메뉴 건너뛰기




Volumn 69, Issue , 1998, Pages 249-307

The atypical serine proteases of the complement system

Author keywords

[No Author keywords available]

Indexed keywords

COMPLEMENT; SERINE PROTEINASE;

EID: 0031804633     PISSN: 00652776     EISSN: None     Source Type: Book Series    
DOI: None     Document Type: Review
Times cited : (47)

References (220)
  • 1
    • 0024412763 scopus 로고
    • Structure and function of the complement receptors CR1 (CD35) and CR2 (CD21)
    • Ahearn, J. M., and Fearon, D. T. (1989). Structure and function of the complement receptors CR1 (CD35) and CR2 (CD21). Adv. Immunol. 46, 183-219.
    • (1989) Adv. Immunol. , vol.46 , pp. 183-219
    • Ahearn, J.M.1    Fearon, D.T.2
  • 2
    • 0019731550 scopus 로고
    • Clr and Cls subcomponents of human complement: Two serine proteinases lacking the "histidine loop" disulphide bridge
    • Arlaud, G. J., and Gagnon, J. (1981). Clr and Cls subcomponents of human complement: two serine proteinases lacking the "histidine loop" disulphide bridge. Biosci. Rep. 1, 779-784.
    • (1981) Biosci. Rep. , vol.1 , pp. 779-784
    • Arlaud, G.J.1    Gagnon, J.2
  • 3
    • 0020582458 scopus 로고
    • Complete amino acid sequence of the catalytic chain of human complement subcomponent Clr
    • Arlaud, G. J., and Gagnon, J. (1983). Complete amino acid sequence of the catalytic chain of human complement subcomponent Clr. Biochemistry 22, 1758-1764.
    • (1983) Biochemistry , vol.22 , pp. 1758-1764
    • Arlaud, G.J.1    Gagnon, J.2
  • 4
    • 0021933914 scopus 로고
    • Identification of the peptide bond cleaved during activation of human Clr
    • Arlaud, G. J., and Gagnon, J. (1985). Identification of the peptide bond cleaved during activation of human Clr. FEBS Lett. 180, 234-238.
    • (1985) FEBS Lett , vol.180 , pp. 234-238
    • Arlaud, G.J.1    Gagnon, J.2
  • 5
    • 0027364982 scopus 로고
    • Human complement serine proteases Clr and Cls and their proenzymes
    • L. Lorand and K. G. Mann, eds.).. Academic Press, San Diego, CA
    • Arlaud, G. J., and Thielens, N. M. (1993). Human complement serine proteases Clr and Cls and their proenzymes. In "Methods in Enzymology" (L. Lorand and K. G. Mann, eds.). Vol. 223, pp. 61-82. Academic Press, San Diego, CA.
    • (1993) Methods in Enzymology , vol.223 , pp. 61-82
    • Arlaud, G.J.1    Thielens, N.M.2
  • 6
    • 0022870658 scopus 로고
    • Molecular characterization of the catalytic domains of human complement serine protease Clr
    • Arlaud, G. J., Gagnon, J., Villiers, C. L., and Colomb, M. G. (1986). Molecular characterization of the catalytic domains of human complement serine protease Clr. Biochemistry 25, 5177-5182.
    • (1986) Biochemistry , vol.25 , pp. 5177-5182
    • Arlaud, G.J.1    Gagnon, J.2    Villiers, C.L.3    Colomb, M.G.4
  • 7
    • 0023114358 scopus 로고
    • Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme Clr
    • Arlaud, G. J., Willis, A. C, and Gagnon, J. (1987a). Complete amino acid sequence of the A chain of human complement-classical-pathway enzyme Clr. Biochem. J. 241, 711-720.
    • (1987) Biochem. J. , vol.241 , pp. 711-720
    • Arlaud, G.J.1    Willis, A.C.2    Gagnon, J.3
  • 8
    • 0023137465 scopus 로고
    • A functional model of the human CI complex
    • Arlaud, G. J., Colomb, M. G., and Gagnon, J. (1987b). A functional model of the human CI complex. Immunol. Today 8, 106-111.
    • (1987) Immunol. Today , vol.8 , pp. 106-111
    • Arlaud, G.J.1    Colomb, M.G.2    Gagnon, J.3
  • 9
    • 0023638695 scopus 로고
    • Identification of erythro-β-hydroxyasparagine in the EGF-like domain of human Clr
    • Arlaud, G. J., van Dorsselaer, A., Bell, M., Mancini, A., Aude, C, and Gagnon, J. (1987c). Identification of erythro-β-hydroxyasparagine in the EGF-like domain of human Clr. FEBS Lett. 222, 129-134.
    • (1987) FEBS Lett , vol.222 , pp. 129-134
    • Arlaud, G.J.1    van Dorsselaer, A.2    Bell, M.3    Mancini, A.4    Aude, C.5    Gagnon, J.6
  • 10
    • 0026058727 scopus 로고
    • The lymphocyte glycoprotein CD6 contains a repeated domain structure characteristic of a new family of cell surface and secreted proteins
    • Aruffo, A., Melnick, M. B., Linsley, P. S., and Seed, B. (1991). The lymphocyte glycoprotein CD6 contains a repeated domain structure characteristic of a new family of cell surface and secreted proteins. J. Exp. Med. 174, 949-952.
    • (1991) J. Exp. Med. , vol.174 , pp. 949-952
    • Aruffo, A.1    Melnick, M.B.2    Linsley, P.S.3    Seed, B.4
  • 11
    • 0025985784 scopus 로고
    • Transcriptional termination between the closely linked human complement genes C2 and factor B: Common termination factor for C2 and c-myc?
    • Ashfield, R., Enriquez-Harris, P., and Proudfoot, N. J. (1991). Transcriptional termination between the closely linked human complement genes C2 and factor B: Common termination factor for C2 and c-myc? EMBO J. 10, 4197-4207.
    • (1991) EMBO J , vol.10 , pp. 4197-4207
    • Ashfield, R.1    Enriquez-Harris, P.2    Proudfoot, N.J.3
  • 12
    • 33947094423 scopus 로고
    • Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of α-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases
    • Bachovchin, W. W., and Roberts, J. D. (1978). Nitrogen-15 nuclear magnetic resonance spectroscopy. The state of histidine in the catalytic triad of α-lytic protease. Implications for the charge-relay mechanism of peptide-bond cleavage by serine proteases. J. Amer. Chem. Soc. 100, 8041-8047.
    • (1978) J. Amer. Chem. Soc. , vol.100 , pp. 8041-8047
    • Bachovchin, W.W.1    Roberts, J.D.2
  • 17
    • 0022467696 scopus 로고
    • Primary structure of human complement component C2: Homology to two unrelated protein families
    • Bentley, D. R. (1986). Primary structure of human complement component C2: Homology to two unrelated protein families. Biochem. J. 239, 339-345.
    • (1986) Biochem. J. , vol.239 , pp. 339-345
    • Bentley, D.R.1
  • 18
    • 0032477892 scopus 로고    scopus 로고
    • Solution structure of the epidermal growth factor-like module of human complement protease Clr, an atypical member of the EGF family
    • Bersch, B., Hernandez, J.-F., Marion, D., and Arlaud, G. J. (1998). Solution structure of the epidermal growth factor-like module of human complement protease Clr, an atypical member of the EGF family. Biochemistry 37, 1204-1214.
    • (1998) Biochemistry , vol.37 , pp. 1204-1214
    • Bersch, B.1    Hernandez, J.-F.2    Marion, D.3    Arlaud, G.J.4
  • 19
    • 0015518520 scopus 로고
    • Structure of crystalline α-chymotrypsin. V. The atomic structure of tosyl-α-chymotrypsin at 2.0 Å resolution
    • Birktoft, J. J., and Blow, D. M., (1972). Structure of crystalline α-chymotrypsin. V. The atomic structure of tosyl-α-chymotrypsin at 2.0 Å resolution. J. Mol. Biol. 68, 187-240.
    • (1972) J. Mol. Biol. , vol.68 , pp. 187-240
    • Birktoft, J.J.1    Blow, D.M.2
  • 20
    • 0014689979 scopus 로고
    • Role of a buried acid group in the mechanism of action of chymotrypsin
    • Blow, D. M., Birktoft, J. J., and Hartley, B. S. (1969). Role of a buried acid group in the mechanism of action of chymotrypsin. Nature (London) 221, 337-340.
    • (1969) Nature (London) , vol.221 , pp. 337-340
    • Blow, D.M.1    Birktoft, J.J.2    Hartley, B.S.3
  • 21
    • 0025809960 scopus 로고
    • Complement components Clr/Cls, bone morphogenetic protein 1 and Xenopus laevis developmentally regulated protein UVS.2 share common repeats
    • Bork, P. (1991). Complement components Clr/Cls, bone morphogenetic protein 1 and Xenopus laevis developmentally regulated protein UVS.2 share common repeats. FEBS Lett. 282, 9-12.
    • (1991) FEBS Lett , vol.282 , pp. 9-12
    • Bork, P.1
  • 22
    • 0003338119 scopus 로고
    • Extracellular protein modules: A proposed nomenclature
    • March
    • Bork, P., and Bairoch, A. (1995). Extracellular protein modules: A proposed nomenclature. Trends Biochem. Sci. 20, (Suppl. March), C03.
    • (1995) Trends Biochem. Sci. , vol.20 , pp. C03
    • Bork, P.1    Bairoch, A.2
  • 23
    • 0027190974 scopus 로고
    • The CUB domain. A widespread module in developmentally regulated proteins
    • Bork, P., and Beckmann, G. (1993). The CUB domain. A widespread module in developmentally regulated proteins. J. Mol. Biol. 231, 539-545.
    • (1993) J. Mol. Biol. , vol.231 , pp. 539-545
    • Bork, P.1    Beckmann, G.2
  • 24
    • 0029777325 scopus 로고    scopus 로고
    • Structure and distribution of modules in extracellular proteins
    • Bork, P., Downing, A. K. Kieffer, B., and Campbell, I. D. (1996). Structure and distribution of modules in extracellular proteins. Q. Rev. Biophys. 29, 119-167.
    • (1996) Q. Rev. Biophys. , vol.29 , pp. 119-167
    • Bork, P.1    Downing, A.K.2    Kieffer, B.3    Campbell, I.D.4
  • 25
    • 0026687735 scopus 로고
    • MAZ, a zinc finger protein, binds to c-MYC and C2 gene sequences regulating transcriptional initiation and termination
    • Bossone, S. A., Asselin, C, Patel, A. J., and Marcu, K. B. (1992). MAZ, a zinc finger protein, binds to c-MYC and C2 gene sequences regulating transcriptional initiation and termination. Proc. Natl. Acad. Sci. U. S.A. 89, 7452-7456.
    • (1992) Proc. Natl. Acad. Sci. U. S.A. , vol.89 , pp. 7452-7456
    • Bossone, S.A.1    Asselin, C.2    Patel, A.J.3    Marcu, K.B.4
  • 27
    • 0023213305 scopus 로고
    • Calcium-sensitive transitions and domain structure of human complement subcomponent Clr
    • Busby, T. F., and Ingham, K. C. (1987). Calcium-sensitive transitions and domain structure of human complement subcomponent Clr. Biochemistry 26, 5564-5571.
    • (1987) Biochemistry , vol.26 , pp. 5564-5571
    • Busby, T.F.1    Ingham, K.C.2
  • 28
    • 0023718612 scopus 로고
    • Domain structure, stability, and interactions of human complement Cls: Characterization of a derivative lacking most of the B chain
    • Busby, T. F., and Ingham, K. C. (1988). Domain structure, stability, and interactions of human complement Cls: Characterization of a derivative lacking most of the B chain. Biochemistry 27, 6127-6135.
    • (1988) Biochemistry , vol.27 , pp. 6127-6135
    • Busby, T.F.1    Ingham, K.C.2
  • 29
    • 0025193491 scopus 로고
    • 2-terminal calcium-binding domain of human complement Cls mediates the interaction of Clr with Clq
    • 2-terminal calcium-binding domain of human complement Cls mediates the interaction of Clr with Clq. Biochemistry 29,4613-4618.
    • (1990) Biochemistry , vol.29 , pp. 4613-4618
    • Busby, T.F.1    Ingham, K.C.2
  • 30
    • 0022270721 scopus 로고
    • The structure and genetics of the C2 and factor B genes
    • Campbell, R. D., and Bentley, D. R. (1985). The structure and genetics of the C2 and factor B genes. Immunol. Rev. 87, 19-37.
    • (1985) Immunol. Rev. , vol.87 , pp. 19-37
    • Campbell, R.D.1    Bentley, D.R.2
  • 31
  • 32
    • 0021154191 scopus 로고
    • A molecular map of die human major histocompatibility complex class III region linking complement genes C4, C2, and factor B
    • Carroll, M. C, Campbell, R. D., Bentley, D. R., and Porter, R. R. (1984). A molecular map of die human major histocompatibility complex class III region linking complement genes C4, C2, and factor B. Nature (London) 307, 237-241.
    • (1984) Nature (London) , vol.307 , pp. 237-241
    • Carroll, M.C.1    Campbell, R.D.2    Bentley, D.R.3    Porter, R.R.4
  • 34
    • 0021033488 scopus 로고
    • The serine proteinase chain of human complement component Cls
    • Carter, P. E., Dunbar, B., and Fothergill, J. E. (1983). The serine proteinase chain of human complement component Cls. Biochem. J. 215, 565-571.
    • (1983) Biochem. J. , vol.215 , pp. 565-571
    • Carter, P.E.1    Dunbar, B.2    Fothergill, J.E.3
  • 36
    • 0023105043 scopus 로고
    • Characterization of the primary amino acid sequence of human complement control protein Factor I from an analysis of cDNA clones
    • Catterall, C. F., Lyons, A., Sim, R. B., Day, A. J., and Harris, T. J. R. (1987). Characterization of the primary amino acid sequence of human complement control protein Factor I from an analysis of cDNA clones. Biochem. J. 242, 849-856.
    • (1987) Biochem. J. , vol.242 , pp. 849-856
    • Catterall, C.F.1    Lyons, A.2    Sim, R.B.3    Day, A.J.4    Harris, T.J.R.5
  • 37
    • 0019873323 scopus 로고
    • Refined crystal structure of γchymotrypsin at 1.9 Å resolution. Comparison with other pancreatic serine proteases
    • Cohen, G. H., Silverton, E. W., and Davies, D. R. (1981). Refined crystal structure of γchymotrypsin at 1.9 Å resolution. Comparison with other pancreatic serine proteases. J. Mol. Biol. 148, 449-479.
    • (1981) J. Mol. Biol. , vol.148 , pp. 449-479
    • Cohen, G.H.1    Silverton, E.W.2    Davies, D.R.3
  • 39
    • 0025807693 scopus 로고
    • The superfamily of proteins with von Willebrand factor type A-like domains: One theme common to components of extracellular matrix, hemostasis, cellular adhesion, and defense mechanisms
    • Colombatti, A., and Bonaldo, P. (1991). The superfamily of proteins with von Willebrand factor type A-like domains: One theme common to components of extracellular matrix, hemostasis, cellular adhesion, and defense mechanisms. Blood 77, 2305-2315.
    • (1991) Blood , vol.77 , pp. 2305-2315
    • Colombatti, A.1    Bonaldo, P.2
  • 40
    • 0016817486 scopus 로고
    • Enzymatic activity of the second component of complement
    • Cooper, N. R. (1975). Enzymatic activity of the second component of complement. Biochemistry 14, 4245-4251.
    • (1975) Biochemistry , vol.14 , pp. 4245-4251
    • Cooper, N.R.1
  • 41
    • 0021894435 scopus 로고
    • The classical complement pathway: Activation and regulation of the first complement component
    • Cooper, N. R. (1985). The classical complement pathway: activation and regulation of the first complement component. Adv. Immunol. 37, 151-216.
    • (1985) Adv. Immunol. , vol.37 , pp. 151-216
    • Cooper, N.R.1
  • 42
    • 0001090566 scopus 로고    scopus 로고
    • Complement and viruses
    • J. E. Volanakis and M. M. Frank, Eds.),. Dekker, New York
    • Cooper, N. R. (1998). Complement and viruses. In "The Human Complement System in Health and Disease" (J. E. Volanakis and M. M. Frank, Eds.), pp. 393-407. Dekker, New York.
    • (1998) The Human Complement System in Health and Disease , pp. 393-407
    • Cooper, N.R.1
  • 43
    • 0023204278 scopus 로고
    • The catalytic role of the active site aspartic acid in serine proteases
    • Craik, C. S., Roczniak, S., Largman, C, and Rutter, W. J. (1987). The catalytic role of the active site aspartic acid in serine proteases. Science 237 909-913.
    • (1987) Science , vol.237 , pp. 909-913
    • Craik, C.S.1    Roczniak, S.2    Largman, C.3    Rutter, W.J.4
  • 44
    • 0021932877 scopus 로고
    • DNA polymorphism of the C2 and factor B genes. Detection of a restriction fragment length polymorphism which subdivides haplotypes carrying the C2C and factor B F alleles
    • Cross, S. J., Edwards, J. H., Bentley, D. R., and Campbell, R. D. (1985). DNA polymorphism of the C2 and factor B genes. Detection of a restriction fragment length polymorphism which subdivides haplotypes carrying the C2C and factor B F alleles. Immunogenetics 21, 39-48.
    • (1985) Immunogenetics , vol.21 , pp. 39-48
    • Cross, S.J.1    Edwards, J.H.2    Bentley, D.R.3    Campbell, R.D.4
  • 46
    • 0029020912 scopus 로고
    • Three-dimensional structure of a cysteine-rich repeat from the low-density-lipoprotein receptor
    • Daly, N., Scanlon, M. J., Djordjevic, J. T., Kroon, P. A., and Smith, R. (1995). Three-dimensional structure of a cysteine-rich repeat from the low-density-lipoprotein receptor. Proc. Natl. Acad. Sci. U.S.A. 92, 6334-6338.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 6334-6338
    • Daly, N.1    Scanlon, M.J.2    Djordjevic, J.T.3    Kroon, P.A.4    Smith, R.5
  • 47
    • 0019868113 scopus 로고
    • The C3b inactivator of the human complement system: Homology with serine proteases
    • Davis, A. E. (1981). The C3b inactivator of the human complement system: Homology with serine proteases. FEBS Lett. 134, 147-150.
    • (1981) FEBS Lett , vol.134 , pp. 147-150
    • Davis, A.E.1
  • 48
    • 0020362094 scopus 로고
    • Structural characterization of factor I mediated cleavage of the third component of complement
    • Davis, A. E., III, and Harrison, R. A. (1982). Structural characterization of factor I mediated cleavage of the third component of complement. Biochemistry 21, 5745-5749.
    • (1982) Biochemistry , vol.21 , pp. 5745-5749
    • Davis, A.E.1    Harrison, R.A.2
  • 49
    • 0027427718 scopus 로고
    • CI inhibitor
    • L. Lorand and K. G. Mann, Eds.),. Academic Press, San Diego, CA
    • Davis, A. E. III, Aulak, K. S., Zahedi, K., Bissler, J. J., and Harrison, R. A. (1993). CI inhibitor. In "Methods in Enzymology, Vol. 223" (L. Lorand and K. G. Mann, Eds.), pp. 97-120. Academic Press, San Diego, CA.
    • (1993) Methods in Enzymology , vol.223 , pp. 97-120
    • Davis, A.E.1    Aulak, K.S.2    Zahedi, K.3    Bissler, J.J.4    Harrison, R.A.5
  • 50
    • 0030896835 scopus 로고    scopus 로고
    • Crystallisation and preliminary X-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture
    • Dias, J. M., Carvalho, A. L., Kölln, I., Calvete, J. J., Töpfer-Petersen, E., Varela, P. F., Romero, A., Urbanke, C., and Romao, M. J. (1997). Crystallisation and preliminary X-ray diffraction studies of aSFP, a bovine seminal plasma protein with a single CUB domain architecture. Protein Sci. 6, 725-727.
    • (1997) Protein Sci , vol.6 , pp. 725-727
    • Dias, J.M.1    Carvalho, A.L.2    Kölln, I.3    Calvete, J.J.4    Töpfer-Petersen, E.5    Varela, P.F.6    Romero, A.7    Urbanke, C.8    Romao, M.J.9
  • 51
    • 0026785372 scopus 로고
    • Formation and structure of the C5b-7 complex of the lytic pathway of complement
    • DiScipio, R. G. (1992). Formation and structure of the C5b-7 complex of the lytic pathway of complement. J. Biol. Chem. 267, 17087-17094.
    • (1992) J. Biol. Chem. , vol.267 , pp. 17087-17094
    • DiScipio, R.G.1
  • 54
    • 0029006062 scopus 로고
    • The multiplicity of domains in proteins
    • Doolittle, R. F. (1995). The multiplicity of domains in proteins. Annu. Rev. Biochem. 64, 287-314.
    • (1995) Annu. Rev. Biochem. , vol.64 , pp. 287-314
    • Doolittle, R.F.1
  • 55
    • 0030000090 scopus 로고    scopus 로고
    • Solution structure of a pair of calcium-binding epidermal growth factorlike domains: Implications for the marfan syndrome and other genetic disorders
    • Downing, A. K., Knott, V.,Werner, J. M., Cardy, C. M., Campbell, I. D., and Handford, P. A. (1996). Solution structure of a pair of calcium-binding epidermal growth factorlike domains: implications for the marfan syndrome and other genetic disorders. Cell (Cambridge, Moss.) 85, 597-605.
    • (1996) Cell (Cambridge, Moss.) , vol.85 , pp. 597-605
    • Downing, A.K.1    Knott, V.2    Werner, J.M.3    Cardy, C.M.4    Campbell, I.D.5    Handford, P.A.6
  • 56
    • 0023430773 scopus 로고
    • Molecular mapping of the human major histocompatibility complex by pulsed-field gel electrophoresis
    • Dunham, I, Sargent, C. A., Trowsdale, J., and Campbell, R. D. (1987). Molecular mapping of the human major histocompatibility complex by pulsed-field gel electrophoresis. Proc. Natl. Acad. Sci. U.S.A. 84, 7237-7241.
    • (1987) Proc. Natl. Acad. Sci. U.S.A. , vol.84 , pp. 7237-7241
    • Dunham, I.1    Sargent, C.A.2    Trowsdale, J.3    Campbell, R.D.4
  • 57
    • 0029059228 scopus 로고
    • Identification of amino acids in the C D l l a I-domain important for binding of the leukocyte function-associated antigen-1 (LFA-1) to intercellular adhesion molecule-1 (ICAM-1)
    • Edwards, C. P., Champe, M., Gonzales, T., Wessinger, M. E., Spencer, S. A., Presta, L. G., Berman, P. W., and Bodary, S. C. (1995). Identification of amino acids in the C D l l a I-domain important for binding of the leukocyte function-associated antigen-1 (LFA-1) to intercellular adhesion molecule-1 (ICAM-1). J. Biol. Chem. 270,12635-12640.
    • (1995) J. Biol. Chem. , vol.270 , pp. 12635-12640
    • Edwards, C.P.1    Champe, M.2    Gonzales, T.3    Wessinger, M.E.4    Spencer, S.A.5    Presta, L.G.6    Berman, P.W.7    Bodary, S.C.8
  • 58
    • 0029837728 scopus 로고    scopus 로고
    • Exon structure of the gene encoding the human mannose-binding protein-associated serine protease (MASP) light chain: Comparison with complement Clr and Cls genes
    • Endo, Y., Sato, T., Matsushita, M., and Fujita, T. (1996). Exon structure of the gene encoding the human mannose-binding protein-associated serine protease (MASP) light chain: Comparison with complement Clr and Cls genes. Int. Immunol. 9, 1355-1358.
    • (1996) Int. Immunol. , vol.9 , pp. 1355-1358
    • Endo, Y.1    Sato, T.2    Matsushita, M.3    Fujita, T.4
  • 59
    • 0025044614 scopus 로고
    • Proteolysis of the heavy chain of major histocompatibility complex class I antigens by complement component Cls
    • Eriksson, H.,and Nissen, M. H.(1990). Proteolysis of the heavy chain of major histocompatibility complex class I antigens by complement component Cls. Biochim. Biophys. Acta 1037, 209-215.
    • (1990) Biochim. Biophys. Acta , vol.1037 , pp. 209-215
    • Eriksson, H.1    Nissen, M.H.2
  • 60
    • 0025187838 scopus 로고
    • Substrate specificity of trypsin investigated by using a genetic selection
    • Evnin L. B., Vasquez, J. R., and Craik, C. S. (1990). Substrate specificity of trypsin investigated by using a genetic selection. Proc. Natl. Acad. Sci. U.S.A. 87, 6659-6663.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 6659-6663
    • Evnin, L.B.1    Vasquez, J.R.2    Craik, C.S.3
  • 61
    • 0017348682 scopus 로고
    • Crystal structure of bovine trypsinogen at 1.8 A resolution. II. Crystallographic refinement, refined crystal structure, and comparison with bovine trypsin
    • Fehlhammer, H., Bode, W., and Huber, R. (1977). Crystal structure of bovine trypsinogen at 1.8 A resolution. II. Crystallographic refinement, refined crystal structure, and comparison with bovine trypsin. J. Mol. Biol. 111, 414-438.
    • (1977) J. Mol. Biol. , vol.111 , pp. 414-438
    • Fehlhammer, H.1    Bode, W.2    Huber, R.3
  • 62
    • 0021346086 scopus 로고
    • Residual hemolytic and proteolytic activity expressed by Bb after decay-dissociation of C3b,Bb
    • Fishelson, Z., and Miiller-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    Miiller-Eberhard, H.J.2
  • 63
    • 0020959282 scopus 로고
    • C3-convertase of the alternative complement pathway. Demonstration of an active, stable C3b, Bb (Ni) complex
    • Fishelson, Z., Pangburn, M. K., and Miiller-Eberhard, H. J. (1983). C3-convertase of the alternative complement pathway. Demonstration of an active, stable C3b, Bb (Ni) complex. J. Biol. Chem. 258, 7411-7415.
    • (1983) J. Biol. Chem. , vol.258 , pp. 7411-7415
    • Fishelson, Z.1    Pangburn, M.K.2    Miiller-Eberhard, H.J.3
  • 64
    • 0024317404 scopus 로고
    • The structures of human Clr and Cls and their relationship to other serine proteases
    • Fothergill, J. E., Kemp, G., Paton, N., Carter, P., and Gray, P. (1989). The structures of human Clr and Cls and their relationship to other serine proteases. Behring Inst. Mitt. 84, 72-79.
    • (1989) Behring Inst. Mitt. , vol.84 , pp. 72-79
    • Fothergill, J.E.1    Kemp, G.2    Paton, N.3    Carter, P.4    Gray, P.5
  • 65
    • 0025253834 scopus 로고
    • An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors
    • Freeman, M., Ashkenas, J., Rees, D. J. G., Kingsley, D. M., Copeland, N. G., Jenkins, N. A., and Krieger, M. (1990). An ancient, highly conserved family of cysteine-rich protein domains revealed by cloning type I and type II murine macrophage scavenger receptors. Proc. Natl. Acad. Sci. U.S.A. 87, 8810-8814.
    • (1990) Proc. Natl. Acad. Sci. U.S.A. , vol.87 , pp. 8810-8814
    • Freeman, M.1    Ashkenas, J.2    Rees, D.J.G.3    Kingsley, D.M.4    Copeland, N.G.5    Jenkins, N.A.6    Krieger, M.7
  • 66
    • 0018073707 scopus 로고
    • Human C4-binding protein. II. Role in proteolysis of C4b by C3b-inactivator
    • Fujita, T., Gigli, I., and Nussenzweig, V. (1978). Human C4-binding protein. II. Role in proteolysis of C4b by C3b-inactivator. J. Exp. Med. 148, 1044-1051.
    • (1978) J. Exp. Med. , vol.148 , pp. 1044-1051
    • Fujita, T.1    Gigli, I.2    Nussenzweig, V.3
  • 67
    • 0021164865 scopus 로고
    • Biosynthesis and postsynthetic processing of human C3b/C4b inactivator (Factor I) in three hepatoma cell lines
    • Goldberger, G., Amaout, M. A., Aden, D., Kay, R., Rits, M., and Colten. H. R. (1984). Biosynthesis and postsynthetic processing of human C3b/C4b inactivator (Factor I) in three hepatoma cell lines. J. Biol. Chem. 259, 6492-6497.
    • (1984) J. Biol. Chem. , vol.259 , pp. 6492-6497
    • Goldberger, G.1    Amaout, M.A.2    Aden, D.3    Kay, R.4    Rits, M.5    Colten, H.R.6
  • 68
    • 0023250642 scopus 로고
    • Human complement factor I: Analysis of cDNA-derived primary structure and assignment of its gene to chromosome 4
    • Goldberger, G., Bruns, G. A. P., Rits, M., Edge, M. D., and Kwiatkowski, D. J. (1987). Human complement factor I: Analysis of cDNA-derived primary structure and assignment of its gene to chromosome 4. J. Biol. Chem. 262,10065-10071.
    • (1987) J. Biol. Chem. , vol.262 , pp. 10065-10071
    • Goldberger, G.1    Bruns, G.A.P.2    Rits, M.3    Edge, M.D.4    Kwiatkowski, D.J.5
  • 70
    • 0025287330 scopus 로고
    • Comparative modeling methods: Application to the family of the mammalian serine proteases
    • Greer, J. (1990). Comparative modeling methods: Application to the family of the mammalian serine proteases. Proteins Struct. Fund. Genet. 7, 317-334.
    • (1990) Proteins Struct. Fund. Genet. , vol.7 , pp. 317-334
    • Greer, J.1
  • 71
    • 0024448568 scopus 로고
    • Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6
    • Haefliger, J.-A., Tschopp, J., Vial, N., and Jenne, D. E. (1989). Complete primary structure and functional characterization of the sixth component of the human complement system. Identification of the C5b-binding domain in complement C6. J. Biol. Chem. 264,18041-18051.
    • (1989) J. Biol. Chem. , vol.264 , pp. 18041-18051
    • Haefliger, J.-A.1    Tschopp, J.2    Vial, N.3    Jenne, D.E.4
  • 72
    • 0026520387 scopus 로고
    • Converting trypsin to chymotrypsin: The role of surface loops
    • Hedstrom, L., Szilagyi, L., and Rutter, W. J. (1992). Converting trypsin to chymotrypsin: The role of surface loops. Science 255, 1249-1253.
    • (1992) Science , vol.255 , pp. 1249-1253
    • Hedstrom, L.1    Szilagyi, L.2    Rutter, W.J.3
  • 73
    • 0028133496 scopus 로고
    • Converting trypsin to chymotrypsin: Residue 172 is a substrate specificity determinant
    • Hedstrom L, Perona, J. J., and Rutter, W. J. (1994). Converting trypsin to chymotrypsin: Residue 172 is a substrate specificity determinant. Biochemistry 33, 8757-8763.
    • (1994) Biochemistry , vol.33 , pp. 8757-8763
    • Hedstrom, L.1    Perona, J.J.2    Rutter, W.J.3
  • 74
    • 0030975882 scopus 로고    scopus 로고
    • Chemical synthesis and characterization of the epidermal growth factor-like module of human complement protease Clr
    • Hernandez, J.-F., Bersch, B., Petillot, Y., Gagnon, J., and Arlaud, G. J. (1997). Chemical synthesis and characterization of the epidermal growth factor-like module of human complement protease Clr. J. Peptide Bes. 49, 221-231.
    • (1997) J. Peptide Bes. , vol.49 , pp. 221-231
    • Hernandez, J.-F.1    Bersch, B.2    Petillot, Y.3    Gagnon, J.4    Arlaud, G.J.5
  • 75
    • 0025727461 scopus 로고
    • Identification of the disulfide bonds in human complement Cls
    • Hess, D., Schaller, J., and Rickli, E. E. (1991). Identification of the disulfide bonds in human complement Cls. Biochemistry 30, 2827-2833.
    • (1991) Biochemistry , vol.30 , pp. 2827-2833
    • Hess, D.1    Schaller, J.2    Rickli, E.E.3
  • 76
    • 0024514446 scopus 로고
    • CDNA cloning and expression of human complement component C2
    • Horiuchi, T., Macon, K. J., Kidd, V. J., and Volanakis, J. E. (1989). cDNA cloning and expression of human complement component C2. J. Immunol. 142, 2105-2111.
    • (1989) J. Immunol. , vol.142 , pp. 2105-2111
    • Horiuchi, T.1    Macon, K.J.2    Kidd, V.J.3    Volanakis, J.E.4
  • 77
    • 0025895079 scopus 로고
    • Site-directed mutagenesis of the region around Cys-241 of complement component C2: Evidence for a C4bbinding site
    • Horiuchi, T., Macon, K. J., Engler, J. A., and Volanakis, J. E. (1991). Site-directed mutagenesis of the region around Cys-241 of complement component C2: Evidence for a C4bbinding site. J. Immunol. 147, 584-589.
    • (1991) J. Immunol. , vol.147 , pp. 584-589
    • Horiuchi, T.1    Macon, K.J.2    Engler, J.A.3    Volanakis, J.E.4
  • 78
    • 0027139795 scopus 로고
    • Human complement factor B: CDNA cloning, nucleotide sequencing, phenotypic conversion by site-directed mutagenesis, and expression
    • Horiuchi, T., Kim, S., Matsumoto, M„ Watanabe, I., Fujita, S., and Volanakis, J. E. (1993). Human complement factor B: cDNA cloning, nucleotide sequencing, phenotypic conversion by site-directed mutagenesis, and expression. Mol. Immunol. 30, 1587-1592.
    • (1993) Mol. Immunol. , vol.30 , pp. 1587-1592
    • Horiuchi, T.1    Kim, S.2    Matsumoto, M.3    Watanabe, I.4    Fujita, S.5    Volanakis, J.E.6
  • 79
    • 0029086243 scopus 로고
    • Analysis of the short consensus repeats of human complement factor B by site-directed mutagenesis
    • Hourcade, D. E., Wagner, L. M., and Oglesby, T. J. (1995). Analysis of the short consensus repeats of human complement factor B by site-directed mutagenesis. J. Biol. Chem. 270, 19716-19722.
    • (1995) J. Biol. Chem. , vol.270 , pp. 19716-19722
    • Hourcade, D.E.1    Wagner, L.M.2    Oglesby, T.J.3
  • 80
    • 0020693378 scopus 로고
    • Studies on esterolytic activity of alternative complement component factor B
    • Ikari, N., Hitomi, Y., Ninobe, M., and Fujii, S. (1983). Studies on esterolytic activity of alternative complement component factor B. Biochim. Biophys. Acta 742, 318-323.
    • (1983) Biochim. Biophys. Acta , vol.742 , pp. 318-323
    • Ikari, N.1    Hitomi, Y.2    Ninobe, M.3    Fujii, S.4
  • 82
    • 0027717041 scopus 로고
    • Chemical characterization and location of ionic interactions involved in the assembly of the CI complex of human complement
    • Illy, C, Thielens, N. M., and Arlaud, G. J. (1993). Chemical characterization and location of ionic interactions involved in the assembly of the CI complex of human complement. J. Trot. Chem. 12, 771-781.
    • (1993) J. Trot. Chem. , vol.12 , pp. 771-781
    • Illy, C.1    Thielens, N.M.2    Arlaud, G.J.3
  • 84
    • 0001473574 scopus 로고    scopus 로고
    • Ancient origin of the complement lectin pathway revealed by molecular cloning of mannan-binding protein-associated serine protease from a urochordate, the Japanese ascidian Halocynthia roretzi
    • Ji, X., Azumi, K., Sasaki, M., and Nonaka, M. (1997). Ancient origin of the complement lectin pathway revealed by molecular cloning of mannan-binding protein-associated serine protease from a urochordate, the Japanese ascidian Halocynthia roretzi. Proc. Natl. Acad. Sci. U.S.A. 94, 6340-6345.
    • (1997) Proc. Natl. Acad. Sci. U.S.A. , vol.94 , pp. 6340-6345
    • Ji, X.1    Azumi, K.2    Sasaki, M.3    Nonaka, M.4
  • 85
    • 0027204626 scopus 로고
    • Activation of the C4 and C2 components of complement by a proteinase in serum bactericidal factor, Ra reactive factor
    • Ji, Y.-H., Fujita, T., Hatsuse, H., Takahashi, A., Matsushita, M., and Kawakami, M. (1993). Activation of the C4 and C2 components of complement by a proteinase in serum bactericidal factor, Ra reactive factor. J. Immunol. 150, 571-578.
    • (1993) J. Immunol. , vol.150 , pp. 571-578
    • Ji, Y.-H.1    Fujita, T.2    Hatsuse, H.3    Takahashi, A.4    Matsushita, M.5    Kawakami, M.6
  • 86
    • 0021341820 scopus 로고
    • Amino acid sequence of human factor D of the complement system. Similarity in sequence between factor D and proteases of non-plasma origin
    • Johnson, D. M. A., Gagnon, J., and Reid, K. B. M. (1984). Amino acid sequence of human factor D of the complement system. Similarity in sequence between factor D and proteases of non-plasma origin. FEBS Lett. 166, 347-351.
    • (1984) FEBS Lett , vol.166 , pp. 347-351
    • Johnson, D.M.A.1    Gagnon, J.2    Reid, K.B.M.3
  • 87
    • 0022921590 scopus 로고
    • Cloning and sequencing of full-length cDNA encoding the precursor of human complement component Clr
    • Journet, A., and Tosi, M. (1986). Cloning and sequencing of full-length cDNA encoding the precursor of human complement component Clr. Biochem. J. 240, 783-787.
    • (1986) Biochem. J. , vol.240 , pp. 783-787
    • Journet, A.1    Tosi, M.2
  • 88
    • 0023245340 scopus 로고
    • Human complement proteins D, C2, and B. Active site mapping with peptide thioester substrates
    • Kam, C.-M., McRae, B. J., Harper, J. W., Niemann, M. A., Volanakis, J. E., and Powers, J. C. (1987). Human complement proteins D, C2, and B. Active site mapping with peptide thioester substrates. J. Biol. Chem. 262, 3444-3451.
    • (1987) J. Biol. Chem. , vol.262 , pp. 3444-3451
    • Kam, C.-M.1    McRae, B.J.2    Harper, J.W.3    Niemann, M.A.4    Volanakis, J.E.5    Powers, J.C.6
  • 89
    • 0023915415 scopus 로고
    • Mechanism-based isocoumarin inhibitors for trypsin and blood coagulation serine proteases: New anticoagulants
    • Kam, C.-M., Fujikawa, K,. and Powers, J. C. (1988). Mechanism-based isocoumarin inhibitors for trypsin and blood coagulation serine proteases: New anticoagulants. Biochemistry 27, 2547-2557.
    • (1988) Biochemistry , vol.27 , pp. 2547-2557
    • Kam, C.-M.1    Fujikawa, K.2    Powers, J.C.3
  • 90
    • 0026766511 scopus 로고
    • Substituted isocoumarins as inhibitors of complement serine proteases
    • Kam, C.-M., Oglesby, T. J., Pangburn, M. K., Volanakis, J. E., and Powers, J. C. (1992). Substituted isocoumarins as inhibitors of complement serine proteases. J. Immunol. 149, 163-168.
    • (1992) J. Immunol. , vol.149 , pp. 163-168
    • Kam, C.-M.1    Oglesby, T.J.2    Pangburn, M.K.3    Volanakis, J.E.4    Powers, J.C.5
  • 91
    • 0029015716 scopus 로고
    • Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi
    • Kamata, T., Wright, R., and Takada, Y. (1995). Critical threonine and aspartic acid residues within the I domains of β2 integrins for interactions with intercellular adhesion molecule 1 (ICAM-1) and C3bi. J. Biol Chem. 270, 12531-12535.
    • (1995) J. Biol Chem. , vol.270 , pp. 12531-12535
    • Kamata, T.1    Wright, R.2    Takada, Y.3
  • 92
    • 0022871113 scopus 로고
    • Genetic studies of low abundance human plasma proteins. III. Polymorphism of the Clr subcomponent of the first complement component
    • Kamboh, M. I., and Ferrell, R. E. (1986). Genetic studies of low abundance human plasma proteins. III. Polymorphism of the Clr subcomponent of the first complement component. Am. J. Hum. Genet. 39, 826-831.
    • (1986) Am. J. Hum. Genet. , vol.39 , pp. 826-831
    • Kamboh, M.I.1    Ferrell, R.E.2
  • 93
    • 0019144945 scopus 로고
    • The human complement system. Assembly of the classical pathway C3-convertase
    • Kerr, M. A. (1980). The human complement system. Assembly of the classical pathway C3-convertase. Biochem. J. 189, 173-181.
    • (1980) Biochem. J. , vol.189 , pp. 173-181
    • Kerr, M.A.1
  • 94
    • 0028559926 scopus 로고
    • Mutational analysis of the substrate binding site of human complement factor D
    • Kim, S., Narayana, S. V. L., and Volanakis, J. E. (1994). Mutational analysis of the substrate binding site of human complement factor D. Biochemistry 33, 14393-14399.
    • (1994) Biochemistry , vol.33 , pp. 14393-14399
    • Kim, S.1    Narayana, S.V.L.2    Volanakis, J.E.3
  • 95
    • 0029066097 scopus 로고
    • Catalytic role of a surface loop of the complement serine protease factor D
    • Kim, S., Narayana, S. V. L., and Volanakis, J. E. (1995a). Catalytic role of a surface loop of the complement serine protease factor D. J. Immunol. 154, 6073-6079.
    • (1995) J. Immunol. , vol.154 , pp. 6073-6079
    • Kim, S.1    Narayana, S.V.L.2    Volanakis, J.E.3
  • 96
    • 0028787418 scopus 로고
    • Crystal structure of a complement factor D mutant expressing enhanced catalytic activity
    • Kim, S., Narayana, S. V. L., and Volanakis, J. E. (1995b). Crystal structure of a complement factor D mutant expressing enhanced catalytic activity. J. Biol. Chem. 270, 24399-24405.
    • (1995) J. Biol. Chem. , vol.270 , pp. 24399-24405
    • Kim, S.1    Narayana, S.V.L.2    Volanakis, J.E.3
  • 97
    • 0019889789 scopus 로고
    • Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: Neutron structure of trypsin
    • Kossiakoff, A. A., and Spencer, S. A. (1981). Direct determination of the protonation states of aspartic acid-102 and histidine-57 in the tetrahedral intermediate of the serine proteases: Neutron structure of trypsin. Biochemistry 20, 6462-6474.
    • (1981) Biochemistry , vol.20 , pp. 6462-6474
    • Kossiakoff, A.A.1    Spencer, S.A.2
  • 98
    • 0026244229 scopus 로고
    • Molscript: A program to produce both detailed and schematic plots of protein structures
    • Kraulis, P. J. (1991). MOLSCRIPT: A program to produce both detailed and schematic plots of protein structures. J. Appl. Crystallogr. 24, 946-950.
    • (1991) J. Appl. Crystallogr. , vol.24 , pp. 946-950
    • Kraulis, P.J.1
  • 99
    • 0025761266 scopus 로고
    • Sites within the C3b/C4b receptor important for the specificity of ligand binding
    • Krych, M., Hourcade, D., and Atkinson, J. P. (1991). Sites within the C3b/C4b receptor important for the specificity of ligand binding. Proc. Natl. Acad. Sci. U.S.A. 88,4353-4357.
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 4353-4357
    • Krych, M.1    Hourcade, D.2    Atkinson, J.P.3
  • 100
  • 101
    • 0015913182 scopus 로고
    • Reaction mechanisms of the alternative pathway of complement fixation
    • Lachmann, P. J., and Nicol, P. A. E. (1973). Reaction mechanisms of the alternative pathway of complement fixation. Lancet 1, 465-467.
    • (1973) Lancet , vol.1 , pp. 465-467
    • Lachmann, P.J.1    Nicol, P.A.E.2
  • 102
    • 0031009289 scopus 로고    scopus 로고
    • Structure and assembly of the catalytic region of human complement protease Clr: A three-dimensional model based on chemical cross-linking and homology modeling
    • Lacroix, M., Rossi, V., Gaboriaud, C, Chevallier, S., Jaquinod, M., Thielens, N. M., Gagnon, J., and Arlaud, G. J. (1997). Structure and assembly of the catalytic region of human complement protease Clr: a three-dimensional model based on chemical cross-linking and homology modeling. Biochemistry 36, 6270-6282.
    • (1997) Biochemistry , vol.36 , pp. 6270-6282
    • Lacroix, M.1    Rossi, V.2    Gaboriaud, C.3    Chevallier, S.4    Jaquinod, M.5    Thielens, N.M.6    Gagnon, J.7    Arlaud, G.J.8
  • 103
    • 0024591143 scopus 로고
    • Isolation and functional characterization of the proenzyme form of the catalytic domains of human Clr
    • Lacroix, M. B., Aude, C. A., Arlaud, G. J., and Colomb, M. G. (1989). Isolation and functional characterization of the proenzyme form of the catalytic domains of human Clr. Biochem. J. 257, 885-891.
    • (1989) Biochem. J. , vol.257 , pp. 885-891
    • Lacroix, M.B.1    Aude, C.A.2    Arlaud, G.J.3    Colomb, M.G.4
  • 104
    • 0023573905 scopus 로고
    • Subunit interactions in the first component of complement
    • Lakatos, S. (1987). Subunit interactions in the first component of complement, CI. Biochem. Biophys. Res. Commun. 149, 378-384.
    • (1987) CI. Biochem. Biophys. Res. Commun. , vol.149 , pp. 378-384
    • Lakatos, S.1
  • 105
    • 0021745965 scopus 로고
    • Isolation and characterization of a 33,000-Dalton fragment of complement factor B with catalytic and C3b binding activity
    • Lambris, J. D., and Müller-Eberhard, H. J. (1984). Isolation and characterization of a 33,000-Dalton fragment of complement factor B with catalytic and C3b binding activity. J. Biol. Chem. 259, 12685-12690.
    • (1984) J. Biol. Chem. , vol.259 , pp. 12685-12690
    • Lambris, J.D.1    Müller-Eberhard, H.J.2
  • 106
    • 0028986196 scopus 로고
    • Crystal structure of the A domain from the α subunit of integrin CR3 (CDllb/CD18)
    • Lee, J. O., Rieu, P., Arnaout, M. A., and Liddington, R. (1995a). Crystal structure of the A domain from the α subunit of integrin CR3 (CDllb/CD18). Cell (Cambridge, Mass.) 80, 631-638.
    • (1995) Cell (Cambridge, Mass.) , vol.80 , pp. 631-638
    • Lee, J.O.1    Rieu, P.2    Arnaout, M.A.3    Liddington, R.4
  • 107
    • 0029646107 scopus 로고
    • Two conformations of the integrin A-domain (I-domain): A pathway for activation?
    • Lee, J.-O., Bankston, L. A., Arnaout, M. A., and Liddington, R. C. (1995b). Two conformations of the integrin A-domain (I-domain): A pathway for activation? Structure 3, 1333-1340.
    • (1995) Structure , vol.3 , pp. 1333-1340
    • Lee, J.-O.1    Bankston, L.A.2    Arnaout, M.A.3    Liddington, R.C.4
  • 108
    • 0018256647 scopus 로고
    • Mechanism of action of factor D of the alternative complement pathway
    • Lesavre, P. H., and Müller-Eberhard, H. J. (1978). Mechanism of action of factor D of the alternative complement pathway. J. Exp. Med. 148, 1498-1509.
    • (1978) J. Exp. Med. , vol.148 , pp. 1498-1509
    • Lesavre, P.H.1    Müller-Eberhard, H.J.2
  • 109
    • 0022551346 scopus 로고
    • Nucleotide sequence of the cDNA coding for human complement Clr
    • Leytus, S. P., Kurachi, K., Sakariassen, K. S., and Davie, E. W. (1986). Nucleotide sequence of the cDNA coding for human complement Clr. Biochemistry 25, 4855-4863.
    • (1986) Biochemistry , vol.25 , pp. 4855-4863
    • Leytus, S.P.1    Kurachi, K.2    Sakariassen, K.S.3    Davie, E.W.4
  • 111
    • 0022924380 scopus 로고
    • Complement deficiencies 1. The first component: Clq, Clr, CLS
    • Loos, M., and Heinz, H. P. (1986). Complement deficiencies 1. The first component: Clq, Clr, Cls. Prog. Allergy 39, 212-231.
    • (1986) Prog. Allergy , vol.39 , pp. 212-231
    • Loos, M.1    Heinz, H.P.2
  • 113
    • 0026762783 scopus 로고
    • Recombinant human complement subcomponent Cls lacking β-hydroxyasparagine, sialic acid, and one of its two carbohydrate chains still reassembles with Clq and Clr to form a functional CI complex
    • Luo, C, Thielens, N. M., Gagnon, J., Gal, P., Sarvari, M., Tseng, Y., Tosi, M., Zavodszky, P., Arlaud, G. J., and Schumaker, V. N. (1992). Recombinant human complement subcomponent Cls lacking β-hydroxyasparagine, sialic acid, and one of its two carbohydrate chains still reassembles with Clq and Clr to form a functional CI complex. Biochemistry 31, 4254-4262.
    • (1992) Biochemistry , vol.31 , pp. 4254-4262
    • Luo, C.1    Thielens, N.M.2    Gagnon, J.3    Gal, P.4    Sarvari, M.5    Tseng, Y.6    Tosi, M.7    Zavodszky, P.8    Arlaud, G.J.9    Schumaker, V.N.10
  • 114
    • 0023568351 scopus 로고
    • Molecular cloning of cDNA for human complement component Cls. The complete amino acid sequence
    • Mackinnon, C. M., Carter, P. E., Smith, S. J., Dunbar, B., and Fothergill, J. E. (1987). Molecular cloning of cDNA for human complement component Cls. The complete amino acid sequence. Eur. J. Biochem. 169, 547-553.
    • (1987) Eur. J. Biochem. , vol.169 , pp. 547-553
    • Mackinnon, C.M.1    Carter, P.E.2    Smith, S.J.3    Dunbar, B.4    Fothergill, J.E.5
  • 115
    • 0023009759 scopus 로고
    • Functional analysis of activated Cls, a subcomponent of the first component of human complement, by monoclonal antibodies
    • Matsumoto, M., and Nagaki, K. (1986). Functional analysis of activated Cls, a subcomponent of the first component of human complement, by monoclonal antibodies. J. Immunol. 137, 2907-2912.
    • (1986) J. Immunol. , vol.137 , pp. 2907-2912
    • Matsumoto, M.1    Nagaki, K.2
  • 116
    • 0024596328 scopus 로고
    • Probing the C4-binding site on Cls with monoclonal antibodies. Evidence for a C4/C4bbinding site on the gamma domain
    • Matsumoto, M., Nagaki, K., Kitamura, H., Kuramitsu, S., Nagasawa, S., and Seya, T. (1989). Probing the C4-binding site on Cls with monoclonal antibodies. Evidence for a C4/C4bbinding site on the gamma domain. J. Immunol. 142, 2743-2750.
    • (1989) J. Immunol. , vol.142 , pp. 2743-2750
    • Matsumoto, M.1    Nagaki, K.2    Kitamura, H.3    Kuramitsu, S.4    Nagasawa, S.5    Seya, T.6
  • 117
    • 0026445745 scopus 로고
    • Activation of the classical complement pathway by mannose-binding protein in association with a novel Cls-like serine protease
    • Matsushita, M., and Fujita, T. (1992). Activation of the classical complement pathway by mannose-binding protein in association with a novel Cls-like serine protease. J. Exp. Med. 176, 1497-1502.
    • (1992) J. Exp. Med. , vol.176 , pp. 1497-1502
    • Matsushita, M.1    Fujita, T.2
  • 118
    • 0028805766 scopus 로고
    • Cleavage of the third component of complement by mannose-binding protein-associated serine protease (MASP) with subsequent complement activation
    • Matsushita, M. and Fujita, T. (1995). Cleavage of the third component of complement by mannose-binding protein-associated serine protease (MASP) with subsequent complement activation. Immunohiology 194, 443-448.
    • (1995) Immunohiology , vol.194 , pp. 443-448
    • Matsushita, M.1    Fujita, T.2
  • 119
    • 0001894601 scopus 로고    scopus 로고
    • Inhibition of mannose-binding protein-associated serine protease (MASP) by CI inhibitor (CI INH)
    • abstract
    • Matsushita, M., and Fujita, T. (1996). Inhibition of mannose-binding protein-associated serine protease (MASP) by CI inhibitor (CI INH). Mol. Immunol. 33, 44 (abstract).
    • (1996) Mol. Immunol. , vol.33 , pp. 44
    • Matsushita, M.1    Fujita, T.2
  • 120
    • 0019767919 scopus 로고
    • Mapping the substrate binding site of human Clr and Cls with peptide thioesters: Development of new sensitive substrates
    • McRae, B. J., Lin, T.-Y., and Powers, J. C. (1981). Mapping the substrate binding site of human Clr and Cls with peptide thioesters: Development of new sensitive substrates. J. Biol. Chem. 256, 12362-12366.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12362-12366
    • McRae, B.J.1    Lin, T.-Y.2    Powers, J.C.3
  • 121
    • 0020401149 scopus 로고
    • Unique role of the complement receptor CR1 in the degradation of C3b associated with immune complexes
    • Medof, M. E., Iida, K., Mold, C, and Nussenzweig, V. (1982). Unique role of the complement receptor CR1 in the degradation of C3b associated with immune complexes. J. Exp. Med. 156, 1739-1754.
    • (1982) J. Exp. Med. , vol.156 , pp. 1739-1754
    • Medof, M.E.1    Iida, K.2    Mold, C.3    Nussenzweig, V.4
  • 122
    • 0024369008 scopus 로고
    • Calorimetric investigation of the domain structure of human complement Cls: Reversible unfolding of the short consensus repeat units
    • Medved, L. V., Busby, T. F., and Ingham, K. C. (1989). Calorimetric investigation of the domain structure of human complement Cls: Reversible unfolding of the short consensus repeat units. Biochemistry 28, 5408-5414.
    • (1989) Biochemistry , vol.28 , pp. 5408-5414
    • Medved, L.V.1    Busby, T.F.2    Ingham, K.C.3
  • 123
    • 0027483226 scopus 로고
    • A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CDllb/CD18) is essential for ligand binding
    • Michishita, M., Videm, V., and Arnaout, A. (1993). A novel divalent cation-binding site in the A domain of the β2 integrin CR3 (CDllb/CD18) is essential for ligand binding. Cell (Cambridge, Mass.) 72, 857-867.
    • (1993) Cell (Cambridge, Mass.) , vol.72 , pp. 857-867
    • Michishita, M.1    Videm, V.2    Arnaout, A.3
  • 124
    • 0023057194 scopus 로고
    • Adipsin, the adipocyte serine protease: Gene structure and control of expression by tumor necrosis factor
    • Min, H. Y., and Spiegelman, B. M. (1986). Adipsin, the adipocyte serine protease: gene structure and control of expression by tumor necrosis factor. Nucleic Acids Res. 14,8879-8892.
    • (1986) Nucleic Acids Res , vol.14 , pp. 8879-8892
    • Min, H.Y.1    Spiegelman, B.M.2
  • 125
    • 0021348357 scopus 로고
    • Complete primary structure for the zymogen of human complement factor B
    • Mole, J. E., Anderson, J. K., Davison, E. A., and Woods, D. E. (1984). Complete primary structure for the zymogen of human complement factor B. J. Biol. Chem. 259,3407-3412.
    • (1984) J. Biol. Chem. , vol.259 , pp. 3407-3412
    • Mole, J.E.1    Anderson, J.K.2    Davison, E.A.3    Woods, D.E.4
  • 126
    • 0025874771 scopus 로고
    • Complement deficiency and disease
    • Morgan, B. P., and Walport, M. J. (1991). Complement deficiency and disease. Immunol. Today 12, 301-306.
    • (1991) Immunol. Today , vol.12 , pp. 301-306
    • Morgan, B.P.1    Walport, M.J.2
  • 127
    • 0343038483 scopus 로고
    • Cleavage of C2 by CI into the antigenically distinct fragments C2a and C2b: Demonstration of binding of C2b to C4
    • Nagasawa, S., and Stroud, R. M. (1977). Cleavage of C2 by CI into the antigenically distinct fragments C2a and C2b: Demonstration of binding of C2b to C4. Proa Nad. Acad. Set. U.S.A. 74, 2998-3001.
    • (1977) Proa Nad. Acad. Set. U.S.A. , vol.74 , pp. 2998-3001
    • Nagasawa, S.1    Stroud, R.M.2
  • 128
    • 0021958688 scopus 로고
    • Purification and characterization of the C3-convertase of the classical pathway of human complement system by size exclusion high-performance liquid chromatography
    • Nagasawa, S., Kobayashi, C, Maki-Suzuki, T., Yamashita, N., and Koyama, J. (1985). Purification and characterization of the C3-convertase of the classical pathway of human complement system by size exclusion high-performance liquid chromatography. J. Biochem. 97, 493-499.
    • (1985) J. Biochem. , vol.97 , pp. 493-499
    • Nagasawa, S.1    Kobayashi, C.2    Maki-Suzuki, T.3    Yamashita, N.4    Koyama, J.5
  • 130
    • 0021276528 scopus 로고
    • Amino acid sequence of human factor D of the alternative complement pathway
    • Niemann, M. A., Bhown, A. S., Bennett, J. C, and Volanakis, J. E. (1984). Amino acid sequence of human factor D of the alternative complement pathway. Biochemistry 23, 2482-2486.
    • (1984) Biochemistry , vol.23 , pp. 2482-2486
    • Niemann, M.A.1    Bhown, A.S.2    Bennett, J.C.3    Volanakis, J.E.4
  • 131
    • 0025370167 scopus 로고
    • Inhibition of factor I by diisopropylfluorophosphate. Evidence of conformational changes in factor I induced by C3b and additional studies on the specificity of factor I
    • Nilsson-Ekdahl, K., Nilsson, U. R., and Nilsson, B. (1990). Inhibition of factor I by diisopropylfluorophosphate. Evidence of conformational changes in factor I induced by C3b and additional studies on the specificity of factor I. J. Immunol. 144, 4269-4274.
    • (1990) J. Immunol. , vol.144 , pp. 4269-4274
    • Nilsson-Ekdahl, K.1    Nilsson, U.R.2    Nilsson, B.3
  • 132
    • 0025233651 scopus 로고
    • Limited proteolysis of β2-microglobulin at Lys-58 by complement component Cls
    • Nissen, M. H., Roepstorff, P., Thim, L., Dunbar, B., and Fothergill, J. E. (1990). Limited proteolysis of β2-microglobulin at Lys-58 by complement component Cls. Eur. J. Biochem. 189, 423-429.
    • (1990) Eur. J. Biochem. , vol.189 , pp. 423-429
    • Nissen, M.H.1    Roepstorff, P.2    Thim, L.3    Dunbar, B.4    Fothergill, J.E.5
  • 133
    • 0025894780 scopus 로고
    • Three-dimensional structure of a complement control protein module in solution
    • Norman, D. C, 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.C.1    Barlow, P.N.2    Baron, M.3    Day, A.J.4    Sim, R.B.5    Campbell, I.D.6
  • 134
    • 0028910256 scopus 로고
    • Substrate specificities of the protease of mouse serum Ra-reactive factor
    • Ogata, R. T., Low, P. J., and Kawakami, M. (1995). Substrate specificities of the protease of mouse serum Ra-reactive factor. J. Immunol. 154, 2351-2357.
    • (1995) J. Immunol. , vol.154 , pp. 2351-2357
    • Ogata, R.T.1    Low, P.J.2    Kawakami, M.3
  • 135
    • 0023719006 scopus 로고
    • Evidence for a C4b binding site on the C2b domain of C2
    • Oglesby, T. J., Accavitti, M. A., and Volanakis, J. E. (1988). Evidence for a C4b binding site on the C2b domain of C2. J. Immunol. 141, 926-931.
    • (1988) J. Immunol. , vol.141 , pp. 926-931
    • Oglesby, T.J.1    Accavitti, M.A.2    Volanakis, J.E.3
  • 136
    • 0022521480 scopus 로고
    • The C3-convertase of the alternative pathway of human complement. Enzymic properties of the bimolecular proteinase
    • Pangburn, M. K., and Miiller-Eberhard, H. J. (1986). The C3-convertase of the alternative pathway of human complement. Enzymic properties of the bimolecular proteinase. Biochem. J. 235, 723-730.
    • (1986) Biochem. J. , vol.235 , pp. 723-730
    • Pangburn, M.K.1    Miiller-Eberhard, H.J.2
  • 137
    • 0019501478 scopus 로고
    • Formation of the initial C3-convertases of the alternative complement pathway. Acquisition of C3b-like activities by spontaneous hydrolysis of the putative thioester in native C3
    • Pangburn, M. K., Schreiber, R. D., and Muller-Eberhard, H. J. (1981). Formation of the initial C3-convertases of the alternative complement pathway. Acquisition of C3b-like activities by spontaneous hydrolysis of the putative thioester in native C3. J. Exp. Med. 154, 856-867.
    • (1981) J. Exp. Med. , vol.154 , pp. 856-867
    • Pangburn, M.K.1    Schreiber, R.D.2    Muller-Eberhard, H.J.3
  • 138
    • 0020594206 scopus 로고
    • The reaction of iodine and thiol-blocking reagents with human complement components C2 and factor B
    • Parkes, C, Gagnon, J., and Kerr, M. A. (1983). The reaction of iodine and thiol-blocking reagents with human complement components C2 and factor B. Biochem. J. 213,201-209.
    • (1983) Biochem. J. , vol.213 , pp. 201-209
    • Parkes, C.1    Gagnon, J.2    Kerr, M.A.3
  • 140
    • 0026148460 scopus 로고
    • Exons-original building blocks of proteins
    • Patthy, L. (1991). Exons-original building blocks of proteins. Bioessays 13, 187-192.
    • (1991) Bioessays , vol.13 , pp. 187-192
    • Patthy, L.1
  • 141
    • 0027487510 scopus 로고
    • Modular design of proteases of coagulation, fibrinolysis, and complement activation: Implications for protein engineering and structure-function studies
    • L. Lorand and K. G. Mann, Eds.),. Academic Press, San Diego, CA
    • Patthy, L. (1993). Modular design of proteases of coagulation, fibrinolysis, and complement activation: implications for protein engineering and structure-function studies. In "Methods in Enzymology, Vol. 222" (L. Lorand and K. G. Mann, Eds.), pp. 10-21. Academic Press, San Diego, CA.
    • (1993) Methods in Enzymology , vol.222 , pp. 10-21
    • Patthy, L.1
  • 143
    • 0024386066 scopus 로고
    • Models for the CI complex determined by physical techniques
    • Perkins, S. J. (1989). Models for the CI complex determined by physical techniques. Behring Inst. Mitt. 84, 129-141.
    • (1989) Behring Inst. Mitt. , vol.84 , pp. 129-141
    • Perkins, S.J.1
  • 144
    • 0027371944 scopus 로고
    • Identity of the putative serine-proteinase fold in proteins of the complement system with nine relevant crystal structures
    • Perkins, S. J., and Smith, K. F. (1993). Identity of the putative serine-proteinase fold in proteins of the complement system with nine relevant crystal structures. Biochem. J. 295, 109-114.
    • (1993) Biochem. J. , vol.295 , pp. 109-114
    • Perkins, S.J.1    Smith, K.F.2
  • 146
    • 0028360720 scopus 로고
    • The secondary structure of the von Willebrand factor type A domain in factor B of human complement by Fourier transform infrared spectroscopy
    • Perkins, S. J., Smith, K. F., Williams, S. C, Haris, P. I., Chapman, D., and Sim, R. B. (1994). The secondary structure of the von Willebrand factor type A domain in factor B of human complement by Fourier transform infrared spectroscopy. J. Mol. Biol. 238, 104-119.
    • (1994) J. Mol. Biol. , vol.238 , pp. 104-119
    • Perkins, S.J.1    Smith, K.F.2    Williams, S.C.3    Haris, P.I.4    Chapman, D.5    Sim, R.B.6
  • 147
    • 0028914722 scopus 로고
    • Structural basis of substrate specificity in the serine proteases
    • Perona, J. J., and Craik, C. S. (1995). Structural basis of substrate specificity in the serine proteases. Protein Sci. 4, 337-360.
    • (1995) Protein Sci , vol.4 , pp. 337-360
    • Perona, J.J.1    Craik, C.S.2
  • 149
    • 0028905227 scopus 로고
    • Structural origins of substrate discrimination in trypsin and chymotrypsin
    • Perona J. J., Hedstrom, L., Rutter, W. J., and Fletterick, R. J. (1995). Structural origins of substrate discrimination in trypsin and chymotrypsin. Biochemistry 34, 1489-1499.
    • (1995) Biochemistry , vol.34 , pp. 1489-1499
    • Perona, J.J.1    Hedstrom, L.2    Rutter, W.J.3    Fletterick, R.J.4
  • 151
    • 0014167220 scopus 로고
    • Enhancement of the hemolytic activity of the second component of human complement by oxidation
    • Polley, M. J., and Müller-Eberhard, H. J. (1967). Enhancement of the hemolytic activity of the second component of human complement by oxidation.J. Exp. Med. 126,1013-1025.
    • (1967) J. Exp. Med. , vol.126 , pp. 1013-1025
    • Polley, M.J.1    Müller-Eberhard, H.J.2
  • 152
    • 0023187398 scopus 로고
    • Alternative complement pathway activation fragment Ba binds to C3b. Evidence that formation of the factor B-C3b complex involves two discrete points of contact
    • Pryzdial, E. L. G., and Isenman, D. E. (1987). Alternative complement pathway activation fragment Ba binds to C3b. Evidence that formation of the factor B-C3b complex involves two discrete points of contact. J. Biol. Chem. 262, 1519-1525.
    • (1987) J. Biol. Chem. , vol.262 , pp. 1519-1525
    • Pryzdial, E.L.G.1    Isenman, D.E.2
  • 153
    • 0028822128 scopus 로고
    • Crystal structure of the I-domain from the CDlla/CD18 (LFA-1, Α1Β2) integrin
    • Qu, A., and Leahy, D. J. (1995). Crystal structure of the I-domain from the CDlla/CD18 (LFA-1, Α1Β2) integrin. Proc. Natl. Acad. Sci. U.S.A. 92, 10277-10281.
    • (1995) Proc. Natl. Acad. Sci. U.S.A. , vol.92 , pp. 10277-10281
    • Qu, A.1    Leahy, D.J.2
  • 155
    • 0001680436 scopus 로고
    • The complement system. A major effector mechanism in humoral immunity
    • Reid, K. B. M. (1995). The complement system. A major effector mechanism in humoral immunity. Immunologist 3, 206-211.
    • (1995) Immunologist , vol.3 , pp. 206-211
    • Reid, K.B.M.1
  • 156
    • 0022916085 scopus 로고
    • Complement system proteins which interact with C3b and C4b. A superfamily of structurally related proteins
    • Reid, K. B. M., Bentley, D. R., Campbell, R. D., Chung, L. P., Sim, R. B.,Kristensen, T., and Tack, B. F. (1986). Complement system proteins which interact with C3b and C4b. A superfamily of structurally related proteins. Immunol. Today 7, 230-234.
    • (1986) Immunol. Today , vol.7 , pp. 230-234
    • Reid, K.B.M.1    Bentley, D.R.2    Campbell, R.D.3    Chung, L.P.4    Sim, R.B.5    Kristensen, T.6    Tack, B.F.7
  • 157
    • 0022416122 scopus 로고
    • Exon shuffling and intron insertion in serine protease genes
    • Rogers, J. (1985). Exon shuffling and intron insertion in serine protease genes. Nature (London) 315, 458-459.
    • (1985) Nature (London) , vol.315 , pp. 458-459
    • Rogers, J.1
  • 159
    • 0029010484 scopus 로고
    • Structure of the catalytic region of human complement protease Cls: Study by chemical cross-linking and three-dimensional homology modeling
    • Rossi, V., Gaboriaud, C, Lacroix, M., Ulrich, J., Fontecilla-Camps, J. C, Gagnon, J., and Arlaud, G. J. (1995). Structure of the catalytic region of human complement protease Cls: Study by chemical cross-linking and three-dimensional homology modeling. Biochemistry 34, 7311-7321.
    • (1995) Biochemistry , vol.34 , pp. 7311-7321
    • Rossi, V.1    Gaboriaud, C.2    Lacroix, M.3    Ulrich, J.4    Fontecilla-Camps, J.C.5    Gagnon, J.6    Arlaud, G.J.7
  • 160
    • 0031964708 scopus 로고    scopus 로고
    • Baculovimsmediated expression of truncated modular fragments from the catalytic region of human complement serine protease Cls. Evidence for the involvement of both complement control protein modules in the recognition of the C4 protein substrate
    • Rossi, V., Bally, I., Thielens, N. M., Esser, A. F., and Arlaud, G. J. (1998). Baculovimsmediated expression of truncated modular fragments from the catalytic region of human complement serine protease Cls. Evidence for the involvement of both complement control protein modules in the recognition of the C4 protein substrate. J. Biol. Chem. 273, 1232-1239.
    • (1998) J. Biol. Chem. , vol.273 , pp. 1232-1239
    • Rossi, V.1    Bally, I.2    Thielens, N.M.3    Esser, A.F.4    Arlaud, G.J.5
  • 161
    • 0025103056 scopus 로고
    • Proteolytic activity of the different fragments of factor B on the third component of complement (C3): Involvement of the N-terminal domain of Bb in magnesium binding
    • Sánchez-Corral, P., Antón, L. C, Alcolea, J. M., Marqués, G., Sánchez, A., and Vivanco, F. (1990). Proteolytic activity of the different fragments of factor B on the third component of complement (C3): Involvement of the N-terminal domain of Bb in magnesium binding. Mol. Immunol. 27, 891-900.
    • (1990) Mol. Immunol. , vol.27 , pp. 891-900
    • Sánchez-Corral, P.1    Antón, L.C.2    Alcolea, J.M.3    Marqués, G.4    Sánchez, A.5    Vivanco, F.6
  • 162
    • 0028343828 scopus 로고
    • Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein
    • Sato, T., Endo, Y., Matsushita, M., and Fujita, T. (1994). Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein. Int. Immunol. 6, 665-669.
    • (1994) Int. Immunol. , vol.6 , pp. 665-669
    • Sato, T.1    Endo, Y.2    Matsushita, M.3    Fujita, T.4
  • 163
    • 0017835784 scopus 로고
    • The atomic structure of crystalline porcine pancreatic elastase at 2.5 resolution. Comparison with the structure of α-chymotrypsin
    • Sawyer, L., Shotton, D. M., Campbell, J. W., Wendell, P. L., Muirhead, H., Watson, H. C, Diamond, R., and Ladner, R. C. (1978). The atomic structure of crystalline porcine pancreatic elastase at 2.5 resolution. Comparison with the structure of α-chymotrypsin. J. Mol. Biol. 118, 137-208.
    • (1978) J. Mol. Biol. , vol.118 , pp. 137-208
    • Sawyer, L.1    Shotton, D.M.2    Campbell, J.W.3    Wendell, P.L.4    Muirhead, H.5    Watson, H.C.6    Diamond, R.7    Ladner, R.C.8
  • 164
    • 0014211618 scopus 로고
    • On the size of the active site in proteases. I. Papain
    • Schechter, I., and Berger, A. (1967). On the size of the active site in proteases. I. Papain. Biochem. Biophys. Res. Commun. 27, 157-162.
    • (1967) Biochem. Biophys. Res. Commun. , vol.27 , pp. 157-162
    • Schechter, I.1    Berger, A.2
  • 167
    • 0028924417 scopus 로고
    • Human factor H and C4b-binding protein serve as factor I-cofactors both encompassing inactivation of C3b and C4b
    • Seya, T., Nakamura, K., Masaki, T., Ichihara-Itoh, C, Matsumoto, M., and Nagasawa, S. (1995). Human factor H and C4b-binding protein serve as factor I-cofactors both encompassing inactivation of C3b and C4b. Mol. Immunol. 32, 355-360.
    • (1995) Mol. Immunol. , vol.32 , pp. 355-360
    • Seya, T.1    Nakamura, K.2    Masaki, T.3    Ichihara-Itoh, C.4    Matsumoto, M.5    Nagasawa, S.6
  • 168
    • 0000700968 scopus 로고
    • Evidence for an active site histidine in trypsin through use of a specific reagent, l-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from Nα-tosyl-L-Iysine
    • Shaw, E., Mares-Guia, M., and Cohen, W. (1965). Evidence for an active site histidine in trypsin through use of a specific reagent, l-chloro-3-tosylamido-7-amino-2-heptanone, the chloromethyl ketone derived from Nα-tosyl-L-Iysine. Biochemistry 4, 2219-2224.
    • (1965) Biochemistry , vol.4 , pp. 2219-2224
    • Shaw, E.1    Mares-Guia, M.2    Cohen, W.3
  • 171
    • 0017625758 scopus 로고
    • The structure and enzymic activities of the Clr and Cls subcomponents of CI, the first component of human serum complement
    • Sim, R. B., Porter, R. R., Reid, K. B. M., and Gigli, I. (1977). The structure and enzymic activities of the Clr and Cls subcomponents of CI, the first component of human serum complement. Biochem. J. 163, 219-227.
    • (1977) Biochem. J. , vol.163 , pp. 219-227
    • Sim, R.B.1    Porter, R.R.2    Reid, K.B.M.3    Gigli, I.4
  • 172
    • 0018776213 scopus 로고
    • CI inhibitor-dependent dissociation of human complement component CI bound to immune complexes
    • Sim, R. B., Arlaud, G. J., and Colomb, M. G. (1979). CI inhibitor-dependent dissociation of human complement component CI bound to immune complexes. Biochem. J. 179, 449-457.
    • (1979) Biochem. J. , vol.179 , pp. 449-457
    • Sim, R.B.1    Arlaud, G.J.2    Colomb, M.G.3
  • 173
    • 0021351421 scopus 로고
    • MHC class III products: An electron microscopic study of the C3-convertases of human complement
    • Smith, C. A., Vogel, C.-W., and Miiller-Eberhard, H. J. (1984). MHC class III products: An electron microscopic study of the C3-convertases of human complement. J. Exp. Med. 159, 324-329.
    • (1984) J. Exp. Med. , vol.159 , pp. 324-329
    • Smith, C.A.1    Vogel, C.-W.2    Miiller-Eberhard, H.J.3
  • 174
    • 0022530764 scopus 로고
    • Human complement component Cls. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation
    • Spycher, S. E., Nick, H., and Rickli, E. E. (1986). Human complement component Cls. Partial sequence determination of the heavy chain and identification of the peptide bond cleaved during activation. Eur. J. Biochem. 156, 49-57.
    • (1986) Eur. J. Biochem. , vol.156 , pp. 49-57
    • Spycher, S.E.1    Nick, H.2    Rickli, E.E.3
  • 176
    • 0027078415 scopus 로고
    • The new enzymology of precursor processing endoproteases
    • Steiner, D. F., Smeekens, S. P., Ohagi, S., and Chan, S. J. (1992). The new enzymology of precursor processing endoproteases. J. Biol. Chem. 267, 23435-23438.
    • (1992) J. Biol. Chem. , vol.267 , pp. 23435-23438
    • Steiner, D.F.1    Smeekens, S.P.2    Ohagi, S.3    Chan, S.J.4
  • 177
    • 0020033478 scopus 로고
    • Ultrastructure of the first component of human complement: Electron microscopy of the cross-linked complex
    • Strang, C. J., Siegel, R. C, Phillips, M. L., Poon, P. H., and Schumaker, V. N. (1982). Ultrastructure of the first component of human complement: electron microscopy of the cross-linked complex. Proc. Natl. Acad. Sci. U.S.A. 79, 586-590.
    • (1982) Proc. Natl. Acad. Sci. U.S.A. , vol.79 , pp. 586-590
    • Strang, C.J.1    Siegel, R.C.2    Phillips, M.L.3    Poon, P.H.4    Schumaker, V.N.5
  • 179
    • 0022259920 scopus 로고
    • The LDL receptor gene: A mosaic of exons shared with different proteins
    • Sudhof, T. C, Goldstein, J. L., Brown, M. S., and Russell, D. W. (1985). The LDL receptor gene: a mosaic of exons shared with different proteins. Science 228, 815-822.
    • (1985) Science , vol.228 , pp. 815-822
    • Sudhof, T.C.1    Goldstein, J.L.2    Brown, M.S.3    Russell, D.W.4
  • 181
    • 0027378207 scopus 로고
    • A new member of the Cls family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum
    • Takada, F., Takayama, Y., Hatsuse, H., and Kawakami, M. (1993). A new member of the Cls family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum. Biochem. Biophys. Res. Commun. 196, 1003-1009.
    • (1993) Biochem. Biophys. Res. Commun. , vol.196 , pp. 1003-1009
    • Takada, F.1    Takayama, Y.2    Hatsuse, H.3    Kawakami, M.4
  • 182
    • 0028965411 scopus 로고
    • Localization of the genes for the 100-kDa complement-activating components of Ra-reactive factor to human 3q27-q28 and mouse 16B2-B3
    • Takada, F., Seki, N., Matsuda, Y. I., Takayama, Y., and Kawakami, M. (1995). Localization of the genes for the 100-kDa complement-activating components of Ra-reactive factor to human 3q27-q28 and mouse 16B2-B3. Genomics 25, 757-759.
    • (1995) Genomics , vol.25 , pp. 757-759
    • Takada, F.1    Seki, N.2    Matsuda, Y.I.3    Takayama, Y.4    Kawakami, M.5
  • 183
    • 0027244953 scopus 로고
    • Presence of a serine protease in the complement-activating component of the complement-dependent bactericidal factor, RaRF, in mouse serum
    • Takahashi, A., Takayama, Y., Hatsuse, H., and Kawakami, M. (1993). Presence of a serine protease in the complement-activating component of the complement-dependent bactericidal factor, RaRF, in mouse serum. Biochem. Biophys. Res. Commun. 190, 681-687.
    • (1993) Biochem. Biophys. Res. Commun. , vol.190 , pp. 681-687
    • Takahashi, A.1    Takayama, Y.2    Hatsuse, H.3    Kawakami, M.4
  • 184
    • 0028213533 scopus 로고
    • A 100-kDa protein in the C4-activating component of Ra-reactive factor is a new serine protease having module organization similar to Clr and Cls
    • Takayama, Y., Takada, F., Takahashi, A., and Kawakami, M. (1994). A 100-kDa protein in the C4-activating component of Ra-reactive factor is a new serine protease having module organization similar to Clr and Cls. J. Immunol. 152, 2308-2316.
    • (1994) J. Immunol. , vol.152 , pp. 2308-2316
    • Takayama, Y.1    Takada, F.2    Takahashi, A.3    Kawakami, M.4
  • 187
    • 0025219614 scopus 로고
    • Chemical and functional characterization of a fragment of Cls containing the epidermal growth factor homology region
    • Thielens, N. M., van Dorsselaer, A., Gagnon, J., and Arlaud, G. J. (1990a). Chemical and functional characterization of a fragment of Cls containing the epidermal growth factor homology region. Biochemistry 29, 3570-3578.
    • (1990) Biochemistry , vol.29 , pp. 3570-3578
    • Thielens, N.M.1    van Dorsselaer, A.2    Gagnon, J.3    Arlaud, G.J.4
  • 189
    • 0028104075 scopus 로고
    • Activation of human complement serine proteinase Clr is down-regulated by a calcium-dependent intramolecular control that is released in the CI complex through a signal transmitted by Clq
    • Thielens, N. M., Illy, C, Bally, I. M., and Arlaud, G. J. (1994). Activation of human complement serine proteinase Clr is down-regulated by a calcium-dependent intramolecular control that is released in the CI complex through a signal transmitted by Clq. Biochem. J. 301, 378-384.
    • (1994) Biochem. J. , vol.301 , pp. 378-384
    • Thielens, N.M.1    Illy, C.2    Bally, I.M.3    Arlaud, G.J.4
  • 190
    • 0021950964 scopus 로고
    • Carbohydrate composition of the second, third, and fifth components and factors B and D of human complement
    • Tomana, M., Niemann, M., Garner, C, and Volanakis J. E. (1985). Carbohydrate composition of the second, third, and fifth components and factors B and D of human complement. Mol. Immunol. 22, 107-111.
    • (1985) Mol. Immunol. , vol.22 , pp. 107-111
    • Tomana, M.1    Niemann, M.2    Garner, C.3    Volanakis, J.E.4
  • 191
    • 0023621387 scopus 로고
    • Complete cDNA sequence of human complement Cls and close physical linkage of the homologous genes Cls and Clr
    • Tosi, M., Duponchel, C, Meo, T., and Julier, C. (1987). Complete cDNA sequence of human complement Cls and close physical linkage of the homologous genes Cls and Clr. Biochemistry 26, 8516-8524.
    • (1987) Biochemistry , vol.26 , pp. 8516-8524
    • Tosi, M.1    Duponchel, C.2    Meo, T.3    Julier, C.4
  • 192
    • 0024974981 scopus 로고
    • Complement genes Clr and Cls feature an intronless serine protease domain closely related to haptoglobin
    • Tosi, M., Duponchel, C, and Meo, T. (1989). Complement genes Clr and Cls feature an intronless serine protease domain closely related to haptoglobin. J. Mol. Biol. 208, 709-714.
    • (1989) J. Mol. Biol. , vol.208 , pp. 709-714
    • Tosi, M.1    Duponchel, C.2    Meo, T.3
  • 193
    • 0019168322 scopus 로고
    • Assembly of subcomponents Clr and Cls of first component of complement: Electron microscopy and ultracentrifugal studies
    • Tschopp, J„ Villiger, W., Fuchs, H., Kilchherr, E, and Engel, J. (1980). Assembly of subcomponents Clr and Cls of first component of complement: Electron microscopy and ultracentrifugal studies. Proc. Natl. Acad. Sci. U.S.A. 77, 7014-7018.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 7014-7018
    • Tschopp, J.1    Villiger, W.2    Fuchs, H.3    Kilchherr, E.4    Engel, J.5
  • 194
    • 0030948650 scopus 로고    scopus 로고
    • Surface loops adjacent to the putative cation-binding site of the complement factor B von Willebrand factor type A module determine C3b binding specificity
    • Tuckwell, D. S., Xu, Y., Newham, P., Humphries, M. J., and Volanakis, J. E. (1997). Surface loops adjacent to the putative cation-binding site of the complement factor B von Willebrand factor type A module determine C3b binding specificity. Biochemistry 36, 6605-6613.
    • (1997) Biochemistry , vol.36 , pp. 6605-6613
    • Tuckwell, D.S.1    Xu, Y.2    Newham, P.3    Humphries, M.J.4    Volanakis, J.E.5
  • 195
    • 0023110172 scopus 로고
    • Probing functional sites on complement protein B with monoclonal antibodies
    • Ueda A., Kearney, J. F., Roux, K. H., and Volanakis, J. E. (1987). Probing functional sites on complement protein B with monoclonal antibodies.J. Immunol. 138, 1143-1149.
    • (1987) J. Immunol. , vol.138 , pp. 1143-1149
    • Ueda, A.1    Kearney, J.F.2    Roux, K.H.3    Volanakis, J.E.4
  • 197
  • 198
    • 0019985763 scopus 로고
    • Structural features of the first component of human complement, CI, as revealed by surface iodination
    • Villiers, C. L., Chesne, S., Lacroix, M. B., Arlaud, G. J., and Colomb, M. G. (1982). Structural features of the first component of human complement, CI, as revealed by surface iodination. Biochem. J. 203, 185-191.
    • (1982) Biochem. J. , vol.203 , pp. 185-191
    • Villiers, C.L.1    Chesne, S.2    Lacroix, M.B.3    Arlaud, G.J.4    Colomb, M.G.5
  • 199
    • 0021932431 scopus 로고
    • Domain structure and associated functions of subcomponents Clr and Cls of the first component of human complement
    • Villiers, C. L., Arlaud, G. J., and Colomb, M. G, (1985). Domain structure and associated functions of subcomponents Clr and Cls of the first component of human complement. Proc. Natl. Acad. Sci. U.S.A. 82, 4477-4481.
    • (1985) Proc. Natl. Acad. Sci. U.S.A. , vol.82 , pp. 4477-4481
    • Villiers, C.L.1    Arlaud, G.J.2    Colomb, M.G.3
  • 200
    • 0025101346 scopus 로고
    • Participation of C3 and its ligands in complement activation
    • Volanakis, J. E. (1990). Participation of C3 and its ligands in complement activation. Curr. Top. Microbiol. Immunol. 153, 1-21.
    • (1990) Curr. Top. Microbiol. Immunol. , vol.153 , pp. 1-21
    • Volanakis, J.E.1
  • 201
    • 0023227856 scopus 로고
    • Isolation of complement protein D from urine of patients with Fanconi's syndrome
    • Volanakis, J. E., and Macon, K. J. (1987). Isolation of complement protein D from urine of patients with Fanconi's syndrome. Anal. Biochem. 163, 242-246.
    • (1987) Anal. Biochem. , vol.163 , pp. 242-246
    • Volanakis, J.E.1    Macon, K.J.2
  • 202
    • 0029935480 scopus 로고    scopus 로고
    • Complement factor D, a novel serine protease
    • Volanakis, J. E., and Narayana, S. V. L. (1996). Complement factor D, a novel serine protease. Protein Sci. 5, 553-564.
    • (1996) Protein Sci , vol.5 , pp. 553-564
    • Volanakis, J.E.1    Narayana, S.V.L.2
  • 203
    • 0018982021 scopus 로고
    • Partial amino acid sequence of human factor D: Homology with serine proteases
    • Volanakis, J. E., Bhown, A. S., Bennett, J. C, and Mole, J. E. (1980). Partial amino acid sequence of human factor D: Homology with serine proteases. Proc. Natl. Acad. Sci. U.S.A. 77, 1116-1119.
    • (1980) Proc. Natl. Acad. Sci. U.S.A. , vol.77 , pp. 1116-1119
    • Volanakis, J.E.1    Bhown, A.S.2    Bennett, J.C.3    Mole, J.E.4
  • 204
  • 205
    • 0028037085 scopus 로고
    • The organization of the human complement factor I gene (IF): A member of the serine protease gene family
    • Vyse, T. J., Bates, G. P., Walport, M. J., and Morley, B. J. (1994). The organization of the human complement factor I gene (IF): A member of the serine protease gene family. Genomics 24, 90-98.
    • (1994) Genomics , vol.24 , pp. 90-98
    • Vyse, T.J.1    Bates, G.P.2    Walport, M.J.3    Morley, B.J.4
  • 207
    • 0023042319 scopus 로고
    • Functional model of subcomponent CI of human complement
    • Weiss, V., Fauser, C, and Engel, J. (1986). Functional model of subcomponent CI of human complement. J. Mol. Biol. 189, 573-581.
    • (1986) J. Mol. Biol. , vol.189 , pp. 573-581
    • Weiss, V.1    Fauser, C.2    Engel, J.3
  • 209
    • 0022289842 scopus 로고
    • Nucleotide sequence from the neurogenic locus notch implies a gene product that shares homology with proteins containing EGF-like repeats
    • Wharton, K. A., Johansen, K. M., Xu, T., and Artavanis-Tsakonas, S. (1985). Nucleotide sequence from the neurogenic locus notch implies a gene product that shares homology with proteins containing EGF-like repeats. Cell (Cambridge, Mass.) 43, 567-581.
    • (1985) Cell (Cambridge, Mass.) , vol.43 , pp. 567-581
    • Wharton, K.A.1    Johansen, K.M.2    Xu, T.3    Artavanis-Tsakonas, S.4
  • 211
    • 0023667822 scopus 로고
    • Cell-specific expression of the human complement protein B gene: Evidence for the role of two distinct 5'-flanking elements
    • Wu, L.-C, Morley, B. J., and Campbell, R. D. (1987). Cell-specific expression of the human complement protein B gene: Evidence for the role of two distinct 5'-flanking elements. Cell (Cambridge, Mass.) 48, 331-342.
    • (1987) Cell (Cambridge, Mass.) , vol.48 , pp. 331-342
    • Wu, L.-C.1    Morley, B.J.2    Campbell, R.D.3
  • 212
    • 0031570468 scopus 로고    scopus 로고
    • Contribution of the complement control protein modules of C2 in C4b binding assessed by analysis of C2/factor B chimeras
    • Xu, Y., and Volanakis, J. E. (1997). Contribution of the complement control protein modules of C2 in C4b binding assessed by analysis of C2/factor B chimeras.J. Immunol. 158,5958-5665.
    • (1997) J. Immunol. , vol.158 , pp. 5958-15665
    • Xu, Y.1    Volanakis, J.E.2
  • 214
    • 0028215971 scopus 로고
    • Recombinant and native zymogen forms of human complement factor D
    • Yamauchi, Y., Stevens, J. W., Macon, K. J., and Volanakis, J. E. (1994). Recombinant and native zymogen forms of human complement factor D.J. Immunol. 152, 3645-3653.
    • (1994) J. Immunol. , vol.152 , pp. 3645-3653
    • Yamauchi, Y.1    Stevens, J.W.2    Macon, K.J.3    Volanakis, J.E.4
  • 215
    • 0022655287 scopus 로고
    • CNBr cleavage of the light chain of human complement Factor I and alignment of the fragments
    • Yuan, J.-M., Hsiung, L.-M., and Gagnon, J. (1986). CNBr cleavage of the light chain of human complement Factor I and alignment of the fragments. Biochem. J. 233, 339-345.
    • (1986) Biochem. J. , vol.233 , pp. 339-345
    • Yuan, J.-M.1    Hsiung, L.-M.2    Gagnon, J.3
  • 217
    • 0025279104 scopus 로고
    • Allelic associations of multiple restriction fragment length polymorphisms of the gene encoding complement protein C2
    • Zhu, Z.-B., and Volanakis, J. E. (1990). Allelic associations of multiple restriction fragment length polymorphisms of the gene encoding complement protein C2. Am. J. Hum. Genet. 46, 956-962.
    • (1990) Am. J. Hum. Genet. , vol.46 , pp. 956-962
    • Zhu, Z.-B.1    Volanakis, J.E.2
  • 218
    • 0026531873 scopus 로고
    • A variable number of tandem repeats (VNTR) locus within the human complement C2 gene is associated with a retroposon derived from a human endogenous retrovirus
    • Zhu, Z.-B., Hsieh, S. L., Bentley, D. R., Campbell, R. D., and Volanakis, J. E. (1992). A variable number of tandem repeats (VNTR) locus within the human complement C2 gene is associated with a retroposon derived from a human endogenous retrovirus. J. Exp. Med. 175, 1783-1787.
    • (1992) J. Exp. Med. , vol.175 , pp. 1783-1787
    • Zhu, Z.-B.1    Hsieh, S.L.2    Bentley, D.R.3    Campbell, R.D.4    Volanakis, J.E.5
  • 219
    • 0028297151 scopus 로고
    • Ancestry of SINE-R.C2 a human-specific retroposon
    • Zhu, Z.-B., Jian, B., and Volanakis, J. E. (1994). Ancestry of SINE-R.C2 a human-specific retroposon. Hum. Genet. 93, 545-551.
    • (1994) Hum. Genet. , vol.93 , pp. 545-551
    • Zhu, Z.-B.1    Jian, B.2    Volanakis, J.E.3
  • 220
    • 0018355771 scopus 로고
    • Active disassembly of the first complement component, C1, by C1 inactivator
    • Ziccardi, R. J., and Cooper, N. R. (1979). Active disassembly of the first complement component, C1, by C1 inactivator. J. Immunol. 123, 788-792.
    • (1979) J. Immunol. , vol.123 , pp. 788-792
    • Ziccardi, R.J.1    Cooper, N.R.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.