메뉴 건너뛰기




Volumn 52, Issue 23, 2013, Pages 3949-3962

Functional anatomy of complement factor H

Author keywords

[No Author keywords available]

Indexed keywords

AGE-RELATED MACULAR DEGENERATION; COMPLEMENT SYSTEMS; MOLECULAR PATTERNS; MOLECULAR UNDERSTANDING; PROTEOLYTIC CASCADE; SEQUENCE VARIATIONS; SINGLE NUCLEOTIDE POLYMORPHISMS; THREE-DIMENSIONAL ARCHITECTURE;

EID: 84878910014     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi4003452     Document Type: Article
Times cited : (99)

References (109)
  • 1
    • 77955883153 scopus 로고    scopus 로고
    • Complement: A key system for immune surveillance and homeostasis
    • Ricklin, D., Hajishengallis, G., Yang, K., and Lambris, J. D. (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
  • 2
    • 36849084660 scopus 로고    scopus 로고
    • Translational mini-review series on complement factor H: Genetics and disease associations of human complement factor H
    • de Cordoba, S. R. and de Jorge, E. G. (2008) Translational mini-review series on complement factor H: Genetics and disease associations of human complement factor H Clin. Exp. Immunol. 151, 1-13
    • (2008) Clin. Exp. Immunol. , vol.151 , pp. 1-13
    • De Cordoba, S.R.1    De Jorge, E.G.2
  • 4
    • 33750859976 scopus 로고    scopus 로고
    • Structure of C3b reveals conformational changes that underlie complement activity
    • Janssen, B. J., Christodoulidou, A., McCarthy, A., Lambris, J. D., and 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
  • 5
    • 0028124668 scopus 로고
    • Specificity of the thioester-containing reactive site of human C3 and its significance to complement activation
    • Sahu, A., Kozel, T. R., and Pangburn, M. K. (1994) Specificity of the thioester-containing reactive site of human C3 and its significance to complement activation Biochem. J. 302, 429-436
    • (1994) Biochem. J. , vol.302 , pp. 429-436
    • Sahu, A.1    Kozel, T.R.2    Pangburn, M.K.3
  • 6
    • 77953266787 scopus 로고    scopus 로고
    • The amplification loop of the complement pathways
    • Lachmann, P. J. (2009) The amplification loop of the complement pathways Adv. Immunol. 104, 115-149
    • (2009) Adv. Immunol. , vol.104 , pp. 115-149
    • Lachmann, P.J.1
  • 7
    • 0012042656 scopus 로고
    • Control of the amplification convertase of complement by the plasma protein beta1H
    • Weiler, J. M., Daha, M. R., Austen, K. F., and Fearon, D. T. (1976) Control of the amplification convertase of complement by the plasma protein beta1H Proc. Natl. Acad. Sci. U.S.A. 73, 3268-3272
    • (1976) Proc. Natl. Acad. Sci. U.S.A. , vol.73 , pp. 3268-3272
    • Weiler, J.M.1    Daha, M.R.2    Austen, K.F.3    Fearon, D.T.4
  • 8
    • 0020409537 scopus 로고
    • Purification and structural studies on the complement-system control protein β 1H (Factor H)
    • Sim, R. B. and DiScipio, R. G. (1982) Purification and structural studies on the complement-system control protein β 1H (Factor H) Biochem. J. 205, 285-293
    • (1982) Biochem. J. , vol.205 , pp. 285-293
    • Sim, R.B.1    Discipio, R.G.2
  • 9
    • 0025314311 scopus 로고
    • Discrimination between activators and nonactivators of the alternative pathway of complement: Regulation via a sialic acid/polyanion binding site on factor H
    • Meri, S. and Pangburn, M. K. (1990) Discrimination between activators and nonactivators of the alternative pathway of complement: Regulation via a sialic acid/polyanion binding site on factor H Proc. Natl. Acad. Sci. U.S.A. 87, 3982-3986
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 3982-3986
    • Meri, S.1    Pangburn, M.K.2
  • 10
    • 0035008505 scopus 로고    scopus 로고
    • Structure and flexibility of the multiple domain proteins that regulate complement activation
    • Kirkitadze, M. D. and Barlow, P. N. (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
  • 11
    • 0033921990 scopus 로고    scopus 로고
    • Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement
    • Pangburn, M. K. (2000) Host recognition and target differentiation by factor H, a regulator of the alternative pathway of complement Immunopharmacology 49, 149-157
    • (2000) Immunopharmacology , vol.49 , pp. 149-157
    • Pangburn, M.K.1
  • 12
    • 0017704496 scopus 로고
    • Human complement C3b inactivator: Isolation, characterization, and demonstration of an absolute requirement for the serum protein β1H for cleavage of C3b and C4b in solution
    • Pangburn, M. K., Schreiber, R. D., and Muller-Eberhard, H. J. (1977) Human complement C3b inactivator: Isolation, characterization, and demonstration of an absolute requirement for the serum protein β1H for cleavage of C3b and C4b in solution J. Exp. Med. 146, 257-270
    • (1977) J. Exp. Med. , vol.146 , pp. 257-270
    • Pangburn, M.K.1    Schreiber, R.D.2    Muller-Eberhard, H.J.3
  • 13
    • 0017088173 scopus 로고
    • Modulation of C3b hemolytic activity by a plasma protein distinct from C3b inactivator
    • Whaley, K. and Ruddy, S. (1976) Modulation of C3b hemolytic activity by a plasma protein distinct from C3b inactivator Science 193, 1011-1013
    • (1976) Science , vol.193 , pp. 1011-1013
    • Whaley, K.1    Ruddy, S.2
  • 14
    • 68249086824 scopus 로고    scopus 로고
    • Complement evasion strategies of pathogens: Acquisition of inhibitors and beyond
    • Blom, A. M., Hallstrom, T., and Riesbeck, K. (2009) Complement evasion strategies of pathogens: Acquisition of inhibitors and beyond Mol. Immunol. 46, 2808-2817
    • (2009) Mol. Immunol. , vol.46 , pp. 2808-2817
    • Blom, A.M.1    Hallstrom, T.2    Riesbeck, K.3
  • 15
    • 84875968524 scopus 로고    scopus 로고
    • Complement in immune and inflammatory disorders: Pathophysiological mechanisms
    • Ricklin, D. and Lambris, J. D. (2013) 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
  • 16
    • 29744453472 scopus 로고    scopus 로고
    • Opportunities for new therapies based on the natural regulators of complement activation
    • Brook, E., Herbert, A. P., Jenkins, H. T., Soares, D. C., and Barlow, P. N. (2005) Opportunities for new therapies based on the natural regulators of complement activation Ann. N.Y. Acad. Sci. 1056, 176-188
    • (2005) Ann. N.Y. Acad. Sci. , vol.1056 , pp. 176-188
    • Brook, E.1    Herbert, A.P.2    Jenkins, H.T.3    Soares, D.C.4    Barlow, P.N.5
  • 17
    • 20144373025 scopus 로고    scopus 로고
    • Successful plasma therapy for atypical hemolytic uremic syndrome caused by factor H deficiency owing to a novel mutation in the complement cofactor protein domain 15
    • Licht, C., Weyersberg, A., Heinen, S., Stapenhorst, L., Devenge, J., Beck, B., Waldherr, R., Kirschfink, M., Zipfel, P. F., and Hoppe, B. (2005) Successful plasma therapy for atypical hemolytic uremic syndrome caused by factor H deficiency owing to a novel mutation in the complement cofactor protein domain 15 Am. J. Kidney Dis. 45, 415-421
    • (2005) Am. J. Kidney Dis. , vol.45 , pp. 415-421
    • Licht, C.1    Weyersberg, A.2    Heinen, S.3    Stapenhorst, L.4    Devenge, J.5    Beck, B.6    Waldherr, R.7    Kirschfink, M.8    Zipfel, P.F.9    Hoppe, B.10
  • 19
    • 77954761090 scopus 로고    scopus 로고
    • Treatment with human complement factor H rapidly reverses renal complement deposition in factor H-deficient mice
    • Fakhouri, F., de Jorge, E. G., Brune, F., Azam, P., Cook, H. T., and Pickering, M. C. (2010) Treatment with human complement factor H rapidly reverses renal complement deposition in factor H-deficient mice Kidney Int. 78, 279-286
    • (2010) Kidney Int. , vol.78 , pp. 279-286
    • Fakhouri, F.1    De Jorge, E.G.2    Brune, F.3    Azam, P.4    Cook, H.T.5    Pickering, M.C.6
  • 20
    • 79151485902 scopus 로고    scopus 로고
    • Production of biologically active complement factor H in therapeutically useful quantities
    • Schmidt, C. Q., Slingsby, F. C., Richards, A., and Barlow, P. N. (2011) Production of biologically active complement factor H in therapeutically useful quantities Protein Expression Purif. 76, 254-263
    • (2011) Protein Expression Purif. , vol.76 , pp. 254-263
    • Schmidt, C.Q.1    Slingsby, F.C.2    Richards, A.3    Barlow, P.N.4
  • 21
    • 84878103661 scopus 로고    scopus 로고
    • Rational Engineering of a Minimized Immune Inhibitor with Unique Triple-Targeting Properties
    • Schmidt, C. Q., Bai, H., Lin, Z., Risitano, A. M., Barlow, P. N., Ricklin, D., and Lambris, J. D. (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
  • 22
    • 36849044745 scopus 로고    scopus 로고
    • Translational mini-review series on complement factor H: Structural and functional correlations for factor H
    • Schmidt, C. Q., Herbert, A. P., Hocking, H. G., Uhrin, D., and Barlow, P. N. (2008) Translational mini-review series on complement factor H: Structural and functional correlations for factor H Clin. Exp. Immunol. 151, 14-24
    • (2008) Clin. Exp. Immunol. , vol.151 , pp. 14-24
    • Schmidt, C.Q.1    Herbert, A.P.2    Hocking, H.G.3    Uhrin, D.4    Barlow, P.N.5
  • 23
    • 77954315059 scopus 로고    scopus 로고
    • Complement control protein factor H: The good, the bad, and the inadequate
    • Ferreira, V. P., Pangburn, M. K., and Cortes, C. (2010) Complement control protein factor H: The good, the bad, and the inadequate Mol. Immunol. 47, 2187-2197
    • (2010) Mol. Immunol. , vol.47 , pp. 2187-2197
    • Ferreira, V.P.1    Pangburn, M.K.2    Cortes, C.3
  • 24
    • 84855282981 scopus 로고    scopus 로고
    • Complement Factor H-ligand interactions: Self-association, multivalency and dissociation constants
    • Perkins, S. J., Nan, R., Li, K., Khan, S., and Miller, A. (2011) Complement Factor H-ligand interactions: Self-association, multivalency and dissociation constants Immunobiology 217, 281-297
    • (2011) Immunobiology , vol.217 , pp. 281-297
    • Perkins, S.J.1    Nan, R.2    Li, K.3    Khan, S.4    Miller, A.5
  • 27
    • 33947160639 scopus 로고    scopus 로고
    • Synthesis of complement factor H by retinal pigment epithelial cells is down-regulated by oxidized photoreceptor outer segments
    • Chen, M., Forrester, J. V., and Xu, H. (2007) Synthesis of complement factor H by retinal pigment epithelial cells is down-regulated by oxidized photoreceptor outer segments Exp. Eye Res. 84, 635-645
    • (2007) Exp. Eye Res. , vol.84 , pp. 635-645
    • Chen, M.1    Forrester, J.V.2    Xu, H.3
  • 28
    • 0024561914 scopus 로고
    • Structure-function relationships of the complement components
    • Reid, K. B. and Day, A. J. (1989) Structure-function relationships of the complement components Immunol. Today 10, 177-180
    • (1989) Immunol. Today , vol.10 , pp. 177-180
    • Reid, K.B.1    Day, A.J.2
  • 30
    • 0025894780 scopus 로고
    • Three-dimensional structure of a complement control protein module in solution
    • Norman, D. G., Barlow, P. N., Baron, M., Day, A. J., Sim, R. B., and Campbell, I. D. (1991) Three-dimensional structure of a complement control protein module in solution J. Mol. Biol. 219, 717-725
    • (1991) J. Mol. Biol. , vol.219 , pp. 717-725
    • Norman, D.G.1    Barlow, P.N.2    Baron, M.3    Day, A.J.4    Sim, R.B.5    Campbell, I.D.6
  • 33
    • 33745202838 scopus 로고    scopus 로고
    • Disease-associated sequence variations congregate in a polyanion-recognition patch on human factor H revealed in 3D structure
    • Herbert, A. P., Uhrin, D., Lyon, M., Pangburn, M. K., and Barlow, P. N. (2006) Disease-associated sequence variations congregate in a polyanion-recognition patch on human factor H revealed in 3D structure J. Biol. Chem. 281, 16512-16520
    • (2006) J. Biol. Chem. , vol.281 , pp. 16512-16520
    • Herbert, A.P.1    Uhrin, D.2    Lyon, M.3    Pangburn, M.K.4    Barlow, P.N.5
  • 34
    • 33646164894 scopus 로고    scopus 로고
    • Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome
    • Jokiranta, T. S., Jaakola, V. P., Lehtinen, M. J., Parepalo, M., Meri, S., and Goldman, A. (2006) Structure of complement factor H carboxyl-terminus reveals molecular basis of atypical haemolytic uremic syndrome EMBO J. 25, 1784-1794
    • (2006) EMBO J. , vol.25 , pp. 1784-1794
    • Jokiranta, T.S.1    Jaakola, V.P.2    Lehtinen, M.J.3    Parepalo, M.4    Meri, S.5    Goldman, A.6
  • 36
    • 34547102526 scopus 로고    scopus 로고
    • Structure shows that a glycosaminoglycan and protein recognition site in factor H is perturbed by age-related macular degeneration-linked single nucleotide polymorphism
    • Herbert, A. P., Deakin, J. A., Schmidt, C. Q., Blaum, B. S., Egan, C., Ferreira, V. P., Pangburn, M. K., Lyon, M., Uhrin, D., and Barlow, P. N. (2007) Structure shows that a glycosaminoglycan and protein recognition site in factor H is perturbed by age-related macular degeneration-linked single nucleotide polymorphism J. Biol. Chem. 282, 18960-18968
    • (2007) J. Biol. Chem. , vol.282 , pp. 18960-18968
    • Herbert, A.P.1    Deakin, J.A.2    Schmidt, C.Q.3    Blaum, B.S.4    Egan, C.5    Ferreira, V.P.6    Pangburn, M.K.7    Lyon, M.8    Uhrin, D.9    Barlow, P.N.10
  • 37
    • 44049086967 scopus 로고    scopus 로고
    • Structure of the N-terminal Region of Complement Factor H and Conformational Implications of Disease-linked Sequence Variations
    • Hocking, H. G., Herbert, A. P., Kavanagh, D., Soares, D. C., Ferreira, V. P., Pangburn, M. K., Uhrin, D., and Barlow, P. N. (2008) Structure of the N-terminal Region of Complement Factor H and Conformational Implications of Disease-linked Sequence Variations J. Biol. Chem. 283, 9475-9487
    • (2008) J. Biol. Chem. , vol.283 , pp. 9475-9487
    • Hocking, H.G.1    Herbert, A.P.2    Kavanagh, D.3    Soares, D.C.4    Ferreira, V.P.5    Pangburn, M.K.6    Uhrin, D.7    Barlow, P.N.8
  • 38
    • 67649230210 scopus 로고    scopus 로고
    • Structure of complement fragment C3b-factor H and implications for host protection by complement regulators
    • Wu, J., Wu, Y. Q., Ricklin, D., Janssen, B. J., Lambris, J. D., and 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
  • 42
    • 0025727462 scopus 로고
    • Oligomeric domain structure of human complement factor H by X-ray and neutron solution scattering
    • Perkins, S. J., Nealis, A. S., and Sim, R. B. (1991) Oligomeric domain structure of human complement factor H by X-ray and neutron solution scattering Biochemistry 30, 2847-2857
    • (1991) Biochemistry , vol.30 , pp. 2847-2857
    • Perkins, S.J.1    Nealis, A.S.2    Sim, R.B.3
  • 43
    • 0026645955 scopus 로고
    • Ultrastructures and interactions of complement factors H and i
    • DiScipio, R. G. (1992) Ultrastructures and interactions of complement factors H and I J. Immunol. 149, 2592-2599
    • (1992) J. Immunol. , vol.149 , pp. 2592-2599
    • Discipio, R.G.1
  • 44
    • 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. and Perkins, S. J. (2001) 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. 309, 1117-1138
    • (2001) J. Mol. Biol. , vol.309 , pp. 1117-1138
    • Aslam, M.1    Perkins, S.J.2
  • 45
    • 36349016373 scopus 로고    scopus 로고
    • The regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties
    • Okemefuna, A. I., Gilbert, H. E., Griggs, K. M., Ormsby, R. J., Gordon, D. L., and Perkins, S. J. (2008) The regulatory SCR-1/5 and cell surface-binding SCR-16/20 fragments of factor H reveal partially folded-back solution structures and different self-associative properties J. Mol. Biol. 375, 80-101
    • (2008) J. Mol. Biol. , vol.375 , pp. 80-101
    • Okemefuna, A.I.1    Gilbert, H.E.2    Griggs, K.M.3    Ormsby, R.J.4    Gordon, D.L.5    Perkins, S.J.6
  • 46
    • 43949161834 scopus 로고
    • Complement factor H and related proteins: An expanding family of complement-regulatory proteins?
    • Zipfel, P. F. and Skerka, C. (1994) Complement factor H and related proteins: An expanding family of complement-regulatory proteins? Immunol. Today 15, 121-126
    • (1994) Immunol. Today , vol.15 , pp. 121-126
    • Zipfel, P.F.1    Skerka, C.2
  • 47
    • 47749126514 scopus 로고    scopus 로고
    • Factor H family proteins and human diseases
    • Jozsi, M. and Zipfel, P. F. (2008) Factor H family proteins and human diseases Trends Immunol. 29, 380-387
    • (2008) Trends Immunol. , vol.29 , pp. 380-387
    • Jozsi, M.1    Zipfel, P.F.2
  • 50
    • 0021690952 scopus 로고
    • Lysine residues, but not carbohydrates, are required for the regulatory function of H on the amplification C3 convertase of complement
    • Jouvin, M. H., Kazatchkine, M. D., Cahour, A., and Bernard, N. (1984) Lysine residues, but not carbohydrates, are required for the regulatory function of H on the amplification C3 convertase of complement J. Immunol. 133, 3250-3254
    • (1984) J. Immunol. , vol.133 , pp. 3250-3254
    • Jouvin, M.H.1    Kazatchkine, M.D.2    Cahour, A.3    Bernard, N.4
  • 51
    • 0020684529 scopus 로고
    • Kinetic and thermodynamic analysis of the control of C3b by the complement regulatory proteins factors H and i
    • Pangburn, M. K. and Muller-Eberhard, H. J. (1983) Kinetic and thermodynamic analysis of the control of C3b by the complement regulatory proteins factors H and I Biochemistry 22, 178-185
    • (1983) Biochemistry , vol.22 , pp. 178-185
    • Pangburn, M.K.1    Muller-Eberhard, H.J.2
  • 52
  • 53
    • 0029850245 scopus 로고    scopus 로고
    • Mapping of the domains required for decay acceleration activity of the human factor H-like protein 1 and factor H
    • Kuhn, S. and Zipfel, P. F. (1996) Mapping of the domains required for decay acceleration activity of the human factor H-like protein 1 and factor H Eur. J. Immunol. 26, 2383-2387
    • (1996) Eur. J. Immunol. , vol.26 , pp. 2383-2387
    • Kuhn, S.1    Zipfel, P.F.2
  • 54
    • 0018317786 scopus 로고
    • Human alternative complement pathway: Membrane-associated sialic acid regulates the competition between B and β1 H for cell-bound C3b
    • Kazatchkine, M. D., Fearon, D. T., and Austen, K. F. (1979) Human alternative complement pathway: Membrane-associated sialic acid regulates the competition between B and β1 H for cell-bound C3b J. Immunol. 122, 75-81
    • (1979) J. Immunol. , vol.122 , pp. 75-81
    • Kazatchkine, M.D.1    Fearon, D.T.2    Austen, K.F.3
  • 55
    • 0030589294 scopus 로고    scopus 로고
    • Identification of a heparin binding domain in the seventh short consensus repeat of complement factor H
    • Blackmore, T. K., Sadlon, T. A., Ward, H. M., Lublin, D. M., and Gordon, D. L. (1996) Identification of a heparin binding domain in the seventh short consensus repeat of complement factor H J. Immunol. 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
  • 57
    • 0032473556 scopus 로고    scopus 로고
    • A novel sialic acid binding site on factor H mediates serum resistance of sialylated Neisseria gonorrhoeae
    • Ram, S., Sharma, A. K., Simpson, S. D., Gulati, S., McQuillen, D. P., Pangburn, M. K., and Rice, P. A. (1998) A novel sialic acid binding site on factor H mediates serum resistance of sialylated Neisseria gonorrhoeae J. Exp. Med. 187, 743-752
    • (1998) J. Exp. Med. , vol.187 , pp. 743-752
    • Ram, S.1    Sharma, A.K.2    Simpson, S.D.3    Gulati, S.4    McQuillen, D.P.5    Pangburn, M.K.6    Rice, P.A.7
  • 58
    • 0033648173 scopus 로고    scopus 로고
    • Pinpointing the putative heparin/sialic acid-binding residues in the 'sushi' domain 7 of factor H: A molecular modeling study
    • Ranganathan, S., Male, D. A., Ormsby, R. J., Giannakis, E., and Gordon, D. L. (2000) Pinpointing the putative heparin/sialic acid-binding residues in the 'sushi' domain 7 of factor H: A molecular modeling study Pac. Symp. Biocomput. 2000 155-167
    • (2000) Pac. Symp. Biocomput. 2000 , pp. 155-167
    • Ranganathan, S.1    Male, D.A.2    Ormsby, R.J.3    Giannakis, E.4    Gordon, D.L.5
  • 59
    • 0028260801 scopus 로고
    • Regulation of alternative pathway complement activation by glycosaminoglycans: Specificity of the polyanion binding site on factor H
    • Meri, S. and Pangburn, M. K. (1994) Regulation of alternative pathway complement activation by glycosaminoglycans: Specificity of the polyanion binding site on factor H Biochem. Biophys. Res. Commun. 198, 52-59
    • (1994) Biochem. Biophys. Res. Commun. , vol.198 , pp. 52-59
    • Meri, S.1    Pangburn, M.K.2
  • 60
    • 77957271118 scopus 로고    scopus 로고
    • Complement factor H and age-related macular degeneration: The role of glycosaminoglycan recognition in disease pathology
    • Clark, S. J., Bishop, P. N., and Day, A. J. (2010) Complement factor H and age-related macular degeneration: The role of glycosaminoglycan recognition in disease pathology Biochem. Soc. Trans. 38, 1342-1348
    • (2010) Biochem. Soc. Trans. , vol.38 , pp. 1342-1348
    • Clark, S.J.1    Bishop, P.N.2    Day, A.J.3
  • 62
    • 17044431125 scopus 로고    scopus 로고
    • Factor H is a dermatan sulfate-binding protein: Identification of a dermatan sulfate-mediated protease that cleaves factor H
    • Saito, A. and Munakata, H. (2005) Factor H is a dermatan sulfate-binding protein: Identification of a dermatan sulfate-mediated protease that cleaves factor H J. Biochem. 137, 225-233
    • (2005) J. Biochem. , vol.137 , pp. 225-233
    • Saito, A.1    Munakata, H.2
  • 63
    • 33747700932 scopus 로고    scopus 로고
    • H384 allotypic variant of factor H associated with age-related macular degeneration has different heparin-binding properties from the non-disease-associated form
    • Clark, S. J., Higman, V. A., Mulloy, B., Perkins, S. J., Lea, S. M., Sim, R. B., and Day, A. J. (2006) H384 allotypic variant of factor H associated with age-related macular degeneration has different heparin-binding properties from the non-disease-associated form J. Biol. Chem. 281, 24713-24720
    • (2006) J. Biol. Chem. , vol.281 , pp. 24713-24720
    • Clark, S.J.1    Higman, V.A.2    Mulloy, B.3    Perkins, S.J.4    Lea, S.M.5    Sim, R.B.6    Day, A.J.7
  • 65
    • 0026044042 scopus 로고
    • Localization of the heparin-binding site on complement factor H
    • Pangburn, M. K., Atkinson, M. A., and Meri, S. (1991) Localization of the heparin-binding site on complement factor H J. Biol. Chem. 266, 16847-16853
    • (1991) J. Biol. Chem. , vol.266 , pp. 16847-16853
    • Pangburn, M.K.1    Atkinson, M.A.2    Meri, S.3
  • 67
    • 33750336175 scopus 로고    scopus 로고
    • Critical role of the C-terminal domains of factor H in regulating complement activation at cell surfaces
    • Ferreira, V. P., Herbert, A. P., Hocking, H. G., Barlow, P. N., and Pangburn, M. K. (2006) Critical role of the C-terminal domains of factor H in regulating complement activation at cell surfaces J. Immunol. 177, 6308-6316
    • (2006) J. Immunol. , vol.177 , pp. 6308-6316
    • Ferreira, V.P.1    Herbert, A.P.2    Hocking, H.G.3    Barlow, P.N.4    Pangburn, M.K.5
  • 68
    • 22644433305 scopus 로고    scopus 로고
    • Complement escape of human pathogenic bacteria by acquisition of complement regulators
    • Kraiczy, P. and Wurzner, R. (2006) Complement escape of human pathogenic bacteria by acquisition of complement regulators Mol. Immunol. 43, 31-44
    • (2006) Mol. Immunol. , vol.43 , pp. 31-44
    • Kraiczy, P.1    Wurzner, R.2
  • 71
    • 0033214998 scopus 로고    scopus 로고
    • Regulation of complement activation by C-reactive protein: Targeting the complement inhibitory activity of factor H by an interaction with short consensus repeat domains 7 and 8-11
    • Jarva, H., Jokiranta, T. S., Hellwage, J., Zipfel, P. F., and Meri, S. (1999) Regulation of complement activation by C-reactive protein: Targeting the complement inhibitory activity of factor H by an interaction with short consensus repeat domains 7 and 8-11 J. Immunol. 163, 3957-3962
    • (1999) J. Immunol. , vol.163 , pp. 3957-3962
    • Jarva, H.1    Jokiranta, T.S.2    Hellwage, J.3    Zipfel, P.F.4    Meri, S.5
  • 73
    • 58849092356 scopus 로고    scopus 로고
    • Binding of the long pentraxin PTX3 to factor H: Interacting domains and function in the regulation of complement activation
    • Deban, L., Jarva, H., Lehtinen, M. J., Bottazzi, B., Bastone, A., Doni, A., Jokiranta, T. S., Mantovani, A., and Meri, S. (2008) Binding of the long pentraxin PTX3 to factor H: Interacting domains and function in the regulation of complement activation J. Immunol. 181, 8433-8440
    • (2008) J. Immunol. , vol.181 , pp. 8433-8440
    • Deban, L.1    Jarva, H.2    Lehtinen, M.J.3    Bottazzi, B.4    Bastone, A.5    Doni, A.6    Jokiranta, T.S.7    Mantovani, A.8    Meri, S.9
  • 77
    • 35348980673 scopus 로고    scopus 로고
    • C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack
    • Trouw, L. A., Bengtsson, A. A., Gelderman, K. A., Dahlback, B., Sturfelt, G., and Blom, A. M. (2007) C4b-binding protein and factor H compensate for the loss of membrane-bound complement inhibitors to protect apoptotic cells against excessive complement attack J. Biol. Chem. 282, 28540-28548
    • (2007) J. Biol. Chem. , vol.282 , pp. 28540-28548
    • Trouw, L.A.1    Bengtsson, A.A.2    Gelderman, K.A.3    Dahlback, B.4    Sturfelt, G.5    Blom, A.M.6
  • 78
    • 0034613686 scopus 로고    scopus 로고
    • C-Reactive protein binds to apoptotic cells, protects the cells from assembly of the terminal complement components, and sustains an antiinflammatory innate immune response: Implications for systemic autoimmunity
    • Gershov, D., Kim, S., Brot, N., and Elkon, K. B. (2000) C-Reactive protein binds to apoptotic cells, protects the cells from assembly of the terminal complement components, and sustains an antiinflammatory innate immune response: Implications for systemic autoimmunity J. Exp. Med. 192, 1353-1364
    • (2000) J. Exp. Med. , vol.192 , pp. 1353-1364
    • Gershov, D.1    Kim, S.2    Brot, N.3    Elkon, K.B.4
  • 79
    • 37349123478 scopus 로고    scopus 로고
    • Implications of the progressive self-association of wild-type human factor H for complement regulation and disease
    • Nan, R., Gor, J., and Perkins, S. J. (2008) Implications of the progressive self-association of wild-type human factor H for complement regulation and disease J. Mol. Biol. 375, 891-900
    • (2008) J. Mol. Biol. , vol.375 , pp. 891-900
    • Nan, R.1    Gor, J.2    Perkins, S.J.3
  • 80
    • 67651095769 scopus 로고    scopus 로고
    • Electrostatic interactions contribute to the folded-back conformation of wild type human factor H
    • Okemefuna, A. I., Nan, R., Gor, J., and Perkins, S. J. (2009) Electrostatic interactions contribute to the folded-back conformation of wild type human factor H J. Mol. Biol. 391, 98-118
    • (2009) J. Mol. Biol. , vol.391 , pp. 98-118
    • Okemefuna, A.I.1    Nan, R.2    Gor, J.3    Perkins, S.J.4
  • 81
    • 56949096518 scopus 로고    scopus 로고
    • Uncontrolled zinc- and copper-induced oligomerisation of the human complement regulator factor H and its possible implications for function and disease
    • Nan, R., Gor, J., Lengyel, I., and Perkins, S. J. (2008) Uncontrolled zinc- and copper-induced oligomerisation of the human complement regulator factor H and its possible implications for function and disease J. Mol. Biol. 384, 1341-1352
    • (2008) J. Mol. Biol. , vol.384 , pp. 1341-1352
    • Nan, R.1    Gor, J.2    Lengyel, I.3    Perkins, S.J.4
  • 82
    • 84862183665 scopus 로고    scopus 로고
    • Bivalent and co-operative binding of complement factor H to heparan sulfate and heparin
    • Khan, S., Nan, R., Gor, J., Mulloy, B., and Perkins, S. J. (2012) Bivalent and co-operative binding of complement factor H to heparan sulfate and heparin Biochem. J. 444, 417-428
    • (2012) Biochem. J. , vol.444 , pp. 417-428
    • Khan, S.1    Nan, R.2    Gor, J.3    Mulloy, B.4    Perkins, S.J.5
  • 84
    • 0037396993 scopus 로고    scopus 로고
    • Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome
    • Manuelian, T., Hellwage, J., Meri, S., Caprioli, J., Noris, M., Heinen, S., Jozsi, M., Neumann, H. P., Remuzzi, G., and Zipfel, P. F. (2003) Mutations in factor H reduce binding affinity to C3b and heparin and surface attachment to endothelial cells in hemolytic uremic syndrome J. Clin. Invest. 111, 1181-1190
    • (2003) J. Clin. Invest. , vol.111 , pp. 1181-1190
    • Manuelian, T.1    Hellwage, J.2    Meri, S.3    Caprioli, J.4    Noris, M.5    Heinen, S.6    Jozsi, M.7    Neumann, H.P.8    Remuzzi, G.9    Zipfel, P.F.10
  • 86
    • 0037795620 scopus 로고    scopus 로고
    • Release of endogenous anti-inflammatory complement regulators FHL-1 and factor H protects synovial fibroblasts during rheumatoid arthritis
    • Friese, M. A., Manuelian, T., Junnikkala, S., Hellwage, J., Meri, S., Peter, H. H., Gordon, D. L., Eibel, H., and Zipfel, P. F. (2003) Release of endogenous anti-inflammatory complement regulators FHL-1 and factor H protects synovial fibroblasts during rheumatoid arthritis Clin. Exp. Immunol. 132, 485-495
    • (2003) Clin. Exp. Immunol. , vol.132 , pp. 485-495
    • Friese, M.A.1    Manuelian, T.2    Junnikkala, S.3    Hellwage, J.4    Meri, S.5    Peter, H.H.6    Gordon, D.L.7    Eibel, H.8    Zipfel, P.F.9
  • 88
    • 1642518600 scopus 로고    scopus 로고
    • Attachment of the soluble complement regulator factor H to cell and tissue surfaces: Relevance for pathology
    • Jozsi, M., Manuelian, T., Heinen, S., Oppermann, M., and Zipfel, P. F. (2004) Attachment of the soluble complement regulator factor H to cell and tissue surfaces: relevance for pathology Histol. Histopathol. 19, 251-258
    • (2004) Histol. Histopathol. , vol.19 , pp. 251-258
    • Jozsi, M.1    Manuelian, T.2    Heinen, S.3    Oppermann, M.4    Zipfel, P.F.5
  • 89
    • 33846911766 scopus 로고    scopus 로고
    • The C-terminus of complement factor H is essential for host cell protection
    • Jozsi, M., Oppermann, M., Lambris, J. D., and Zipfel, P. F. (2007) The C-terminus of complement factor H is essential for host cell protection Mol. Immunol. 44, 2697-2706
    • (2007) Mol. Immunol. , vol.44 , pp. 2697-2706
    • Jozsi, M.1    Oppermann, M.2    Lambris, J.D.3    Zipfel, P.F.4
  • 90
    • 80053025476 scopus 로고    scopus 로고
    • Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings
    • Maciejewski, M., Tjandra, N., and Barlow, P. N. (2011) Estimation of interdomain flexibility of N-terminus of factor H using residual dipolar couplings Biochemistry 50, 8138-8149
    • (2011) Biochemistry , vol.50 , pp. 8138-8149
    • Maciejewski, M.1    Tjandra, N.2    Barlow, P.N.3
  • 91
    • 81755172091 scopus 로고    scopus 로고
    • Use of time-resolved FRET to validate crystal structure of complement regulatory complex between C3b and factor H (N terminus)
    • Pechtl, I. C., Neely, R. K., Dryden, D. T., Jones, A. C., and Barlow, P. N. (2011) Use of time-resolved FRET to validate crystal structure of complement regulatory complex between C3b and factor H (N terminus) Protein Sci. 20, 2102-2112
    • (2011) Protein Sci. , vol.20 , pp. 2102-2112
    • Pechtl, I.C.1    Neely, R.K.2    Dryden, D.T.3    Jones, A.C.4    Barlow, P.N.5
  • 92
    • 79953190798 scopus 로고    scopus 로고
    • Disease-associated N-terminal complement factor H mutations perturb cofactor and decay-accelerating activities
    • Pechtl, I. C., Kavanagh, D., McIntosh, N., Harris, C. L., and Barlow, P. N. (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
  • 94
    • 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, R. S., Lambris, J. D., and 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
  • 96
    • 0021346086 scopus 로고
    • Residual hemolytic and proteolytic activity expressed by Bb after decay-dissociation of C3b,Bb
    • Fishelson, Z. and Muller-Eberhard, H. J. (1984) Residual hemolytic and proteolytic activity expressed by Bb after decay-dissociation of C3b,Bb J. Immunol. 132, 1425-1429
    • (1984) J. Immunol. , vol.132 , pp. 1425-1429
    • Fishelson, Z.1    Muller-Eberhard, H.J.2
  • 99
    • 84934437828 scopus 로고    scopus 로고
    • Disease-associated sequence variations in factor H: A structural biology approach
    • Herbert, A. P., Soares, D. C., Pangburn, M. K., and Barlow, P. N. (2006) Disease-associated sequence variations in factor H: A structural biology approach Adv. Exp. Med. Biol. 586, 313-327
    • (2006) Adv. Exp. Med. Biol. , vol.586 , pp. 313-327
    • Herbert, A.P.1    Soares, D.C.2    Pangburn, M.K.3    Barlow, P.N.4
  • 101
    • 33947593444 scopus 로고    scopus 로고
    • Associative and structural properties of the region of complement factor H encompassing the Tyr402His disease-related polymorphism and its interactions with heparin
    • Fernando, A. N., Furtado, P. B., Clark, S. J., Gilbert, H. E., Day, A. J., Sim, R. B., and Perkins, S. J. (2007) Associative and structural properties of the region of complement factor H encompassing the Tyr402His disease-related polymorphism and its interactions with heparin J. Mol. Biol. 368, 564-581
    • (2007) J. Mol. Biol. , vol.368 , pp. 564-581
    • Fernando, A.N.1    Furtado, P.B.2    Clark, S.J.3    Gilbert, H.E.4    Day, A.J.5    Sim, R.B.6    Perkins, S.J.7
  • 103
    • 84875990477 scopus 로고    scopus 로고
    • Complement in immune and inflammatory disorders: Therapeutic interventions
    • Ricklin, D. and Lambris, J. D. (2013) 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
  • 104
    • 84934440020 scopus 로고    scopus 로고
    • Progress and trends in complement therapeutics
    • Ricklin, D. and Lambris, J. D. (2013) Progress and trends in complement therapeutics Adv. Exp. Med. Biol. 734, 1-22
    • (2013) Adv. Exp. Med. Biol. , vol.734 , pp. 1-22
    • Ricklin, D.1    Lambris, J.D.2
  • 105
    • 84874660903 scopus 로고    scopus 로고
    • Intravitreal human complement factor H in a rat model of laser-induced choroidal neovascularisation
    • Kim, S. J., Kim, J., Lee, J., Cho, S. Y., Kang, H. J., Kim, K. Y., and Jin, D. K. (2013) Intravitreal human complement factor H in a rat model of laser-induced choroidal neovascularisation Br. J. Ophthalmol. 97, 367-370
    • (2013) Br. J. Ophthalmol. , vol.97 , pp. 367-370
    • Kim, S.J.1    Kim, J.2    Lee, J.3    Cho, S.Y.4    Kang, H.J.5    Kim, K.Y.6    Jin, D.K.7
  • 106
    • 0033516648 scopus 로고    scopus 로고
    • A cluster of positively charged amino acids in the C4BP α-chain is crucial for C4b binding and factor i cofactor function
    • Blom, A. M., Webb, J., Villoutreix, B. O., and Dahlback, B. (1999) A cluster of positively charged amino acids in the C4BP α-chain is crucial for C4b binding and factor I cofactor function J. Biol. Chem. 274, 19237-19245
    • (1999) J. Biol. Chem. , vol.274 , pp. 19237-19245
    • Blom, A.M.1    Webb, J.2    Villoutreix, B.O.3    Dahlback, B.4
  • 107
    • 0035920160 scopus 로고    scopus 로고
    • Structural requirements for the complement regulatory activities of C4BP
    • Blom, A. M., Kask, L., and Dahlback, B. (2001) Structural requirements for the complement regulatory activities of C4BP J. Biol. Chem. 276, 27136-27144
    • (2001) J. Biol. Chem. , vol.276 , pp. 27136-27144
    • Blom, A.M.1    Kask, L.2    Dahlback, B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.