메뉴 건너뛰기




Volumn 75, Issue 3, 2016, Pages 578-585

Extensive glycosylation of ACPA-IgG variable domains modulates binding to citrullinated antigens in rheumatoid arthritis

Author keywords

[No Author keywords available]

Indexed keywords

CYCLIC CITRULLINATED PEPTIDE ANTIBODY; IMMUNOGLOBULIN; MONOCLONAL ANTIBODY; AUTOANTIBODY; AUTOANTIGEN; CITRULLINE; IMMUNOGLOBULIN G; POLYSACCHARIDE;

EID: 84960109858     PISSN: 00034967     EISSN: 14682060     Source Type: Journal    
DOI: 10.1136/annrheumdis-2014-206598     Document Type: Article
Times cited : (166)

References (46)
  • 1
    • 0038011833 scopus 로고    scopus 로고
    • Evolving concepts of rheumatoid arthritis
    • Firestein GS. Evolving concepts of rheumatoid arthritis. Nature 2003;423:356-61.
    • (2003) Nature , vol.423 , pp. 356-361
    • Firestein, G.S.1
  • 3
    • 84857922958 scopus 로고    scopus 로고
    • The influence of ACPA status and characteristics on the course of RA
    • Willemze A, Trouw LA, Toes RE, et al. The influence of ACPA status and characteristics on the course of RA. Nat Rev Rheumatol 2012;8:144-52.
    • (2012) Nat Rev Rheumatol , vol.8 , pp. 144-152
    • Willemze, A.1    Trouw, L.A.2    Toes, R.E.3
  • 4
    • 27744550413 scopus 로고    scopus 로고
    • Refining the complex rheumatoid arthritis phenotype based on specificity of the HLA-DRB1 shared epitope for antibodies to citrullinated proteins
    • Huizinga TW, Amos CI, van der Helm-van Mil AH, et al. Refining the complex rheumatoid arthritis phenotype based on specificity of the HLA-DRB1 shared epitope for antibodies to citrullinated proteins. Arthritis Rheum 2005;52:3433-8.
    • (2005) Arthritis Rheum , vol.52 , pp. 3433-3438
    • Huizinga, T.W.1    Amos, C.I.2    Van Der-Helm-Van Mil, A.H.3
  • 5
    • 1042290337 scopus 로고    scopus 로고
    • Specific autoantibodies precede the symptoms of rheumatoid arthritis: A study of serial measurements in blood donors
    • Nielen MM, van Schaardenburg D, Reesink HW, et al. Specific autoantibodies precede the symptoms of rheumatoid arthritis: a study of serial measurements in blood donors. Arthritis Rheum 2004;50:380-6.
    • (2004) Arthritis Rheum , vol.50 , pp. 380-386
    • Nielen, M.M.1    Van Schaardenburg, D.2    Reesink, H.W.3
  • 6
    • 77955464379 scopus 로고    scopus 로고
    • Epitope spreading of the anti-citrullinated protein antibody response occurs before disease onset and is associated with the disease course of early arthritis
    • van der Woude D, Rantapaa-Dahlqvist S, Ioan-Facsinay A, et al. Epitope spreading of the anti-citrullinated protein antibody response occurs before disease onset and is associated with the disease course of early arthritis. Ann Rheum Dis 2010;69:1554-61.
    • (2010) Ann Rheum Dis , vol.69 , pp. 1554-1561
    • Van Der-Woude, D.1    Rantapaa-Dahlqvist, S.2    Ioan-Facsinay, A.3
  • 7
    • 33845622856 scopus 로고    scopus 로고
    • Isotype distribution of anti-cyclic citrullinated peptide antibodies in undifferentiated arthritis and rheumatoid arthritis reflects an ongoing immune response
    • Verpoort KN, Jol-van der Zijde CM, Papendrecht-van der Voort EA, et al. Isotype distribution of anti-cyclic citrullinated peptide antibodies in undifferentiated arthritis and rheumatoid arthritis reflects an ongoing immune response. Arthritis Rheum 2006;54:3799-808.
    • (2006) Arthritis Rheum , vol.54 , pp. 3799-3808
    • Verpoort, K.N.1    Jol-Van Der-Zijde, C.M.2    Papendrecht-Van Der-Voort, E.A.3
  • 8
    • 84898013615 scopus 로고    scopus 로고
    • Bone loss before the clinical onset of rheumatoid arthritis in subjects with anticitrullinated protein antibodies
    • Kleyer A, Finzel S, Rech J, et al. Bone loss before the clinical onset of rheumatoid arthritis in subjects with anticitrullinated protein antibodies. Ann Rheum Dis 2014;73:854-60.
    • (2014) Ann Rheum Dis , vol.73 , pp. 854-860
    • Kleyer, A.1    Finzel, S.2    Rech, J.3
  • 9
    • 70350475800 scopus 로고    scopus 로고
    • Immune complexes from rheumatoid arthritis synovial fluid induce FcgammaRIIa dependent and rheumatoid factor correlated production of tumour necrosis factor-alpha by peripheral blood mononuclear cells
    • Mathsson L, Lampa J, Mullazehi M, et al. Immune complexes from rheumatoid arthritis synovial fluid induce FcgammaRIIa dependent and rheumatoid factor correlated production of tumour necrosis factor-alpha by peripheral blood mononuclear cells. Arthritis Res Ther 2006;8:R64.
    • (2006) Arthritis Res Ther , vol.8 , pp. R64
    • Mathsson, L.1    Lampa, J.2    Mullazehi, M.3
  • 10
    • 78650779270 scopus 로고    scopus 로고
    • Immune complexes containing citrullinated fibrinogen costimulate macrophages via Toll-like receptor 4 and Fcgamma receptor
    • Sokolove J, Zhao X, Chandra PE, et al. Immune complexes containing citrullinated fibrinogen costimulate macrophages via Toll-like receptor 4 and Fcgamma receptor. Arthritis Rheum 2011;63:53-62.
    • (2011) Arthritis Rheum , vol.63 , pp. 53-62
    • Sokolove, J.1    Zhao, X.2    Chandra, P.E.3
  • 11
    • 84942878137 scopus 로고    scopus 로고
    • Toll-like receptor triggering augments activation of human mast cells by anti-citrullinated protein antibodies
    • Suurmond J, Rivellese F, Dorjee AL, et al. Toll-like receptor triggering augments activation of human mast cells by anti-citrullinated protein antibodies. Ann Rheum Dis 2015;74:1915-23.
    • (2015) Ann Rheum Dis , vol.74 , pp. 1915-1923
    • Suurmond, J.1    Rivellese, F.2    Dorjee, A.L.3
  • 12
    • 84876104421 scopus 로고    scopus 로고
    • NETs are a source of citrullinated autoantigens and stimulate inflammatory responses in rheumatoid arthritis
    • Khandpur R, Carmona-Rivera C, Vivekanandan-Giri A, et al. NETs are a source of citrullinated autoantigens and stimulate inflammatory responses in rheumatoid arthritis. Sci Transl Med 2013;5:178ra140.
    • (2013) Sci Transl Med , vol.5 , pp. 178ra140
    • Khandpur, R.1    Carmona-Rivera, C.2    Vivekanandan-Giri, A.3
  • 13
    • 67650065027 scopus 로고    scopus 로고
    • Anti-cyclic citrullinated peptide antibodies from rheumatoid arthritis patients activate complement via both the classical and alternative pathways
    • Trouw LA, Haisma EM, Levarht EW, et al. Anti-cyclic citrullinated peptide antibodies from rheumatoid arthritis patients activate complement via both the classical and alternative pathways. Arthritis Rheum 2009;60:1923-31.
    • (2009) Arthritis Rheum , vol.60 , pp. 1923-1931
    • Trouw, L.A.1    Haisma, E.M.2    Levarht, E.W.3
  • 14
    • 84860561645 scopus 로고    scopus 로고
    • Induction of osteoclastogenesis and bone loss by human autoantibodies against citrullinated vimentin
    • Harre U, Georgess D, Bang H, et al. Induction of osteoclastogenesis and bone loss by human autoantibodies against citrullinated vimentin. J Clin Invest 2012;122:1791-802.
    • (2012) J Clin Invest , vol.122 , pp. 1791-1802
    • Harre, U.1    Georgess, D.2    Bang, H.3
  • 15
    • 78751701595 scopus 로고    scopus 로고
    • Anti-citrullinated protein antibodies have a low avidity compared with antibodies against recall antigens
    • Suwannalai P, Scherer HU, van der Woude D, et al. Anti-citrullinated protein antibodies have a low avidity compared with antibodies against recall antigens. Ann Rheum Dis 2011;70:373-9.
    • (2011) Ann Rheum Dis , vol.70 , pp. 373-379
    • Suwannalai, P.1    Scherer, H.U.2    Van Der-Woude, D.3
  • 16
    • 0023945481 scopus 로고
    • The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis
    • Arnett FC, Edworthy SM, Bloch DA, et al. The American Rheumatism Association 1987 revised criteria for the classification of rheumatoid arthritis. Arthritis Rheum 1988;31:315-24.
    • (1988) Arthritis Rheum , vol.31 , pp. 315-324
    • Arnett, F.C.1    Edworthy, S.M.2    Bloch, D.A.3
  • 17
    • 84890823064 scopus 로고    scopus 로고
    • MuSK IgG4 autoantibodies cause myasthenia gravis by inhibiting binding between MuSK and Lrp4
    • Huijbers MG, Zhang W, Klooster R, et al. MuSK IgG4 autoantibodies cause myasthenia gravis by inhibiting binding between MuSK and Lrp4. Proc Natl Acad Sci USA 2013;110:20783-8.
    • (2013) Proc Natl Acad Sci USA , vol.110 , pp. 20783-20788
    • Huijbers, M.G.1    Zhang, W.2    Klooster, R.3
  • 18
    • 34548585130 scopus 로고    scopus 로고
    • Accuracy of serologic tests and HLA-DQ typing for diagnosing celiac disease
    • Hadithi M, von Blomberg BM, Crusius JB, et al. Accuracy of serologic tests and HLA-DQ typing for diagnosing celiac disease. Ann Intern Med 2007;147:294-302.
    • (2007) Ann Intern Med , vol.147 , pp. 294-302
    • Hadithi, M.1    Von Blomberg, B.M.2    Crusius, J.B.3
  • 19
    • 54949088976 scopus 로고    scopus 로고
    • Marked differences in fine specificity and isotype usage of the anti-citrullinated protein antibody in health and disease
    • Ioan-Facsinay A, Willemze A, Robinson DB, et al. Marked differences in fine specificity and isotype usage of the anti-citrullinated protein antibody in health and disease. Arthritis Rheum 2008;58:3000-8.
    • (2008) Arthritis Rheum , vol.58 , pp. 3000-3008
    • Ioan-Facsinay, A.1    Willemze, A.2    Robinson, D.B.3
  • 20
    • 29244441748 scopus 로고    scopus 로고
    • Anti-Sa antibodies and antibodies against cyclic citrullinated peptide are not equivalent as predictors of severe outcomes in patients with recent-onset polyarthritis
    • Boire G, Cossette P, de Brum-Fernandes AJ, et al. Anti-Sa antibodies and antibodies against cyclic citrullinated peptide are not equivalent as predictors of severe outcomes in patients with recent-onset polyarthritis. Arthritis Res Ther 2005;7: R592-603.
    • (2005) Arthritis Res Ther , vol.7 , pp. R592-603
    • Boire, G.1    Cossette, P.2    De Brum-Fernandes, A.J.3
  • 21
    • 84877590149 scopus 로고    scopus 로고
    • The concentration of anticitrullinated protein antibodies in serum and synovial fluid in relation to total immunoglobulin concentrations
    • Willemze A, Shi J, Mulder M, et al. The concentration of anticitrullinated protein antibodies in serum and synovial fluid in relation to total immunoglobulin concentrations. Ann Rheum Dis 2013;72:1059-63.
    • (2013) Ann Rheum Dis , vol.72 , pp. 1059-1063
    • Willemze, A.1    Shi, J.2    Mulder, M.3
  • 22
    • 84871091936 scopus 로고    scopus 로고
    • Recognition of citrullinated and carbamylated proteins by human antibodies: Specificity, cross-reactivity and the 'AMC-Senshu' method
    • Shi J, Willemze A, Janssen GM, et al. Recognition of citrullinated and carbamylated proteins by human antibodies: specificity, cross-reactivity and the 'AMC-Senshu' method. Ann Rheum Dis 2013;72:148-50.
    • (2013) Ann Rheum Dis , vol.72 , pp. 148-150
    • Shi, J.1    Willemze, A.2    Janssen, G.M.3
  • 23
    • 49449095723 scopus 로고    scopus 로고
    • Hydrophilic interaction chromatography-based high-throughput sample preparation method for N-glycan analysis from total human plasma glycoproteins
    • Ruhaak LR, Huhn C, Waterreus WJ, et al. Hydrophilic interaction chromatography-based high-throughput sample preparation method for N-glycan analysis from total human plasma glycoproteins. Anal Chem 2008;80:6119-26.
    • (2008) Anal Chem , vol.80 , pp. 6119-6126
    • Ruhaak, L.R.1    Huhn, C.2    Waterreus, W.J.3
  • 24
    • 79953292549 scopus 로고    scopus 로고
    • Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides
    • Selman MH, Hemayatkar M, Deelder AM, et al. Cotton HILIC SPE microtips for microscale purification and enrichment of glycans and glycopeptides. Anal Chem 2011;83:2492-9.
    • (2011) Anal Chem , vol.83 , pp. 2492-2499
    • Selman, M.H.1    Hemayatkar, M.2    Deelder, A.M.3
  • 25
    • 33847414974 scopus 로고    scopus 로고
    • A potential pitfall in 18O-based N-linked glycosylation site mapping
    • Angel PM, Lim JM, Wells L, et al. A potential pitfall in 18O-based N-linked glycosylation site mapping. Rapid Commun Mass Spectrom 2007;21:674-82.
    • (2007) Rapid Commun Mass Spectrom , vol.21 , pp. 674-682
    • Angel, P.M.1    Lim, J.M.2    Wells, L.3
  • 26
    • 0036067603 scopus 로고    scopus 로고
    • Nanoscale LC-MS(n): Technical design and applications to peptide and protein analysis
    • Meiring HD, van der Heeft E, ten Hove GJ, et al. Nanoscale LC-MS(n): technical design and applications to peptide and protein analysis. Journal of Separation Science 2002;25:557-68.
    • (2002) Journal of Separation Science , vol.25 , pp. 557-568
    • Meiring, H.D.1    Van Der-Heeft, E.2    Ten Hove, G.J.3
  • 27
    • 84884765647 scopus 로고    scopus 로고
    • ACPA fine-specificity profiles in early rheumatoid arthritis patients do not correlate with clinical features at baseline or with disease progression
    • van Beers JJ, Willemze A, Jansen JJ, et al. ACPA fine-specificity profiles in early rheumatoid arthritis patients do not correlate with clinical features at baseline or with disease progression. Arthritis Res Ther 2013;15:R140.
    • (2013) Arthritis Res Ther , vol.15 , pp. R140
    • Van Beers, J.J.1    Willemze, A.2    Jansen, J.J.3
  • 28
    • 13544276336 scopus 로고    scopus 로고
    • Glycosylation of recombinant antibody therapeutics
    • Jefferis R. Glycosylation of recombinant antibody therapeutics. Biotechnol Prog 2005;21:11-16.
    • (2005) Biotechnol Prog , vol.21 , pp. 11-16
    • Jefferis, R.1
  • 29
    • 38949143338 scopus 로고    scopus 로고
    • Remarkable selective glycosylation of the immunoglobulin variable region in follicular lymphoma
    • McCann KJ, Ottensmeier CH, Callard A, et al. Remarkable selective glycosylation of the immunoglobulin variable region in follicular lymphoma. Mol Immunol 2008;45:1567-72.
    • (2008) Mol Immunol , vol.45 , pp. 1567-1572
    • McCann, K.J.1    Ottensmeier, C.H.2    Callard, A.3
  • 30
    • 79954416352 scopus 로고    scopus 로고
    • Progesterone induces a switch in oligosaccharyltransferase isoform expression: Consequences on IgG N-glycosylation
    • Prados MB, La Blunda J, Szekeres-Bartho J, et al. Progesterone induces a switch in oligosaccharyltransferase isoform expression: consequences on IgG N-glycosylation. Immunol Lett 2011;137:28-37.
    • (2011) Immunol Lett , vol.137 , pp. 28-37
    • Prados, M.B.1    La Blunda, J.2    Szekeres-Bartho, J.3
  • 31
    • 0033558335 scopus 로고    scopus 로고
    • Position effects of variable region carbohydrate on the affinity and in vivo behavior of an anti-(1->6) dextran antibody
    • Coloma MJ, Trinh RK, Martinez AR, et al. Position effects of variable region carbohydrate on the affinity and in vivo behavior of an anti-(1->6) dextran antibody. J Immunol 1999;162:2162-70.
    • (1999) J Immunol , vol.162 , pp. 2162-2170
    • Coloma, M.J.1    Trinh, R.K.2    Martinez, A.R.3
  • 33
    • 84918590946 scopus 로고    scopus 로고
    • Anti-citrullinated protein antibodies acquire a pro-inflammatory Fc glycosylation phenotype prior to the onset of rheumatoid arthritis
    • Rombouts Y, Ewing E, van de Stadt LA, et al. Anti-citrullinated protein antibodies acquire a pro-inflammatory Fc glycosylation phenotype prior to the onset of rheumatoid arthritis. Ann Rheum Dis 2015;74:234-41.
    • (2015) Ann Rheum Dis , vol.74 , pp. 234-241
    • Rombouts, Y.1    Ewing, E.2    Van De-Stadt, L.A.3
  • 34
    • 84910647104 scopus 로고    scopus 로고
    • IgG Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes
    • Bondt A, Rombouts Y, Selman MH, et al. IgG Fab glycosylation analysis using a new mass spectrometric high-throughput profiling method reveals pregnancy-associated changes. Mol Cell Proteomics 2014;13:3029-39.
    • (2014) Mol Cell Proteomics , vol.13 , pp. 3029-3039
    • Bondt, A.1    Rombouts, Y.2    Selman, M.H.3
  • 35
    • 77952378813 scopus 로고    scopus 로고
    • Glutamine-linked and non-consensus asparagine-linked oligosaccharides present in human recombinant antibodies define novel protein glycosylation motifs
    • Valliere-Douglass JF, Eakin CM, Wallace A, et al. Glutamine-linked and non-consensus asparagine-linked oligosaccharides present in human recombinant antibodies define novel protein glycosylation motifs. J Biol Chem 2010;285:16012-22.
    • (2010) J Biol Chem , vol.285 , pp. 16012-16022
    • Valliere-Douglass, J.F.1    Eakin, C.M.2    Wallace, A.3
  • 36
    • 70450270692 scopus 로고    scopus 로고
    • Asparagine-linked oligosaccharides present on a non-consensus amino acid sequence in the CH1 domain of human antibodies
    • Valliere-Douglass JF, Kodama P, Mujacic M, et al. Asparagine-linked oligosaccharides present on a non-consensus amino acid sequence in the CH1 domain of human antibodies. J Biol Chem 2009;284:32493-506.
    • (2009) J Biol Chem , vol.284 , pp. 32493-32506
    • Valliere-Douglass, J.F.1    Kodama, P.2    Mujacic, M.3
  • 37
    • 0025909201 scopus 로고
    • Antibody variable region glycosylation: Position effects on antigen binding and carbohydrate structure
    • Wright A, Tao MH, Kabat EA, et al. Antibody variable region glycosylation: position effects on antigen binding and carbohydrate structure. EMBO J 1991;10: 2717-23.
    • (1991) EMBO J , vol.10 , pp. 2717-2723
    • Wright, A.1    Tao, M.H.2    Kabat, E.A.3
  • 38
    • 0030428215 scopus 로고    scopus 로고
    • Humanization of an anti-human IL-6 mouse monoclonal antibody glycosylated in its heavy chain variable region
    • Sato K, Ohtomo T, Hirata Y, et al. Humanization of an anti-human IL-6 mouse monoclonal antibody glycosylated in its heavy chain variable region. Hum Antibodies Hybridomas 1996;7:175-83.
    • (1996) Hum Antibodies Hybridomas , vol.7 , pp. 175-183
    • Sato, K.1    Ohtomo, T.2    Hirata, Y.3
  • 39
    • 0039725069 scopus 로고    scopus 로고
    • Variable domain-linked oligosaccharides of a human monoclonal IgG: Structure and influence on antigen binding
    • Leibiger H, Wustner D, Stigler RD, et al. Variable domain-linked oligosaccharides of a human monoclonal IgG: structure and influence on antigen binding. Biochem J 1999;338(Pt 2):529-38.
    • (1999) Biochem J , vol.338 , pp. 529-538
    • Leibiger, H.1    Wustner, D.2    Stigler, R.D.3
  • 40
    • 84903459040 scopus 로고    scopus 로고
    • Redemption of autoantibodies on anergic B cells by variable-region glycosylation and mutation away from self-reactivity
    • Sabouri Z, Schofield P, Horikawa K, et al. Redemption of autoantibodies on anergic B cells by variable-region glycosylation and mutation away from self-reactivity. Proc Natl Acad Sci USA 2014;111:E2567-75.
    • (2014) Proc Natl Acad Sci USA , vol.111 , pp. E2567-E2575
    • Sabouri, Z.1    Schofield, P.2    Horikawa, K.3
  • 41
    • 84875614928 scopus 로고    scopus 로고
    • Monoclonal anti-citrullinated protein antibodies selected on citrullinated fibrinogen have distinct targets with different cross-reactivity patterns
    • van de Stadt LA, van Schouwenburg PA, Bryde S, et al. Monoclonal anti-citrullinated protein antibodies selected on citrullinated fibrinogen have distinct targets with different cross-reactivity patterns. Rheumatology (Oxford) 2013;52:631-5.
    • (2013) Rheumatology (Oxford) , vol.52 , pp. 631-635
    • Van De-Stadt, L.A.1    Van Schouwenburg, P.A.2    Bryde, S.3
  • 42
    • 77956187222 scopus 로고    scopus 로고
    • Analytical and functional aspects of antibody sialylation
    • Stadlmann J, Pabst M, Altmann F. Analytical and functional aspects of antibody sialylation. J Clin Immunol 2010;30(Suppl 1):15-19.
    • (2010) J Clin Immunol , vol.30 , pp. 15-19
    • Stadlmann, J.1    Pabst, M.2    Altmann, F.3
  • 43
    • 78649840358 scopus 로고    scopus 로고
    • Glycosylation of surface Ig creates a functional bridge between human follicular lymphoma and microenvironmental lectins
    • Coelho V, Krysov S, Ghaemmaghami AM, et al. Glycosylation of surface Ig creates a functional bridge between human follicular lymphoma and microenvironmental lectins. Proc Natl Acad Sci USA 2010;107:18587-92.
    • (2010) Proc Natl Acad Sci USA , vol.107 , pp. 18587-18592
    • Coelho, V.1    Krysov, S.2    Ghaemmaghami, A.M.3
  • 44
    • 84877587255 scopus 로고    scopus 로고
    • Monoclonal IgG antibodies generated from joint-derived B cells of RA patients have a strong bias toward citrullinated autoantigen recognition
    • Amara K, Steen J, Murray F, et al. Monoclonal IgG antibodies generated from joint-derived B cells of RA patients have a strong bias toward citrullinated autoantigen recognition. J Exp Med 2013;210:445-55.
    • (2013) J Exp Med , vol.210 , pp. 445-455
    • Amara, K.1    Steen, J.2    Murray, F.3
  • 45
    • 84889635694 scopus 로고    scopus 로고
    • Low-avidity anticitrullinated protein antibodies (ACPA) are associated with a higher rate of joint destruction in rheumatoid arthritis
    • Suwannalai P, Britsemmer K, Knevel R, et al. Low-avidity anticitrullinated protein antibodies (ACPA) are associated with a higher rate of joint destruction in rheumatoid arthritis. Ann Rheum Dis 2014;73:270-6.
    • (2014) Ann Rheum Dis , vol.73 , pp. 270-276
    • Suwannalai, P.1    Britsemmer, K.2    Knevel, R.3
  • 46
    • 84860442529 scopus 로고    scopus 로고
    • Avidity maturation of anti-citrullinated protein antibodies in rheumatoid arthritis
    • Suwannalai P, van de Stadt LA, Radner H, et al. Avidity maturation of anti-citrullinated protein antibodies in rheumatoid arthritis. Arthritis Rheum 2012;64:1323-8.
    • (2012) Arthritis Rheum , vol.64 , pp. 1323-1328
    • Suwannalai, P.1    Van De-Stadt, L.A.2    Radner, H.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.