메뉴 건너뛰기




Volumn 287, Issue 43, 2012, Pages 36096-36104

Constant domain-regulated antibody catalysis

Author keywords

[No Author keywords available]

Indexed keywords

CATALYTIC FUNCTIONS; CATALYTIC MECHANISMS; CATALYTIC SITES; DIESTERS; HEAVY AND LIGHT CHAINS; HIGH AFFINITY; HYDROLYTIC ACTIVITIES; HYDROLYTIC REACTIONS; IMMUNE FUNCTION; MODEL PEPTIDES; NONCOVALENT; PHOSPHONATES; POLYCLONAL; POLYCLONAL IGG; STRUCTURAL BASIS;

EID: 84867837936     PISSN: 00219258     EISSN: 1083351X     Source Type: Journal    
DOI: 10.1074/jbc.M112.401075     Document Type: Article
Times cited : (13)

References (62)
  • 1
  • 2
    • 38749103119 scopus 로고    scopus 로고
    • The immunoglobulin constant region contributes to affinity and specificity
    • Torres, M., and Casadevall, A. (2008) The immunoglobulin constant region contributes to affinity and specificity. Trends Immunol. 29, 91-97
    • (2008) Trends Immunol. , vol.29 , pp. 91-97
    • Torres, M.1    Casadevall, A.2
  • 3
    • 13544277164 scopus 로고    scopus 로고
    • Variable-region-identical antibodies differing in isotype demonstrate differences in fine specificity and idiotype
    • Torres, M., May, R., Scharff, M. D., and Casadevall, A. (2005) Variable-region-identical antibodies differing in isotype demonstrate differences in fine specificity and idiotype. J. Immunol. 174, 2132-2142 (Pubitemid 40223957)
    • (2005) Journal of Immunology , vol.174 , Issue.4 , pp. 2132-2142
    • Torres, M.1    May, R.2    Scharff, M.D.3    Casadevall, A.4
  • 4
    • 77950627194 scopus 로고    scopus 로고
    • Circular dichroism reveals evidence of coupling between immunoglobulin constant and variable region secondary structure
    • Janda, A., and Casadevall, A. (2010) Circular dichroism reveals evidence of coupling between immunoglobulin constant and variable region secondary structure. Mol. Immunol. 47, 1421-1425
    • (2010) Mol. Immunol. , vol.47 , pp. 1421-1425
    • Janda, A.1    Casadevall, A.2
  • 5
    • 0030918906 scopus 로고    scopus 로고
    • The repertoire of serum IgM in normal mice is largely independent of external antigenic contact
    • DOI 10.1002/eji.1830270635
    • Haury, M., Sundblad, A., Grandien, A., Barreau, C., Coutinho, A., and Nobrega, A. (1997) The repertoire of serum IgM in normal mice is largely independent of external antigenic contact. Eur. J. Immunol. 27, 1557-1563 (Pubitemid 27254850)
    • (1997) European Journal of Immunology , vol.27 , Issue.6 , pp. 1557-1563
    • Haury, M.1    Sundblad, A.2    Grandien, A.3    Barreau, C.4    Coutinho, A.5    Nobrega, A.6
  • 6
    • 35648946344 scopus 로고    scopus 로고
    • Epigenetics of antigen-receptor gene assembly
    • Murre, C. (2007) Epigenetics of antigen-receptor gene assembly. Curr. Opin. Genet. Dev. 17, 415-421
    • (2007) Curr. Opin. Genet. Dev. , vol.17 , pp. 415-421
    • Murre, C.1
  • 7
    • 0037805717 scopus 로고    scopus 로고
    • Broadly distributed chemical reactivity of natural antibodies expressed in coordination with specific antigen binding activity
    • DOI 10.1074/jbc.M301468200
    • Planque, S., Taguchi, H., Burr, G., Bhatia, G., Karle, S., Zhou, Y. X., Nishiyama, Y., and Paul, S. (2003) Broadly distributed chemical reactivity of natural antibodies expressed in coordination with specific antigen binding activity. J. Biol. Chem. 278, 20436-20443 (Pubitemid 36799246)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.22 , pp. 20436-20443
    • Planque, S.1    Taguchi, H.2    Burr, G.3    Bhatia, G.4    Karle, S.5    Zhou, Y.-X.6    Nishiyama, Y.7    Paul, S.8
  • 8
    • 0028835286 scopus 로고
    • Site-directed mutagenesis of proteolytic antibody light chain
    • Gao, Q. S., Sun, M., Rees, A. R., and Paul, S. (1995) Site-directed mutagenesis of proteolytic antibody light chain. J. Mol. Biol. 253, 658-664
    • (1995) J. Mol. Biol. , vol.253 , pp. 658-664
    • Gao, Q.S.1    Sun, M.2    Rees, A.R.3    Paul, S.4
  • 9
    • 70450260534 scopus 로고    scopus 로고
    • A human germ line antibody light chain with hydrolytic properties associated with multimerization status
    • Sharma, V., Heriot, W., Trisler, K., and Smider, V. (2009) A human germ line antibody light chain with hydrolytic properties associated with multimerization status. J. Biol. Chem. 284, 33079-33087
    • (2009) J. Biol. Chem. , vol.284 , pp. 33079-33087
    • Sharma, V.1    Heriot, W.2    Trisler, K.3    Smider, V.4
  • 12
    • 0033507846 scopus 로고    scopus 로고
    • Innate antibody catalysis
    • DOI 10.1016/S0161-5890(99)00141-8, PII S0161589099001418
    • Gololobov, G., Sun, M., and Paul, S. (1999) Innate antibody catalysis. Mol. Immunol. 36, 1215-1222 (Pubitemid 30137202)
    • (1999) Molecular Immunology , vol.36 , Issue.18 , pp. 1215-1222
    • Gololobov, G.1    Sun, M.2    Paul, S.3
  • 14
    • 0029028102 scopus 로고
    • Unexpected presence of polyreactive catalytic antibodies in IgG from unimmunized donors and decreased levels in rheumatoid arthritis
    • Kalaga, R., Li, L., O'Dell, J. R., and Paul, S. (1995) Unexpected presence of polyreactive catalytic antibodies in IgG from unimmunized donors and decreased levels in rheumatoid arthritis. J. Immunol. 155, 2695-2702
    • (1995) J. Immunol. , vol.155 , pp. 2695-2702
    • Kalaga, R.1    Li, L.2    O'Dell, J.R.3    Paul, S.4
  • 15
    • 78049451477 scopus 로고    scopus 로고
    • Proteolysis activity of IgM antibodies from rheumatoid arthritis patients' sera: Evidence of atypical catalytic site
    • Kamalanathan, A. S., Goulvestre, C., Weill, B., and Vijayalakshmi, M. A. (2010) Proteolysis activity of IgM antibodies from rheumatoid arthritis patients' sera: evidence of atypical catalytic site. J. Mol. Recognit. 23, 577-582
    • (2010) J. Mol. Recognit. , vol.23 , pp. 577-582
    • Kamalanathan, A.S.1    Goulvestre, C.2    Weill, B.3    Vijayalakshmi, M.A.4
  • 17
    • 0029072696 scopus 로고
    • Natural catalytic antibodies: Peptide-hydrolyzing activities of Bence Jones proteins and VL fragment
    • Paul, S., Li, L., Kalaga, R., Wilkins-Stevens, P., Stevens, F. J., and Solomon, A. (1995) Natural catalytic antibodies: peptide-hydrolyzing activities of Bence Jones proteins and VL fragment. J. Biol. Chem. 270, 15257-15261
    • (1995) J. Biol. Chem. , vol.270 , pp. 15257-15261
    • Paul, S.1    Li, L.2    Kalaga, R.3    Wilkins-Stevens, P.4    Stevens, F.J.5    Solomon, A.6
  • 18
    • 0027340737 scopus 로고
    • Immunoglobulin V(H)3 gene products: Natural ligands for HIV gp120
    • Berberian, L., Goodglick, L., Kipps, T. J., and Braun, J. (1993) Immunoglobulin VH3 gene products: natural ligands for HIV gp120. Science 261, 1588-1591 (Pubitemid 23319603)
    • (1993) Science , vol.261 , Issue.5128 , pp. 1588-1591
    • Berberian, L.1    Goodglick, L.2    Kipps, T.J.3    Braun, J.4
  • 23
    • 0037424141 scopus 로고    scopus 로고
    • Carrier-dependent specificity of antibodies to a conserved peptide determinant of gp120
    • DOI 10.1016/S0264-410X(02)00504-2, PII S0264410X02005042
    • Karle, S., Nishiyama, Y., Taguchi, H., Zhou, Y. X., Luo, J., Planque, S., Hanson, C., and Paul, S. (2003) Carrier-dependent specificity of antibodies to a conserved peptide determinant of gp120. Vaccine 21, 1213-1218 (Pubitemid 36139951)
    • (2003) Vaccine , vol.21 , Issue.11-12 , pp. 1213-1218
    • Karle, S.1    Nishiyama, Y.2    Taguchi, H.3    Zhou, Y.-X.4    Luo, J.5    Planque, S.6    Hanson, C.7    Paul, S.8
  • 24
    • 1542379780 scopus 로고    scopus 로고
    • Toward selective covalent inactivation of pathogenic antibodies: A phosphonate diester analog of vasoactive intestinal peptide that inactivates catalytic autoantibodies
    • DOI 10.1074/jbc.M310950200
    • Nishiyama, Y., Bhatia, G., Bangale, Y., Planque, S., Mitsuda, Y., Taguchi, H., Karle, S., and Paul, S. (2004) Toward selective covalent inactivation of pathogenic antibodies: a phosphate diester analog of vasoactive intestinal peptide that inactivates catalytic autoantibodies. J. Biol. Chem. 279, 7877-7883 (Pubitemid 38294674)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.9 , pp. 7877-7883
    • Nishiyama, Y.1    Bhatia, G.2    Bangale, Y.3    Planque, S.4    Mitsuda, Y.5    Taguchi, H.6    Karle, S.7    Paul, S.8
  • 25
    • 0037098449 scopus 로고    scopus 로고
    • Covalent reactivity of phosphonate monophenyl esters with serine proteinases: An overlooked feature of presumed transition state analogs
    • DOI 10.1016/S0003-9861(02)00087-5, PII S0003986102000875
    • Nishiyama, Y., Taguchi, H., Luo, J. Q., Zhou, Y. X., Burr, G., Karle, S., and Paul, S. (2002) Covalent reactivity of phosphonate monophenyl esters with serine proteinases: an overlooked feature of presumed transition state analogs. Arch. Biochem. Biophys. 402, 281-288 (Pubitemid 34848648)
    • (2002) Archives of Biochemistry and Biophysics , vol.402 , Issue.2 , pp. 281-288
    • Nishiyama, Y.1    Taguchi, H.2    Luo, J.-Q.3    Zhou, Y.-X.4    Burr, G.5    Karle, S.6    Paul, S.7
  • 26
    • 0028672813 scopus 로고
    • Amino acid and peptide phosphonate derivatives as specific inhibitors of serine peptidases
    • Oleksyszyn, J., and Powers, J. C. (1994) Amino acid and peptide phosphonate derivatives as specific inhibitors of serine peptidases. Methods Enzymol. 244, 423-441
    • (1994) Methods Enzymol. , vol.244 , pp. 423-441
    • Oleksyszyn, J.1    Powers, J.C.2
  • 27
    • 35848938690 scopus 로고    scopus 로고
    • Naturally occurring catalytic antibodies: Evidence for preferred development of the catalytic function in IgA class antibodies
    • DOI 10.1007/s12033-007-0003-7
    • Mitsuda, Y., Planque, S., Hara, M., Kyle, R., Taguchi, H., Nishiyama, Y., and Paul, S. (2007) Naturally occurring catalytic antibodies: evidence for preferred development of the catalytic function in IgA class antibodies. Mol. Biotechnol. 36, 113-122 (Pubitemid 350135917)
    • (2007) Molecular Biotechnology , vol.36 , Issue.2 , pp. 113-122
    • Mitsuda, Y.1    Planque, S.2    Hara, M.3    Kyle, R.4    Taguchi, H.5    Nishiyama, Y.6    Paul, S.7
  • 29
    • 0035099128 scopus 로고    scopus 로고
    • Human and murine immunoglobulin expression vector cassettes
    • McLean, G. R., Nakouzi, A., Casadevall, A., and Green, N. S. (2000) Human and murine immunoglobulin expression vector cassettes. Mol. Immunol. 37, 837-845
    • (2000) Mol. Immunol. , vol.37 , pp. 837-845
    • McLean, G.R.1    Nakouzi, A.2    Casadevall, A.3    Green, N.S.4
  • 30
    • 69949142744 scopus 로고    scopus 로고
    • Antigen-specific proteolysis by hybrid antibodies containing promiscuous proteolytic light chains paired with an antigen-binding heavy chain
    • Sapparapu, G., Planque, S. A., Nishiyama, Y., Foung, S. K., and Paul, S. (2009) Antigen-specific proteolysis by hybrid antibodies containing promiscuous proteolytic light chains paired with an antigen-binding heavy chain. J. Biol. Chem. 284, 24622-24633
    • (2009) J. Biol. Chem. , vol.284 , pp. 24622-24633
    • Sapparapu, G.1    Planque, S.A.2    Nishiyama, Y.3    Foung, S.K.4    Paul, S.5
  • 31
    • 61349140658 scopus 로고    scopus 로고
    • Exceptional amyloid β peptide hydrolyzing activity of nonphysiological immunoglobulin variable domain scaffolds
    • Taguchi, H., Planque, S., Sapparapu, G., Boivin, S., Hara, M., Nishiyama, Y., and Paul, S. (2008) Exceptional amyloid β peptide hydrolyzing activity of nonphysiological immunoglobulin variable domain scaffolds. J. Biol. Chem. 283, 36724-36733
    • (2008) J. Biol. Chem. , vol.283 , pp. 36724-36733
    • Taguchi, H.1    Planque, S.2    Sapparapu, G.3    Boivin, S.4    Hara, M.5    Nishiyama, Y.6    Paul, S.7
  • 32
    • 84455204799 scopus 로고    scopus 로고
    • Signal peptidase I: Cleaving the way to mature proteins
    • Auclair, S. M., Bhanu, M. K., and Kendall, D. A. (2012) Signal peptidase I: cleaving the way to mature proteins. Protein Sci. 21, 13-25
    • (2012) Protein Sci. , vol.21 , pp. 13-25
    • Auclair, S.M.1    Bhanu, M.K.2    Kendall, D.A.3
  • 33
    • 33646489776 scopus 로고    scopus 로고
    • Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates
    • Radisky, E. S., Lee, J. M., Lu, C. J., and Koshland, D. E., Jr. (2006) Insights into the serine protease mechanism from atomic resolution structures of trypsin reaction intermediates. Proc. Natl. Acad. Sci. U.S.A. 103, 6835-6840
    • (2006) Proc. Natl. Acad. Sci. U.S.A. , vol.103 , pp. 6835-6840
    • Radisky, E.S.1    Lee, J.M.2    Lu, C.J.3    Koshland Jr., D.E.4
  • 35
    • 84858764644 scopus 로고    scopus 로고
    • Anti-integrase abzymes from the sera of HIV-infected patients specifically hydrolyze integrase but nonspecifically cleave short oligopeptides
    • Odintsova, E. S., Baranova, S. V., Dmitrenok, P. S., Calmels, C., Parissi, V., Andreola, M. L., Buneva, V. N., and Nevinsky, G. A. (2012) Anti-integrase abzymes from the sera of HIV-infected patients specifically hydrolyze integrase but nonspecifically cleave short oligopeptides. J. Mol. Recognit. 25, 193-207
    • (2012) J. Mol. Recognit. , vol.25 , pp. 193-207
    • Odintsova, E.S.1    Baranova, S.V.2    Dmitrenok, P.S.3    Calmels, C.4    Parissi, V.5    Andreola, M.L.6    Buneva, V.N.7    Nevinsky, G.A.8
  • 36
    • 0030157640 scopus 로고    scopus 로고
    • Natural catalytic antibodies
    • Paul, S. (1996) Natural catalytic antibodies. Mol. Biotechnol. 5, 197-207
    • (1996) Mol. Biotechnol. , vol.5 , pp. 197-207
    • Paul, S.1
  • 37
    • 34247547763 scopus 로고    scopus 로고
    • Molecular characterization of Waldenstrom's macroglobulinemia reveals frequent occurrence of two B-cell clones having distinct IgH VDJ sequences
    • DOI 10.1158/1078-0432.CCR-06-2788
    • Kriangkum, J., Taylor, B. J., Treon, S. P., Mant, M. J., Reiman, T., Belch, A. R., and Pilarski, L. M. (2007) Molecular characterization of Waldenstrom's macroglobulinemia reveals frequent occurrence of two B-cell clones having distinct IgH VDJ sequences. Clin. Cancer Res. 13, 2005-2013 (Pubitemid 46649866)
    • (2007) Clinical Cancer Research , vol.13 , Issue.7 , pp. 2005-2013
    • Kriangkum, J.1    Taylor, B.J.2    Treon, S.P.3    Mant, M.J.4    Reiman, T.5    Belch, A.R.6    Pilarski, L.M.7
  • 38
    • 0037103306 scopus 로고    scopus 로고
    • Typical waldenstrom macroglobulinemia is derived from a B-cell arrested after cessation of somatic mutation but prior to isotype switch events
    • Sahota, S. S., Forconi, F., Ottensmeier, C. H., Provan, D., Oscier, D. G., Hamblin, T. J., and Stevenson, F. K. (2002) Typical Waldenstrom macroglobulinemia is derived from a B-cell arrested after cessation of somatic mutation but prior to isotype switch events. Blood 100, 1505-1507 (Pubitemid 34864315)
    • (2002) Blood , vol.100 , Issue.4 , pp. 1505-1507
    • Sahota, S.S.1    Forconi, F.2    Ottensmeier, C.H.3    Provan, D.4    Oscier, D.G.5    Hamblin, T.J.6    Stevenson, F.K.7
  • 39
    • 20344406467 scopus 로고    scopus 로고
    • Lymphoplasmacytic lymphoma/Waldenström's macroglobulinemia derives from an extensively hypermutated B cell that lacks ongoing somatic hypermutation
    • DOI 10.1016/j.leukres.2004.12.008, PII S0145212605000354
    • Walsh, S. H., Laurell, A., Sundström, G., Roos, G., Sundström, C., and Rosenquist, R. (2005) Lymphoplasmacytic lymphoma/Waldenström's macroglobulinemia derives from an extensively hypermutated B cell that lacks ongoing somatic hypermutation. Leuk. Res. 29, 729-734 (Pubitemid 40779478)
    • (2005) Leukemia Research , vol.29 , Issue.7 , pp. 729-734
    • Walsh, S.H.1    Laurell, A.2    Sundstrom, G.3    Roos, G.4    Sundstrom, C.5    Rosenquist, R.6
  • 40
    • 33748320722 scopus 로고    scopus 로고
    • Immunoglobulin heavy chain sequence analysis in Waldenstrom's macroglobulinemia and immunoglobulin M monoclonal gammopathy of undetermined significance
    • Rollett, R. A., Wilkinson, E. J., Gonzalez, D., Fenton, J. A., Short, M. A., Evans, P. A., Rawstron, A. C., and Owen, R. G. (2006) Immunoglobulin heavy chain sequence analysis in Waldenstrom's macroglobulinemia and immunoglobulin M monoclonal gammopathy of undetermined significance. Clin. Lymphoma Myeloma 7, 70-72 (Pubitemid 44322773)
    • (2006) Clinical Lymphoma and Myeloma , vol.7 , Issue.1 , pp. 70-72
    • Rollett, R.A.1    Wilkinson, E.J.2    Gonzalez, D.3    Fenton, J.A.L.4    Short, M.A.5    Evans, P.A.S.6    Rawstron, A.C.7    Owen, R.G.8
  • 41
    • 25444490970 scopus 로고    scopus 로고
    • Problems in using statistical analysis of replacement and silent mutations in antibody genes for determining antigen-driven affinity selection
    • DOI 10.1111/j.1365-2567.2005.02208.x
    • Bose, B., and Sinha, S. (2005) Problems in using statistical analysis of replacement and silent mutations in antibody genes for determining antigen-driven affinity selection. Immunology 116, 172-183 (Pubitemid 41368659)
    • (2005) Immunology , vol.116 , Issue.2 , pp. 172-183
    • Bose, B.1    Sinha, S.2
  • 43
    • 34250778996 scopus 로고    scopus 로고
    • Exosites in the substrate specificity of blood coagulation reactions
    • DOI 10.1111/j.1538-7836.2007.02496.x, State of the Art 2007: XXI Congress of the International Society on Thrombosis and Haemostasis
    • Bock, P. E., Panizzi, P., and Verhamme, I. M. (2007) Exosites in the substrate specificity of blood coagulation reactions. J. Thromb. Haemost. 5, 81-94 (Pubitemid 46958821)
    • (2007) Journal of Thrombosis and Haemostasis , vol.5 , Issue.SUPPL. 1 , pp. 81-94
    • Bock, P.E.1    Panizzi, P.2    Verhamme, I.M.A.3
  • 44
    • 0003187567 scopus 로고    scopus 로고
    • The atomic structure of protein-protein recognition sites
    • DOI 10.1006/jmbi.1998.2439
    • Lo Conte, L., Chothia, C., and Janin, J. (1999) The atomic structure of protein-protein recognition sites. J. Mol. Biol. 285, 2177-2198 (Pubitemid 29078179)
    • (1999) Journal of Molecular Biology , vol.285 , Issue.5 , pp. 2177-2198
    • Conte, L.L.1    Chothia, C.2    Janin, J.3
  • 45
    • 0027374633 scopus 로고
    • Hemostatic molecular markers in nephrotic syndrome
    • Chen, T. Y., Huang, C. C., and Tsao, C. J. (1993) Hemostatic molecular markers in nephrotic syndrome. Am. J. Hematol. 44, 276-279
    • (1993) Am. J. Hematol. , vol.44 , pp. 276-279
    • Chen, T.Y.1    Huang, C.C.2    Tsao, C.J.3
  • 46
    • 84861097723 scopus 로고    scopus 로고
    • Increased serum baseline tryptase levels and extensive skin involvement are predictors for the severity of mast cell activation episodes in children with mastocytosis
    • Alvarez-Twose, I., Vañó-Galván, S., Sánchez-Muñoz, L., Morgado, J. M., Matito, A., Torrelo, A., Jaén, P., Schwartz, L. B., Orfao, A., and Escribano, L. (2012) Increased serum baseline tryptase levels and extensive skin involvement are predictors for the severity of mast cell activation episodes in children with mastocytosis. Allergy 67, 813-821
    • (2012) Allergy , vol.67 , pp. 813-821
    • Alvarez-Twose, I.1    Vañó-Galván, S.2    Sánchez- Muñoz, L.3    Morgado, J.M.4    Matito, A.5    Torrelo, A.6    Jaén, P.7    Schwartz, L.B.8    Orfao, A.9    Escribano, L.10
  • 48
    • 38149124883 scopus 로고    scopus 로고
    • Catalytic features and eradication ability of antibody light-chain UA15-L against Helicobacter pylori
    • Hifumi, E., Morihara, F., Hatiuchi, K., Okuda, T., Nishizono, A., and Uda, T. (2008) Catalytic features and eradication ability of antibody light-chain UA15-L against Helicobacter pylori. J. Biol. Chem. 283, 899-907
    • (2008) J. Biol. Chem. , vol.283 , pp. 899-907
    • Hifumi, E.1    Morihara, F.2    Hatiuchi, K.3    Okuda, T.4    Nishizono, A.5    Uda, T.6
  • 49
    • 84860903184 scopus 로고    scopus 로고
    • Highly efficient method of preparing human catalytic antibody light chains and their biological characteristics
    • Hifumi, E., Honjo, E., Fujimoto, N., Arakawa, M., Nishizono, A., and Uda, T. (2012) Highly efficient method of preparing human catalytic antibody light chains and their biological characteristics. FASEB J. 26, 1607-1615
    • (2012) FASEB J. , vol.26 , pp. 1607-1615
    • Hifumi, E.1    Honjo, E.2    Fujimoto, N.3    Arakawa, M.4    Nishizono, A.5    Uda, T.6
  • 50
    • 0024382917 scopus 로고
    • Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody
    • Paul, S., Volle, D. J., Beach, C. M., Johnson, D. R., Powell, M. J., and Massey, R. J. (1989) Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody. Science 244, 1158-1162 (Pubitemid 19170484)
    • (1989) Science , vol.244 , Issue.4909 , pp. 1158-1162
    • Paul, S.1    Volle, D.J.2    Beach, C.M.3    Johnson, D.R.4    Powell, M.J.5    Massey, R.J.6
  • 54
    • 78049502057 scopus 로고    scopus 로고
    • Identification of anti-prothrombin antibodies in the anti-phospholipid syndrome that display the prothrombinase activity
    • Yang, Y. H., Chang, C. J., Chuang, Y. H., Hsu, H. Y., Chen, P. P., and Chiang, B. L. (2010) Identification of anti-prothrombin antibodies in the anti-phospholipid syndrome that display the prothrombinase activity. Rheumatology 49, 34-42
    • (2010) Rheumatology , vol.49 , pp. 34-42
    • Yang, Y.H.1    Chang, C.J.2    Chuang, Y.H.3    Hsu, H.Y.4    Chen, P.P.5    Chiang, B.L.6
  • 61
    • 0032532015 scopus 로고    scopus 로고
    • Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: A role for flexibility and geometry
    • Roux, K. H., Strelets, L., Brekke, O. H., Sandlie, I., and Michaelsen, T. E. (1998) Comparisons of the ability of human IgG3 hinge mutants, IgM, IgE, and IgA2, to form small immune complexes: a role for flexibility and geometry. J. Immunol. 161, 4083-4090 (Pubitemid 28468987)
    • (1998) Journal of Immunology , vol.161 , Issue.8 , pp. 4083-4090
    • Roux, K.H.1    Strelets, L.2    Brekke, O.H.3    Sandlie, I.4    Michaelsen, T.E.5
  • 62
    • 0033103203 scopus 로고    scopus 로고
    • Structural aspects of human IgM antibodies expressed in chronic B lymphocytic leukemia
    • DOI 10.1016/S1380-2933(98)00025-6, PII S1380293398000256
    • Ramsland, P. A., Brock, C. R., Moses, J., Robinson, B. G., Edmundson, A. B., and Raison, R. L. (1999) Structural aspects of human IgM antibodies expressed in chronic B lymphocytic leukemia. Immunotechnology 4, 217-229 (Pubitemid 29170030)
    • (1999) Immunotechnology , vol.4 , Issue.3-4 , pp. 217-229
    • Ramsland, P.A.1    Brock, C.R.2    Moses, J.3    Robinson, B.G.4    Edmundson, A.B.5    Raison, R.L.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.