메뉴 건너뛰기




Volumn 78, Issue 2, 2013, Pages 181-193

Humoral Pattern Recognition and the Complement System

Author keywords

[No Author keywords available]

Indexed keywords

ACETIC ACID DERIVATIVE; ACETYLCHOLINE; ACETYLCYSTEINE; ALANINE; C REACTIVE PROTEIN; CARBOHYDRATE; CHEMICALCOMPOSITION; COLLAGEN; COLLECTIN; COMPLEMENT COMPONENT C1Q; COMPLEMENT COMPONENT C1R; COMPLEMENT COMPONENT C1S; COMPLEMENT COMPONENT C3A; COMPLEMENT COMPONENT C3B; COMPLEMENT COMPONENT C4B; COMPLEMENT FACTOR H; DIMER; FICOLIN; GLYCINE; HOMODIMER; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M; LECTIN; MANNOSE BINDING LECTIN; MEMBRANE PROTEIN; OLIGOMER; OXIDIZED LOW DENSITY LIPOPROTEIN; PROTEIN CLP 1; SIALIC ACID DERIVATIVE; TETRAMER; UNCLASSIFIED DRUG;

EID: 84880682970     PISSN: 03009475     EISSN: 13653083     Source Type: Journal    
DOI: 10.1111/sji.12070     Document Type: Review
Times cited : (123)

References (102)
  • 1
    • 0024955886 scopus 로고
    • Approaching the asymptote? Evolution and revolution in immunology
    • Janeway CA Jr. Approaching the asymptote? Evolution and revolution in immunology. Cold Spring Harb Symp Quant Biol 1989;54(Pt 1):1-13.
    • (1989) Cold Spring Harb Symp Quant Biol , vol.54 , Issue.PT 1 , pp. 1-13
    • Janeway Jr., C.A.1
  • 2
    • 0028201732 scopus 로고
    • Tolerance, danger, and the extended family
    • Matzinger P. Tolerance, danger, and the extended family. Annu Rev Immunol 1994;12:991-1045.
    • (1994) Annu Rev Immunol , vol.12 , pp. 991-1045
    • Matzinger, P.1
  • 4
    • 84857546470 scopus 로고    scopus 로고
    • Beyond pattern recognition: five immune checkpoints for scaling the microbial threat
    • Blander JM, Sander LE. Beyond pattern recognition: five immune checkpoints for scaling the microbial threat. Nat Rev Immunol 2012;12:215-25.
    • (2012) Nat Rev Immunol , vol.12 , pp. 215-225
    • Blander, J.M.1    Sander, L.E.2
  • 5
    • 0344012497 scopus 로고    scopus 로고
    • The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties
    • Gaboriaud C, Juanhuix J, Gruez A et al. The crystal structure of the globular head of complement protein C1q provides a basis for its versatile recognition properties. J Biol Chem 2003;278:46974-82.
    • (2003) J Biol Chem , vol.278 , pp. 46974-46982
    • Gaboriaud, C.1    Juanhuix, J.2    Gruez, A.3
  • 6
    • 0033947551 scopus 로고    scopus 로고
    • C1q: structure, function, and receptors
    • Kishore U, Reid KB. C1q: structure, function, and receptors. Immunopharmacology 2000;49:159-70.
    • (2000) Immunopharmacology , vol.49 , pp. 159-170
    • Kishore, U.1    Reid, K.B.2
  • 7
    • 0022395838 scopus 로고
    • Structural model of the collagen-like region of C1q comprising the kink region and the fibre-like packing of the six triple helices
    • Kilchherr E, Hofmann H, Steigemann W, Engel J. Structural model of the collagen-like region of C1q comprising the kink region and the fibre-like packing of the six triple helices. J Mol Biol 1985;186:403-15.
    • (1985) J Mol Biol , vol.186 , pp. 403-415
    • Kilchherr, E.1    Hofmann, H.2    Steigemann, W.3    Engel, J.4
  • 8
    • 4544320857 scopus 로고    scopus 로고
    • C1q and tumor necrosis factor superfamily: modularity and versatility
    • Kishore U, Gaboriaud C, Waters P et al. C1q and tumor necrosis factor superfamily: modularity and versatility. Trends Immunol 2004;25:551-61.
    • (2004) Trends Immunol , vol.25 , pp. 551-561
    • Kishore, U.1    Gaboriaud, C.2    Waters, P.3
  • 9
    • 0021894435 scopus 로고
    • The classical complement pathway: activation and regulation of the first complement component
    • Cooper NR. The classical complement pathway: activation and regulation of the first complement component. Adv Immunol 1985;37:151-216.
    • (1985) Adv Immunol , vol.37 , pp. 151-216
    • Cooper, N.R.1
  • 10
    • 70349284531 scopus 로고    scopus 로고
    • The human IgM pentamer is a mushroom-shaped molecule with a flexural bias
    • Czajkowsky DM, Shao Z. The human IgM pentamer is a mushroom-shaped molecule with a flexural bias. Proc Natl Acad Sci U S A 2009;106:14960-5.
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 14960-14965
    • Czajkowsky, D.M.1    Shao, Z.2
  • 12
    • 0036469280 scopus 로고    scopus 로고
    • The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex
    • Budayova-Spano M, Lacroix M, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C. The crystal structure of the zymogen catalytic domain of complement protease C1r reveals that a disruptive mechanical stress is required to trigger activation of the C1 complex. EMBO J 2002;21:231-9.
    • (2002) EMBO J , vol.21 , pp. 231-239
    • Budayova-Spano, M.1    Lacroix, M.2    Thielens, N.M.3    Arlaud, G.J.4    Fontecilla-Camps, J.C.5    Gaboriaud, C.6
  • 13
    • 0030053692 scopus 로고    scopus 로고
    • The reaction mechanism of the internal thioester in the human complement component C4
    • Dodds AW, Ren XD, Willis AC, Law SK. The reaction mechanism of the internal thioester in the human complement component C4. Nature 1996;379:177-9.
    • (1996) Nature , vol.379 , pp. 177-179
    • Dodds, A.W.1    Ren, X.D.2    Willis, A.C.3    Law, S.K.4
  • 14
    • 0031043135 scopus 로고    scopus 로고
    • The internal thioester and the covalent binding properties of the complement proteins C3 and C4
    • Law SK, Dodds AW. The internal thioester and the covalent binding properties of the complement proteins C3 and C4. Protein Sci 1997;6:263-74.
    • (1997) Protein Sci , vol.6 , pp. 263-274
    • Law, S.K.1    Dodds, A.W.2
  • 15
    • 34249697602 scopus 로고    scopus 로고
    • The phylogeny of the complement system and the origins of the classical pathway
    • Dodds AW, Matsushita M. The phylogeny of the complement system and the origins of the classical pathway. Immunobiology 2007;212:233-43.
    • (2007) Immunobiology , vol.212 , pp. 233-243
    • Dodds, A.W.1    Matsushita, M.2
  • 16
    • 3042752926 scopus 로고    scopus 로고
    • Origin of the classical complement pathway: lamprey orthologue of mammalian C1q acts as a lectin
    • Matsushita M, Matsushita A, Endo Y et al. Origin of the classical complement pathway: lamprey orthologue of mammalian C1q acts as a lectin. Proc Natl Acad Sci U S A 2004;101:10127-31.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 10127-10131
    • Matsushita, M.1    Matsushita, A.2    Endo, Y.3
  • 17
    • 57649162572 scopus 로고    scopus 로고
    • Discrimination between host and pathogens by the complement system
    • Pangburn MK, Ferreira VP, Cortes C. Discrimination between host and pathogens by the complement system. Vaccine 2008;26(Suppl. 8):I15-21.
    • (2008) Vaccine , vol.26 , Issue.SUPPL. 8
    • Pangburn, M.K.1    Ferreira, V.P.2    Cortes, C.3
  • 18
    • 33645850696 scopus 로고    scopus 로고
    • Mannan-binding lectin (MBL)-mediated opsonization is enhanced by the alternative pathway amplification loop
    • Brouwer N, Dolman KM, van Zwieten R et al. Mannan-binding lectin (MBL)-mediated opsonization is enhanced by the alternative pathway amplification loop. Mol Immunol 2006;43:2051-60.
    • (2006) Mol Immunol , vol.43 , pp. 2051-2060
    • Brouwer, N.1    Dolman, K.M.2    van Zwieten, R.3
  • 19
    • 9644280856 scopus 로고    scopus 로고
    • The quantitative role of alternative pathway amplification in classical pathway induced terminal complement activation
    • Harboe M, Ulvund G, Vien L, Fung M, Mollnes TE. The quantitative role of alternative pathway amplification in classical pathway induced terminal complement activation. Clin Exp Immunol 2004;138:439-46.
    • (2004) Clin Exp Immunol , vol.138 , pp. 439-446
    • Harboe, M.1    Ulvund, G.2    Vien, L.3    Fung, M.4    Mollnes, T.E.5
  • 20
    • 0036748150 scopus 로고    scopus 로고
    • Which came first, the lectin/classical pathway or the alternative pathway of complement?
    • Dodds AW. Which came first, the lectin/classical pathway or the alternative pathway of complement? Immunobiology 2002;205:340-54.
    • (2002) Immunobiology , vol.205 , pp. 340-354
    • Dodds, A.W.1
  • 21
    • 0036584407 scopus 로고    scopus 로고
    • Evolution of the lectin-complement pathway and its role in innate immunity
    • Fujita T. Evolution of the lectin-complement pathway and its role in innate immunity. Nat Rev Immunol 2002;2:346-53.
    • (2002) Nat Rev Immunol , vol.2 , pp. 346-353
    • Fujita, T.1
  • 22
    • 84867324414 scopus 로고    scopus 로고
    • Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function
    • Degn SE, Jensen L, Hansen AG et al. Mannan-binding lectin-associated serine protease (MASP)-1 is crucial for lectin pathway activation in human serum, whereas neither MASP-1 nor MASP-3 is required for alternative pathway function. J Immunol 2012;189:3957-69.
    • (2012) J Immunol , vol.189 , pp. 3957-3969
    • Degn, S.E.1    Jensen, L.2    Hansen, A.G.3
  • 23
    • 84863001154 scopus 로고    scopus 로고
    • Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2
    • Heja D, Kocsis A, Dobo J et al. Revised mechanism of complement lectin-pathway activation revealing the role of serine protease MASP-1 as the exclusive activator of MASP-2. Proc Natl Acad Sci U S A 2012;109:10498-503.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 10498-10503
    • Heja, D.1    Kocsis, A.2    Dobo, J.3
  • 24
    • 33846618236 scopus 로고    scopus 로고
    • Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway
    • Moller-Kristensen M, Thiel S, Sjoholm A, Matsushita M, Jensenius JC. Cooperation between MASP-1 and MASP-2 in the generation of C3 convertase through the MBL pathway. Int Immunol 2007;19:141-9.
    • (2007) Int Immunol , vol.19 , pp. 141-149
    • Moller-Kristensen, M.1    Thiel, S.2    Sjoholm, A.3    Matsushita, M.4    Jensenius, J.C.5
  • 25
    • 84862023318 scopus 로고    scopus 로고
    • Monospecific Inhibitors Show That Both Mannan-binding Lectin-associated Serine Protease-1 (MASP-1) and -2 Are Essential for Lectin Pathway Activation and Reveal Structural Plasticity of MASP-2
    • Heja D, Harmat V, Fodor K et al. Monospecific Inhibitors Show That Both Mannan-binding Lectin-associated Serine Protease-1 (MASP-1) and -2 Are Essential for Lectin Pathway Activation and Reveal Structural Plasticity of MASP-2. J Biol Chem 2012;287:20290-300.
    • (2012) J Biol Chem , vol.287 , pp. 20290-20300
    • Heja, D.1    Harmat, V.2    Fodor, K.3
  • 26
    • 84861758824 scopus 로고    scopus 로고
    • Mannan-binding lectin (MBL)-associated serine protease-1 (MASP-1), a serine protease associated with humoral pattern-recognition molecules: normal and acute-phase levels in serum and stoichiometry of lectin pathway components
    • Thiel S, Jensen L, Degn SE et al. Mannan-binding lectin (MBL)-associated serine protease-1 (MASP-1), a serine protease associated with humoral pattern-recognition molecules: normal and acute-phase levels in serum and stoichiometry of lectin pathway components. Clin Exp Immunol 2012;169:38-48.
    • (2012) Clin Exp Immunol , vol.169 , pp. 38-48
    • Thiel, S.1    Jensen, L.2    Degn, S.E.3
  • 27
    • 76149085506 scopus 로고    scopus 로고
    • Essential role of mannose-binding lectin-associated serine protease-1 in activation of the complement factor D
    • Takahashi M, Ishida Y, Iwaki D et al. Essential role of mannose-binding lectin-associated serine protease-1 in activation of the complement factor D. J Exp Med 2010;207:29-37.
    • (2010) J Exp Med , vol.207 , pp. 29-37
    • Takahashi, M.1    Ishida, Y.2    Iwaki, D.3
  • 28
    • 0032860314 scopus 로고    scopus 로고
    • C-type lectin-like domains
    • Drickamer K. C-type lectin-like domains. Curr Opin Struct Biol 1999;9:585-90.
    • (1999) Curr Opin Struct Biol , vol.9 , pp. 585-590
    • Drickamer, K.1
  • 29
    • 0026439234 scopus 로고
    • Engineering galactose-binding activity into a C-type mannose-binding protein
    • Drickamer K. Engineering galactose-binding activity into a C-type mannose-binding protein. Nature 1992;360:183-6.
    • (1992) Nature , vol.360 , pp. 183-186
    • Drickamer, K.1
  • 30
    • 0031820273 scopus 로고    scopus 로고
    • The C-type lectin superfamily in the immune system
    • Weis WI, Taylor ME, Drickamer K. The C-type lectin superfamily in the immune system. Immunol Rev 1998;163:19-34.
    • (1998) Immunol Rev , vol.163 , pp. 19-34
    • Weis, W.I.1    Taylor, M.E.2    Drickamer, K.3
  • 31
    • 33845786617 scopus 로고    scopus 로고
    • Identification and characterization of a novel human collectin CL-K1
    • Keshi H, Sakamoto T, Kawai T et al. Identification and characterization of a novel human collectin CL-K1. Microbiol Immunol 2006;50:1001-13.
    • (2006) Microbiol Immunol , vol.50 , pp. 1001-1013
    • Keshi, H.1    Sakamoto, T.2    Kawai, T.3
  • 32
    • 15744379234 scopus 로고    scopus 로고
    • Characterization of the oligomer structure of recombinant human mannan-binding lectin
    • Jensen PH, Weilguny D, Matthiesen F, McGuire KA, Shi L, Hojrup P. Characterization of the oligomer structure of recombinant human mannan-binding lectin. J Biol Chem 2005;280:11043-51.
    • (2005) J Biol Chem , vol.280 , pp. 11043-11051
    • Jensen, P.H.1    Weilguny, D.2    Matthiesen, F.3    McGuire, K.A.4    Shi, L.5    Hojrup, P.6
  • 33
    • 0033525189 scopus 로고    scopus 로고
    • Molecular determinants of oligomer formation and complement fixation in mannose-binding proteins
    • Wallis R, Drickamer K. Molecular determinants of oligomer formation and complement fixation in mannose-binding proteins. J Biol Chem 1999;274:3580-9.
    • (1999) J Biol Chem , vol.274 , pp. 3580-3589
    • Wallis, R.1    Drickamer, K.2
  • 34
    • 0029126382 scopus 로고
    • Distinct physicochemical characteristics of human mannose binding protein expressed by individuals of differing genotype
    • Lipscombe RJ, Sumiya M, Summerfield JA, Turner MW. Distinct physicochemical characteristics of human mannose binding protein expressed by individuals of differing genotype. Immunology 1995;85:660-7.
    • (1995) Immunology , vol.85 , pp. 660-667
    • Lipscombe, R.J.1    Sumiya, M.2    Summerfield, J.A.3    Turner, M.W.4
  • 35
    • 34247631620 scopus 로고    scopus 로고
    • Identification of the site of human mannan-binding lectin involved in the interaction with its partner serine proteases: the essential role of Lys55
    • Teillet F, Lacroix M, Thiel S et al. Identification of the site of human mannan-binding lectin involved in the interaction with its partner serine proteases: the essential role of Lys55. J Immunol 2007;178:5710-6.
    • (2007) J Immunol , vol.178 , pp. 5710-5716
    • Teillet, F.1    Lacroix, M.2    Thiel, S.3
  • 36
    • 34250822219 scopus 로고    scopus 로고
    • Localization and characterization of the mannose-binding lectin (MBL)-associated-serine protease-2 binding site in rat ficolin-A: equivalent binding sites within the collagenous domains of MBLs and ficolins
    • Girija UV, Dodds AW, Roscher S, Reid KB, Wallis R. Localization and characterization of the mannose-binding lectin (MBL)-associated-serine protease-2 binding site in rat ficolin-A: equivalent binding sites within the collagenous domains of MBLs and ficolins. J Immunol 2007;179:455-62.
    • (2007) J Immunol , vol.179 , pp. 455-462
    • Girija, U.V.1    Dodds, A.W.2    Roscher, S.3    Reid, K.B.4    Wallis, R.5
  • 37
    • 1842740356 scopus 로고    scopus 로고
    • Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: indirect effects of naturally occurring mutations on protease binding and activation
    • Wallis R, Shaw JM, Uitdehaag J, Chen CB, Torgersen D, Drickamer K. Localization of the serine protease-binding sites in the collagen-like domain of mannose-binding protein: indirect effects of naturally occurring mutations on protease binding and activation. J Biol Chem 2004;279:14065-73.
    • (2004) J Biol Chem , vol.279 , pp. 14065-14073
    • Wallis, R.1    Shaw, J.M.2    Uitdehaag, J.3    Chen, C.B.4    Torgersen, D.5    Drickamer, K.6
  • 38
    • 33847400443 scopus 로고    scopus 로고
    • Conformational changes in mannan-binding lectin bound to ligand surfaces
    • Dong M, Xu S, Oliveira CL et al. Conformational changes in mannan-binding lectin bound to ligand surfaces. J Immunol 2007;178:3016-22.
    • (2007) J Immunol , vol.178 , pp. 3016-3022
    • Dong, M.1    Xu, S.2    Oliveira, C.L.3
  • 39
    • 67651115625 scopus 로고    scopus 로고
    • Mannan-binding lectin: structure, oligomerization, and flexibility studied by atomic force microscopy
    • Jensenius H, Klein DC, van Hecke M, Oosterkamp TH, Schmidt T, Jensenius JC. Mannan-binding lectin: structure, oligomerization, and flexibility studied by atomic force microscopy. J Mol Biol 2009;391:246-59.
    • (2009) J Mol Biol , vol.391 , pp. 246-259
    • Jensenius, H.1    Klein, D.C.2    van Hecke, M.3    Oosterkamp, T.H.4    Schmidt, T.5    Jensenius, J.C.6
  • 40
    • 0026464832 scopus 로고
    • Structure of a C-type mannose-binding protein complexed with an oligosaccharide
    • Weis WI, Drickamer K, Hendrickson WA. Structure of a C-type mannose-binding protein complexed with an oligosaccharide. Nature 1992;360:127-34.
    • (1992) Nature , vol.360 , pp. 127-134
    • Weis, W.I.1    Drickamer, K.2    Hendrickson, W.A.3
  • 41
    • 0034738657 scopus 로고    scopus 로고
    • Detection of structural gene mutations and promoter polymorphisms in the mannan-binding lectin (MBL) gene by polymerase chain reaction with sequence-specific primers
    • Steffensen R, Thiel S, Varming K, Jersild C, Jensenius JC. Detection of structural gene mutations and promoter polymorphisms in the mannan-binding lectin (MBL) gene by polymerase chain reaction with sequence-specific primers. J Immunol Methods 2000;241:33-42.
    • (2000) J Immunol Methods , vol.241 , pp. 33-42
    • Steffensen, R.1    Thiel, S.2    Varming, K.3    Jersild, C.4    Jensenius, J.C.5
  • 42
    • 0033532164 scopus 로고    scopus 로고
    • Molecular cloning of a novel human collectin from liver (CL-L1)
    • Ohtani K, Suzuki Y, Eda S et al. Molecular cloning of a novel human collectin from liver (CL-L1). J Biol Chem 1999;274:13681-9.
    • (1999) J Biol Chem , vol.274 , pp. 13681-13689
    • Ohtani, K.1    Suzuki, Y.2    Eda, S.3
  • 43
    • 0035941356 scopus 로고    scopus 로고
    • The membrane-type collectin CL-P1 is a scavenger receptor on vascular endothelial cells
    • Ohtani K, Suzuki Y, Eda S et al. The membrane-type collectin CL-P1 is a scavenger receptor on vascular endothelial cells. J Biol Chem 2001;276:44222-8.
    • (2001) J Biol Chem , vol.276 , pp. 44222-44228
    • Ohtani, K.1    Suzuki, Y.2    Eda, S.3
  • 44
    • 63649145842 scopus 로고    scopus 로고
    • Scavenger receptor collectin placenta 1 (CL-P1) predominantly mediates zymosan phagocytosis by human vascular endothelial cells
    • Jang S, Ohtani K, Fukuoh A et al. Scavenger receptor collectin placenta 1 (CL-P1) predominantly mediates zymosan phagocytosis by human vascular endothelial cells. J Biol Chem 2009;284:3956-65.
    • (2009) J Biol Chem , vol.284 , pp. 3956-3965
    • Jang, S.1    Ohtani, K.2    Fukuoh, A.3
  • 45
    • 78650637010 scopus 로고    scopus 로고
    • Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin with microbial-binding activity
    • Hansen S, Selman L, Palaniyar N et al. Collectin 11 (CL-11, CL-K1) is a MASP-1/3-associated plasma collectin with microbial-binding activity. J Immunol 2010;185:6096-104.
    • (2010) J Immunol , vol.185 , pp. 6096-6104
    • Hansen, S.1    Selman, L.2    Palaniyar, N.3
  • 46
    • 34249680284 scopus 로고    scopus 로고
    • Interactions between mannose-binding lectin and MASPs during complement activation by the lectin pathway
    • Wallis R. Interactions between mannose-binding lectin and MASPs during complement activation by the lectin pathway. Immunobiology 2007;212:289-99.
    • (2007) Immunobiology , vol.212 , pp. 289-299
    • Wallis, R.1
  • 47
    • 84876803133 scopus 로고    scopus 로고
    • Collectin-11/MASP complex formation triggers activation of the lectin complement pathway-the fifth lectin pathway initiation complex
    • Ma YJ, Skjoedt MO, Garred P. Collectin-11/MASP complex formation triggers activation of the lectin complement pathway-the fifth lectin pathway initiation complex. J Innate Immun. 2012;5:242-50.
    • (2012) J Innate Immun , vol.5 , pp. 242-250
    • Ma, Y.J.1    Skjoedt, M.O.2    Garred, P.3
  • 48
    • 0027278514 scopus 로고
    • Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains
    • Ichijo H, Hellman U, Wernstedt C et al. Molecular cloning and characterization of ficolin, a multimeric protein with fibrinogen- and collagen-like domains. J Biol Chem 1993;268:14505-13.
    • (1993) J Biol Chem , vol.268 , pp. 14505-14513
    • Ichijo, H.1    Hellman, U.2    Wernstedt, C.3
  • 49
    • 4744376266 scopus 로고    scopus 로고
    • Identification of the mouse H-ficolin gene as a pseudogene and orthology between mouse ficolins A/B and human L-/M-ficolins
    • Endo Y, Liu Y, Kanno K, Takahashi M, Matsushita M, Fujita T. Identification of the mouse H-ficolin gene as a pseudogene and orthology between mouse ficolins A/B and human L-/M-ficolins. Genomics 2004;84:737-44.
    • (2004) Genomics , vol.84 , pp. 737-744
    • Endo, Y.1    Liu, Y.2    Kanno, K.3    Takahashi, M.4    Matsushita, M.5    Fujita, T.6
  • 50
    • 18344409247 scopus 로고    scopus 로고
    • Human L-ficolin: plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen-like (FBG) domain
    • Le Y, Lee SH, Kon OL, Lu J. Human L-ficolin: plasma levels, sugar specificity, and assignment of its lectin activity to the fibrinogen-like (FBG) domain. FEBS Lett 1998;425:367-70.
    • (1998) FEBS Lett , vol.425 , pp. 367-370
    • Le, Y.1    Lee, S.H.2    Kon, O.L.3    Lu, J.4
  • 51
    • 0032516814 scopus 로고    scopus 로고
    • Cloning and characterization of the Hakata antigen, a member of the ficolin/opsonin p35 lectin family
    • Sugimoto R, Yae Y, Akaiwa M et al. Cloning and characterization of the Hakata antigen, a member of the ficolin/opsonin p35 lectin family. J Biol Chem 1998;273:20721-7.
    • (1998) J Biol Chem , vol.273 , pp. 20721-20727
    • Sugimoto, R.1    Yae, Y.2    Akaiwa, M.3
  • 52
    • 9144249121 scopus 로고    scopus 로고
    • L-ficolin is a pattern recognition molecule specific for acetyl groups
    • Krarup A, Thiel S, Hansen A, Fujita T, Jensenius JC. L-ficolin is a pattern recognition molecule specific for acetyl groups. J Biol Chem 2004;279:47513-9.
    • (2004) J Biol Chem , vol.279 , pp. 47513-47519
    • Krarup, A.1    Thiel, S.2    Hansen, A.3    Fujita, T.4    Jensenius, J.C.5
  • 53
    • 0025490665 scopus 로고
    • Serological studies of an SLE-associated antigen-antibody system discovered as a precipitation reaction in agarose gel: the HAKATA antigen-antibody system
    • Inaba S, Okochi K, Yae Y, Niklasson F, de Verder CH. Serological studies of an SLE-associated antigen-antibody system discovered as a precipitation reaction in agarose gel: the HAKATA antigen-antibody system. Fukuoka Igaku Zasshi 1990;81:284-91.
    • (1990) Fukuoka Igaku Zasshi , vol.81 , pp. 284-291
    • Inaba, S.1    Okochi, K.2    Yae, Y.3    Niklasson, F.4    de Verder, C.H.5
  • 54
    • 0025740319 scopus 로고
    • Isolation and characterization of a thermolabile beta-2 macroglycoprotein ('thermolabile substance' or 'Hakata antigen') detected by precipitating (auto) antibody in sera of patients with systemic lupus erythematosus
    • Yae Y, Inaba S, Sato H, Okochi K, Tokunaga F, Iwanaga S. Isolation and characterization of a thermolabile beta-2 macroglycoprotein ('thermolabile substance' or 'Hakata antigen') detected by precipitating (auto) antibody in sera of patients with systemic lupus erythematosus. Biochim Biophys Acta 1991;1078:369-76.
    • (1991) Biochim Biophys Acta , vol.1078 , pp. 369-376
    • Yae, Y.1    Inaba, S.2    Sato, H.3    Okochi, K.4    Tokunaga, F.5    Iwanaga, S.6
  • 55
    • 0028828690 scopus 로고
    • Hucolin, a new corticosteroid-binding protein from human plasma with structural similarities to ficolins, transforming growth factor-beta 1-binding proteins
    • Edgar PF. Hucolin, a new corticosteroid-binding protein from human plasma with structural similarities to ficolins, transforming growth factor-beta 1-binding proteins. FEBS Lett 1995;375:159-61.
    • (1995) FEBS Lett , vol.375 , pp. 159-161
    • Edgar, P.F.1
  • 56
    • 0029018314 scopus 로고
    • EBP-37, a new elastin-binding protein in human plasma: structural similarity to ficolins, transforming growth factor-beta 1-binding proteins
    • Harumiya S, Omori A, Sugiura T, Fukumoto Y, Tachikawa H, Fujimoto D. EBP-37, a new elastin-binding protein in human plasma: structural similarity to ficolins, transforming growth factor-beta 1-binding proteins. J Biochem 1995;117:1029-35.
    • (1995) J Biochem , vol.117 , pp. 1029-1035
    • Harumiya, S.1    Omori, A.2    Sugiura, T.3    Fukumoto, Y.4    Tachikawa, H.5    Fujimoto, D.6
  • 57
    • 0030068057 scopus 로고    scopus 로고
    • A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin
    • Matsushita M, Endo Y, Taira S et al. A novel human serum lectin with collagen- and fibrinogen-like domains that functions as an opsonin. J Biol Chem 1996;271:2448-54.
    • (1996) J Biol Chem , vol.271 , pp. 2448-2454
    • Matsushita, M.1    Endo, Y.2    Taira, S.3
  • 58
    • 0030587494 scopus 로고    scopus 로고
    • Cloning and characterization of the human lectin P35 gene and its related gene
    • Endo Y, Sato Y, Matsushita M, Fujita T. Cloning and characterization of the human lectin P35 gene and its related gene. Genomics 1996;36:515-21.
    • (1996) Genomics , vol.36 , pp. 515-521
    • Endo, Y.1    Sato, Y.2    Matsushita, M.3    Fujita, T.4
  • 59
    • 0030034860 scopus 로고    scopus 로고
    • Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9
    • Lu J, Tay PN, Kon OL, Reid KB. Human ficolin: cDNA cloning, demonstration of peripheral blood leucocytes as the major site of synthesis and assignment of the gene to chromosome 9. Biochem J 1996;313(Pt 2):473-8.
    • (1996) Biochem J , vol.313 , Issue.PT 2 , pp. 473-478
    • Lu, J.1    Tay, P.N.2    Kon, O.L.3    Reid, K.B.4
  • 60
    • 0033060134 scopus 로고    scopus 로고
    • Hakata antigen, a new member of the ficolin/opsonin p35 family, is a novel human lectin secreted into bronchus/alveolus and bile
    • Akaiwa M, Yae Y, Sugimoto R et al. Hakata antigen, a new member of the ficolin/opsonin p35 family, is a novel human lectin secreted into bronchus/alveolus and bile. J Histochem Cytochem 1999;47:777-86.
    • (1999) J Histochem Cytochem , vol.47 , pp. 777-786
    • Akaiwa, M.1    Yae, Y.2    Sugimoto, R.3
  • 61
    • 12844264792 scopus 로고    scopus 로고
    • Effect of capsulation of opportunistic pathogenic bacteria on binding of the pattern recognition molecules mannan-binding lectin, L-ficolin, and H-ficolin
    • Krarup A, Sorensen UB, Matsushita M, Jensenius JC, Thiel S. Effect of capsulation of opportunistic pathogenic bacteria on binding of the pattern recognition molecules mannan-binding lectin, L-ficolin, and H-ficolin. Infect Immun 2005;73:1052-60.
    • (2005) Infect Immun , vol.73 , pp. 1052-1060
    • Krarup, A.1    Sorensen, U.B.2    Matsushita, M.3    Jensenius, J.C.4    Thiel, S.5
  • 62
    • 0035102553 scopus 로고    scopus 로고
    • Detection of serum thermolabile beta-2 macroglycoprotein (Hakata antigen) by enzyme-linked immunosorbent assay using polysaccharide produced by Aerococcus viridans
    • Tsujimura M, Ishida C, Sagara Y et al. Detection of serum thermolabile beta-2 macroglycoprotein (Hakata antigen) by enzyme-linked immunosorbent assay using polysaccharide produced by Aerococcus viridans. Clin Diagn Lab Immunol 2001;8:454-9.
    • (2001) Clin Diagn Lab Immunol , vol.8 , pp. 454-459
    • Tsujimura, M.1    Ishida, C.2    Sagara, Y.3
  • 63
    • 0036844208 scopus 로고    scopus 로고
    • Serum concentration of Hakata antigen, a member of the ficolins, is linked with inhibition of Aerococcus viridans growth
    • Tsujimura M, Miyazaki T, Kojima E et al. Serum concentration of Hakata antigen, a member of the ficolins, is linked with inhibition of Aerococcus viridans growth. Clin Chim Acta 2002;325:139-46.
    • (2002) Clin Chim Acta , vol.325 , pp. 139-146
    • Tsujimura, M.1    Miyazaki, T.2    Kojima, E.3
  • 65
    • 0037111532 scopus 로고    scopus 로고
    • Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2
    • Cseh S, Vera L, Matsushita M, Fujita T, Arlaud GJ, Thielens NM. Characterization of the interaction between L-ficolin/p35 and mannan-binding lectin-associated serine proteases-1 and -2. J Immunol 2002;169:5735-43.
    • (2002) J Immunol , vol.169 , pp. 5735-5743
    • Cseh, S.1    Vera, L.2    Matsushita, M.3    Fujita, T.4    Arlaud, G.J.5    Thielens, N.M.6
  • 66
    • 0034163330 scopus 로고    scopus 로고
    • Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease
    • Matsushita M, Endo Y, Fujita T. Cutting edge: complement-activating complex of ficolin and mannose-binding lectin-associated serine protease. J Immunol 2000;164:2281-4.
    • (2000) J Immunol , vol.164 , pp. 2281-2284
    • Matsushita, M.1    Endo, Y.2    Fujita, T.3
  • 67
    • 28344454827 scopus 로고    scopus 로고
    • M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement
    • Frederiksen PD, Thiel S, Larsen CB, Jensenius JC. M-ficolin, an innate immune defence molecule, binds patterns of acetyl groups and activates complement. Scand J Immunol 2005;62:462-73.
    • (2005) Scand J Immunol , vol.62 , pp. 462-473
    • Frederiksen, P.D.1    Thiel, S.2    Larsen, C.B.3    Jensenius, J.C.4
  • 68
    • 0033781775 scopus 로고    scopus 로고
    • M-ficolin is expressed on monocytes and is a lectin binding to N-acetyl-D-glucosamine and mediates monocyte adhesion and phagocytosis of Escherichia coli
    • Teh C, Le Y, Lee SH, Lu J. M-ficolin is expressed on monocytes and is a lectin binding to N-acetyl-D-glucosamine and mediates monocyte adhesion and phagocytosis of Escherichia coli. Immunology 2000;101:225-32.
    • (2000) Immunology , vol.101 , pp. 225-232
    • Teh, C.1    Le, Y.2    Lee, S.H.3    Lu, J.4
  • 69
    • 23844486704 scopus 로고    scopus 로고
    • Human M-ficolin is a secretory protein that activates the lectin complement pathway
    • Liu Y, Endo Y, Iwaki D et al. Human M-ficolin is a secretory protein that activates the lectin complement pathway. J Immunol 2005;175:3150-6.
    • (2005) J Immunol , vol.175 , pp. 3150-3156
    • Liu, Y.1    Endo, Y.2    Iwaki, D.3
  • 70
    • 0029821215 scopus 로고    scopus 로고
    • Biosynthesis of human ficolin, an Escherichia coli-binding protein, by monocytes: comparison with the synthesis of two macrophage-specific proteins, C1q and the mannose receptor
    • Lu J, Le Y, Kon OL, Chan J, Lee SH. Biosynthesis of human ficolin, an Escherichia coli-binding protein, by monocytes: comparison with the synthesis of two macrophage-specific proteins, C1q and the mannose receptor. Immunology 1996;89:289-94.
    • (1996) Immunology , vol.89 , pp. 289-294
    • Lu, J.1    Le, Y.2    Kon, O.L.3    Chan, J.4    Lee, S.H.5
  • 71
    • 77953402526 scopus 로고    scopus 로고
    • Characteristics and Biological Variations of M-Ficolin, a Pattern Recognition Molecule, in Plasma
    • Wittenborn T, Thiel S, Jensen L, Nielsen HJ, Jensenius JC. Characteristics and Biological Variations of M-Ficolin, a Pattern Recognition Molecule, in Plasma. J Innate Immun 2010;2:167-80.
    • (2010) J Innate Immun , vol.2 , pp. 167-180
    • Wittenborn, T.1    Thiel, S.2    Jensen, L.3    Nielsen, H.J.4    Jensenius, J.C.5
  • 72
    • 77954671539 scopus 로고    scopus 로고
    • Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain
    • Honoré C, Rørvig S, Hummelshøj T, Skjoedt M-O, Borregaard N, Garred P. Tethering of Ficolin-1 to cell surfaces through recognition of sialic acid by the fibrinogen-like domain. J Leukoc Biol 2010;88:145-58.
    • (2010) J Leukoc Biol , vol.88 , pp. 145-158
    • Honoré, C.1    Rørvig, S.2    Hummelshøj, T.3    Skjoedt, M.-O.4    Borregaard, N.5    Garred, P.6
  • 73
    • 77949878087 scopus 로고    scopus 로고
    • Carbohydrate recognition properties of human ficolins: glycan array screening reveals the sialic acid binding specificity of M-ficolin
    • Gout E, Garlatti V, Smith DF et al. Carbohydrate recognition properties of human ficolins: glycan array screening reveals the sialic acid binding specificity of M-ficolin. J Biol Chem 2010;285:6612-22.
    • (2010) J Biol Chem , vol.285 , pp. 6612-6622
    • Gout, E.1    Garlatti, V.2    Smith, D.F.3
  • 74
    • 16344380083 scopus 로고    scopus 로고
    • Inherent specificities in natural antibodies: a key to immune defense against pathogen invasion
    • Baumgarth N, Tung JW, Herzenberg LA. Inherent specificities in natural antibodies: a key to immune defense against pathogen invasion. Springer Semin Immunopathol 2005;26:347-62.
    • (2005) Springer Semin Immunopathol , vol.26 , pp. 347-362
    • Baumgarth, N.1    Tung, J.W.2    Herzenberg, L.A.3
  • 75
    • 0017073905 scopus 로고
    • Circular-dichroism and electron-microscopy studies of human subcomponent C1q before and after limited proteolysis by pepsin
    • Brodsky-Doyle B, Leonard KR, Reid KB. Circular-dichroism and electron-microscopy studies of human subcomponent C1q before and after limited proteolysis by pepsin. Biochem J 1976;159:279-86.
    • (1976) Biochem J , vol.159 , pp. 279-286
    • Brodsky-Doyle, B.1    Leonard, K.R.2    Reid, K.B.3
  • 76
    • 0019856780 scopus 로고
    • Semi-flexible joint in the C1q subunit of the first component of human complement
    • Schumaker VN, Poon PH, Seegan GW, Smith CA. Semi-flexible joint in the C1q subunit of the first component of human complement. J Mol Biol 1981;148:191-7.
    • (1981) J Mol Biol , vol.148 , pp. 191-197
    • Schumaker, V.N.1    Poon, P.H.2    Seegan, G.W.3    Smith, C.A.4
  • 77
    • 0023890913 scopus 로고
    • Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36. Structural homology with the complement factor C1q
    • Voss T, Eistetter H, Schafer KP, Engel J. Macromolecular organization of natural and recombinant lung surfactant protein SP 28-36. Structural homology with the complement factor C1q. J Mol Biol 1988;201:219-27.
    • (1988) J Mol Biol , vol.201 , pp. 219-227
    • Voss, T.1    Eistetter, H.2    Schafer, K.P.3    Engel, J.4
  • 78
    • 0031009906 scopus 로고    scopus 로고
    • Two oligomeric forms of plasma ficolin have differential lectin activity
    • Ohashi T, Erickson HP. Two oligomeric forms of plasma ficolin have differential lectin activity. J Biol Chem 1997;272:14220-6.
    • (1997) J Biol Chem , vol.272 , pp. 14220-14226
    • Ohashi, T.1    Erickson, H.P.2
  • 79
    • 73349128762 scopus 로고    scopus 로고
    • MAp44, a human protein associated with pattern recognition molecules of the complement system and regulating the lectin pathway of complement activation
    • Degn SE, Hansen AG, Steffensen R, Jacobsen C, Jensenius JC, Thiel S. MAp44, a human protein associated with pattern recognition molecules of the complement system and regulating the lectin pathway of complement activation. J Immunol 2009;183:7371-8.
    • (2009) J Immunol , vol.183 , pp. 7371-7378
    • Degn, S.E.1    Hansen, A.G.2    Steffensen, R.3    Jacobsen, C.4    Jensenius, J.C.5    Thiel, S.6
  • 80
    • 0041856103 scopus 로고    scopus 로고
    • X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement
    • Gregory LA, Thielens NM, Arlaud GJ, Fontecilla-Camps JC, Gaboriaud C. X-ray structure of the Ca2+-binding interaction domain of C1s. Insights into the assembly of the C1 complex of complement. J Biol Chem 2003;278:32157-64.
    • (2003) J Biol Chem , vol.278 , pp. 32157-32164
    • Gregory, L.A.1    Thielens, N.M.2    Arlaud, G.J.3    Fontecilla-Camps, J.C.4    Gaboriaud, C.5
  • 81
    • 3142733778 scopus 로고    scopus 로고
    • The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin
    • Gregory LA, Thielens NM, Matsushita M et al. The X-ray structure of human mannan-binding lectin-associated protein 19 (MAp19) and its interaction site with mannan-binding lectin and L-ficolin. J Biol Chem 2004;279:29391-7.
    • (2004) J Biol Chem , vol.279 , pp. 29391-29397
    • Gregory, L.A.1    Thielens, N.M.2    Matsushita, M.3
  • 82
    • 0035871632 scopus 로고    scopus 로고
    • Interaction properties of human mannan-binding lectin (MBL)-associated serine proteases-1 and -2, MBL-associated protein 19, and MBL
    • Thielens NM, Cseh S, Thiel S et al. Interaction properties of human mannan-binding lectin (MBL)-associated serine proteases-1 and -2, MBL-associated protein 19, and MBL. J Immunol 2001;166:5068-77.
    • (2001) J Immunol , vol.166 , pp. 5068-5077
    • Thielens, N.M.1    Cseh, S.2    Thiel, S.3
  • 83
    • 0034613383 scopus 로고    scopus 로고
    • Interaction of mannose-binding protein with associated serine proteases: effects of naturally occurring mutations
    • Wallis R, Dodd RB. Interaction of mannose-binding protein with associated serine proteases: effects of naturally occurring mutations. J Biol Chem 2000;275:30962-9.
    • (2000) J Biol Chem , vol.275 , pp. 30962-30969
    • Wallis, R.1    Dodd, R.B.2
  • 84
    • 0035854681 scopus 로고    scopus 로고
    • Stoichiometry of complexes between mannose-binding protein and its associated serine proteases. Defining functional units for complement activation
    • Chen CB, Wallis R. Stoichiometry of complexes between mannose-binding protein and its associated serine proteases. Defining functional units for complement activation. J Biol Chem 2001;276:25894-902.
    • (2001) J Biol Chem , vol.276 , pp. 25894-25902
    • Chen, C.B.1    Wallis, R.2
  • 85
    • 84880694323 scopus 로고    scopus 로고
    • Co-complexes of MASP-1 and MASP-2 associated with the soluble pattern recognition molecules drive lectin pathway activation in a manner inhibitable by MAp44.
    • Degn SE, Jensen L, Olszowski T, Jensenius JC, Thiel S. Co-complexes of MASP-1 and MASP-2 associated with the soluble pattern recognition molecules drive lectin pathway activation in a manner inhibitable by MAp44. J Immunol (in press).
    • J Immunol
    • Degn, S.E.1    Jensen, L.2    Olszowski, T.3    Jensenius, J.C.4    Thiel, S.5
  • 86
    • 4444375264 scopus 로고    scopus 로고
    • The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions
    • Harmat V, Gal P, Kardos J et al. The structure of MBL-associated serine protease-2 reveals that identical substrate specificities of C1s and MASP-2 are realized through different sets of enzyme-substrate interactions. J Mol Biol 2004;342:1533-46.
    • (2004) J Mol Biol , vol.342 , pp. 1533-1546
    • Harmat, V.1    Gal, P.2    Kardos, J.3
  • 87
    • 29644445934 scopus 로고    scopus 로고
    • Functional characterization of complement proteases C1s/mannan-binding lectin-associated serine protease-2 (MASP-2) chimeras reveals the higher C4 recognition efficacy of the MASP-2 complement control protein modules
    • Rossi V, Teillet F, Thielens NM, Bally I, Arlaud GJ. Functional characterization of complement proteases C1s/mannan-binding lectin-associated serine protease-2 (MASP-2) chimeras reveals the higher C4 recognition efficacy of the MASP-2 complement control protein modules. J Biol Chem 2005;280:41811-8.
    • (2005) J Biol Chem , vol.280 , pp. 41811-41818
    • Rossi, V.1    Teillet, F.2    Thielens, N.M.3    Bally, I.4    Arlaud, G.J.5
  • 88
    • 54449087793 scopus 로고    scopus 로고
    • Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins
    • Teillet F, Gaboriaud C, Lacroix M, Martin L, Arlaud GJ, Thielens NM. Crystal structure of the CUB1-EGF-CUB2 domain of human MASP-1/3 and identification of its interaction sites with mannan-binding lectin and ficolins. J Biol Chem 2008;283:25715-24.
    • (2008) J Biol Chem , vol.283 , pp. 25715-25724
    • Teillet, F.1    Gaboriaud, C.2    Lacroix, M.3    Martin, L.4    Arlaud, G.J.5    Thielens, N.M.6
  • 89
    • 14044278783 scopus 로고    scopus 로고
    • The two major oligomeric forms of human mannan-binding lectin: chemical characterization, carbohydrate-binding properties, and interaction with MBL-associated serine proteases
    • Teillet F, Dublet B, Andrieu JP, Gaboriaud C, Arlaud GJ, Thielens NM. The two major oligomeric forms of human mannan-binding lectin: chemical characterization, carbohydrate-binding properties, and interaction with MBL-associated serine proteases. J Immunol 2005;174:2870-7.
    • (2005) J Immunol , vol.174 , pp. 2870-2877
    • Teillet, F.1    Dublet, B.2    Andrieu, J.P.3    Gaboriaud, C.4    Arlaud, G.J.5    Thielens, N.M.6
  • 90
    • 80855128787 scopus 로고    scopus 로고
    • Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: implications for complement activation
    • Gingras AR, Girija UV, Keeble AH et al. Structural basis of mannan-binding lectin recognition by its associated serine protease MASP-1: implications for complement activation. Structure 2011;19:1635-43.
    • (2011) Structure , vol.19 , pp. 1635-1643
    • Gingras, A.R.1    Girija, U.V.2    Keeble, A.H.3
  • 91
    • 25844471033 scopus 로고    scopus 로고
    • A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations
    • Gal P, Harmat V, Kocsis A et al. A true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations. J Biol Chem 2005;280:33435-44.
    • (2005) J Biol Chem , vol.280 , pp. 33435-33444
    • Gal, P.1    Harmat, V.2    Kocsis, A.3
  • 92
    • 84873388516 scopus 로고    scopus 로고
    • Recombinant expression of the autocatalytic complement protease MASP-1 is crucially dependent on co-expression with its inhibitor, C1 inhibitor
    • Degn SE, Thiel S, Jensenius JC. Recombinant expression of the autocatalytic complement protease MASP-1 is crucially dependent on co-expression with its inhibitor, C1 inhibitor. Protein Expr Purif 2013;88:173-82.
    • (2013) Protein Expr Purif , vol.88 , pp. 173-182
    • Degn, S.E.1    Thiel, S.2    Jensenius, J.C.3
  • 93
    • 70249107186 scopus 로고    scopus 로고
    • MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity
    • Dobó J, Harmat V, Beinrohr L, Sebestyén E, Závodszky P, Gál P. MASP-1, a promiscuous complement protease: structure of its catalytic region reveals the basis of its broad specificity. J Immunol 2009;183:1207-14.
    • (2009) J Immunol , vol.183 , pp. 1207-1214
    • Dobó, J.1    Harmat, V.2    Beinrohr, L.3    Sebestyén, E.4    Závodszky, P.5    Gál, P.6
  • 94
    • 84866528696 scopus 로고    scopus 로고
    • Crystal structure and functional characterization of the complement regulator mannose-binding lectin (MBL)/ficolin-associated protein-1 (MAP-1)
    • Skjoedt MO, Roversi P, Hummelshoj T et al. Crystal structure and functional characterization of the complement regulator mannose-binding lectin (MBL)/ficolin-associated protein-1 (MAP-1). J Biol Chem 2012;287:32913-21.
    • (2012) J Biol Chem , vol.287 , pp. 32913-32921
    • Skjoedt, M.O.1    Roversi, P.2    Hummelshoj, T.3
  • 95
    • 0015187752 scopus 로고
    • The chemistry and structure of collagen
    • Traub W, Piez KA. The chemistry and structure of collagen. Adv Protein Chem 1971;25:243-352.
    • (1971) Adv Protein Chem , vol.25 , pp. 243-352
    • Traub, W.1    Piez, K.A.2
  • 96
    • 0032913989 scopus 로고    scopus 로고
    • Sequence dependent conformational variations of collagen triple-helical structure
    • Kramer RZ, Bella J, Mayville P, Brodsky B, Berman HM. Sequence dependent conformational variations of collagen triple-helical structure. Nat Struct Biol 1999;6:454-7.
    • (1999) Nat Struct Biol , vol.6 , pp. 454-457
    • Kramer, R.Z.1    Bella, J.2    Mayville, P.3    Brodsky, B.4    Berman, H.M.5
  • 97
    • 0028533911 scopus 로고
    • Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil
    • Sheriff S, Chang CY, Ezekowitz RA. Human mannose-binding protein carbohydrate recognition domain trimerizes through a triple alpha-helical coiled-coil. Nat Struct Biol 1994;1:789-94.
    • (1994) Nat Struct Biol , vol.1 , pp. 789-794
    • Sheriff, S.1    Chang, C.Y.2    Ezekowitz, R.A.3
  • 98
    • 33947509607 scopus 로고    scopus 로고
    • Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain
    • Tanio M, Kondo S, Sugio S, Kohno T. Trivalent recognition unit of innate immunity system: crystal structure of trimeric human M-ficolin fibrinogen-like domain. J Biol Chem 2007;282:3889-95.
    • (2007) J Biol Chem , vol.282 , pp. 3889-3895
    • Tanio, M.1    Kondo, S.2    Sugio, S.3    Kohno, T.4
  • 99
    • 33846486352 scopus 로고    scopus 로고
    • Structural insights into the innate immune recognition specificities of L- and H-ficolins
    • Garlatti V, Belloy N, Martin L et al. Structural insights into the innate immune recognition specificities of L- and H-ficolins. EMBO J 2007;26:623-33.
    • (2007) EMBO J , vol.26 , pp. 623-633
    • Garlatti, V.1    Belloy, N.2    Martin, L.3
  • 100
    • 0028233879 scopus 로고
    • Molecular structure of pulmonary surfactant protein D (SP-D)
    • Crouch E, Persson A, Chang D, Heuser J. Molecular structure of pulmonary surfactant protein D (SP-D). J Biol Chem 1994;269:17311-9.
    • (1994) J Biol Chem , vol.269 , pp. 17311-17319
    • Crouch, E.1    Persson, A.2    Chang, D.3    Heuser, J.4
  • 101
    • 0015247268 scopus 로고
    • The three-dimensional conformation of M and A globulin molecules
    • Feinstein A, Munn EA, Richardson NE. The three-dimensional conformation of M and A globulin molecules. Ann N Y Acad Sci 1971;190:104-21.
    • (1971) Ann N Y Acad Sci , vol.190 , pp. 104-121
    • Feinstein, A.1    Munn, E.A.2    Richardson, N.E.3
  • 102
    • 0022358372 scopus 로고
    • Immunoglobulin M possesses two binding sites for complement subcomponent C1q, and soluble 1:1 and 2:1 complexes are formed in solution at reduced ionic strength
    • Poon PH, Phillips ML, Schumaker VN. Immunoglobulin M possesses two binding sites for complement subcomponent C1q, and soluble 1:1 and 2:1 complexes are formed in solution at reduced ionic strength. J Biol Chem 1985;260:9357-65.
    • (1985) J Biol Chem , vol.260 , pp. 9357-9365
    • Poon, P.H.1    Phillips, M.L.2    Schumaker, V.N.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.