메뉴 건너뛰기




Volumn 31, Issue 11, 2009, Pages 1161-1171

Catalytic antibodies: Balancing between Dr. Jekyll and Mr. Hyde

Author keywords

Abzymes; Anti DNA antibodies; Autoimmunity; Catalytic vaccines; Transition state

Indexed keywords

ABZYME; BLOOD CLOTTING FACTOR 8 ANTIBODY; CATALYTIC ANTIBODY; DNA; DNA VACCINE; GLYCOPROTEIN GP 120; IMMUNOGLOBULIN M ANTIBODY; PROTHROMBIN ANTIBODY; UNCLASSIFIED DRUG;

EID: 70549085026     PISSN: 02659247     EISSN: None     Source Type: Journal    
DOI: 10.1002/bies.200900020     Document Type: Review
Times cited : (35)

References (114)
  • 3
    • 0015956495 scopus 로고
    • Towards a network theory of the immune system
    • Jerne NK. 1974. Towards a network theory of the immune system. Ann Immunol (Paris) 125C: 373-389
    • (1974) Ann Immunol (Paris) , vol.125 C , pp. 373-389
    • Jerne, N.K.1
  • 4
    • 84912208190 scopus 로고
    • Chemical achievement and hope for the future
    • Pauling L. 1948. Chemical achievement and hope for the future. Am Sci 36: 51-58
    • (1948) Am Sci , vol.36 , pp. 51-58
    • Pauling, L.1
  • 5
    • 0029118432 scopus 로고
    • Antiidiotypic antibodies as functional internal images of enzyme-active sites
    • Friboulet A, Izadyar L, Avalle B, et al. 1995. Antiidiotypic antibodies as functional internal images of enzyme-active sites. Ann N Y Acad Sci 750: 265-270
    • (1995) Ann N Y Acad Sci , vol.750 , pp. 265-270
    • Friboulet, A.1    Izadyar, L.2    Avalle, B.3
  • 7
    • 0016635322 scopus 로고
    • The antibody-enzyme analogy. Comparison of enzymes and antibodies specific for phosphopyridoxyltyrosine
    • Raso V, Stollar BD. 1975. The antibody-enzyme analogy. Comparison of enzymes and antibodies specific for phosphopyridoxyltyrosine. Biochemistry 14: 591-599
    • (1975) Biochemistry , vol.14 , pp. 591-599
    • Raso, V.1    Stollar, B.D.2
  • 8
    • 0024483498 scopus 로고
    • Monoclonal antibodies as catalysts and templates for organic chemical reactions
    • Green BS. 1989. Monoclonal antibodies as catalysts and templates for organic chemical reactions. Adv Biotechnol Process 11: 359-393
    • (1989) Adv Biotechnol Process , vol.11 , pp. 359-393
    • Green, B.S.1
  • 9
    • 0019154676 scopus 로고
    • Monoclonal immunoglobulin G augments hydrolysis of an ester of the homologous hapten: An esterase-like activity of the antibody-containing site?
    • Kohen F, Kim JB, Lindner HR, et al. 1980. Monoclonal immunoglobulin G augments hydrolysis of an ester of the homologous hapten: an esterase-like activity of the antibody-containing site? FEBS Lett 111: 427-431
    • (1980) FEBS Lett , vol.111 , pp. 427-431
    • Kohen, F.1    Kim, J.B.2    Lindner, H.R.3
  • 11
    • 0024573728 scopus 로고
    • A new strategy for the generation of catalytic antibodies
    • DOI 10.1038/338269a0
    • Shokat KM, Leumann CJ, Sugasawara R, et al. 1989. A new strategy for the generation of catalytic antibodies. Nature 338: 269-271 (Pubitemid 19086931)
    • (1989) Nature , vol.338 , Issue.6212 , pp. 269-271
    • Shokat, K.M.1    Leumann, C.J.2    Sugasawara, R.3    Schultz, P.G.4
  • 12
    • 0033791659 scopus 로고    scopus 로고
    • Critical analysis of antibody catalysis
    • Hilvert D. 2000. Critical analysis of antibody catalysis. Annu Rev Biochem 69: 751-793
    • (2000) Annu Rev Biochem , vol.69 , pp. 751-793
    • Hilvert, D.1
  • 13
    • 0027772297 scopus 로고
    • Catalytic antibodies: The rerouting of chemical reactions
    • Janda KD. 1993. Catalytic antibodies: the rerouting of chemical reactions. Biochem Soc Trans 21: 1090-1095 (Pubitemid 24011793)
    • (1993) Biochemical Society Transactions , vol.21 , Issue.4 , pp. 1090-1095
    • Janda, K.D.1
  • 15
    • 0023759322 scopus 로고
    • Induction of an antibody that catalyzes the hydrolysis of an amide bond
    • Janda KD, Schloeder D, Benkovic SJ, et al. 1988. Induction of an antibody that catalyzes the hydrolysis of an amide bond. Science 241: 1188-1191 (Pubitemid 18215996)
    • (1988) Science , vol.241 , Issue.4870 , pp. 1188-1191
    • Janda, K.D.1    Schloeder, D.2    Benkovic, S.J.3    Lerner, R.A.4
  • 16
    • 0024382917 scopus 로고
    • Catalytic hydrolysis of vasoactive intestinal peptide by human autoantibody
    • Paul S, Volle DJ, Beach CM, et al. 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
  • 17
    • 0028952371 scopus 로고
    • Cleavage of supercoiled plasmid DNA by autoantibody Fab fragment: Application of the flow linear dichroism technique
    • Gololobov GV, Chernova EA, Schourov DV, et al. 1995. Cleavage of supercoiled plasmid DNA by autoantibody Fab fragment: application of the flow linear dichroism technique. Proc Natl Acad Sci U S A 92: 254-257
    • (1995) Proc Natl Acad Sci U S A , vol.92 , pp. 254-257
    • Gololobov, G.V.1    Chernova, E.A.2    Schourov, D.V.3
  • 19
    • 0025072986 scopus 로고
    • Affinity chromatography of catalytic autoantibody to vasoactive intestinal peptide
    • Paul S, Volle DJ, Mei S. 1990. Affinity chromatography of catalytic autoantibody to vasoactive intestinal peptide. J Immunol 145: 1196-1199 (Pubitemid 20258723)
    • (1990) Journal of Immunology , vol.145 , Issue.4 , pp. 1196-1199
    • Paul, S.1    Volle, D.J.2    Mei, S.3
  • 20
    • 0024307033 scopus 로고
    • Topoisomerase I from human placenta. Functional activity of products of expression of cloned cDNA fragments
    • Bronshtein IB, Shuster AM, Shevchenko LV, et al. 1989. Topoisomerase I from human placenta. Functional activity of products of expression of cloned cDNA fragments. Mol Biol (Mosk) 23: 1553-1557
    • (1989) Mol Biol (Mosk) , vol.23 , pp. 1553-1557
    • Bronshtein, I.B.1    Shuster, A.M.2    Shevchenko, L.V.3
  • 21
    • 0026714355 scopus 로고
    • DNA-specific antiidiotypic antibodies in the sera of patients with autoimmune diseases
    • Bronshtein IB, Shuster AM, Gololobov GV, et al. 1992. DNA-specific antiidiotypic antibodies in the sera of patients with autoimmune diseases. FEBS Lett 314: 259-263
    • (1992) FEBS Lett , vol.314 , pp. 259-263
    • Bronshtein, I.B.1    Shuster, A.M.2    Gololobov, G.V.3
  • 22
    • 0031852497 scopus 로고    scopus 로고
    • Functional mimicry: Elicitation of a monoclonal anti-idiotypic antibody hydrolizing beta-lactams
    • Avalle B, Thomas D, Friboulet A. 1998. Functionalmimicry: elicitation of a monoclonal anti-idiotypic antibody hydrolizing beta-lactams. FASEB J 12: 1055-1060 (Pubitemid 28359587)
    • (1998) FASEB Journal , vol.12 , Issue.11 , pp. 1055-1060
    • Avalle, B.1    Thomas, D.2    Friboulet, A.3
  • 23
    • 0028435833 scopus 로고
    • Catalytic activity of anti-ground state antibodies, antibody subunits, and human autoantibodies
    • discussion 253-1245
    • Paul S. 1994. Catalytic activity of anti-ground state antibodies, antibody subunits, and human autoantibodies. Appl Biochem Biotechnol 47: 241- 53; discussion 253-1245
    • (1994) Appl Biochem Biotechnol , vol.47 , pp. 241-253
    • Paul, S.1
  • 24
    • 0034129159 scopus 로고    scopus 로고
    • DNA hydrolysis by monoclonal autoantibody BV 04-01
    • discussion 103-5, 145-153
    • Rodkey LS, Gololobov G, Rumbley CA, et al. 2000. DNA hydrolysis by monoclonal autoantibody BV 04-01. Appl Biochem Biotechnol. 83: 95- 103; discussion 103-5, 145-153
    • (2000) Appl Biochem Biotechnol. , vol.83 , pp. 95-103
    • Rodkey, L.S.1    Gololobov, G.2    Rumbley, C.A.3
  • 25
    • 0031426339 scopus 로고    scopus 로고
    • DNA hydrolysis by monoclonal anti-ssDNA autoantibody BV 04-01: Origins of catalytic activity
    • Gololobov GV, Rumbley CA, Rumbley JN, et al. 1997. DNA hydrolysis by monoclonal anti-ssDNA autoantibody BV 04-01: origins of catalytic activity. Mol Immunol 34: 1083-1093
    • (1997) Mol Immunol , vol.34 , pp. 1083-1093
    • Gololobov, G.V.1    Rumbley, C.A.2    Rumbley, J.N.3
  • 26
    • 0028438989 scopus 로고
    • DNA-protein complexes. Natural targets for DNA-hydrolyzing antibodies
    • discussion 314-1305
    • Gololobov GV, Mikhalap SV, Starov AV, et al. 1994. DNA-protein complexes. Natural targets for DNA-hydrolyzing antibodies. Appl Biochem Biotechnol 47: 305-14; discussion 314-1305
    • (1994) Appl Biochem Biotechnol , vol.47 , pp. 305-314
    • Gololobov, G.V.1    Mikhalap, S.V.2    Starov, A.V.3
  • 27
    • 0032430807 scopus 로고    scopus 로고
    • Novel functional activities of anti-DNA autoantibodies from sera of patients with lymphoproliferative and autoimmune diseases
    • Kozyr AV, Kolesnikov AV, Aleksandrova ES, et al. 1998. Novel functional activities of anti-DNA autoantibodies from sera of patients with lymphoproliferative and autoimmune diseases. Appl Biochem Biotechnol 75: 45-61.
    • (1998) Appl Biochem Biotechnol , vol.75 , pp. 45-61
    • Kozyr, A.V.1    Kolesnikov, A.V.2    Aleksandrova, E.S.3
  • 28
    • 0024709616 scopus 로고
    • Bent DNA is a structural feature of scaffoldattached regions in Drosophila melanogaster interphase nuclei
    • Homberger HP. 1989. Bent DNA is a structural feature of scaffoldattached regions in Drosophila melanogaster interphase nuclei. Chromosoma 98: 99-104.
    • (1989) Chromosoma , vol.98 , pp. 99-104
    • Homberger, H.P.1
  • 29
    • 0029018511 scopus 로고
    • Transition-state stabilization as a measure of the efficiency of antibody catalysis
    • Stewart JD, Benkovic SJ. 1995. Transition-state stabilization as a measure of the efficiency of antibody catalysis. Nature 375: 388-391
    • (1995) Nature , vol.375 , pp. 388-391
    • Stewart, J.D.1    Benkovic, S.J.2
  • 30
    • 0037173617 scopus 로고    scopus 로고
    • Screening inhibitors of anthrax lethal factor
    • DOI 10.1038/418386a
    • Tonello F, Seveso M, Marin O, et al. 2002. Screening inhibitors of anthrax lethal factor. Nature 418: 386. (Pubitemid 34826833)
    • (2002) Nature , vol.418 , Issue.6896 , pp. 386
    • Tonello, F.1    Seveso, M.2    Marin, O.3    Mock, M.4    Montecucco, C.5
  • 31
    • 0028835286 scopus 로고
    • Site-directed mutagenesis of proteolytic antibody light chain
    • Gao QS, Sun M, Rees AR, et al. 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
  • 33
    • 33646234449 scopus 로고    scopus 로고
    • Crystal structure of a glycosylated Fab from an IgM cryoglobulin with properties of a natural proteolytic antibody
    • Ramsland PA, Terzyan SS, Cloud G, et al. 2006. Crystal structure of a glycosylated Fab from an IgM cryoglobulin with properties of a natural proteolytic antibody. Biochem J 395: 473-481
    • (2006) Biochem J , vol.395 , pp. 473-481
    • Ramsland, P.A.1    Terzyan, S.S.2    Cloud, G.3
  • 34
    • 0016311758 scopus 로고
    • Do immunoglobulins have proteolytic activity?
    • Erhan S, Greller LD. 1974. Do immunoglobulins have proteolytic activity? Nature 251: 353-355
    • (1974) Nature , vol.251 , pp. 353-355
    • Erhan, S.1    Greller, L.D.2
  • 35
    • 0029072696 scopus 로고
    • Natural catalytic antibodies: Peptidehydrolyzing activities of Bence Jones proteins and VL fragment
    • Paul S, Li L, Kalaga R, et al. 1995. Natural catalytic antibodies: peptidehydrolyzing 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
  • 36
    • 0036837368 scopus 로고    scopus 로고
    • Catalytic antibodies in clinical and experimental pathology: Human and mouse models
    • Ponomarenko NA, Durova OM, Vorobiev II, et al. 2002. Catalytic antibodies in clinical and experimental pathology: human and mouse models. J Immunol Methods 269: 197-211.
    • (2002) J Immunol Methods , vol.269 , pp. 197-211
    • Ponomarenko, N.A.1    Durova, O.M.2    Vorobiev, I.I.3
  • 37
    • 61349140658 scopus 로고    scopus 로고
    • Exceptional amyloid beta peptide hydrolyzing activity of nonphysiological immunoglobulin variable domain scaffolds
    • Taguchi H, Planque S, Sapparapu G, et al. 2008. Exceptional amyloid beta 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
  • 38
    • 37549028838 scopus 로고    scopus 로고
    • Routes to covalent catalysis by reactive selection for nascent protein nucleophiles
    • Reshetnyak AV, Armentano MF, Ponomarenko NA, et al. 2007. Routes to covalent catalysis by reactive selection for nascent protein nucleophiles. J Am Chem Soc 129: 16175-16182
    • (2007) J Am Chem Soc , vol.129 , pp. 16175-16182
    • Reshetnyak, A.V.1    Armentano, M.F.2    Ponomarenko, N.A.3
  • 39
    • 66249092759 scopus 로고    scopus 로고
    • Investigations into the development of catalytic activity in anti-acetylcholinesterase idiotypic and anti-idiotypic antibodies
    • Johnson G, Moore SW. 2009. Investigations into the development of catalytic activity in anti-acetylcholinesterase idiotypic and anti-idiotypic antibodies. J Mol Recognit 22: 188-196
    • (2009) J Mol Recognit , vol.22 , pp. 188-196
    • Johnson, G.1    Moore, S.W.2
  • 43
    • 33744962513 scopus 로고    scopus 로고
    • Heavy and light chain variable single domains of an anti-DNA binding antibody hydrolyze both double- And single-stranded DNAs without sequence specificity
    • Kim YR, Kim JS, Lee SH, et al. 2006. Heavy and light chain variable single domains of an anti-DNA binding antibody hydrolyze both double- and single-stranded DNAs without sequence specificity. J Biol Chem 281: 15287-15295
    • (2006) J Biol Chem , vol.281 , pp. 15287-15295
    • Kim, Y.R.1    Kim, J.S.2    Lee, S.H.3
  • 44
    • 33846693701 scopus 로고    scopus 로고
    • Cell-penetrating autoantibody induces caspase-mediated apoptosis through catalytic hydrolysis of DNA
    • DOI 10.1016/j.bmc.2006.12.037, PII S096808960601042X
    • Lee EJ, Jang EJ, Lee E, et al. 2007. Cell-penetrating autoantibody induces caspase-mediated apoptosis through catalytic hydrolysis of DNA. Bioorg Med Chem 15: 2016-2023 (Pubitemid 46188403)
    • (2007) Bioorganic and Medicinal Chemistry , vol.15 , Issue.5 , pp. 2016-2023
    • Lee, E.-J.1    Jang, E.-J.2    Lee, E.3    Yu, J.4    Chung, H.Y.5    Jang, Y.-J.6
  • 45
    • 0034129295 scopus 로고    scopus 로고
    • Autoantibodies to nuclear antigens: Correlation between cytotoxicity and DNA-hydrolyzing activity
    • discussion 268-259, 297-313.
    • Kozyr AV, Kolesnikov AV, Zelenova NA, et al. 2000. Autoantibodies to nuclear antigens: correlation between cytotoxicity and DNA-hydrolyzing activity. Appl Biochem Biotechnol 83: 255-68; discussion 268-259, 297-313.
    • (2000) Appl Biochem Biotechnol , vol.83 , pp. 255-268
    • Kozyr, A.V.1    Kolesnikov, A.V.2    Zelenova, N.A.3
  • 46
    • 0027548494 scopus 로고
    • Isolation and characteristics of catalytic antibodies to DNA in systemic lupus erythematosis
    • Gololobov GV, Bogomolova AE, Iadav RP, et al. 1993. Isolation and characteristics of catalytic antibodies to DNA in systemic lupus erythematosis. Biokhimiia 58: 313-318
    • (1993) Biokhimiia , vol.58 , pp. 313-318
    • Gololobov, G.V.1    Bogomolova, A.E.2    Iadav, R.P.3
  • 47
    • 0035178128 scopus 로고    scopus 로고
    • Anti-DNA autoantibodies reveal toxicity to tumor cell lines
    • Kozyr AV, Sashchenko LP, Kolesnikov AV, et al. 2002. Anti-DNA autoantibodies reveal toxicity to tumor cell lines. Immunol Lett 80: 41-47.
    • (2002) Immunol Lett , vol.80 , pp. 41-47
    • Kozyr, A.V.1    Sashchenko, L.P.2    Kolesnikov, A.V.3
  • 49
    • 0028609559 scopus 로고
    • Molecular and structural analysis of nuclear localizing anti-DNA lupus antibodies
    • Foster MH, Kieber-Emmons T, Ohliger M, et al. 1994. Molecular and structural analysis of nuclear localizing anti-DNA lupus antibodies. Immunol Res 13: 186-206.
    • (1994) Immunol Res , vol.13 , pp. 186-206
    • Foster, M.H.1    Kieber-Emmons, T.2    Ohliger, M.3
  • 50
    • 72849113767 scopus 로고    scopus 로고
    • DNA-hydrolyzing activity of IgG antibodies from the sera of patients with diseases caused by different bacterial infections
    • Doi: 10.1111/j.1582-4934.2008.00441.x
    • Parkhomenko TA, Odintsova ES, Buneva VN, et al. 2008. DNA-hydrolyzing activity of IgG antibodies from the sera of patients with diseases caused by different bacterial infections. J Cell Mol Med Doi: 10.1111/j.1582-4934.2008. 00441.x
    • (2008) J Cell Mol Med
    • Parkhomenko, T.A.1    Odintsova, E.S.2    Buneva, V.N.3
  • 52
    • 0027130670 scopus 로고
    • Acute hyperglycemia enhances proteolysis in normal man
    • Flakoll PJ, Hill JO, Abumrad NN. 1993. Acute hyperglycemia enhances proteolysis in normal man. Am J Physiol 265: E715-21.
    • (1993) Am J Physiol , vol.265
    • Flakoll, P.J.1    Hill, J.O.2    Abumrad, N.N.3
  • 53
    • 33947104061 scopus 로고    scopus 로고
    • Characterization of immune complexes of idiotypic catalytic and anti-idiotypic inhibitory antibodies in plasma of type 1 diabetic subjects
    • DOI 10.1016/j.molimm.2007.01.012, PII S0161589007000363
    • Pagetta A, Tramentozzi E, Corbetti L, et al. 2007. Characterization of immune complexes of idiotypic catalytic and anti-idiotypic inhibitory antibodies in plasma of type 1 diabetic subjects. Mol Immunol 44: 2870-2883 (Pubitemid 46412495)
    • (2007) Molecular Immunology , vol.44 , Issue.11 , pp. 2870-2883
    • Pagetta, A.1    Tramentozzi, E.2    Corbetti, L.3    Frasson, M.4    Brunati, A.M.5    Finotti, P.6
  • 54
    • 0035823550 scopus 로고    scopus 로고
    • An Endoplasmic Reticulum Protein Implicated in Chaperoning Peptides to Major Histocompatibility of Class I Is an Aminopeptidase
    • DOI 10.1074/jbc.M103383200
    • Menoret A, Li Z, Niswonger ML, et al. 2001. An endoplasmic reticulum protein implicated in chaperoning peptides to major histocompatibility of class I is an aminopeptidase. J Biol Chem 276: 33313-33318 (Pubitemid 37384537)
    • (2001) Journal of Biological Chemistry , vol.276 , Issue.36 , pp. 33313-33318
    • Menoret, A.1    Li, Z.2    Niswonger, M.L.3    Altmeyer, A.4    Srivastava, P.K.5
  • 55
    • 0028926783 scopus 로고
    • Catalytic activity of anti-thyroglobulin antibodies
    • Li L, Paul S, Tyutyulkova S, et al. 1995. Catalytic activity of anti-thyroglobulin antibodies. J Immunol 154: 3328-3332
    • (1995) J Immunol , vol.154 , pp. 3328-3332
    • Li, L.1    Paul, S.2    Tyutyulkova, S.3
  • 57
    • 0024555485 scopus 로고
    • Factor VIII gene and hemophilia A
    • White GC II, Shoemaker CB. 1989. Factor VIII gene and hemophilia A. Blood 73: 1-12.
    • (1989) Blood , vol.73 , pp. 1-12
    • White II, G.C.1    Shoemaker, C.B.2
  • 58
    • 0026548917 scopus 로고
    • Incidence of development of factor VIII and factor IX inhibitors in haemophiliacs
    • Ehrenforth S, Kreuz W, Scharrer I, et al. 1992. Incidence of development of factor VIII and factor IX inhibitors in haemophiliacs. Lancet 339: 594-598
    • (1992) Lancet , vol.339 , pp. 594-598
    • Ehrenforth, S.1    Kreuz, W.2    Scharrer, I.3
  • 61
    • 47249156490 scopus 로고    scopus 로고
    • Factor VIII hydrolysis mediated by anti-factor VIII autoantibodies in acquired hemophilia
    • Wootla B, Dasgupta S, Dimitrov JD, et al. 2008. Factor VIII hydrolysis mediated by anti-factor VIII autoantibodies in acquired hemophilia. J Immunol 180: 7714-7720
    • (2008) J Immunol , vol.180 , pp. 7714-7720
    • Wootla, B.1    Dasgupta, S.2    Dimitrov, J.D.3
  • 63
    • 0031876557 scopus 로고    scopus 로고
    • Autoantibodies to human prothrombin and clinical manifestations in 207 patients with systemic lupus erythematosus
    • Bertolaccini ML, Atsumi T, KhamashtaMA, et al. 1998. Autoantibodies to human prothrombin and clinical manifestations in 207 patients with systemic lupus erythematosus. J Rheumatol 25: 1104-1108 (Pubitemid 28350883)
    • (1998) Journal of Rheumatology , vol.25 , Issue.6 , pp. 1104-1108
    • Bertolaccini, M.L.1    Atsumi, T.2    Khamashta, M.A.3    Amengual, O.4    Hughes, G.R.V.5
  • 64
    • 0030716933 scopus 로고    scopus 로고
    • High antibody levels to prothrombin imply a risk of deep venous thrombosis and pulmonary embolism in middle-aged men. a nested case-control study
    • Palosuo T, Virtamo J, Haukka J, et al. 1997. High antibody levels to prothrombin imply a risk of deep venous thrombosis and pulmonary embolism in middle-aged men - A nested case-control study. Thromb Haemostasis 78: 1178-1182 (Pubitemid 27464582)
    • (1997) Thrombosis and Haemostasis , vol.78 , Issue.4 , pp. 1178-1182
    • Palosuo, T.1    Virtamo, J.2    Haukka, J.3    Taylor, P.R.4    Aho, K.5    Puurunen, M.6    Vaarala, O.7
  • 67
    • 63749088424 scopus 로고    scopus 로고
    • Immunoglobulin a with protease activity secreted in human milk activates PAR-2 receptors, of intestinal epithelial cells HT-29, and promotes beta-defensin-2 expression
    • Barrera GJ, Portillo R, Mijares A, et al. 2009. Immunoglobulin A with protease activity secreted in human milk activates PAR-2 receptors, of intestinal epithelial cells HT-29, and promotes beta-defensin-2 expression. Immunol Lett 123: 52-59
    • (2009) Immunol Lett , vol.123 , pp. 52-59
    • Barrera, G.J.1    Portillo, R.2    Mijares, A.3
  • 68
  • 69
    • 0242438618 scopus 로고    scopus 로고
    • Catalytic antibodies in healthy humans and patients with autoimmune and viral diseases
    • Nevinsky GA, Buneva VN. 2003. Catalytic antibodies in healthy humans and patients with autoimmune and viral diseases. J Cell Mol Med 7: 265-276 (Pubitemid 37372046)
    • (2003) Journal of Cellular and Molecular Medicine , vol.7 , Issue.3 , pp. 265-276
    • Nevinsky, G.A.1    Buneva, V.N.2
  • 70
    • 0035823071 scopus 로고    scopus 로고
    • Antibody catalysis of the oxidation of water
    • Wentworth P Jr., Jones LH, Wentworth AD, et al. 2001. Antibody catalysis of the oxidation of water. Science 293: 1806-1811
    • (2001) Science , vol.293 , pp. 1806-1811
    • Wentworth Jr., P.1    Jones, L.H.2    Wentworth, A.D.3
  • 71
    • 0037073888 scopus 로고    scopus 로고
    • Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation
    • Wentworth P Jr., McDunn JE, Wentworth AD, et al. 2002. Evidence for antibody-catalyzed ozone formation in bacterial killing and inflammation. Science 298: 2195-2199
    • (2002) Science , vol.298 , pp. 2195-2199
    • Wentworth Jr., P.1    McDunn, J.E.2    Wentworth, A.D.3
  • 74
    • 31544465918 scopus 로고    scopus 로고
    • Immunoglobulins can utilize riboflavin (Vitamin B2) to activate the antibody-catalyzed water oxidation pathway
    • DOI 10.1016/j.imlet.2005.11.020, PII S0165247805003640, Catalytic Antibodies
    • Nieva J, Kerwin L, Wentworth AD, et al. 2006. Immunoglobulins can utilize riboflavin (Vitamin B2) to activate the antibody-catalyzed water oxidation pathway. Immunol Lett 103: 33-38 (Pubitemid 43162943)
    • (2006) Immunology Letters , vol.103 , Issue.1 , pp. 33-38
    • Nieva, J.1    Kerwin, L.2    Wentworth, A.D.3    Lerner, R.A.4    Wentworth Jr., P.5
  • 75
    • 33745137784 scopus 로고    scopus 로고
    • Effect of ozone produced from antibody-catalyzed water oxidation on pathogenesis of atherosclerosis
    • Peng KJ, Huang YS, An LN, et al. 2006. Effect of ozone produced from antibody-catalyzed water oxidation on pathogenesis of atherosclerosis. Acta Biochim Biophys Sin (Shanghai) 38: 417-422
    • (2006) Acta Biochim Biophys Sin (Shanghai) , vol.38 , pp. 417-422
    • Peng, K.J.1    Huang, Y.S.2    An, L.N.3
  • 76
    • 33846513576 scopus 로고    scopus 로고
    • Autoantibodies closely relate to the elevation level of in vivo hydrogen peroxide and tissue damage in systemic lupus erythematosus
    • DOI 10.1089/dna.2006.25.563
    • Wang Y, Qiao B, Han X, et al. 2006. Autoantibodies closely relate to the elevation level of in vivo hydrogen peroxide and tissue damage in systemic lupus erythematosus. DNA Cell Biol 25: 563-570 (Pubitemid 46150667)
    • (2006) DNA and Cell Biology , vol.25 , Issue.10 , pp. 563-570
    • Wang, Y.1    Qiao, B.2    Wang, Y.3    Han, X.4    Chu, Y.5    Xiong, S.6
  • 78
    • 0041878841 scopus 로고    scopus 로고
    • Antibody-catalyzed water oxidation: State-of-the-art immunity or ancient history?
    • Parren PW, Leusen JH, van de Winkel JG. 2003. Antibody-catalyzed water oxidation: state-of-the-art immunity or ancient history? Trends Immunol 24: 467-469
    • (2003) Trends Immunol , vol.24 , pp. 467-469
    • Parren, P.W.1    Leusen, J.H.2    Van De Winkel, J.G.3
  • 81
    • 4444362840 scopus 로고    scopus 로고
    • Current progress in beta-amyloid immunotherapy
    • Schenk D, Hagen M, Seubert P. 2004. Current progress in beta-amyloid immunotherapy. Curr Opin Immunol 16: 599-606.
    • (2004) Curr Opin Immunol , vol.16 , pp. 599-606
    • Schenk, D.1    Hagen, M.2    Seubert, P.3
  • 82
    • 0345060484 scopus 로고    scopus 로고
    • Degradation of beta-Amyloid by Proteolytic Antibody Light Chains
    • DOI 10.1021/bi035038d
    • Rangan SK, Liu R, Brune D, et al. 2003. Degradation of beta-amyloid by proteolytic antibody light chains. Biochemistry 42: 14328-14334 (Pubitemid 37499430)
    • (2003) Biochemistry , vol.42 , Issue.48 , pp. 14328-14334
    • Rangan, S.K.1    Liu, R.2    Brune, D.3    Planque, S.4    Paul, S.5    Sierks, M.R.6
  • 84
    • 31544453588 scopus 로고    scopus 로고
    • Catalytic activity of autoantibodies toward myelin basic protein correlates with the scores on the multiple sclerosis expanded disability status scale
    • Ponomarenko NA, Durova OM, Vorobiev II, et al. 2006. Catalytic activity of autoantibodies toward myelin basic protein correlates with the scores on the multiple sclerosis expanded disability status scale. Immunol Lett 103: 45-50.
    • (2006) Immunol Lett , vol.103 , pp. 45-50
    • Ponomarenko, N.A.1    Durova, O.M.2    Vorobiev, I.I.3
  • 85
    • 20644470832 scopus 로고    scopus 로고
    • Hydrolysis of myelin basic protein by polyclonal catalytic IgGs from the sera of patients with multiple sclerosis
    • Polosukhina DI, Kanyshkova TG, Doronin BM, et al. 2004. Hydrolysis of myelin basic protein by polyclonal catalytic IgGs from the sera of patients with multiple sclerosis. J Cell Mol Med 8: 359-368
    • (2004) J Cell Mol Med , vol.8 , pp. 359-368
    • Polosukhina, D.I.1    Kanyshkova, T.G.2    Doronin, B.M.3
  • 86
    • 31044444492 scopus 로고    scopus 로고
    • Autoantibodies to myelin basic protein catalyze site-specific degradation of their antigen
    • Ponomarenko NA, Durova OM, Vorobiev II, et al. 2006. Autoantibodies to myelin basic protein catalyze site-specific degradation of their antigen. Proc Natl Acad Sci U S A 103: 281-286
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 281-286
    • Ponomarenko, N.A.1    Durova, O.M.2    Vorobiev, I.I.3
  • 87
    • 34248178431 scopus 로고    scopus 로고
    • Substrate specificity of catalytic autoantibodies in neurodegenerative processes
    • Belogurov AA, Kurkova IN, Misikov VK, et al. 2007. Substrate speci- ficity of catalytic autoantibodies in neurodegenerative processes. Dokl Biochem Biophys 413: 61-64
    • (2007) Dokl Biochem Biophys , vol.413 , pp. 61-64
    • Belogurov, A.A.1    Kurkova, I.N.2    Misikov, V.K.3
  • 88
    • 40449119704 scopus 로고    scopus 로고
    • Recognition and degradation of myelin basic protein peptides by serum autoantibodies: Novel biomarker for multiple sclerosis
    • Belogurov AA Jr., Kurkova IN, Friboulet A, et al. 2008. Recognition and degradation of myelin basic protein peptides by serum autoantibodies: novel biomarker for multiple sclerosis. J Immunol 180: 1258-1267
    • (2008) J Immunol , vol.180 , pp. 1258-1267
    • Belogurov Jr., A.A.1    Kurkova, I.N.2    Friboulet, A.3
  • 89
    • 33748178872 scopus 로고    scopus 로고
    • Differences in susceptibility of MBP charge isomers to digestion by stromelysin-1 (MMP-3) and release of an immunodominant epitope
    • D'Souza CA, Moscarello MA. 2006. Differences in susceptibility of MBP charge isomers to digestion by stromelysin-1 (MMP-3) and release of an immunodominant epitope. Neurochem Res 31: 1045-1054
    • (2006) Neurochem Res , vol.31 , pp. 1045-1054
    • D'Souza, C.A.1    Moscarello, M.A.2
  • 90
    • 25444524820 scopus 로고    scopus 로고
    • Autocatalytic cleavage of myelin basic protein: An alternative to molecular mimicry
    • D'Souza CA, Wood DD, She YM, et al. 2005. Autocatalytic cleavage of myelin basic protein: an alternative to molecular mimicry. Biochemistry 44: 12905-12913
    • (2005) Biochemistry , vol.44 , pp. 12905-12913
    • D'Souza, C.A.1    Wood, D.D.2    She, Y.M.3
  • 91
    • 30644473886 scopus 로고    scopus 로고
    • Myelin basic protein, an autoantigen in multiple sclerosis, is selectively processed by human trypsin 4
    • DOI 10.1016/j.febslet.2005.12.067, PII S0014579305015528
    • Medveczky P, Antal J, Patthy A, et al. 2006. Myelin basic protein, an autoantigen in multiple sclerosis, is selectively processed by human trypsin 4. FEBS Lett 580: 545-552 (Pubitemid 43089684)
    • (2006) FEBS Letters , vol.580 , Issue.2 , pp. 545-552
    • Medveczky, P.1    Antal, J.2    Patthy, A.3    Kekesi, K.4    Juhasz, G.5    Szilagyi, L.6    Graf, L.7
  • 92
    • 0034625091 scopus 로고    scopus 로고
    • Deimination ofmyelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D
    • Pritzker LB, Joshi S, Gowan JJ, et al. 2000. Deimination ofmyelin basic protein. 1. Effect of deimination of arginyl residues of myelin basic protein on its structure and susceptibility to digestion by cathepsin D. Biochemistry 39: 5374-5381
    • (2000) Biochemistry , vol.39 , pp. 5374-5381
    • Pritzker, L.B.1    Joshi, S.2    Gowan, J.J.3
  • 93
    • 33645210449 scopus 로고    scopus 로고
    • Deimination of membranebound myelin basic protein in multiple sclerosis exposes an immunodominant epitope
    • Musse AA, Boggs JM, Harauz G. 2006. Deimination of membranebound myelin basic protein in multiple sclerosis exposes an immunodominant epitope. Proc Natl Acad Sci U S A 103: 4422-4427
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4422-4427
    • Musse, A.A.1    Boggs, J.M.2    Harauz, G.3
  • 94
    • 33645243957 scopus 로고    scopus 로고
    • Structural insight into the role of myelin basic protein in multiple sclerosis
    • Husted C. 2006. Structural insight into the role of myelin basic protein in multiple sclerosis. Proc Natl Acad Sci U S A 103: 4339-4340
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 4339-4340
    • Husted, C.1
  • 96
    • 0036837369 scopus 로고    scopus 로고
    • Targeted destruction of the HIV-1 coat protein gp41 by a catalytic antibody light chain
    • Hifumi E, Mitsuda Y, Ohara K, et al. 2002. Targeted destruction of the HIV-1 coat protein gp41 by a catalytic antibody light chain. J Immunol Methods 269: 283-298
    • (2002) J Immunol Methods , vol.269 , pp. 283-298
    • Hifumi, E.1    Mitsuda, Y.2    Ohara, K.3
  • 99
    • 46349092352 scopus 로고    scopus 로고
    • Expression, purification, and in vivo administration of a promising anti-idiotypic HIV-1 vaccine
    • Gach JS, Quendler H, Ferko B, et al. 2008. Expression, purification, and in vivo administration of a promising anti-idiotypic HIV-1 vaccine. Mol Biotechnol 39: 119-125
    • (2008) Mol Biotechnol , vol.39 , pp. 119-125
    • Gach, J.S.1    Quendler, H.2    Ferko, B.3
  • 101
    • 30144438492 scopus 로고    scopus 로고
    • Induction of a protein-targeted catalytic response in autoimmune prone mice: Antibody-mediated cleavage of HIV-1 glycoprotein GP120
    • Ponomarenko NA, Vorobiev II, Alexandrova ES, et al. 2006. Induction of a protein-targeted catalytic response in autoimmune prone mice: antibody-mediated cleavage of HIV-1 glycoprotein GP120. Biochemistry 45: 324-330
    • (2006) Biochemistry , vol.45 , pp. 324-330
    • Ponomarenko, N.A.1    Vorobiev, I.I.2    Alexandrova, E.S.3
  • 104
    • 70350757719 scopus 로고    scopus 로고
    • Strategies for induction of catalytic antibodies toward HIV-1 glycoprotein gp120 in autoimmune prone mice
    • Doi:10.1016/j.molimm.2008.12.020
    • Durova OM, Vorobiev II, Smirnov IV, et al. 2009. Strategies for induction of catalytic antibodies toward HIV-1 glycoprotein gp120 in autoimmune prone mice. Mol Immunol Doi:10.1016/j.molimm.2008.12.020
    • (2009) Mol Immunol
    • Durova, O.M.1    Vorobiev, I.I.2    Smirnov, I.V.3
  • 105
    • 0035912801 scopus 로고    scopus 로고
    • In vivo activity in a catalytic antibody-prodrug system: Antibody catalyzed etoposide prodrug activation for selective chemotherapy
    • Shabat D, Lode HN, Pertl U, et al. 2001. In vivo activity in a catalytic antibody-prodrug system: antibody catalyzed etoposide prodrug activation for selective chemotherapy. Proc Natl Acad Sci U S A 98: 7528-7533
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 7528-7533
    • Shabat, D.1    Lode, H.N.2    Pertl, U.3
  • 106
    • 33847635657 scopus 로고    scopus 로고
    • Neurodegeneration in autoimmune demyelination: Recent mechanistic insights reveal novel therapeutic targets
    • DOI 10.1016/j.jneuroim.2006.11.026, PII S0165572806004656, Inflammation, Neurodegeneration and Neuroprotection in the Central Nervous System
    • Aktas O, Waiczies S, Zipp F. 2007. Neurodegeneration in autoimmune demyelination: recent mechanistic insights reveal novel therapeutic targets. J Neuroimmunol 184: 17-26. (Pubitemid 46365988)
    • (2007) Journal of Neuroimmunology , vol.184 , Issue.1-2 , pp. 17-26
    • Aktas, O.1    Waiczies, S.2    Zipp, F.3
  • 107
    • 38549163108 scopus 로고    scopus 로고
    • Catalytic methods for the destruction of chemical warfare agents under ambient conditions
    • Smith BM. 2008. Catalytic methods for the destruction of chemical warfare agents under ambient conditions. Chem Soc Rev 37: 470-478
    • (2008) Chem Soc Rev , vol.37 , pp. 470-478
    • Smith, B.M.1
  • 108
    • 0036837150 scopus 로고    scopus 로고
    • Immunologically driven chemical engineering of antibodies for catalytic activity
    • Dias S, Jovic F, Renard PY, et al. 2002. Immunologically driven chemical engineering of antibodies for catalytic activity. J Immunol Methods 269: 81-98.
    • (2002) J Immunol Methods , vol.269 , pp. 81-98
    • Dias, S.1    Jovic, F.2    Renard, P.Y.3
  • 109
    • 0033013184 scopus 로고    scopus 로고
    • A comparison of flexible and constrained haptens in eliciting antibody catalysts for paraoxon hydrolysis
    • Spivak DA, Hoffman TZ, Moore AH, et al. 1999. A comparison of flexible and constrained haptens in eliciting antibody catalysts for paraoxon hydrolysis. Bioorg Med Chem 7: 1145-1150
    • (1999) Bioorg Med Chem , vol.7 , pp. 1145-1150
    • Spivak, D.A.1    Hoffman, T.Z.2    Moore, A.H.3
  • 110
    • 0029671436 scopus 로고    scopus 로고
    • Toward antibody-directed "abzyme" prodrug therapy, ADAPT: Carbamate prodrug activation by a catalytic antibody and its in vitro application to human tumor cell killing
    • Wentworth P, Datta A, Blakey D, et al. 1996. Toward antibody-directed "abzyme" prodrug therapy, ADAPT: carbamate prodrug activation by a catalytic antibody and its in vitro application to human tumor cell killing. Proc Natl Acad Sci U S A 93: 799-803.
    • (1996) Proc Natl Acad Sci U S A , vol.93 , pp. 799-803
    • Wentworth, P.1    Datta, A.2    Blakey, D.3
  • 111
    • 34247251294 scopus 로고    scopus 로고
    • Antibody-catalyzed anaerobic destruction of methamphetamine
    • Xu Y, Hixon MS, Yamamoto N, et al. 2007. Antibody-catalyzed anaerobic destruction of methamphetamine. Proc Natl Acad Sci U S A 104: 3681-3686
    • (2007) Proc Natl Acad Sci U S A , vol.104 , pp. 3681-3686
    • Xu, Y.1    Hixon, M.S.2    Yamamoto, N.3
  • 112
    • 0031065219 scopus 로고    scopus 로고
    • Immunotherapy for cocaine addiction
    • Landry DW. 1997. Immunotherapy for cocaine addiction. Sci Am 276: 42-45
    • (1997) Sci Am , vol.276 , pp. 42-45
    • Landry, D.W.1
  • 113
    • 33845662807 scopus 로고    scopus 로고
    • Identification and characterization of single chain anti-cocaine catalytic antibodies
    • McKenzie KM, Mee JM, Rogers CJ, et al. 2007. Identification and characterization of single chain anti-cocaine catalytic antibodies. J Mol Biol 365: 722-731
    • (2007) J Mol Biol , vol.365 , pp. 722-731
    • McKenzie, K.M.1    Mee, J.M.2    Rogers, C.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.