading to complement activation via the lectin pathway. J Biol Chem. 2007;282:7844–7851.
    • (2007) J Biol Chem , vol.282 , pp. 7844-7851
    • Wallis, R.1    Dodds, A.W.2    Mitchell, D.A.3    Sim, R.B.4    Reid, K.B.5    Schwaeble, W.J.6
  • 54
    • 84880807089 scopus 로고    scopus 로고
    • Human complement control and complement evasion by pathogenic microbes–tipping the balance
    • Zipfel PF, Hallstrom T, Riesbeck K. Human complement control and complement evasion by pathogenic microbes–tipping the balance. Mol Immunol. 2013;56:152–160.
    • (2013) Mol Immunol , vol.56 , pp. 152-160
    • Zipfel, P.F.1    Hallstrom, T.2    Riesbeck, K.3
  • 56
    • 67649221223 scopus 로고    scopus 로고
    • Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor
    • Rooijakkers SH, Wu J, Ruyken M, et al. Structural and functional implications of the alternative complement pathway C3 convertase stabilized by a staphylococcal inhibitor. Nat Immunol. 2009;10:721–727.
    • (2009) Nat Immunol , vol.10 , pp. 721-727
    • Rooijakkers, S.H.1    Wu, J.2    Ruyken, M.3
  • 57
    • 0016817802 scopus 로고
    • Properdin: initiation of alternative complement pathway
    • Fearon DT, Austen KF. Properdin: initiation of alternative complement pathway. Proc Natl Acad Sci USA. 1975;72:3220–3224.
    • (1975) Proc Natl Acad Sci USA , vol.72 , pp. 3220-3224
    • Fearon, D.T.1    Austen, K.F.2
  • 58
    • 80052162537 scopus 로고    scopus 로고
    • Complement in health and disease
    • Carroll MV, Sim RB. Complement in health and disease. Adv Drug Deliv Rev. 2011;63:965–975.
    • (2011) Adv Drug Deliv Rev , vol.63 , pp. 965-975
    • Carroll, M.V.1    Sim, R.B.2
  • 60
    • 5444259851 scopus 로고    scopus 로고
    • The complement system in regulation of adaptive immunity
    • Carroll MC. The complement system in regulation of adaptive immunity. Nat Immunol. 2004;5:981–986.
    • (2004) Nat Immunol , vol.5 , pp. 981-986
    • Carroll, M.C.1
  • 61
    • 34848864365 scopus 로고    scopus 로고
    • Properdin can initiate complement activation by binding specific target surfaces and providing a platform for de novo convertase assembly
    • Spitzer D, Mitchell LM, Atkinson JP, Hourcade DE. Properdin can initiate complement activation by binding specific target surfaces and providing a platform for de novo convertase assembly. J Immunol. 2007;179:2600–2608.
    • (2007) J Immunol , vol.179 , pp. 2600-2608
    • Spitzer, D.1    Mitchell, L.M.2    Atkinson, J.P.3    Hourcade, D.E.4
  • 62
    • 79251498910 scopus 로고    scopus 로고
    • Native properdin binds to Chlamydia pneumoniae and promotes complement activation
    • Cortes C, Ferreira VP, Pangburn MK. Native properdin binds to Chlamydia pneumoniae and promotes complement activation. Infect Immun. 2011;79:724–731.
    • (2011) Infect Immun , vol.79 , pp. 724-731
    • Cortes, C.1    Ferreira, V.P.2    Pangburn, M.K.3
  • 63
    • 57349187924 scopus 로고    scopus 로고
    • Complement activation by tubular cells is mediated by properdin binding
    • Gaarkeuken H, Siezenga MA, Zuidwijk K, et al. Complement activation by tubular cells is mediated by properdin binding. Am J Physiol Renal Physiol. 2008;295:F1397–F1403.
    • (2008) Am J Physiol Renal Physiol , vol.295 , pp. F1397-F1403
    • Gaarkeuken, H.1    Siezenga, M.A.2    Zuidwijk, K.3
  • 64
    • 84866133160 scopus 로고    scopus 로고
    • Factor h and properdin recognize different epitopes on renal tubular epithelial heparan sulfate
    • Zaferani A, Vives RR, van der Pol P, et al. Factor h and properdin recognize different epitopes on renal tubular epithelial heparan sulfate. J Biol Chem. 2012;287:31471–31481.
    • (2012) J Biol Chem , vol.287 , pp. 31471-31481
    • Zaferani, A.1    Vives, R.R.2    van der Pol, P.3
  • 65
    • 55949096010 scopus 로고    scopus 로고
    • Properdin: new roles in pattern recognition and target clearance
    • Kemper C, Hourcade DE. Properdin: new roles in pattern recognition and target clearance. Mol Immunol. 2008;45:4048–4056.
    • (2008) Mol Immunol , vol.45 , pp. 4048-4056
    • Kemper, C.1    Hourcade, D.E.2
  • 66
    • 47249130305 scopus 로고    scopus 로고
    • Properdin binds to late apoptotic and necrotic cells independently of C3b and regulates alternative pathway complement activation
    • Xu W, Berger SP, Trouw LA, et al. Properdin binds to late apoptotic and necrotic cells independently of C3b and regulates alternative pathway complement activation. J Immunol. 2008;180:7613–7621.
    • (2008) J Immunol , vol.180 , pp. 7613-7621
    • Xu, W.1    Berger, S.P.2    Trouw, L.A.3
  • 67
    • 84879094559 scopus 로고    scopus 로고
    • Identification of a novel mode of complement activation on stimulated platelets mediated by properdin and C3(H2O)
    • Saggu G, Cortes C, Emch HN, Ramirez G, Worth RG, Ferreira VP. Identification of a novel mode of complement activation on stimulated platelets mediated by properdin and C3(H2O). J Immunol. 2013;190:6457–6467.
    • (2013) J Immunol , vol.190 , pp. 6457-6467
    • Saggu, G.1    Cortes, C.2    Emch, H.N.3    Ramirez, G.4    Worth, R.G.5    Ferreira, V.P.6
  • 68
    • 38349097639 scopus 로고    scopus 로고
    • Activator-specific requirement of properdin in the initiation and amplification of the alternative pathway complement
    • Kimura Y, Miwa T, Zhou L, Song WC. Activator-specific requirement of properdin in the initiation and amplification of the alternative pathway complement. Blood. 2008;111:732–740.
    • (2008) Blood , vol.111 , pp. 732-740
    • Kimura, Y.1    Miwa, T.2    Zhou, L.3    Song, W.C.4
  • 70
    • 84939262939 scopus 로고    scopus 로고
    • Neutrophil extracellular traps can activate alternative complement pathways
    • Wang H, Wang C, Zhao MH, Chen M. Neutrophil extracellular traps can activate alternative complement pathways. Clin Exp Immunol. 2015;181:518–527.
    • (2015) Clin Exp Immunol , vol.181 , pp. 518-527
    • Wang, H.1    Wang, C.2    Zhao, M.H.3    Chen, M.4
  • 71
    • 77956221152 scopus 로고    scopus 로고
    • An evaluation of the role of properdin in alternative pathway activation on Neisseria meningitidis and Neisseria gonorrhoeae
    • Agarwal S, Ferreira VP, Cortes C, Pangburn MK, Rice PA, Ram S. An evaluation of the role of properdin in alternative pathway activation on Neisseria meningitidis and Neisseria gonorrhoeae. J Immunol. 2010;185:507–516.
    • (2010) J Immunol , vol.185 , pp. 507-516
    • Agarwal, S.1    Ferreira, V.P.2    Cortes, C.3    Pangburn, M.K.4    Rice, P.A.5    Ram, S.6
  • 72
    • 84883693955 scopus 로고    scopus 로고
    • Properdin and factor H: opposing players on the alternative complement pathway “see-saw
    • Kouser L, Abdul-Aziz M, Nayak A, Stover CM, Sim RB, Kishore U. Properdin and factor H: opposing players on the alternative complement pathway “see-saw”. Front Immunol. 2013;4:93.
    • (2013) Front Immunol , vol.4 , pp. 93
    • Kouser, L.1    Abdul-Aziz, M.2    Nayak, A.3    Stover, C.M.4    Sim, R.B.5    Kishore, U.6
  • 73
    • 0028846849 scopus 로고
    • Characterization of mutant forms of recombinant human properdin lacking single thrombospondin type I repeats. Identification of modules important for function
    • Higgins JM, Wiedemann H, Timpl R, Reid KB. Characterization of mutant forms of recombinant human properdin lacking single thrombospondin type I repeats. Identification of modules important for function. J Immunol. 1995;155:5777–5785.
    • (1995) J Immunol , vol.155 , pp. 5777-5785
    • Higgins, J.M.1    Wiedemann, H.2    Timpl, R.3    Reid, K.B.4
  • 74
    • 6344245769 scopus 로고    scopus 로고
    • The dimeric and trimeric solution structures of the multidomain complement protein properdin by X-ray scattering, analytical ultracentrifugation and constrained modelling
    • Sun Z, Reid K, Perkins SJ. The dimeric and trimeric solution structures of the multidomain complement protein properdin by X-ray scattering, analytical ultracentrifugation and constrained modelling. J Mol Biol. 2004;343:1327–1343.
    • (2004) J Mol Biol , vol.343 , pp. 1327-1343
    • Sun, Z.1    Reid, K.2    Perkins, S.J.3
  • 75
    • 84882447182 scopus 로고    scopus 로고
    • Structural basis for the stabilization of the complement alternative pathway C3 convertase by properdin
    • Alcorlo M, Tortajada A, Rodriguez de Cordoba S, Llorca O. Structural basis for the stabilization of the complement alternative pathway C3 convertase by properdin. Proc Natl Acad Sci USA. 2013;110:13504–13509.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 13504-13509
    • Alcorlo, M.1    Tortajada, A.2    Rodriguez de Cordoba, S.3    Llorca, O.4
  • 76
    • 0028260801 scopus 로고
    • Regulation of alternative pathway complement activation by glycosaminoglycans: specificity of the polyanion binding site on factor H
    • Meri S, Pangburn MK. Regulation of alternative pathway complement activation by glycosaminoglycans: specificity of the polyanion binding site on factor H. Biochem Biophys Res Commun. 1994;198:52–59.
    • (1994) Biochem Biophys Res Commun , vol.198 , pp. 52-59
    • Meri, S.1    Pangburn, M.K.2
  • 77
    • 0035933335 scopus 로고    scopus 로고
    • Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling
    • Aslam M, Perkins SJ. Folded-back solution structure of monomeric factor H of human complement by synchrotron X-ray and neutron scattering, analytical ultracentrifugation and constrained molecular modelling. J Mol Biol. 2001;309:1117–1138.
    • (2001) J Mol Biol , vol.309 , pp. 1117-1138
    • Aslam, M.1    Perkins, S.J.2
  • 78
    • 67649230210 scopus 로고    scopus 로고
    • Structure of complement fragment C3b-factor H and implications for host protection by complement regulators
    • Wu J, Wu YQ, Ricklin D, Janssen BJ, Lambris JD, Gros P. Structure of complement fragment C3b-factor H and implications for host protection by complement regulators. Nat Immunol. 2009;10:728–733.
    • (2009) Nat Immunol , vol.10 , pp. 728-733
    • Wu, J.1    Wu, Y.Q.2    Ricklin, D.3    Janssen, B.J.4    Lambris, J.D.5    Gros, P.6
  • 79
    • 79953772478 scopus 로고    scopus 로고
    • Structural basis for engagement by complement factor H of C3b on a self surface
    • Morgan HP, Schmidt CQ, Guariento M, et al. Structural basis for engagement by complement factor H of C3b on a self surface. Nat Struct Mol Biol. 2011;18:463–470.
    • (2011) Nat Struct Mol Biol , vol.18 , pp. 463-470
    • Morgan, H.P.1    Schmidt, C.Q.2    Guariento, M.3
  • 80
    • 79952612300 scopus 로고    scopus 로고
    • Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement
    • Kajander T, Lehtinen MJ, Hyvarinen S, et al. Dual interaction of factor H with C3d and glycosaminoglycans in host-nonhost discrimination by complement. Proc Natl Acad Sci USA. 2011;108:2897–2902.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 2897-2902
    • Kajander, T.1    Lehtinen, M.J.2    Hyvarinen, S.3
  • 81
    • 53149104792 scopus 로고    scopus 로고
    • A new map of glycosaminoglycan and C3b binding sites on factor H
    • Schmidt CQ, Herbert AP, Kavanagh D, et al. A new map of glycosaminoglycan and C3b binding sites on factor H. J Immunol. 2008;181:2610–2619.
    • (2008) J Immunol , vol.181 , pp. 2610-2619
    • Schmidt, C.Q.1    Herbert, A.P.2    Kavanagh, D.3
  • 82
    • 0030589294 scopus 로고    scopus 로고
    • Identification of a heparin binding domain in the seventh short consensus repeat of complement factor H
    • Blackmore TK, Sadlon TA, Ward HM, Lublin DM, Gordon DL. Identification of a heparin binding domain in the seventh short consensus repeat of complement factor H. J Immunol. 1996;157:5422–5427.
    • (1996) J Immunol , vol.157 , pp. 5422-5427
    • Blackmore, T.K.1    Sadlon, T.A.2    Ward, H.M.3    Lublin, D.M.4    Gordon, D.L.5
  • 83
    • 33644555185 scopus 로고    scopus 로고
    • Localization of the third heparin-binding site in the human complement regulator factor H 1
    • Ormsby RJ, Jokiranta TS, Duthy TG, et al. Localization of the third heparin-binding site in the human complement regulator factor H 1. Mol Immunol. 2006;43:1624–1632.
    • (2006) Mol Immunol , vol.43 , pp. 1624-1632
    • Ormsby, R.J.1    Jokiranta, T.S.2    Duthy, T.G.3
  • 84
    • 79961235437 scopus 로고    scopus 로고
    • Structural basis for complement factor I control and its disease-associated sequence polymorphisms
    • Roversi P, Johnson S, Caesar JJ, et al. Structural basis for complement factor I control and its disease-associated sequence polymorphisms. Proc Natl Acad Sci USA. 2011;108:12839–12844.
    • (2011) Proc Natl Acad Sci USA , vol.108 , pp. 12839-12844
    • Roversi, P.1    Johnson, S.2    Caesar, J.J.3
  • 85
    • 84961792791 scopus 로고    scopus 로고
    • Regulators of complement activity mediate inhibitory mechanisms through a common C3b-binding mode
    • Forneris F, Wu J, Xue X, et al. Regulators of complement activity mediate inhibitory mechanisms through a common C3b-binding mode. EMBO J. 2016;35:1133–1149.
    • (2016) EMBO J , vol.35 , pp. 1133-1149
    • Forneris, F.1    Wu, J.2    Xue, X.3
  • 86
    • 39749127834 scopus 로고    scopus 로고
    • Receptors for complement C5a. The importance of C5aR and the enigmatic role of C5L2
    • Lee H, Whitfeld PL, Mackay CR. Receptors for complement C5a. The importance of C5aR and the enigmatic role of C5L2. Immunol Cell Biol. 2008;86:153–160.
    • (2008) Immunol Cell Biol , vol.86 , pp. 153-160
    • Lee, H.1    Whitfeld, P.L.2    Mackay, C.R.3
  • 87
    • 0034141908 scopus 로고    scopus 로고
    • Functional role of the noncatalytic subunit of complement C5 convertase
    • Rawal N, Pangburn MK. Functional role of the noncatalytic subunit of complement C5 convertase. J Immunol. 2000;164:1379–1385.
    • (2000) J Immunol , vol.164 , pp. 1379-1385
    • Rawal, N.1    Pangburn, M.K.2
  • 88
    • 0032479161 scopus 로고    scopus 로고
    • C5 convertase of the alternative pathway of complement. Kinetic analysis of the free and surface-bound forms of the enzyme
    • Rawal N, Pangburn MK. C5 convertase of the alternative pathway of complement. Kinetic analysis of the free and surface-bound forms of the enzyme. J Biol Chem. 1998;273:16828–16835.
    • (1998) J Biol Chem , vol.273 , pp. 16828-16835
    • Rawal, N.1    Pangburn, M.K.2
  • 89
    • 0141643292 scopus 로고    scopus 로고
    • Formation of high affinity C5 convertase of the classical pathway of complement
    • Rawal N, Pangburn MK. Formation of high affinity C5 convertase of the classical pathway of complement. J Biol Chem. 2003;278:38476–38483.
    • (2003) J Biol Chem , vol.278 , pp. 38476-38483
    • Rawal, N.1    Pangburn, M.K.2
  • 90
    • 0017254518 scopus 로고
    • Cobra venom factor: evidence for its being altered cobra C3 (the third component of complement)
    • Alper CA, Balavitch D. Cobra venom factor: evidence for its being altered cobra C3 (the third component of complement). Science. 1976;191:1275–1276.
    • (1976) Science , vol.191 , pp. 1275-1276
    • Alper, C.A.1    Balavitch, D.2
  • 91
    • 77957916119 scopus 로고    scopus 로고
    • Cobra venom factor: structure, function, and humanization for therapeutic complement depletion
    • Vogel CW, Fritzinger DC. Cobra venom factor: structure, function, and humanization for therapeutic complement depletion. Toxicon. 2010;56:1198–1222.
    • (2010) Toxicon , vol.56 , pp. 1198-1222
    • Vogel, C.W.1    Fritzinger, D.C.2
  • 94
    • 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. Crystal structure of C5b-6 suggests structural basis for priming assembly of the membrane attack complex. J Biol Chem. 2012;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
  • 95
    • 84861163710 scopus 로고    scopus 로고
    • Assembly and regulation of the membrane attack complex based on structures of C5b6 and sC5b9
    • Hadders MA, Bubeck D, Roversi P, et al. Assembly and regulation of the membrane attack complex based on structures of C5b6 and sC5b9. Cell Rep. 2012;1:200–207.
    • (2012) Cell Rep , vol.1 , pp. 200-207
    • Hadders, M.A.1    Bubeck, D.2    Roversi, P.3
  • 96
    • 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. Structure of complement C6 suggests a mechanism for initiation and unidirectional, sequential assembly of membrane attack complex (MAC). J Biol Chem. 2012;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
  • 97
    • 0017700990 scopus 로고
    • Enhancement of C56-initiated lysis by cell-bound C3 fragments: evidence for a mechanism independent of the prior binding of C56 to C3b
    • Yamamoto KI, Lint TF, Gewurz H. Enhancement of C56-initiated lysis by cell-bound C3 fragments: evidence for a mechanism independent of the prior binding of C56 to C3b. J Immunol. 1977;119:1346–1350.
    • (1977) J Immunol , vol.119 , pp. 1346-1350
    • Yamamoto, K.I.1    Lint, T.F.2    Gewurz, H.3
  • 98
    • 0017188554 scopus 로고
    • A new activity of complement component C3: cell-bound C3b potentiates lysis of erythrocytes by C5b,6 and terminal components
    • Hammer CH, Abramovitz AS, Mayer MM. A new activity of complement component C3: cell-bound C3b potentiates lysis of erythrocytes by C5b,6 and terminal components. J Immunol. 1976;117:830–834.
    • (1976) J Immunol , vol.117 , pp. 830-834
    • Hammer, C.H.1    Abramovitz, A.S.2    Mayer, M.M.3
  • 99
    • 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, Muller-Eberhard HJ. The membrane attack complex of complement: relation of C7 to the metastable membrane binding site of the intermediate complex C5b-7. J Immunol. 1985;135:445–451.
    • (1985) J Immunol , vol.135 , pp. 445-451
    • Preissner, K.T.1    Podack, E.R.2    Muller-Eberhard, H.J.3
  • 100
    • 0019861225 scopus 로고
    • Role of the beta subunit in interaction of the eighth component of human complement with the membrane-bound cytolytic complex
    • Monahan JB, Sodetz JM. Role of the beta subunit in interaction of the eighth component of human complement with the membrane-bound cytolytic complex. J Biol Chem. 1981;256:3258–3262.
    • (1981) J Biol Chem , vol.256 , pp. 3258-3262
    • Monahan, J.B.1    Sodetz, J.M.2
  • 101
    • 0014900566 scopus 로고
    • Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase
    • Bokisch VA, Muller-Eberhard HJ. Anaphylatoxin inactivator of human plasma: its isolation and characterization as a carboxypeptidase. J Clin Invest. 1970;49:2427–2436.
    • (1970) J Clin Invest , vol.49 , pp. 2427-2436
    • Bokisch, V.A.1    Muller-Eberhard, H.J.2
  • 103
    • 0019500177 scopus 로고
    • Response of human neutrophils to C5a: a role for the oligosaccharide moiety of human C5ades Arg-74 but not of C5a in biologic activity
    • Gerard C, Chenoweth DE, Hugli TE. Response of human neutrophils to C5a: a role for the oligosaccharide moiety of human C5ades Arg-74 but not of C5a in biologic activity. J Immunol. 1981;127:1978–1982.
    • (1981) J Immunol , vol.127 , pp. 1978-1982
    • Gerard, C.1    Chenoweth, D.E.2    Hugli, T.E.3
  • 104
    • 0024493978 scopus 로고
    • Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance data
    • Zuiderweg ER, Nettesheim DG, Mollison KW, Carter GW. Tertiary structure of human complement component C5a in solution from nuclear magnetic resonance data. Biochemistry. 1989;28:172–185.
    • (1989) Biochemistry , vol.28 , pp. 172-185
    • Zuiderweg, E.R.1    Nettesheim, D.G.2    Mollison, K.W.3    Carter, G.W.4
  • 105
    • 45549085597 scopus 로고    scopus 로고
    • Structure of and influence of a tick complement inhibitor on human complement component 5
    • Fredslund F, Laursen NS, Roversi P, et al. Structure of and influence of a tick complement inhibitor on human complement component 5. Nat Immunol. 2008;9:753–760.
    • (2008) Nat Immunol , vol.9 , pp. 753-760
    • Fredslund, F.1    Laursen, N.S.2    Roversi, P.3
  • 106
    • 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. Structural definition of the C5a C terminus by two-dimensional nuclear magnetic resonance spectroscopy. Proteins. 1997;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
  • 107
    • 84885333791 scopus 로고    scopus 로고
    • Structural insight on the recognition of surface-bound opsonins by the integrin I domain of complement receptor 3
    • Bajic G, Yatime L, Sim RB, Vorup-Jensen T, Andersen GR. Structural insight on the recognition of surface-bound opsonins by the integrin I domain of complement receptor 3. Proc Natl Acad Sci USA. 2013;110:16426–16431.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 16426-16431
    • Bajic, G.1    Yatime, L.2    Sim, R.B.3    Vorup-Jensen, T.4    Andersen, G.R.5
  • 108
    • 84875939215 scopus 로고    scopus 로고
    • Efficient chemical synthesis of human complement protein C3a
    • Ghassemian A, Wang CI, Yau MK, et al. Efficient chemical synthesis of human complement protein C3a. Chem Commun (Camb). 2013;49:2356–2358.
    • (2013) Chem Commun (Camb) , vol.49 , pp. 2356-2358
    • Ghassemian, A.1    Wang, C.I.2    Yau, M.K.3
  • 111
    • 84961761065 scopus 로고    scopus 로고
    • Structural basis for therapeutic inhibition of complement C5
    • Jore MM, Johnson S, Sheppard D, et al. Structural basis for therapeutic inhibition of complement C5. Nat Struct Mol Biol. 2016;23:378–386.
    • (2016) Nat Struct Mol Biol , vol.23 , pp. 378-386
    • Jore, M.M.1    Johnson, S.2    Sheppard, D.3
  • 112
    • 84928780593 scopus 로고    scopus 로고
    • Structural basis for the targeting of complement anaphylatoxin C5a using a mixed L-RNA/L-DNA aptamer
    • Yatime L, Maasch C, Hoehlig K, Klussmann S, Andersen GR, Vater A. Structural basis for the targeting of complement anaphylatoxin C5a using a mixed L-RNA/L-DNA aptamer. Nat Commun. 2015;6:6481.
    • (2015) Nat Commun , vol.6 , pp. 6481
    • Yatime, L.1    Maasch, C.2    Hoehlig, K.3    Klussmann, S.4    Andersen, G.R.5    Vater, A.6
  • 113
    • 0027310539 scopus 로고
    • Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria
    • Takeda J, Miyata T, Kawagoe K, et al. Deficiency of the GPI anchor caused by a somatic mutation of the PIG-A gene in paroxysmal nocturnal hemoglobinuria. Cell. 1993;73:703–711.
    • (1993) Cell , vol.73 , pp. 703-711
    • Takeda, J.1    Miyata, T.2    Kawagoe, K.3
  • 114
    • 0027412627 scopus 로고
    • The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis
    • Miyata T, Takeda J, Iida Y, et al. The cloning of PIG-A, a component in the early step of GPI-anchor biosynthesis. Science. 1993;259:1318–1320.
    • (1993) Science , vol.259 , pp. 1318-1320
    • Miyata, T.1    Takeda, J.2    Iida, Y.3
  • 115
    • 84908565749 scopus 로고    scopus 로고
    • Paroxysmal nocturnal hemoglobinuria
    • Brodsky RA. Paroxysmal nocturnal hemoglobinuria. Blood. 2014;124:2804–2811.
    • (2014) Blood , vol.124 , pp. 2804-2811
    • Brodsky, R.A.1
  • 116
    • 84948808911 scopus 로고    scopus 로고
    • Complement in hemolytic anemia
    • Brodsky RA. Complement in hemolytic anemia. Blood. 2015;126:2459–2465.
    • (2015) Blood , vol.126 , pp. 2459-2465
    • Brodsky, R.A.1
  • 118
    • 70350279315 scopus 로고    scopus 로고
    • Atypical Hemolytic-Uremic Syndrome
    • Noris M, Remuzzi G. Atypical Hemolytic-Uremic Syndrome. N Engl J Med. 2009;361:1676–1687.
    • (2009) N Engl J Med , vol.361 , pp. 1676-1687
    • Noris, M.1    Remuzzi, G.2
  • 119
    • 84893799889 scopus 로고    scopus 로고
    • Genetic variants in C5 and poor response to eculizumab
    • Nishimura J, Yamamoto M, Hayashi S, et al. Genetic variants in C5 and poor response to eculizumab. N Engl J Med. 2014;370:632–639.
    • (2014) N Engl J Med , vol.370 , pp. 632-639
    • Nishimura, J.1    Yamamoto, M.2    Hayashi, S.3
  • 120
    • 34248165965 scopus 로고    scopus 로고
    • The structure of OMCI, a novel lipocalin inhibitor of the complement system
    • Roversi P, Lissina O, Johnson S, et al. The structure of OMCI, a novel lipocalin inhibitor of the complement system. J Mol Biol. 2007;369:784–793.
    • (2007) J Mol Biol , vol.369 , pp. 784-793
    • Roversi, P.1    Lissina, O.2    Johnson, S.3
  • 121
    • 34247263765 scopus 로고    scopus 로고
    • In vivo characterization and therapeutic efficacy of a C5-specific inhibitor from the soft tick Ornithodoros moubata
    • Hepburn NJ, Williams AS, Nunn MA, et al. In vivo characterization and therapeutic efficacy of a C5-specific inhibitor from the soft tick Ornithodoros moubata. J Biol Chem. 2007;282:8292–8299.
    • (2007) J Biol Chem , vol.282 , pp. 8292-8299
    • Hepburn, N.J.1    Williams, A.S.2    Nunn, M.A.3
  • 122
    • 34948844450 scopus 로고    scopus 로고
    • Staphylococcal complement evasion by various convertase-blocking molecules
    • Jongerius I, Kohl J, Pandey MK, et al. Staphylococcal complement evasion by various convertase-blocking molecules. J Exp Med. 2007;204:2461–2471.
    • (2007) J Exp Med , vol.204 , pp. 2461-2471
    • Jongerius, I.1    Kohl, J.2    Pandey, M.K.3
  • 124
    • 77649257894 scopus 로고    scopus 로고
    • Structural basis for inhibition of complement C5 by the SSL7 protein from Staphylococcus aureus
    • Laursen NS, Gordon N, Hermans S, Lorenz N, Jackson N, Wines B. Structural basis for inhibition of complement C5 by the SSL7 protein from Staphylococcus aureus. Proc Natl Acad Sci USA. 2010;107:3681–3686.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 3681-3686
    • Laursen, N.S.1    Gordon, N.2    Hermans, S.3    Lorenz, N.4    Jackson, N.5    Wines, B.6
  • 125
    • 14044268137 scopus 로고    scopus 로고
    • The staphylococcal superantigen-like protein 7 binds IgA and complement C5 and inhibits IgA-Fc alpha RI binding and serum killing of bacteria
    • Langley R, Wines B, Willoughby N, Basu I, Proft T, Fraser JD. The staphylococcal superantigen-like protein 7 binds IgA and complement C5 and inhibits IgA-Fc alpha RI binding and serum killing of bacteria. J Immunol. 2005;174:2926–2933.
    • (2005) J Immunol , vol.174 , pp. 2926-2933
    • Langley, R.1    Wines, B.2    Willoughby, N.3    Basu, I.4    Proft, T.5    Fraser, J.D.6
  • 126
    • 84948716605 scopus 로고    scopus 로고
    • Complement, a target for therapy in inflammatory and degenerative diseases
    • Morgan BP, Harris CL. Complement, a target for therapy in inflammatory and degenerative diseases. Nat Rev Drug Discov. 2015;14:857–877.
    • (2015) Nat Rev Drug Discov , vol.14 , pp. 857-877
    • Morgan, B.P.1    Harris, C.L.2
  • 127
    • 0017874834 scopus 로고
    • A new function of the activated third component of complement: binding to C5, an essential step for C5 activation
    • Vogt W, Schmidt G, Buttlar B, Dieminger L. A new function of the activated third component of complement: binding to C5, an essential step for C5 activation. Immunology. 1978;34:29–40.
    • (1978) Immunology , vol.34 , pp. 29-40
    • Vogt, W.1    Schmidt, G.2    Buttlar, B.3    Dieminger, L.4
  • 128
    • 84946551191 scopus 로고    scopus 로고
    • Molecular insights into the surface-specific arrangement of complement C5 convertase enzymes
    • Berends ET, Gorham RD Jr, Ruyken M, et al. Molecular insights into the surface-specific arrangement of complement C5 convertase enzymes. BMC Biol. 2015;13:93.
    • (2015) BMC Biol , vol.13 , pp. 93
    • Berends, E.T.1    Gorham, R.D.2    Ruyken, M.3
  • 129
    • 0023195099 scopus 로고
    • Covalent association of C3b with C4b within C5 convertase of the classical complement pathway
    • Takata Y, Kinoshita T, Kozono H, et al. Covalent association of C3b with C4b within C5 convertase of the classical complement pathway. J Exp Med. 1987;165:1494–1507.
    • (1987) J Exp Med , vol.165 , pp. 1494-1507
    • Takata, Y.1    Kinoshita, T.2    Kozono, H.3
  • 130
    • 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
    • Kim YU, Carroll MC, Isenman DE, 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    Carroll, M.C.2    Isenman, D.E.3
  • 131
    • 0025897023 scopus 로고
    • Reconstitution of C5 convertase of the alternative complement pathway with isolated C3b dimer and factors B and D
    • Hong K, Kinoshita T, Pramoonjago P, Kim YU, Seya T, Inoue K. Reconstitution of C5 convertase of the alternative complement pathway with isolated C3b dimer and factors B and D. J Immunol. 1991;146:1868–1873.
    • (1991) J Immunol , vol.146 , pp. 1868-1873
    • Hong, K.1    Kinoshita, T.2    Pramoonjago, P.3    Kim, Y.U.4    Seya, T.5    Inoue, K.6
  • 132
    • 0024159572 scopus 로고
    • C5 convertase of the alternative complement pathway: covalent linkage between two C3b molecules within the trimolecular complex enzyme
    • Kinoshita T, Takata Y, Kozono H, Takeda J, Hong KS, 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.S.5    Inoue, K.6
  • 133
    • 84929625665 scopus 로고    scopus 로고
    • Structural basis for the function of complement component C4 within the classical and lectin pathways of complement
    • Mortensen S, Kidmose RT, Petersen SV, Szilagyi A, Prohaszka Z, Andersen GR. Structural basis for the function of complement component C4 within the classical and lectin pathways of complement. J Immunol. 2015;194:5488–5496.
    • (2015) J Immunol , vol.194 , pp. 5488-5496
    • Mortensen, S.1    Kidmose, R.T.2    Petersen, S.V.3    Szilagyi, A.4    Prohaszka, Z.5    Andersen, G.R.6
  • 134
    • 84878103661 scopus 로고    scopus 로고
    • Rational engineering of a minimized immune inhibitor with unique triple-targeting properties
    • Schmidt CQ, Bai H, Lin Z, et al. Rational engineering of a minimized immune inhibitor with unique triple-targeting properties. J Immunol. 2013;190:5712–5721.
    • (2013) J Immunol , vol.190 , pp. 5712-5721
    • Schmidt, C.Q.1    Bai, H.2    Lin, Z.3
  • 135
    • 84876819390 scopus 로고    scopus 로고
    • International Union of Basic and Clinical Pharmacology. [corrected]. LXXXVII. Complement peptide C5a, C4a, and C3a receptors
    • Klos A, Wende E, Wareham KJ, Monk PN. International Union of Basic and Clinical Pharmacology. [corrected]. LXXXVII. Complement peptide C5a, C4a, and C3a receptors. Pharmacol Rev. 2013;65:500–543.
    • (2013) Pharmacol Rev , vol.65 , pp. 500-543
    • Klos, A.1    Wende, E.2    Wareham, K.J.3    Monk, P.N.4
  • 136
    • 84872221774 scopus 로고    scopus 로고
    • Structure-function of the G protein-coupled receptor superfamily
    • Katritch V, Cherezov V, Stevens RC. Structure-function of the G protein-coupled receptor superfamily. Annu Rev Pharmacol Toxicol. 2013;53:531–556.
    • (2013) Annu Rev Pharmacol Toxicol , vol.53 , pp. 531-556
    • Katritch, V.1    Cherezov, V.2    Stevens, R.C.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.