메뉴 건너뛰기




Volumn 35, Issue 10, 2016, Pages 1133-1149

Regulators of complement activity mediate inhibitory mechanisms through a common C3b-binding mode

Author keywords

cofactor activity; complement; decay accelerating activity; immune evasion; regulators of complement activity

Indexed keywords

COMPLEMENT COMPONENT C3B; COMPLEMENT COMPONENT C3B RECEPTOR; DECAY ACCELERATING FACTOR; MEMBRANE COFACTOR PROTEIN; REGULATOR PROTEIN; SMALLPOX INHIBITOR OF COMPLEMENT ENZYME; UNCLASSIFIED DRUG; VACCINIA VIRUS COMPLEMENT CONTROL PROTEIN; VIRUS ENZYME; CD46 PROTEIN, HUMAN; CR1 PROTEIN, HUMAN; MATRIX PROTEIN; SPICE PROTEIN, VARIOLA VIRUS;

EID: 84961792791     PISSN: 02614189     EISSN: 14602075     Source Type: Journal    
DOI: 10.15252/embj.201593673     Document Type: Article
Times cited : (88)

References (109)
  • 1
    • 0026077255 scopus 로고
    • Contribution of the repeating domains of membrane cofactor protein (CD46) of the complement system to ligand binding and cofactor activity
    • Adams EM, Brown MC, Nunge M, Krych M, Atkinson JP, (1991) Contribution of the repeating domains of membrane cofactor protein (CD46) of the complement system to ligand binding and cofactor activity. J Immunol 147: 3005-3011
    • (1991) J Immunol , vol.147 , pp. 3005-3011
    • Adams, E.M.1    Brown, M.C.2    Nunge, M.3    Krych, M.4    Atkinson, J.P.5
  • 3
  • 4
    • 78650056746 scopus 로고    scopus 로고
    • Domain swapping reveals complement control protein modules critical for imparting cofactor and decay-accelerating activities in vaccinia virus complement control protein
    • Ahmad M, Raut S, Pyaram K, Kamble A, Mullick J, Sahu A, (2010) Domain swapping reveals complement control protein modules critical for imparting cofactor and decay-accelerating activities in vaccinia virus complement control protein. J Immunol 185: 6128-6137
    • (2010) J Immunol , vol.185 , pp. 6128-6137
    • Ahmad, M.1    Raut, S.2    Pyaram, K.3    Kamble, A.4    Mullick, J.5    Sahu, A.6
  • 5
    • 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
  • 8
    • 0037392907 scopus 로고    scopus 로고
    • A CR1 polymorphism associated with constitutive erythrocyte CR1 levels affects binding to C4b but not C3b
    • Birmingham DJ, Chen W, Liang G, Schmitt HC, Gavit K, Nagaraja HN, (2003) A CR1 polymorphism associated with constitutive erythrocyte CR1 levels affects binding to C4b but not C3b. Immunology 108: 531-538
    • (2003) Immunology , vol.108 , pp. 531-538
    • Birmingham, D.J.1    Chen, W.2    Liang, G.3    Schmitt, H.C.4    Gavit, K.5    Nagaraja, H.N.6
  • 12
    • 23644447072 scopus 로고    scopus 로고
    • Evolutionary history of orthopoxvirus proteins similar to human complement regulators
    • Ciulla E, Emery A, Konz D, Krushkal J, (2005) Evolutionary history of orthopoxvirus proteins similar to human complement regulators. Gene 355: 40-47
    • (2005) Gene , vol.355 , pp. 40-47
    • Ciulla, E.1    Emery, A.2    Konz, D.3    Krushkal, J.4
  • 14
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • Collaborative Computational Project, Number 4.
    • Collaborative Computational Project, Number 4 (1994) The CCP4 suite: programs for protein crystallography. Acta Crystallogr D Biol Crystallogr 50: 760-763
    • (1994) Acta Crystallogr D Biol Crystallogr , vol.50 , pp. 760-763
  • 15
    • 77957562699 scopus 로고    scopus 로고
    • Anti-factor H autoantibody-associated hemolytic uremic syndrome: Review of literature of the autoimmune form of HUS
    • Dragon-Durey MA, Blanc C, Garnier A, Hofer J, Sethi SK, Zimmerhackl LB, (2010) Anti-factor H autoantibody-associated hemolytic uremic syndrome: review of literature of the autoimmune form of HUS. Semin Thromb Hemost 36: 633-640
    • (2010) Semin Thromb Hemost , vol.36 , pp. 633-640
    • Dragon-Durey, M.A.1    Blanc, C.2    Garnier, A.3    Hofer, J.4    Sethi, S.K.5    Zimmerhackl, L.B.6
  • 16
    • 27844566613 scopus 로고    scopus 로고
    • Atypical haemolytic uraemic syndrome and mutations in complement regulator genes
    • Dragon-Durey MA, Fremeaux-Bacchi V, (2005) Atypical haemolytic uraemic syndrome and mutations in complement regulator genes. Springer Semin Immunopathol 27: 359-374
    • (2005) Springer Semin Immunopathol , vol.27 , pp. 359-374
    • Dragon-Durey, M.A.1    Fremeaux-Bacchi, V.2
  • 18
    • 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, Tzekou A, Wallace RS, Lambris JD, Gros P, (2010) Structures of C3b in complex with factors B and D give insight into complement convertase formation. Science 330: 1816-1820
    • (2010) Science , vol.330 , pp. 1816-1820
    • Forneris, F.1    Ricklin, D.2    Wu, J.3    Tzekou, A.4    Wallace, R.S.5    Lambris, J.D.6    Gros, P.7
  • 19
    • 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
  • 24
    • 36348990790 scopus 로고    scopus 로고
    • The partly folded back solution structure arrangement of the 30 SCR domains in human complement receptor type 1 (CR1) permits access to its C3b and C4b ligands
    • Furtado PB, Huang CY, Ihyembe D, Hammond RA, Marsh HC, Perkins SJ, (2008) The partly folded back solution structure arrangement of the 30 SCR domains in human complement receptor type 1 (CR1) permits access to its C3b and C4b ligands. J Mol Biol 375: 102-118
    • (2008) J Mol Biol , vol.375 , pp. 102-118
    • Furtado, P.B.1    Huang, C.Y.2    Ihyembe, D.3    Hammond, R.A.4    Marsh, H.C.5    Perkins, S.J.6
  • 25
    • 77956180132 scopus 로고    scopus 로고
    • Molecular Basis for Complement Recognition and Inhibition Determined by Crystallographic Studies of the Staphylococcal Complement Inhibitor (SCIN) Bound to C3c and C3b
    • Garcia BL, Ramyar KX, Tzekou A, Ricklin D, McWhorter WJ, Lambris JD, Geisbrecht BV, (2010) Molecular Basis for Complement Recognition and Inhibition Determined by Crystallographic Studies of the Staphylococcal Complement Inhibitor (SCIN) Bound to C3c and C3b. J Mol Biol 402: 17-29
    • (2010) J Mol Biol , vol.402 , pp. 17-29
    • Garcia, B.L.1    Ramyar, K.X.2    Tzekou, A.3    Ricklin, D.4    McWhorter, W.J.5    Lambris, J.D.6    Geisbrecht, B.V.7
  • 26
    • 84944188105 scopus 로고    scopus 로고
    • Mutational analysis of Kaposica reveals that bridging of MG2 and CUB domains of target protein is crucial for the cofactor activity of RCA proteins
    • Gautam AK, Panse Y, Ghosh P, Reza MJ, Mullick J, Sahu A, (2015) Mutational analysis of Kaposica reveals that bridging of MG2 and CUB domains of target protein is crucial for the cofactor activity of RCA proteins. Proc Natl Acad Sci USA 112: 12794-12799
    • (2015) Proc Natl Acad Sci USA , vol.112 , pp. 12794-12799
    • Gautam, A.K.1    Panse, Y.2    Ghosh, P.3    Reza, M.J.4    Mullick, J.5    Sahu, A.6
  • 28
    • 80052783174 scopus 로고    scopus 로고
    • Beta(2)-glycoprotein I, the major target in antiphospholipid syndrome, is a special human complement regulator
    • Gropp K, Weber N, Reuter M, Micklisch S, Kopka I, Hallstrom T, Skerka C, (2011) beta(2)-glycoprotein I, the major target in antiphospholipid syndrome, is a special human complement regulator. Blood 118: 2774-2783
    • (2011) Blood , vol.118 , pp. 2774-2783
    • Gropp, K.1    Weber, N.2    Reuter, M.3    Micklisch, S.4    Kopka, I.5    Hallstrom, T.6    Skerka, C.7
  • 30
    • 13244291613 scopus 로고    scopus 로고
    • Molecular dissection of interactions between components of the alternative pathway of complement and decay accelerating factor (CD55)
    • Harris CL, Abbott RJ, Smith RA, Morgan BP, Lea SM, (2005) Molecular dissection of interactions between components of the alternative pathway of complement and decay accelerating factor (CD55). J Biol Chem 280: 2569-2578
    • (2005) J Biol Chem , vol.280 , pp. 2569-2578
    • Harris, C.L.1    Abbott, R.J.2    Smith, R.A.3    Morgan, B.P.4    Lea, S.M.5
  • 31
    • 33846024034 scopus 로고    scopus 로고
    • Decay-accelerating factor must bind both components of the complement alternative pathway C3 convertase to mediate efficient decay
    • Harris CL, Pettigrew DM, Lea SM, Morgan BP, (2007) Decay-accelerating factor must bind both components of the complement alternative pathway C3 convertase to mediate efficient decay. J Immunol 178: 352-359
    • (2007) J Immunol , vol.178 , pp. 352-359
    • Harris, C.L.1    Pettigrew, D.M.2    Lea, S.M.3    Morgan, B.P.4
  • 34
    • 0032997017 scopus 로고    scopus 로고
    • Decay acceleration of the complement alternative pathway C3 convertase
    • Hourcade DE, Mitchell LM, Medof ME, (1999) Decay acceleration of the complement alternative pathway C3 convertase. Immunopharmacology 42: 167-173
    • (1999) Immunopharmacology , vol.42 , pp. 167-173
    • Hourcade, D.E.1    Mitchell, L.M.2    Medof, M.E.3
  • 35
    • 33750859976 scopus 로고    scopus 로고
    • Structure of C3b reveals conformational changes that underlie complement activity
    • Janssen BJ, Christodoulidou A, McCarthy A, Lambris JD, Gros P, (2006) Structure of C3b reveals conformational changes that underlie complement activity. Nature 444: 213-216
    • (2006) Nature , vol.444 , pp. 213-216
    • Janssen, B.J.1    Christodoulidou, A.2    McCarthy, A.3    Lambris, J.D.4    Gros, P.5
  • 38
    • 0034623118 scopus 로고    scopus 로고
    • Each of the three binding sites on complement factor H interacts with a distinct site on C3b
    • Jokiranta TS, Hellwage J, Koistinen V, Zipfel PF, Meri S, (2000) Each of the three binding sites on complement factor H interacts with a distinct site on C3b. J Biol Chem 275: 27657-27662
    • (2000) J Biol Chem , vol.275 , pp. 27657-27662
    • Jokiranta, T.S.1    Hellwage, J.2    Koistinen, V.3    Zipfel, P.F.4    Meri, S.5
  • 41
    • 84861425552 scopus 로고    scopus 로고
    • Linking crystallographic model and data quality
    • Karplus PA, Diederichs K, (2012) Linking crystallographic model and data quality. Science 336: 1030-1033
    • (2012) Science , vol.336 , pp. 1030-1033
    • Karplus, P.A.1    Diederichs, K.2
  • 44
    • 0035008505 scopus 로고    scopus 로고
    • Structure and flexibility of the multiple domain proteins that regulate complement activation
    • Kirkitadze MD, Barlow PN, (2001) Structure and flexibility of the multiple domain proteins that regulate complement activation. Immunol Rev 180: 146-161
    • (2001) Immunol Rev , vol.180 , pp. 146-161
    • Kirkitadze, M.D.1    Barlow, P.N.2
  • 46
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel E, Henrick K, (2007) Inference of macromolecular assemblies from crystalline state. J Mol Biol 372: 774-797
    • (2007) J Mol Biol , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 47
    • 0028241363 scopus 로고
    • Analysis of the functional domains of complement receptor type 1 (C3b/C4b receptor; CD35) by substitution mutagenesis
    • Krych M, Clemenza L, Howdeshell D, Hauhart R, Hourcade D, Atkinson JP, (1994) Analysis of the functional domains of complement receptor type 1 (C3b/C4b receptor; CD35) by substitution mutagenesis. J Biol Chem 269: 13273-13278
    • (1994) J Biol Chem , vol.269 , pp. 13273-13278
    • Krych, M.1    Clemenza, L.2    Howdeshell, D.3    Hauhart, R.4    Hourcade, D.5    Atkinson, J.P.6
  • 48
    • 0032502792 scopus 로고    scopus 로고
    • Structure-function analysis of the active sites of complement receptor type 1
    • Krych M, Hauhart R, Atkinson JP, (1998) Structure-function analysis of the active sites of complement receptor type 1. J Biol Chem 273: 8623-8629
    • (1998) J Biol Chem , vol.273 , pp. 8623-8629
    • Krych, M.1    Hauhart, R.2    Atkinson, J.P.3
  • 49
    • 0025761266 scopus 로고
    • Sites within the complement C3b/C4b receptor important for the specificity of ligand binding
    • Krych M, Hourcade D, Atkinson JP, (1991) Sites within the complement C3b/C4b receptor important for the specificity of ligand binding. Proc Natl Acad Sci USA 88: 4353-4357
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 4353-4357
    • Krych, M.1    Hourcade, D.2    Atkinson, J.P.3
  • 50
    • 25444520753 scopus 로고    scopus 로고
    • Synergy between two active sites of human complement receptor type 1 (CD35) in complement regulation: Implications for the structure of the classical pathway C3 convertase and generation of more potent inhibitors
    • Krych-Goldberg M, Hauhart RE, Porzukowiak T, Atkinson JP, (2005) Synergy between two active sites of human complement receptor type 1 (CD35) in complement regulation: implications for the structure of the classical pathway C3 convertase and generation of more potent inhibitors. J Immunol 175: 4528-4535
    • (2005) J Immunol , vol.175 , pp. 4528-4535
    • Krych-Goldberg, M.1    Hauhart, R.E.2    Porzukowiak, T.3    Atkinson, J.P.4
  • 53
    • 0346101755 scopus 로고    scopus 로고
    • A corresponding tyrosine residue in the C2/factor B type A domain is a hot spot in the decay acceleration of the complement C3 convertases
    • Kuttner-Kondo LA, Dybvig MP, Mitchell LM, Muqim N, Atkinson JP, Medof ME, Hourcade DE, (2003) A corresponding tyrosine residue in the C2/factor B type A domain is a hot spot in the decay acceleration of the complement C3 convertases. J Biol Chem 278: 52386-52391
    • (2003) J Biol Chem , vol.278 , pp. 52386-52391
    • Kuttner-Kondo, L.A.1    Dybvig, M.P.2    Mitchell, L.M.3    Muqim, N.4    Atkinson, J.P.5    Medof, M.E.6    Hourcade, D.E.7
  • 54
    • 0035881260 scopus 로고    scopus 로고
    • Characterization of the active sites in decay-accelerating factor
    • Kuttner-Kondo LA, Mitchell L, Hourcade DE, Medof ME, (2001) Characterization of the active sites in decay-accelerating factor. J Immunol 167: 2164-2171
    • (2001) J Immunol , vol.167 , pp. 2164-2171
    • Kuttner-Kondo, L.A.1    Mitchell, L.2    Hourcade, D.E.3    Medof, M.E.4
  • 55
    • 0030004710 scopus 로고    scopus 로고
    • Dissection of CR1, factor H, membrane cofactor protein, and factor B binding and functional sites in the third complement component
    • Lambris JD, Lao Z, Oglesby TJ, Atkinson JP, Hack CE, Becherer JD, (1996) Dissection of CR1, factor H, membrane cofactor protein, and factor B binding and functional sites in the third complement component. J Immunol 156: 4821-4832
    • (1996) J Immunol , vol.156 , pp. 4821-4832
    • Lambris, J.D.1    Lao, Z.2    Oglesby, T.J.3    Atkinson, J.P.4    Hack, C.E.5    Becherer, J.D.6
  • 56
    • 84923080145 scopus 로고    scopus 로고
    • Complement regulators in human disease: Lessons from modern genetics
    • Liszewski MK, Atkinson JP, (2015a) Complement regulators in human disease: lessons from modern genetics. J Intern Med 277: 294-305
    • (2015) J Intern Med , vol.277 , pp. 294-305
    • Liszewski, M.K.1    Atkinson, J.P.2
  • 57
    • 85075591967 scopus 로고    scopus 로고
    • Complement regulator CD46: Genetic variants and disease associations
    • Liszewski MK, Atkinson JP, (2015b) Complement regulator CD46: genetic variants and disease associations. Hum Genomics 9: 7
    • (2015) Hum Genomics , vol.9 , pp. 7
    • Liszewski, M.K.1    Atkinson, J.P.2
  • 59
    • 0032194160 scopus 로고    scopus 로고
    • Membrane cofactor protein: Importance of N- and O-glycosylation for complement regulatory function
    • Liszewski MK, Leung MK, Atkinson JP, (1998) Membrane cofactor protein: importance of N- and O-glycosylation for complement regulatory function. J Immunol 161: 3711-3718
    • (1998) J Immunol , vol.161 , pp. 3711-3718
    • Liszewski, M.K.1    Leung, M.K.2    Atkinson, J.P.3
  • 60
    • 33644843082 scopus 로고    scopus 로고
    • Structure and regulatory profile of the monkeypox inhibitor of complement: Comparison to homologs in vaccinia and variola and evidence for dimer formation
    • Liszewski MK, Leung MK, Hauhart R, Buller RM, Bertram P, Wang X, Rosengard AM, Kotwal GJ, Atkinson JP, (2006) Structure and regulatory profile of the monkeypox inhibitor of complement: comparison to homologs in vaccinia and variola and evidence for dimer formation. J Immunol 176: 3725-3734
    • (2006) J Immunol , vol.176 , pp. 3725-3734
    • Liszewski, M.K.1    Leung, M.K.2    Hauhart, R.3    Buller, R.M.4    Bertram, P.5    Wang, X.6    Rosengard, A.M.7    Kotwal, G.J.8    Atkinson, J.P.9
  • 61
    • 70349233992 scopus 로고    scopus 로고
    • Smallpox inhibitor of complement enzymes (SPICE): Dissecting functional sites and abrogating activity
    • Liszewski MK, Leung MK, Hauhart R, Fang CJ, Bertram P, Atkinson JP, (2009) Smallpox inhibitor of complement enzymes (SPICE): dissecting functional sites and abrogating activity. J Immunol 183: 3150-3159
    • (2009) J Immunol , vol.183 , pp. 3150-3159
    • Liszewski, M.K.1    Leung, M.K.2    Hauhart, R.3    Fang, C.J.4    Bertram, P.5    Atkinson, J.P.6
  • 63
    • 13244253766 scopus 로고    scopus 로고
    • Pdb-care (PDB carbohydrate residue check): A program to support annotation of complex carbohydrate structures in PDB files
    • Lutteke T, von der Lieth CW, (2004) pdb-care (PDB carbohydrate residue check): a program to support annotation of complex carbohydrate structures in PDB files. BMC Bioinformatics 5: 69
    • (2004) BMC Bioinformatics , vol.5 , pp. 69
    • Lutteke, T.1    Von Der Lieth, C.W.2
  • 64
    • 33748434466 scopus 로고    scopus 로고
    • Recent advances in biological and clinical aspects of paroxysmal nocturnal hemoglobinuria
    • Luzzatto L, Gianfaldoni G, (2006) Recent advances in biological and clinical aspects of paroxysmal nocturnal hemoglobinuria. Int J Hematol 84: 104-112
    • (2006) Int J Hematol , vol.84 , pp. 104-112
    • Luzzatto, L.1    Gianfaldoni, G.2
  • 65
    • 84878910014 scopus 로고    scopus 로고
    • Functional anatomy of complement factor H
    • Makou E, Herbert AP, Barlow PN, (2013) Functional anatomy of complement factor H. Biochemistry 52: 3949-3962
    • (2013) Biochemistry , vol.52 , pp. 3949-3962
    • Makou, E.1    Herbert, A.P.2    Barlow, P.N.3
  • 74
    • 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, (2015) Structural Basis for the Function of Complement Component C4 within the Classical and Lectin Pathways of Complement. J Immunol 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
  • 75
    • 0028406273 scopus 로고
    • Structure and function of decay accelerating factor CD55
    • Nicholson-Weller A, Wang CE, (1994) Structure and function of decay accelerating factor CD55. J Lab Clin Med 123: 485-491
    • (1994) J Lab Clin Med , vol.123 , pp. 485-491
    • Nicholson-Weller, A.1    Wang, C.E.2
  • 76
    • 1642545478 scopus 로고    scopus 로고
    • Primitive complement system of invertebrates
    • Nonaka M, Yoshizaki F, (2004) Primitive complement system of invertebrates. Immunol Rev 198: 203-215
    • (2004) Immunol Rev , vol.198 , pp. 203-215
    • Nonaka, M.1    Yoshizaki, F.2
  • 78
    • 84907598707 scopus 로고    scopus 로고
    • Viral regulators of complement activation: Structure, function and evolution
    • Ojha H, Panwar HS, Gorham RD Jr, Morikis D, Sahu A, (2014) Viral regulators of complement activation: structure, function and evolution. Mol Immunol 61: 89-99
    • (2014) Mol Immunol , vol.61 , pp. 89-99
    • Ojha, H.1    Panwar, H.S.2    Gorham, R.D.3    Morikis, D.4    Sahu, A.5
  • 79
    • 0033582520 scopus 로고    scopus 로고
    • Identification of residues within the 727-767 segment of human complement component C3 important for its interaction with factor H and with complement receptor 1 (CR1, CD35)
    • Oran AE, Isenman DE, (1999) Identification of residues within the 727-767 segment of human complement component C3 important for its interaction with factor H and with complement receptor 1 (CR1, CD35). J Biol Chem 274: 5120-5130
    • (1999) J Biol Chem , vol.274 , pp. 5120-5130
    • Oran, A.E.1    Isenman, D.E.2
  • 81
    • 79953190798 scopus 로고    scopus 로고
    • Disease-associated N-terminal complement factor H mutations perturb cofactor and decay-accelerating activities
    • Pechtl IC, Kavanagh D, McIntosh N, Harris CL, Barlow PN, (2011) Disease-associated N-terminal complement factor H mutations perturb cofactor and decay-accelerating activities. J Biol Chem 286: 11082-11090
    • (2011) J Biol Chem , vol.286 , pp. 11082-11090
    • Pechtl, I.C.1    Kavanagh, D.2    McIntosh, N.3    Harris, C.L.4    Barlow, P.N.5
  • 82
    • 78149347784 scopus 로고    scopus 로고
    • Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens
    • Persson BD, Schmitz NB, Santiago C, Zocher G, Larvie M, Scheu U, Casasnovas JM, Stehle T, (2010) Structure of the extracellular portion of CD46 provides insights into its interactions with complement proteins and pathogens. PLoS Pathog 6: e1001122
    • (2010) PLoS Pathog , vol.6 , pp. e1001122
    • Persson, B.D.1    Schmitz, N.B.2    Santiago, C.3    Zocher, G.4    Larvie, M.5    Scheu, U.6    Casasnovas, J.M.7    Stehle, T.8
  • 83
    • 0037109074 scopus 로고    scopus 로고
    • Structure and function in rhodopsin: High-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line
    • Reeves PJ, Callewaert N, Contreras R, Khorana HG, (2002) Structure and function in rhodopsin: high-level expression of rhodopsin with restricted and homogeneous N-glycosylation by a tetracycline-inducible N-acetylglucosaminyltransferase I-negative HEK293S stable mammalian cell line. Proc Natl Acad Sci USA 99: 13419-13424
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 13419-13424
    • Reeves, P.J.1    Callewaert, N.2    Contreras, R.3    Khorana, H.G.4
  • 85
    • 77955883153 scopus 로고    scopus 로고
    • Complement: A key system for immune surveillance and homeostasis
    • Ricklin D, Hajishengallis G, Yang K, Lambris JD, (2010) Complement: a key system for immune surveillance and homeostasis. Nat Immunol 11: 785-797
    • (2010) Nat Immunol , vol.11 , pp. 785-797
    • Ricklin, D.1    Hajishengallis, G.2    Yang, K.3    Lambris, J.D.4
  • 86
    • 84875968524 scopus 로고    scopus 로고
    • Complement in immune and inflammatory disorders: Pathophysiological mechanisms
    • Ricklin D, Lambris JD, (2013a) Complement in immune and inflammatory disorders: pathophysiological mechanisms. J Immunol 190: 3831-3838
    • (2013) J Immunol , vol.190 , pp. 3831-3838
    • Ricklin, D.1    Lambris, J.D.2
  • 87
    • 84875990477 scopus 로고    scopus 로고
    • Complement in immune and inflammatory disorders: Therapeutic interventions
    • Ricklin D, Lambris JD, (2013b) Complement in immune and inflammatory disorders: therapeutic interventions. J Immunol 190: 3839-3847
    • (2013) J Immunol , vol.190 , pp. 3839-3847
    • Ricklin, D.1    Lambris, J.D.2
  • 88
    • 0037111449 scopus 로고    scopus 로고
    • Cutting edge: Inhibiting measles virus infection but promoting reproduction: An explanation for splicing and tissue-specific expression of CD46
    • Riley RC, Tannenbaum PL, Abbott DH, Atkinson JP, (2002) Cutting edge: inhibiting measles virus infection but promoting reproduction: an explanation for splicing and tissue-specific expression of CD46. J Immunol 169: 5405-5409
    • (2002) J Immunol , vol.169 , pp. 5405-5409
    • Riley, R.C.1    Tannenbaum, P.L.2    Abbott, D.H.3    Atkinson, J.P.4
  • 89
    • 84949117415 scopus 로고    scopus 로고
    • New functional and structural insights from updated mutational databases for complement factor H, Factor I, membrane cofactor protein and C3
    • Rodriguez E, Rallapalli PM, Osborne AJ, Perkins SJ, (2014) New functional and structural insights from updated mutational databases for complement factor H, Factor I, membrane cofactor protein and C3. Biosci Rep 34: e00146
    • (2014) Biosci Rep , vol.34 , pp. e00146
    • Rodriguez, E.1    Rallapalli, P.M.2    Osborne, A.J.3    Perkins, S.J.4
  • 91
    • 0037173003 scopus 로고    scopus 로고
    • Variola virus immune evasion design: Expression of a highly efficient inhibitor of human complement
    • Rosengard AM, Liu Y, Nie Z, Jimenez R, (2002) Variola virus immune evasion design: expression of a highly efficient inhibitor of human complement. Proc Natl Acad Sci USA 99: 8808-8813
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 8808-8813
    • Rosengard, A.M.1    Liu, Y.2    Nie, Z.3    Jimenez, R.4
  • 93
    • 84878103661 scopus 로고    scopus 로고
    • Rational engineering of a minimized immune inhibitor with unique triple-targeting properties
    • Schmidt CQ, Bai H, Lin Z, Risitano AM, Barlow PN, Ricklin D, Lambris JD, (2013) Rational engineering of a minimized immune inhibitor with unique triple-targeting properties. J Immunol 190: 5712-5721
    • (2013) J Immunol , vol.190 , pp. 5712-5721
    • Schmidt, C.Q.1    Bai, H.2    Lin, Z.3    Risitano, A.M.4    Barlow, P.N.5    Ricklin, D.6    Lambris, J.D.7
  • 94
    • 84936985803 scopus 로고    scopus 로고
    • More than just immune evasion: Hijacking complement by Plasmodium falciparum
    • Schmidt CQ, Kennedy AT, Tham WH, (2015) More than just immune evasion: Hijacking complement by Plasmodium falciparum. Mol Immunol 67: 71-84
    • (2015) Mol Immunol , vol.67 , pp. 71-84
    • Schmidt, C.Q.1    Kennedy, A.T.2    Tham, W.H.3
  • 96
    • 13544260859 scopus 로고    scopus 로고
    • Electrostatic modeling predicts the activities of orthopoxvirus complement control proteins
    • Sfyroera G, Katragadda M, Morikis D, Isaacs SN, Lambris JD, (2005) Electrostatic modeling predicts the activities of orthopoxvirus complement control proteins. J Immunol 174: 2143-2151
    • (2005) J Immunol , vol.174 , pp. 2143-2151
    • Sfyroera, G.1    Katragadda, M.2    Morikis, D.3    Isaacs, S.N.4    Lambris, J.D.5
  • 97
    • 60349127531 scopus 로고    scopus 로고
    • Complement activation and inhibition: A delicate balance
    • Sjoberg AP, Trouw LA, Blom AM, (2009) Complement activation and inhibition: a delicate balance. Trends Immunol 30: 83-90
    • (2009) Trends Immunol , vol.30 , pp. 83-90
    • Sjoberg, A.P.1    Trouw, L.A.2    Blom, A.M.3
  • 99
    • 13844320382 scopus 로고    scopus 로고
    • A complement receptor-1 polymorphism with high frequency in malaria endemic regions of Asia but not Africa
    • Thomas BN, Donvito B, Cockburn I, Fandeur T, Rowe JA, Cohen JH, Moulds JM, (2005) A complement receptor-1 polymorphism with high frequency in malaria endemic regions of Asia but not Africa. Genes Immun 6: 31-36
    • (2005) Genes Immun , vol.6 , pp. 31-36
    • Thomas, B.N.1    Donvito, B.2    Cockburn, I.3    Fandeur, T.4    Rowe, J.A.5    Cohen, J.H.6    Moulds, J.M.7
  • 101
    • 69449090499 scopus 로고    scopus 로고
    • The disease-protective complement factor H allotypic variant Ile62 shows increased binding affinity for C3b and enhanced cofactor activity
    • Tortajada A, Montes T, Martinez-Barricarte R, Morgan BP, Harris CL, de Cordoba SR, (2009) The disease-protective complement factor H allotypic variant Ile62 shows increased binding affinity for C3b and enhanced cofactor activity. Hum Mol Genet 18: 3452-3461
    • (2009) Hum Mol Genet , vol.18 , pp. 3452-3461
    • Tortajada, A.1    Montes, T.2    Martinez-Barricarte, R.3    Morgan, B.P.4    Harris, C.L.5    De Cordoba, S.R.6
  • 106
    • 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, (2009) Structure of complement fragment C3b-factor H and implications for host protection by complement regulators. Nat Immunol 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
  • 107
    • 41149162586 scopus 로고    scopus 로고
    • Identification of hot spots in the variola virus complement inhibitor (SPICE) for human complement regulation
    • Yadav VN, Pyaram K, Mullick J, Sahu A, (2008) Identification of hot spots in the variola virus complement inhibitor (SPICE) for human complement regulation. J Virol 82: 3283-3294
    • (2008) J Virol , vol.82 , pp. 3283-3294
    • Yadav, V.N.1    Pyaram, K.2    Mullick, J.3    Sahu, A.4
  • 108
    • 84880807089 scopus 로고    scopus 로고
    • Human complement control and complement evasion by pathogenic microbes-tipping the balance
    • Zipfel PF, Hallstrom T, Riesbeck K, (2013) Human complement control and complement evasion by pathogenic microbes-tipping the balance. Mol Immunol 56: 152-160
    • (2013) Mol Immunol , vol.56 , pp. 152-160
    • Zipfel, P.F.1    Hallstrom, T.2    Riesbeck, K.3
  • 109
    • 70349437186 scopus 로고    scopus 로고
    • Complement regulators and inhibitory proteins
    • Zipfel PF, Skerka C, (2009) Complement regulators and inhibitory proteins. Nat Rev Immunol 9: 729-740
    • (2009) Nat Rev Immunol , vol.9 , pp. 729-740
    • Zipfel, P.F.1    Skerka, C.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.