메뉴 건너뛰기




Volumn 26, Issue 4, 2005, Pages 485-503

Antibodies as defensive enzymes

Author keywords

Abzymes; Autoimmune disease; Catalytic antibodies; HIV infection; Serine proteases

Indexed keywords

AMYLOID BETA PROTEIN; GLYCOPROTEIN GP 120; IMMUNOGLOBULIN G; IMMUNOGLOBULIN M;

EID: 16344377509     PISSN: 03444325     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00281-004-0191-1     Document Type: Review
Times cited : (40)

References (85)
  • 2
    • 0032698262 scopus 로고    scopus 로고
    • Oxidative stress in systemic lupus erythematosus and allied conditions with vascular involvement
    • Ames PR, Alves J, Murat I, et al (1999) Oxidative stress in systemic lupus erythematosus and allied conditions with vascular involvement. Rheumatology 38:529
    • (1999) Rheumatology , vol.38 , pp. 529
    • Ames, P.R.1    Alves, J.2    Murat, I.3
  • 3
    • 0036948251 scopus 로고    scopus 로고
    • Vasoactive intestinal peptide binding autoantibodies in autoimmune humans and mice
    • Bangale Y, Cavill D, Gordon T, et al (2002) Vasoactive intestinal peptide binding autoantibodies in autoimmune humans and mice. Peptides 23:2251
    • (2002) Peptides , vol.23 , pp. 2251
    • Bangale, Y.1    Cavill, D.2    Gordon, T.3
  • 4
    • 0037387946 scopus 로고    scopus 로고
    • VIPase autoantibodies in Fas-defective mice and patients with autoimmune disease
    • Bangale Y, Karle S, Zhou Y-X, et al (2003) VIPase autoantibodies in Fas-defective mice and patients with autoimmune disease. FASEB J 17:628
    • (2003) FASEB J , vol.17 , pp. 628
    • Bangale, Y.1    Karle, S.2    Zhou, Y.-X.3
  • 5
    • 0027340737 scopus 로고
    • Immunoglobulin VH3 gene products: Natural ligands for HIV gp120
    • Berberian L, Goodglick L, Kipps TJ, et al (1993) Immunoglobulin VH3 gene products: natural ligands for HIV gp120. Science 261:1588
    • (1993) Science , vol.261 , pp. 1588
    • Berberian, L.1    Goodglick, L.2    Kipps, T.J.3
  • 6
    • 0037167576 scopus 로고    scopus 로고
    • Identification of oxidized derivatives of neuroketals
    • Bernoud-Hubac N, Roberts J (2002) Identification of oxidized derivatives of neuroketals. Biochemistry 41:11466
    • (2002) Biochemistry , vol.41 , pp. 11466
    • Bernoud-Hubac, N.1    Roberts, J.2
  • 7
    • 0026788003 scopus 로고
    • A trypsin-like serine protease activity on activated human B cells and various B cell lines
    • Biro A, Sarmay G, Rozsnyay Z, et al (1992) A trypsin-like serine protease activity on activated human B cells and various B cell lines. Eur J Immunol 22:2547
    • (1992) Eur J Immunol , vol.22 , pp. 2547
    • Biro, A.1    Sarmay, G.2    Rozsnyay, Z.3
  • 8
    • 0028985051 scopus 로고
    • 2+ influx induced by beta-amyloid peptide 25-35 in cultured hippocampal neurons results from network excitation
    • 2+ influx induced by beta-amyloid peptide 25-35 in cultured hippocampal neurons results from network excitation. J Neurobiol 26:325
    • (1995) J Neurobiol , vol.26 , pp. 325
    • Brorson, J.R.1    Bindokas, V.P.2    Iwama, T.3
  • 9
    • 0024425654 scopus 로고
    • + B lymphocytes, polyreactive antibodies and the human B-cell repertoire
    • + B lymphocytes, polyreactive antibodies and the human B-cell repertoire. Immunol Today 10:364
    • (1989) Immunol Today , vol.10 , pp. 364
    • Casali, P.1    Notkins, A.L.2
  • 10
    • 0014669634 scopus 로고
    • Studies on antigen-binding activity of macroglobulin antibody subunits and their enzymatic fragments
    • Chavin SI, Franklin EC (1969) Studies on antigen-binding activity of macroglobulin antibody subunits and their enzymatic fragments. J Biol Chem 244:1345
    • (1969) J Biol Chem , vol.244 , pp. 1345
    • Chavin, S.I.1    Franklin, E.C.2
  • 11
    • 0027374633 scopus 로고
    • Hemostatic molecular markers in nephrotic syndrome
    • Chen TY, Huang CC, Tsao CJ (1993) Hemostatic molecular markers in nephrotic syndrome. Am J Hematol 44:276
    • (1993) Am J Hematol , vol.44 , pp. 276
    • Chen, T.Y.1    Huang, C.C.2    Tsao, C.J.3
  • 12
    • 0036127167 scopus 로고    scopus 로고
    • Hydroxynonenal inactivates cathepsin B by forming Michael adducts with active site residues
    • Crabb JW, O'Neil J, Miyagi M, et al (2002) Hydroxynonenal inactivates cathepsin B by forming Michael adducts with active site residues. Protein Sci 11:831
    • (2002) Protein Sci , vol.11 , pp. 831
    • Crabb, J.W.1    O'Neil, J.2    Miyagi, M.3
  • 13
    • 0032516179 scopus 로고    scopus 로고
    • The fraud of Abderhalden's enzymes
    • Deichmann U, Muller-Hill B (1998) The fraud of Abderhalden's enzymes. Nature 393:109
    • (1998) Nature , vol.393 , pp. 109
    • Deichmann, U.1    Muller-Hill, B.2
  • 14
    • 0035902619 scopus 로고    scopus 로고
    • Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease
    • DeMattos RB, Bales KR, Cummins DJ, et al (2001) Peripheral anti-A beta antibody alters CNS and plasma A beta clearance and decreases brain A beta burden in a mouse model of Alzheimer's disease. Proc Natl Acad Sci USA 98:885
    • (2001) Proc Natl Acad Sci USA , vol.98 , pp. 885
    • DeMattos, R.B.1    Bales, K.R.2    Cummins, D.J.3
  • 15
    • 4644275963 scopus 로고    scopus 로고
    • Intravenous immunoglobulins containing antibodies against beta-amyloid for the treatment of Alzheimer's disease
    • Dodel RC, Du Y, Depboylu C, et al (2004) Intravenous immunoglobulins containing antibodies against beta-amyloid for the treatment of Alzheimer's disease. J Neurol Neurosurg Psychiatry 75:1472
    • (2004) J Neurol Neurosurg Psychiatry , vol.75 , pp. 1472
    • Dodel, R.C.1    Du, Y.2    Depboylu, C.3
  • 16
    • 0016311758 scopus 로고
    • Do immunoglobulins have proteolytic activity?
    • Erhan S, Greller LD (1974) Do immunoglobulins have proteolytic activity? Nature 251:353
    • (1974) Nature , vol.251 , pp. 353
    • Erhan, S.1    Greller, L.D.2
  • 18
    • 0028835286 scopus 로고
    • Site-directed mutagenesis of proteolytic antibody light chain
    • Gao Q-S, Sun M, Rees A, et al (1995) Site-directed mutagenesis of proteolytic antibody light chain. J Mol Biol 253:658
    • (1995) J Mol Biol , vol.253 , pp. 658
    • Gao, Q.-S.1    Sun, M.2    Rees, A.3
  • 19
    • 0027410894 scopus 로고
    • Human antibodies reactive with beta-amyloid protein in Alzheimer's disease
    • Gaskin F, Finley J, Fang Q, et al (1993) Human antibodies reactive with beta-amyloid protein in Alzheimer's disease. J Exp Med 177:1181
    • (1993) J Exp Med , vol.177 , pp. 1181
    • Gaskin, F.1    Finley, J.2    Fang, Q.3
  • 21
    • 0028856065 scopus 로고
    • Mapping the Ig superantigen-binding site of HIV-1 gp120
    • Goodglick L, Zevit N, Neshat MS, et al (1995) Mapping the Ig superantigen-binding site of HIV-1 gp120. J Immunol 155:5151
    • (1995) J Immunol , vol.155 , pp. 5151
    • Goodglick, L.1    Zevit, N.2    Neshat, M.S.3
  • 22
    • 0016675949 scopus 로고
    • Hypothesis. Auto-antibodies and immunological theories: An analytical review
    • Grabar P (1975) Hypothesis. Auto-antibodies and immunological theories: an analytical review. Clin Immunol Immunopathol 4:453
    • (1975) Clin Immunol Immunopathol , vol.4 , pp. 453
    • Grabar, P.1
  • 23
    • 0035451678 scopus 로고    scopus 로고
    • A CD19-dependent signaling pathway regulates autoimmunity in lyn-deficient mice
    • Hasegawa M, Fujimoto M, Poe JC, et al (2001) A CD19-dependent signaling pathway regulates autoimmunity in lyn-deficient mice. J Immunol 167:2469
    • (2001) J Immunol , vol.167 , pp. 2469
    • Hasegawa, M.1    Fujimoto, M.2    Poe, J.C.3
  • 24
    • 0035884992 scopus 로고    scopus 로고
    • CD19 can regulate B lymphocyte signal transduction independent of complement activation
    • Hasegawa M, Fujimoto M, Poe JC, et al (2001) CD19 can regulate B lymphocyte signal transduction independent of complement activation. J Immunol 167:3190
    • (2001) J Immunol , vol.167 , pp. 3190
    • Hasegawa, M.1    Fujimoto, M.2    Poe, J.C.3
  • 25
    • 0034992393 scopus 로고    scopus 로고
    • Autoantibodies to amyloid-beta and Alzheimer's disease
    • Hyman BT, Smith C, Buldyrev I, et al (2001) Autoantibodies to amyloid-beta and Alzheimer's disease. Ann Neurol 49:808
    • (2001) Ann Neurol , vol.49 , pp. 808
    • Hyman, B.T.1    Smith, C.2    Buldyrev, I.3
  • 26
    • 0034604269 scopus 로고    scopus 로고
    • Identification of catalytic nucleophile of Escherichia coli gamma-glutamyltranspeptidase by gamma-monofluorophosphono derivative of glutamic acid: N-terminal thr-391 in small subunit is the nucleophile
    • Inoue M, Hiratake J, Suzuki H, et al (2000) Identification of catalytic nucleophile of Escherichia coli gamma-glutamyltranspeptidase by gamma-monofluorophosphono derivative of glutamic acid: N-terminal thr-391 in small subunit is the nucleophile. Biochemistry 39:7764
    • (2000) Biochemistry , vol.39 , pp. 7764
    • Inoue, M.1    Hiratake, J.2    Suzuki, H.3
  • 27
    • 0031866839 scopus 로고    scopus 로고
    • Alpha-1 antitrypsin up-regulates human B cell differentiation selectively into IgE- And IgG4- secreting cells
    • Jeannin P, Lecoanet-Henchoz S, Delneste Y, et al (1998) Alpha-1 antitrypsin up-regulates human B cell differentiation selectively into IgE- and IgG4- secreting cells. Eur J Immunol 28:1815
    • (1998) Eur J Immunol , vol.28 , pp. 1815
    • Jeannin, P.1    Lecoanet-Henchoz, S.2    Delneste, Y.3
  • 28
    • 0034636122 scopus 로고    scopus 로고
    • Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: Characterization of the functional residues in Chromatium vinosum PHB synthase
    • Jia Y, Kappock TJ, Frick T, et al (2000) Lipases provide a new mechanistic model for polyhydroxybutyrate (PHB) synthases: characterization of the functional residues in Chromatium vinosum PHB synthase. Biochemistry 39:3927
    • (2000) Biochemistry , vol.39 , pp. 3927
    • Jia, Y.1    Kappock, T.J.2    Frick, T.3
  • 29
    • 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, et al (1995) Unexpected presence of polyreactive catalytic antibodies in IgG from unimmunized donors and decreased levels in rheumatoid arthritis. J Immunol 155:2695
    • (1995) J Immunol , vol.155 , pp. 2695
    • Kalaga, R.1    Li, L.2    O'Dell, J.3
  • 30
    • 0031019818 scopus 로고    scopus 로고
    • Identification of the B cell superantigen-binding site of HIV-1 gp120
    • Karray S, Zouali M (1997) Identification of the B cell superantigen-binding site of HIV-1 gp120. Proc Natl Acad Sci USA 94:1356
    • (1997) Proc Natl Acad Sci USA , vol.94 , pp. 1356
    • Karray, S.1    Zouali, M.2
  • 31
    • 0033529303 scopus 로고    scopus 로고
    • Chemokines and activated macrophages in HIV gp120-induced neuronal apoptosis
    • Kaul M, Lipton SA (1999) Chemokines and activated macrophages in HIV gp120-induced neuronal apoptosis. Proc Natl Acad Sci USA 96:8212
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 8212
    • Kaul, M.1    Lipton, S.A.2
  • 32
    • 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, Linder 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
    • (1980) FEBS Lett , vol.111 , pp. 427
    • Kohen, F.1    Kim, J.B.2    Linder, H.R.3
  • 33
    • 0019413907 scopus 로고
    • Time-dependent inhibition of tuberculin-induced lymphocyte DNA synthesis by a serine protease inhibitor
    • Ku GS, Quigley JP, Sultzer BM (1981) Time-dependent inhibition of tuberculin-induced lymphocyte DNA synthesis by a serine protease inhibitor. J Immunol 126:2209
    • (1981) J Immunol , vol.126 , pp. 2209
    • Ku, G.S.1    Quigley, J.P.2    Sultzer, B.M.3
  • 34
    • 0021028627 scopus 로고
    • The inhibition of the mitogenic stimulation of B lymphocytes by a serine protease inhibitor: Commitment to proliferation correlates with an enhanced expression of a cell-associated arginine-specific serine enzyme
    • Ku GS, Quigley JP, Sultzer BM (1983) The inhibition of the mitogenic stimulation of B lymphocytes by a serine protease inhibitor: commitment to proliferation correlates with an enhanced expression of a cell-associated arginine-specific serine enzyme. J Immunol 131:2494
    • (1983) J Immunol , vol.131 , pp. 2494
    • Ku, G.S.1    Quigley, J.P.2    Sultzer, B.M.3
  • 35
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong PD, Wyatt R, Robinson J, et al (1998) Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393:648
    • (1998) Nature , vol.393 , pp. 648
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3
  • 36
    • 20244363765 scopus 로고    scopus 로고
    • Catalytic activity of antibodies against factor VIII in patients with hemophilia A
    • Lacroix-Desmazes S, Moreau A, Sooryanarayana, et al (1999) Catalytic activity of antibodies against factor VIII in patients with hemophilia A. Nat Med 5:1044
    • (1999) Nat Med , vol.5 , pp. 1044
    • Lacroix-Desmazes, S.1    Moreau, A.2    Sooryanarayana3
  • 37
    • 0035951380 scopus 로고    scopus 로고
    • A suicide-substrate mechanism for hydrolysis of beta-lactams by an anti-idiotypic catalytic antibody
    • Lefevre S, Debat H, Thomas D, et al (2001) A suicide-substrate mechanism for hydrolysis of beta-lactams by an anti-idiotypic catalytic antibody. FEBS Lett 489:25
    • (2001) FEBS Lett , vol.489 , pp. 25
    • Lefevre, S.1    Debat, H.2    Thomas, D.3
  • 38
    • 0028926783 scopus 로고
    • Catalytic activity of anti-thyroglobulin antibodies
    • Li L, Kaveri S, Tyutyulkova S, et al (1995) Catalytic activity of anti-thyroglobulin antibodies. J Immunol 154:3328
    • (1995) J Immunol , vol.154 , pp. 3328
    • Li, L.1    Kaveri, S.2    Tyutyulkova, S.3
  • 39
    • 3543054598 scopus 로고    scopus 로고
    • Proteolytic antibody light chains alter beta-amyloid aggregation and prevent cytotoxicity
    • Liu R, McAllister C, Lyubchenko Y, et al (2004) Proteolytic antibody light chains alter beta-amyloid aggregation and prevent cytotoxicity. Biochemistry 43:9999
    • (2004) Biochemistry , vol.43 , pp. 9999
    • Liu, R.1    McAllister, C.2    Lyubchenko, Y.3
  • 40
    • 0033952776 scopus 로고    scopus 로고
    • Association between IgM response to IgG damaged by glyoxidation and disease activity in rheumatoid arthritis
    • Lucey MD, Newkirk MM, Neville C, et al (2000) Association between IgM response to IgG damaged by glyoxidation and disease activity in rheumatoid arthritis. J Rheumatol 27:319
    • (2000) J Rheumatol , vol.27 , pp. 319
    • Lucey, M.D.1    Newkirk, M.M.2    Neville, C.3
  • 41
    • 0037110640 scopus 로고    scopus 로고
    • Modeling Alzheimer's disease immune therapy mechanisms: Interactions of human postmortem microglia with antibody-opsonized amyloid beta peptide
    • Lue LF, Walker DG (2002) Modeling Alzheimer's disease immune therapy mechanisms: interactions of human postmortem microglia with antibody-opsonized amyloid beta peptide. J Neurosci Res 70:599
    • (2002) J Neurosci Res , vol.70 , pp. 599
    • Lue, L.F.1    Walker, D.G.2
  • 42
    • 0029834403 scopus 로고    scopus 로고
    • Catalytic cleavage of vasopressin by human Bence Jones proteins at the arginylglycinamide bond
    • Matsuura K, Sinohara H (1996) Catalytic cleavage of vasopressin by human Bence Jones proteins at the arginylglycinamide bond. Biol Chem 377:587
    • (1996) Biol Chem , vol.377 , pp. 587
    • Matsuura, K.1    Sinohara, H.2
  • 44
    • 1842578276 scopus 로고    scopus 로고
    • Catalytic antibody light chain capable of cleaving a chemokine receptor CCR-5 peptide with a high reaction rate constant
    • Mitsuda Y, Hifumi E, Tsuruhata K, et al (2004) Catalytic antibody light chain capable of cleaving a chemokine receptor CCR-5 peptide with a high reaction rate constant. Biotechnol Bioeng 86:217
    • (2004) Biotechnol Bioeng , vol.86 , pp. 217
    • Mitsuda, Y.1    Hifumi, E.2    Tsuruhata, K.3
  • 45
    • 0024448004 scopus 로고
    • Differential sensitivity of anti-IgM-induced and NaF-induced inositol phospholipid metabolism to serine protease inhibitors in BAL17 B lymphoma cells
    • Mizuguchi J, Utsunomiya N, Nakanishi M, et al (1989) Differential sensitivity of anti-IgM-induced and NaF-induced inositol phospholipid metabolism to serine protease inhibitors in BAL17 B lymphoma cells. Biochem J 263:641
    • (1989) Biochem J , vol.263 , pp. 641
    • Mizuguchi, J.1    Utsunomiya, N.2    Nakanishi, M.3
  • 46
    • 0028275340 scopus 로고
    • Isotype choice for chimeric antibodies affects binding properties
    • Morelock MM, Rothlein R, Bright SM, et al (1994) Isotype choice for chimeric antibodies affects binding properties. J Biol Chem 269:13048
    • (1994) J Biol Chem , vol.269 , pp. 13048
    • Morelock, M.M.1    Rothlein, R.2    Bright, S.M.3
  • 47
    • 0037610172 scopus 로고    scopus 로고
    • Autoantibodies to amyloid beta-peptide (Abeta) are increased in Alzheimer's disease patients and Abeta antibodies can enhance Abeta neurotoxicity: Implications for disease pathogenesis and vaccine development
    • Nath A, Hall E, Tuzova M, et al (2003) Autoantibodies to amyloid beta-peptide (Abeta) are increased in Alzheimer's disease patients and Abeta antibodies can enhance Abeta neurotoxicity: implications for disease pathogenesis and vaccine development. Neuromolecular Med 3:29
    • (2003) Neuromolecular Med , vol.3 , pp. 29
    • Nath, A.1    Hall, E.2    Tuzova, M.3
  • 48
    • 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
    • (2003) J Cell Mol Med , vol.7 , pp. 265
    • Nevinsky, G.A.1    Buneva, V.N.2
  • 49
    • 0032444337 scopus 로고    scopus 로고
    • Secretory immunoglobulin a from human milk catalyzes milk protein phosphorylation
    • Nevinsky GA, Kit YYa, Semenov DV, et al (1998) Secretory immunoglobulin A from human milk catalyzes milk protein phosphorylation. Appl Biochem Biotechnol 75:77
    • (1998) Appl Biochem Biotechnol , vol.75 , pp. 77
    • Nevinsky, G.A.1    Kit, Y.Ya.2    Semenov, D.V.3
  • 50
    • 1542379780 scopus 로고    scopus 로고
    • Towards selective covalent inactivation of pathogenic antibodies: A phosphonate diester analog of vasoactive intestinal peptide that inactivates catalytic autoantibodies
    • Nishiyama Y, Bhatia G, Bangale Y, et al (2004) Towards selective covalent inactivation of pathogenic antibodies: a phosphonate diester analog of vasoactive intestinal peptide that inactivates catalytic autoantibodies. J Biol Chem 279:7877
    • (2004) J Biol Chem , vol.279 , pp. 7877
    • Nishiyama, Y.1    Bhatia, G.2    Bangale, Y.3
  • 51
    • 0033583479 scopus 로고    scopus 로고
    • Deficiency in CD22, a B cell-specific inhibitory receptor, is sufficient to predispose to development of high affinity autoantibodies
    • O'Keefe TL, Williams GT, Batista FD, et al (1999) Deficiency in CD22, a B cell-specific inhibitory receptor, is sufficient to predispose to development of high affinity autoantibodies. J Exp Med 189:1307
    • (1999) J Exp Med , vol.189 , pp. 1307
    • O'Keefe, T.L.1    Williams, G.T.2    Batista, F.D.3
  • 52
    • 0028672813 scopus 로고
    • Amino acid and peptide phosphonate derivatives as specific inhibitors of serine peptidases
    • Oleksyszyn J, Powers JC (1994) Amino acid and peptide phosphonate derivatives as specific inhibitors of serine peptidases. Methods Enzymol 244:423
    • (1994) Methods Enzymol , vol.244 , pp. 423
    • Oleksyszyn, J.1    Powers, J.C.2
  • 53
    • 0025253819 scopus 로고
    • Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding
    • Olshevsky U, Helseth E, Furman C, et al (1990) Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding. J Virol 64:5701
    • (1990) J Virol , vol.64 , pp. 5701
    • Olshevsky, U.1    Helseth, E.2    Furman, C.3
  • 54
    • 0030157640 scopus 로고    scopus 로고
    • Natural catalytic antibodies
    • Paul S (1996) Natural catalytic antibodies. Mol Biotechnol 5:197
    • (1996) Mol Biotechnol , vol.5 , pp. 197
    • Paul, S.1
  • 55
    • 4544312378 scopus 로고    scopus 로고
    • Naturally occurring proteolytic antibodies: Selective IgM-catalyzed hydrolysis of HIV gp120
    • Paul S, Karle S, Planque S, et al (2004) Naturally occurring proteolytic antibodies: selective IgM-catalyzed hydrolysis of HIV gp120. J Biol Chem 279:39611
    • (2004) J Biol Chem , vol.279 , pp. 39611
    • Paul, S.1    Karle, S.2    Planque, S.3
  • 57
    • 0038482146 scopus 로고    scopus 로고
    • Specific HIV gp120 cleaving antibodies induced by covalently reactive analog of gp120
    • Paul S, Planque S, Zhou Y-X, et al (2003) Specific HIV gp120 cleaving antibodies induced by covalently reactive analog of gp120. J Biol Chem 278:20429
    • (2003) J Biol Chem , vol.278 , pp. 20429
    • Paul, S.1    Planque, S.2    Zhou, Y.-X.3
  • 58
    • 0035958974 scopus 로고    scopus 로고
    • Phosphonate ester probes for proteolytic antibodies
    • Paul S, Tramontano A, Gololobov G, et al (2001) Phosphonate ester probes for proteolytic antibodies. J Biol Chem 276:28314
    • (2001) J Biol Chem , vol.276 , pp. 28314
    • Paul, S.1    Tramontano, A.2    Gololobov, G.3
  • 59
    • 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
    • (1989) Science , vol.244 , pp. 1158
    • Paul, S.1    Volle, D.J.2    Beach, C.M.3
  • 60
    • 11144356308 scopus 로고    scopus 로고
    • Ontogeny of proteolytic immunity: IgM serine proteases
    • Planque S, Bangale Y, Song X-T, et al (2004) Ontogeny of proteolytic immunity: IgM serine proteases. J Biol Chem 279:14024
    • (2004) J Biol Chem , vol.279 , pp. 14024
    • Planque, S.1    Bangale, Y.2    Song, X.-T.3
  • 61
    • 0037805717 scopus 로고    scopus 로고
    • Broadly distributed chemical reactivity of natural antibodies expressed in coordination with specific antigen binding activity
    • Planque S, Taguchi H, Burr G, et al (2003) Broadly distributed chemical reactivity of natural antibodies expressed in coordination with specific antigen binding activity. J Biol Chem 278:20436
    • (2003) J Biol Chem , vol.278 , pp. 20436
    • Planque, S.1    Taguchi, H.2    Burr, G.3
  • 62
    • 0026322614 scopus 로고
    • CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion
    • Pollard S, Meier W, Chow P, et al (1991) CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion. Proc Natl Acad Sci USA 88:11320
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11320
    • Pollard, S.1    Meier, W.2    Chow, P.3
  • 63
    • 0345060484 scopus 로고    scopus 로고
    • Degradation of β-amyloid by proteolytic antibody light chains
    • Rangan SK, Liu R, Brune D, et al (2003) Degradation of β-amyloid by proteolytic antibody light chains. Biochemistry 42:14328
    • (2003) Biochemistry , vol.42 , pp. 14328
    • Rangan, S.K.1    Liu, R.2    Brune, D.3
  • 64
    • 0025894099 scopus 로고
    • Irreversible inhibition of a monoclonal antibody by a nitrophenyl ester
    • Rao G, Philipp M (1991) Irreversible inhibition of a monoclonal antibody by a nitrophenyl ester. J Protein Chem 10:117
    • (1991) J Protein Chem , vol.10 , pp. 117
    • Rao, G.1    Philipp, M.2
  • 65
    • 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
    • (1975) Biochemistry , vol.14 , pp. 591
    • Raso, V.1    Stollar, B.D.2
  • 66
    • 0031986075 scopus 로고    scopus 로고
    • Characterization of highly purified, inactivated HIV-1 particles isolated by anion exchange chromatography
    • Richieri SP, Bartholomew R, Aloia RC, et al (1998) Characterization of highly purified, inactivated HIV-1 particles isolated by anion exchange chromatography. Vaccine 16:119
    • (1998) Vaccine , vol.16 , pp. 119
    • Richieri, S.P.1    Bartholomew, R.2    Aloia, R.C.3
  • 67
    • 0037403303 scopus 로고    scopus 로고
    • Amylolytic activity of IgM and IgG antibodies from patients with multiple sclerosis
    • Saveliev AN, Ivanen DR, Kulminskaya AA, et al (2003) Amylolytic activity of IgM and IgG antibodies from patients with multiple sclerosis. Immunol Lett 86:291
    • (2003) Immunol Lett , vol.86 , pp. 291
    • Saveliev, A.N.1    Ivanen, D.R.2    Kulminskaya, A.A.3
  • 69
    • 3242694207 scopus 로고    scopus 로고
    • An attenuated immune response is sufficient to enhance cognition in an Alzheimer's disease mouse model immunized with amyloid-beta derivatives
    • Sigurdsson EM, Knudsen E, Asuni A, et al (2004) An attenuated immune response is sufficient to enhance cognition in an Alzheimer's disease mouse model immunized with amyloid-beta derivatives. J Neurosci 24:6277
    • (2004) J Neurosci , vol.24 , pp. 6277
    • Sigurdsson, E.M.1    Knudsen, E.2    Asuni, A.3
  • 70
    • 0029655470 scopus 로고    scopus 로고
    • The role of CD4 in HIV envelope-mediated pathogenesis
    • Siliciano RF (1996) The role of CD4 in HIV envelope-mediated pathogenesis. Curr Top Microbiol Immunol 205:159
    • (1996) Curr Top Microbiol Immunol , vol.205 , pp. 159
    • Siliciano, R.F.1
  • 71
    • 0031583480 scopus 로고    scopus 로고
    • Cleavage specificity of a proteolytic antibody light chain and effects of the heavy chain variable domain
    • Sun M, Gao QS, Kirnarskiy L, et al (1997) Cleavage specificity of a proteolytic antibody light chain and effects of the heavy chain variable domain. J Mol Biol 271:374
    • (1997) J Mol Biol , vol.271 , pp. 374
    • Sun, M.1    Gao, Q.S.2    Kirnarskiy, L.3
  • 72
    • 0037020724 scopus 로고    scopus 로고
    • A mechanism-based probe for gp120-hydrolyzing antibodies
    • Taguchi H, Burr G, Karle S, et al (2002) A mechanism-based probe for gp120-hydrolyzing antibodies. Bioorg Med Chem Lett 12:3167
    • (2002) Bioorg Med Chem Lett , vol.12 , pp. 3167
    • Taguchi, H.1    Burr, G.2    Karle, S.3
  • 75
    • 0029911107 scopus 로고    scopus 로고
    • Human immunodeficiency virus-1 (HIV-1) gp120 superantigen-binding serum antibodies. A host factor in homosexual HIV-1 transmission
    • Townsley-Fuchs J, Kam L, Fairhurst R, et al (1996) Human immunodeficiency virus-1 (HIV-1) gp120 superantigen-binding serum antibodies. A host factor in homosexual HIV-1 transmission. J Clin Invest 98:1794
    • (1996) J Clin Invest , vol.98 , pp. 1794
    • Townsley-Fuchs, J.1    Kam, L.2    Fairhurst, R.3
  • 76
    • 0033816810 scopus 로고    scopus 로고
    • Proteolytic antibodies: Origins, selection and induction
    • Paul S (ed) Karger, Basel
    • Tramontano A, Gololobov G, Paul S (2000) Proteolytic antibodies: origins, selection and induction. In: Paul S (ed) Chemical Immunology: catalytic antibodies, vol 77. Karger, Basel, pp 1-17
    • (2000) Chemical Immunology: Catalytic Antibodies , vol.77 , pp. 1-17
    • Tramontano, A.1    Gololobov, G.2    Paul, S.3
  • 78
    • 0030598850 scopus 로고    scopus 로고
    • Efficient vasoactive intestinal polypeptide hydrolyzing antibody light chains selected from an asthma patient by phage display
    • Tyutyulkova S, Gao Q-S, Thompson A, et al (1996) Efficient vasoactive intestinal polypeptide hydrolyzing antibody light chains selected from an asthma patient by phage display. Biochim Biophys Acta 1316:217
    • (1996) Biochim Biophys Acta , vol.1316 , pp. 217
    • Tyutyulkova, S.1    Gao, Q.-S.2    Thompson, A.3
  • 79
    • 0025863517 scopus 로고
    • Affinity of monoclonal antibodies. Interpretation of the positive cooperative nature of anti-hCG/hCG interactions
    • Van Erp R, Gribnau TC, Sommeren AP van, et al (1991) Affinity of monoclonal antibodies. Interpretation of the positive cooperative nature of anti-hCG/hCG interactions. J Immunol Methods 140:235
    • (1991) J Immunol Methods , vol.140 , pp. 235
    • Van Erp, R.1    Gribnau, T.C.2    Van Sommeren, A.P.3
  • 80
    • 0035939953 scopus 로고    scopus 로고
    • Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate
    • Vocadlo DJ, Davies GJ, Laine R, et al (2001) Catalysis by hen egg-white lysozyme proceeds via a covalent intermediate. Nature 412:835
    • (2001) Nature , vol.412 , pp. 835
    • Vocadlo, D.J.1    Davies, G.J.2    Laine, R.3
  • 81
    • 0029590066 scopus 로고
    • Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes
    • Wagner J, Lerner RA, Barbas CF 3rd (1995) Efficient aldolase catalytic antibodies that use the enamine mechanism of natural enzymes. Science 270:1797
    • (1995) Science , vol.270 , pp. 1797
    • Wagner, J.1    Lerner, R.A.2    Barbas III, C.F.3
  • 82
    • 0020806688 scopus 로고
    • The X-ray crystal structure analysis of the refined complex formed by bovine trypsin and p-amidinophenylpyruvate at 1.4 A resolution
    • Walter J, Bode W (1983) The X-ray crystal structure analysis of the refined complex formed by bovine trypsin and p-amidinophenylpyruvate at 1.4 A resolution. Hoppe-Seyler's Z Physiol Chem 364:S949
    • (1983) Hoppe-Seyler's Z Physiol Chem , vol.364
    • Walter, J.1    Bode, W.2
  • 83
    • 0242318374 scopus 로고    scopus 로고
    • Mutagenesis of the conserved active-site tyrosine changes a retaining sialidase into an inverting sialidase
    • Watson JN, Dookhun V, Borgford TJ, et al (2003) Mutagenesis of the conserved active-site tyrosine changes a retaining sialidase into an inverting sialidase. Biochemistry 42:12682
    • (2003) Biochemistry , vol.42 , pp. 12682
    • Watson, J.N.1    Dookhun, V.2    Borgford, T.J.3
  • 84
    • 0036085702 scopus 로고    scopus 로고
    • Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals
    • Weksler ME, Relkin N, Turkenich R, et al (2002) Patients with Alzheimer disease have lower levels of serum anti-amyloid peptide antibodies than healthy elderly individuals. Exp Gerontol 37:943
    • (2002) Exp Gerontol , vol.37 , pp. 943
    • Weksler, M.E.1    Relkin, N.2    Turkenich, R.3
  • 85
    • 0035823071 scopus 로고    scopus 로고
    • Antibody catalysis of the oxidation of water
    • Wentworth P, Jones LH, Wentworth AD, et al (2001) Antibody catalysis of the oxidation of water. Science 293:1806
    • (2001) Science , vol.293 , pp. 1806
    • Wentworth, P.1    Jones, L.H.2    Wentworth, A.D.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.