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Volumn 44, Issue 10, 2007, Pages 2707-2718

Antibodies to the superantigenic site of HIV-1 gp120: Hydrolytic and binding activities of the light chain subunit

Author keywords

B cell superantigen; Catalytic antibody light chain; HIV gp120; Lupus; Phage library

Indexed keywords

ANTIBODY; DRUG RESIDUE; GLYCOPROTEIN GP 120; PEPTIDE; PROTEIN;

EID: 33846903835     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2006.12.005     Document Type: Article
Times cited : (27)

References (67)
  • 1
    • 0025835081 scopus 로고
    • A VH clonal deficit in human immunodeficiency virus-positive individuals reflects a B-cell maturational arrest
    • Berberian L., Valles-Ayoub Y., Sun N., Martinez-Maza O., and Braun J. A VH clonal deficit in human immunodeficiency virus-positive individuals reflects a B-cell maturational arrest. Blood 78 (1991) 175-179
    • (1991) Blood , vol.78 , pp. 175-179
    • Berberian, L.1    Valles-Ayoub, Y.2    Sun, N.3    Martinez-Maza, O.4    Braun, J.5
  • 2
    • 0027340737 scopus 로고
    • Immunoglobulin VH3 gene products: natural ligands for HIV gp120
    • Berberian L., Goodglick L., Kipps T.J., and Braun J. Immunoglobulin VH3 gene products: natural ligands for HIV gp120. Science 261 (1993) 1588-1591
    • (1993) Science , vol.261 , pp. 1588-1591
    • Berberian, L.1    Goodglick, L.2    Kipps, T.J.3    Braun, J.4
  • 3
    • 0036311444 scopus 로고    scopus 로고
    • New evidence for transmitter role of VIP in the airways: impaired relaxation by a catalytic antibody
    • Berisha H.I., Bratut M., Bangale Y., Colasurdo G., Paul S., and Said S.I. New evidence for transmitter role of VIP in the airways: impaired relaxation by a catalytic antibody. Pulm. Pharmacol. Ther. 15 (2002) 121-127
    • (2002) Pulm. Pharmacol. Ther. , vol.15 , pp. 121-127
    • Berisha, H.I.1    Bratut, M.2    Bangale, Y.3    Colasurdo, G.4    Paul, S.5    Said, S.I.6
  • 4
    • 0028171426 scopus 로고
    • Binding of glycoprotein 120 and peptides from the HIV-1 envelope by autoantibodies in mice with experimentally induced systemic lupus erythematosus and in patients with the disease
    • Bermas B.L., Petri M., Berzofsky J.A., Waisman A., Shearer G.M., and Mozes E. Binding of glycoprotein 120 and peptides from the HIV-1 envelope by autoantibodies in mice with experimentally induced systemic lupus erythematosus and in patients with the disease. AIDS Res. Hum. Retroviruses 10 (1994) 1071-1077
    • (1994) AIDS Res. Hum. Retroviruses , vol.10 , pp. 1071-1077
    • Bermas, B.L.1    Petri, M.2    Berzofsky, J.A.3    Waisman, A.4    Shearer, G.M.5    Mozes, E.6
  • 6
    • 17144456021 scopus 로고    scopus 로고
    • The antibody response in HIV-1 infection
    • Burton D.R., and Montefiori D.C. The antibody response in HIV-1 infection. AIDS 11 Suppl. A (1997) S87-S898
    • (1997) AIDS , vol.11 , Issue.SUPPL. A
    • Burton, D.R.1    Montefiori, D.C.2
  • 7
    • 0034968017 scopus 로고    scopus 로고
    • Lupus-specific autoantibodies in concomitant human immunodeficiency virus and systemic lupus erythematosus: case report and literature review
    • Daikh B.E., and Holyst M.M. Lupus-specific autoantibodies in concomitant human immunodeficiency virus and systemic lupus erythematosus: case report and literature review. Semin. Arthritis Rheum. 30 (2001) 418-425
    • (2001) Semin. Arthritis Rheum. , vol.30 , pp. 418-425
    • Daikh, B.E.1    Holyst, M.M.2
  • 8
    • 0033811260 scopus 로고    scopus 로고
    • Catalyst design for reactions with multiple transition states
    • DeSilva B.S., Wilson G.S., and Schowen R.L. Catalyst design for reactions with multiple transition states. Chem. Immunol. 77 (2000) 33-57
    • (2000) Chem. Immunol. , vol.77 , pp. 33-57
    • DeSilva, B.S.1    Wilson, G.S.2    Schowen, R.L.3
  • 9
    • 0040680982 scopus 로고
    • Reconstitution of immunologic activity by interaction of polypeptide chains of antibodies
    • Edelman G.M., Olins D.E., Gally J.A., and Zinder N.D. Reconstitution of immunologic activity by interaction of polypeptide chains of antibodies. Proc. Natl. Acad. Sci. U.S.A. 50 (1963) 753-761
    • (1963) Proc. Natl. Acad. Sci. U.S.A. , vol.50 , pp. 753-761
    • Edelman, G.M.1    Olins, D.E.2    Gally, J.A.3    Zinder, N.D.4
  • 10
    • 0024791087 scopus 로고
    • Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms
    • Ely K.R., Herron J.N., Harker M., and Edmundson A.B. Three-dimensional structure of a light chain dimer crystallized in water. Conformational flexibility of a molecule in two crystal forms. J. Mol. Biol. 210 (1989) 601-615
    • (1989) J. Mol. Biol. , vol.210 , pp. 601-615
    • Ely, K.R.1    Herron, J.N.2    Harker, M.3    Edmundson, A.B.4
  • 11
    • 0015932715 scopus 로고
    • Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin
    • Fastrez J., and Fersht A.R. Demonstration of the acyl-enzyme mechanism for the hydrolysis of peptides and anilides by chymotrypsin. Biochemistry 12 (1973) 2025-2034
    • (1973) Biochemistry , vol.12 , pp. 2025-2034
    • Fastrez, J.1    Fersht, A.R.2
  • 12
    • 0028835286 scopus 로고
    • Site-directed mutagenesis of proteolytic antibody light chain
    • Gao Q.S., Sun M., Rees A.R., and Paul S. Site-directed mutagenesis of proteolytic antibody light chain. J. Mol. Biol. 253 (1995) 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
  • 13
    • 0028856065 scopus 로고
    • Mapping the Ig superantigen-binding site of HIV-1 gp120
    • Goodglick L., Zevit N., Neshat M.S., and Braun J. Mapping the Ig superantigen-binding site of HIV-1 gp120. J. Immunol. 155 (1995) 5151-5159
    • (1995) J. Immunol. , vol.155 , pp. 5151-5159
    • Goodglick, L.1    Zevit, N.2    Neshat, M.S.3    Braun, J.4
  • 14
    • 0038558241 scopus 로고    scopus 로고
    • Death by a B cell superantigen: In vivo VH-targeted apoptotic supraclonal B cell deletion by a staphylococcal toxin
    • Goodyear C.S., and Silverman G.J. Death by a B cell superantigen: In vivo VH-targeted apoptotic supraclonal B cell deletion by a staphylococcal toxin. J. Exp. Med. 197 (2003) 1125-1139
    • (2003) J. Exp. Med. , vol.197 , pp. 1125-1139
    • Goodyear, C.S.1    Silverman, G.J.2
  • 15
    • 3843064392 scopus 로고    scopus 로고
    • Staphylococcal toxin induced preferential and prolonged in vivo deletion of innate-like B lymphocytes
    • Goodyear C.S., and Silverman G.J. Staphylococcal toxin induced preferential and prolonged in vivo deletion of innate-like B lymphocytes. Proc. Natl. Acad. Sci. U.S.A. 101 (2004) 11392-11397
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 11392-11397
    • Goodyear, C.S.1    Silverman, G.J.2
  • 16
    • 1342345908 scopus 로고    scopus 로고
    • In vivo VL-targeted activation-induced apoptotic supraclonal deletion by a microbial B cell toxin
    • Goodyear C.S., Narita M., and Silverman G.J. In vivo VL-targeted activation-induced apoptotic supraclonal deletion by a microbial B cell toxin. J. Immunol. 172 (2004) 2870-2877
    • (2004) J. Immunol. , vol.172 , pp. 2870-2877
    • Goodyear, C.S.1    Narita, M.2    Silverman, G.J.3
  • 17
    • 0027311936 scopus 로고
    • Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120
    • Gorny M.K., Xu J.Y., Karwowska S., Buchbinder A., and Zolla-Pazner S. Repertoire of neutralizing human monoclonal antibodies specific for the V3 domain of HIV-1 gp120. J. Immunol. 150 (1993) 635-643
    • (1993) J. Immunol. , vol.150 , pp. 635-643
    • Gorny, M.K.1    Xu, J.Y.2    Karwowska, S.3    Buchbinder, A.4    Zolla-Pazner, S.5
  • 18
    • 0034625113 scopus 로고    scopus 로고
    • Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity
    • Graille M., Stura E.A., Corper A.L., Sutton B.J., Taussig M.J., Charbonnier J.B., and Silverman G.J. Crystal structure of a Staphylococcus aureus protein A domain complexed with the Fab fragment of a human IgM antibody: structural basis for recognition of B-cell receptors and superantigen activity. Proc. Natl. Acad. Sci. U.S.A. 97 (2000) 5399-5404
    • (2000) Proc. Natl. Acad. Sci. U.S.A. , vol.97 , pp. 5399-5404
    • Graille, M.1    Stura, E.A.2    Corper, A.L.3    Sutton, B.J.4    Taussig, M.J.5    Charbonnier, J.B.6    Silverman, G.J.7
  • 19
    • 0016197604 scopus 로고
    • Amino acid difference formula to help explain protein evolution
    • Grantham R. Amino acid difference formula to help explain protein evolution. Science 185 (1974) 862-864
    • (1974) Science , vol.185 , pp. 862-864
    • Grantham, R.1
  • 20
    • 0001330135 scopus 로고    scopus 로고
    • Humoral immunity to HIV, SIV, and SHIV
    • Haigwood N.L., and Zolla-Pazner S. Humoral immunity to HIV, SIV, and SHIV. AIDS 12 Suppl. A (1998) S121-S132
    • (1998) AIDS , vol.12 , Issue.SUPPL. A
    • Haigwood, N.L.1    Zolla-Pazner, S.2
  • 21
    • 0001599898 scopus 로고
    • The reaction of p-nitrophenyl esters with chymotrypsin and insulin
    • Hartley B.S., and Kilby B.A. The reaction of p-nitrophenyl esters with chymotrypsin and insulin. Biochem. J. 56 (1954) 288-297
    • (1954) Biochem. J. , vol.56 , pp. 288-297
    • Hartley, B.S.1    Kilby, B.A.2
  • 22
    • 24644457733 scopus 로고    scopus 로고
    • Specific degradation of H. pylori urease by a catalytic antibody light chain
    • Hifumi E., Hatiuchi K., Okuda T., Nishizono A., Okamura Y., and Uda T. Specific degradation of H. pylori urease by a catalytic antibody light chain. FEBS J. 272 (2005) 4497-4505
    • (2005) FEBS J. , vol.272 , pp. 4497-4505
    • Hifumi, E.1    Hatiuchi, K.2    Okuda, T.3    Nishizono, A.4    Okamura, Y.5    Uda, T.6
  • 24
    • 0031764292 scopus 로고    scopus 로고
    • Selective deficit in antibodies specific for the superantigen binding site of gp120 in HIV infection
    • Juompan L., Lambin P., and Zouali M. Selective deficit in antibodies specific for the superantigen binding site of gp120 in HIV infection. FASEB J. 12 (1998) 1473-1480
    • (1998) FASEB J. , vol.12 , pp. 1473-1480
    • Juompan, L.1    Lambin, P.2    Zouali, M.3
  • 25
    • 0037424141 scopus 로고    scopus 로고
    • Carrier-dependent specificity of antibodies to a conserved peptide determinant of gp120
    • Karle S., Nishiyama Y., Taguchi H., Zhou Y.X., Luo J., Planque S., Hanson C., and Paul S. Carrier-dependent specificity of antibodies to a conserved peptide determinant of gp120. Vaccine 21 (2003) 1213-1218
    • (2003) Vaccine , vol.21 , 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
  • 27
    • 0032534677 scopus 로고    scopus 로고
    • Structural basis of the gp120 superantigen-binding site on human immunoglobulins
    • Karray S., Juompan L., Maroun R.C., Isenberg D., Silverman G.J., and Zouali M. Structural basis of the gp120 superantigen-binding site on human immunoglobulins. J. Immunol. 161 (1998) 6681-6688
    • (1998) J. Immunol. , vol.161 , pp. 6681-6688
    • Karray, S.1    Juompan, L.2    Maroun, R.C.3    Isenberg, D.4    Silverman, G.J.5    Zouali, M.6
  • 28
    • 0037100671 scopus 로고    scopus 로고
    • MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform
    • Katoh K., Misawa K., Kuma K., and Miyata T. MAFFT: a novel method for rapid multiple sequence alignment based on fast Fourier transform. Nucleic Acids Res. 30 (2002) 3059-3066
    • (2002) Nucleic Acids Res. , vol.30 , pp. 3059-3066
    • Katoh, K.1    Misawa, K.2    Kuma, K.3    Miyata, T.4
  • 29
    • 13744252890 scopus 로고    scopus 로고
    • MAFFT version 5: improvement in accuracy of multiple sequence alignment
    • Katoh K., Kuma K., Toh H., and Miyata T. MAFFT version 5: improvement in accuracy of multiple sequence alignment. Nucleic Acids Res. 33 (2005) 511-518
    • (2005) Nucleic Acids Res. , vol.33 , pp. 511-518
    • Katoh, K.1    Kuma, K.2    Toh, H.3    Miyata, T.4
  • 30
    • 0032543307 scopus 로고    scopus 로고
    • Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody
    • Kwong P.D., Wyatt R., Robinson J., Sweet R.W., Sodroski J., and Hendrickson W.A. Structure of an HIV gp120 envelope glycoprotein in complex with the CD4 receptor and a neutralizing human antibody. Nature 393 (1998) 648-659
    • (1998) Nature , vol.393 , pp. 648-659
    • Kwong, P.D.1    Wyatt, R.2    Robinson, J.3    Sweet, R.W.4    Sodroski, J.5    Hendrickson, W.A.6
  • 31
    • 0030152056 scopus 로고    scopus 로고
    • Low level formation of potent catalytic IgG fragments mediated by disulfide bond instability
    • Li L., Sun M., Gao Q.S., and Paul S. Low level formation of potent catalytic IgG fragments mediated by disulfide bond instability. Mol. Immunol. 33 (1996) 593-600
    • (1996) Mol. Immunol. , vol.33 , pp. 593-600
    • Li, L.1    Sun, M.2    Gao, Q.S.3    Paul, S.4
  • 32
    • 0034075937 scopus 로고    scopus 로고
    • Proteolytic components of serum IgG preparations
    • Li L., Kalaga R., and Paul S. Proteolytic components of serum IgG preparations. Clin. Exp. Immunol. 120 (2000) 261-266
    • (2000) Clin. Exp. Immunol. , vol.120 , pp. 261-266
    • Li, L.1    Kalaga, R.2    Paul, S.3
  • 33
    • 0018117296 scopus 로고
    • Kinetics of dimerization of the Bence-Jones protein Au
    • Maeda H., Steffen E., and Engel J. Kinetics of dimerization of the Bence-Jones protein Au. Biophys. Chem. 9 (1978) 57-64
    • (1978) Biophys. Chem. , vol.9 , pp. 57-64
    • Maeda, H.1    Steffen, E.2    Engel, J.3
  • 35
    • 0026040192 scopus 로고
    • Vasoactive intestinal peptide hydrolysis by antibody light chains
    • Mei S., Mody B., Eklund S.H., and Paul S. Vasoactive intestinal peptide hydrolysis by antibody light chains. J. Biol. Chem. 266 (1991) 15571-15574
    • (1991) J. Biol. Chem. , vol.266 , pp. 15571-15574
    • Mei, S.1    Mody, B.2    Eklund, S.H.3    Paul, S.4
  • 36
    • 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., Fujinami H., Yamamoto N., and Uda T. Catalytic antibody light chain capable of cleaving a chemokine receptor CCR-5 peptide with a high reaction rate constant. Biotechnol. Bioeng. 86 (2004) 217-225
    • (2004) Biotechnol. Bioeng. , vol.86 , pp. 217-225
    • Mitsuda, Y.1    Hifumi, E.2    Tsuruhata, K.3    Fujinami, H.4    Yamamoto, N.5    Uda, T.6
  • 37
    • 10044297246 scopus 로고    scopus 로고
    • Investigation of active form of catalytic antibody light chain 41S-2-L
    • Mitsuda Y., Tsuruhata K., Hifumi E., Takagi M., and Uda T. Investigation of active form of catalytic antibody light chain 41S-2-L. Immunol. Lett. 96 (2005) 63-71
    • (2005) Immunol. Lett. , vol.96 , pp. 63-71
    • Mitsuda, Y.1    Tsuruhata, K.2    Hifumi, E.3    Takagi, M.4    Uda, T.5
  • 38
    • 0034007276 scopus 로고    scopus 로고
    • Mapping the B cell superantigen binding site for HIV-1 gp120 on a V(H)3 Ig
    • Neshat M.N., Goodglick L., Lim K., and Braun J. Mapping the B cell superantigen binding site for HIV-1 gp120 on a V(H)3 Ig. Int. Immunol. 12 (2000) 305-312
    • (2000) Int. Immunol. , vol.12 , pp. 305-312
    • Neshat, M.N.1    Goodglick, L.2    Lim, K.3    Braun, J.4
  • 39
    • 0037098449 scopus 로고    scopus 로고
    • Covalent reactivity of phosphonate monophenyl esters with serine proteinases: an overlooked feature of presumed transition state analogs
    • Nishiyama Y., Taguchi H., Luo J.Q., Zhou Y.X., Burr G., Karle S., and Paul S. Covalent reactivity of phosphonate monophenyl esters with serine proteinases: an overlooked feature of presumed transition state analogs. Arch. Biochem. Biophys. 402 (2002) 281-288
    • (2002) Arch. Biochem. Biophys. , vol.402 , 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
  • 40
    • 1542379780 scopus 로고    scopus 로고
    • Toward selective covalent inactivation of pathogenic antibodies: a phosphate diester analog of vasoactive intestinal peptide that inactivates catalytic autoantibodies
    • Nishiyama Y., Bhatia G., Bangale Y., Planque S., Mitsuda Y., Taguchi H., Karle S., and Paul S. Toward selective covalent inactivation of pathogenic antibodies: a phosphate diester analog of vasoactive intestinal peptide that inactivates catalytic autoantibodies. J. Biol. Chem. 279 (2004) 7877-7883
    • (2004) J. Biol. Chem. , vol.279 , 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
  • 41
    • 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., Li J., Haseltine W., and Sodroski J. Identification of individual human immunodeficiency virus type 1 gp120 amino acids important for CD4 receptor binding. J. Virol. 64 (1990) 5701-5707
    • (1990) J. Virol. , vol.64 , pp. 5701-5707
    • Olshevsky, U.1    Helseth, E.2    Furman, C.3    Li, J.4    Haseltine, W.5    Sodroski, J.6
  • 42
    • 0036179274 scopus 로고    scopus 로고
    • Human immunodeficiency virus infection and systemic lupus erythematosus. An unusual case and a review of the literature
    • Palacios R., Santos J., Valdivielso P., and Marquez M. Human immunodeficiency virus infection and systemic lupus erythematosus. An unusual case and a review of the literature. Lupus 11 (2002) 60-63
    • (2002) Lupus , vol.11 , pp. 60-63
    • Palacios, R.1    Santos, J.2    Valdivielso, P.3    Marquez, M.4
  • 43
    • 33646146379 scopus 로고    scopus 로고
    • GP120: target for neutralizing HIV-1 antibodies
    • Pantophlet R., and Burton D.R. GP120: target for neutralizing HIV-1 antibodies. Annu. Rev. Immunol. 24 (2006) 739-769
    • (2006) Annu. Rev. Immunol. , vol.24 , pp. 739-769
    • Pantophlet, R.1    Burton, D.R.2
  • 44
    • 0030157640 scopus 로고    scopus 로고
    • Natural catalytic antibodies
    • Paul S. Natural catalytic antibodies. Mol. Biotechnol. 5 (1996) 197-207
    • (1996) Mol. Biotechnol. , vol.5 , pp. 197-207
    • Paul, S.1
  • 45
    • 0025345903 scopus 로고
    • Site specificity of a catalytic vasoactive intestinal peptide antibody. An inhibitory vasoactive intestinal peptide subsequence distant from the scissile peptide bond
    • Paul S., Volle D.J., Powell M.J., and Massey R.J. Site specificity of a catalytic vasoactive intestinal peptide antibody. An inhibitory vasoactive intestinal peptide subsequence distant from the scissile peptide bond. J. Biol. Chem. 265 (1990) 11910-11913
    • (1990) J. Biol. Chem. , vol.265 , pp. 11910-11913
    • Paul, S.1    Volle, D.J.2    Powell, M.J.3    Massey, R.J.4
  • 46
    • 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. Natural catalytic antibodies: peptide-hydrolyzing activities of Bence Jones proteins and VL fragment. J. Biol. Chem. 270 (1995) 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
  • 51
    • 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., Bhatia G., Karle S., Zhou Y.X., Nishiyama Y., and Paul S. Broadly distributed chemical reactivity of natural antibodies expressed in coordination with specific antigen binding activity. J. Biol. Chem. 278 (2003) 20436-20443
    • (2003) J. Biol. Chem. , vol.278 , 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
  • 52
    • 0026322614 scopus 로고
    • CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion
    • Pollard S.R., Meier W., Chow P., Rosa J.J., and Wiley D.C. CD4-binding regions of human immunodeficiency virus envelope glycoprotein gp120 defined by proteolytic digestion. Proc. Natl. Acad. Sci. U.S.A. 88 (1991) 11320-11324
    • (1991) Proc. Natl. Acad. Sci. U.S.A. , vol.88 , pp. 11320-11324
    • Pollard, S.R.1    Meier, W.2    Chow, P.3    Rosa, J.J.4    Wiley, D.C.5
  • 53
    • 0036882396 scopus 로고    scopus 로고
    • Irreversible inhibitors of serine, cysteine, and threonine proteases
    • Powers J.C., Asgian J.L., Ekici O.D., and James K.E. Irreversible inhibitors of serine, cysteine, and threonine proteases. Chem. Rev. 102 (2002) 4639-4750
    • (2002) Chem. Rev. , vol.102 , pp. 4639-4750
    • Powers, J.C.1    Asgian, J.L.2    Ekici, O.D.3    James, K.E.4
  • 54
    • 0025292473 scopus 로고
    • Epitopes recognized by the neutralizing antibodies of an HIV-1-infected individual
    • Profy A.T., Salinas P.A., Eckler L.I., Dunlop N.M., Nara P.L., and Putney S.D. Epitopes recognized by the neutralizing antibodies of an HIV-1-infected individual. J. Immunol. 144 (1990) 4641-4647
    • (1990) J. Immunol. , vol.144 , pp. 4641-4647
    • Profy, A.T.1    Salinas, P.A.2    Eckler, L.I.3    Dunlop, N.M.4    Nara, P.L.5    Putney, S.D.6
  • 56
    • 33747519329 scopus 로고
    • Specific combination of H and L chains of rabbit gamma-globulins
    • Roholt O., Onoue K., and Pressman D. Specific combination of H and L chains of rabbit gamma-globulins. Proc Natl. Acad. Sci. U.S.A. 51 (1964) 173-178
    • (1964) Proc Natl. Acad. Sci. U.S.A. , vol.51 , pp. 173-178
    • Roholt, O.1    Onoue, K.2    Pressman, D.3
  • 58
    • 14244250736 scopus 로고    scopus 로고
    • Autoantibody explosion in systemic lupus erythematosus: more than 100 different antibodies found in SLE patients
    • Sherer Y., Gorstein A., Fritzler M.J., and Shoenfeld Y. Autoantibody explosion in systemic lupus erythematosus: more than 100 different antibodies found in SLE patients. Semin. Arthritis Rheum. 34 (2004) 501-537
    • (2004) Semin. Arthritis Rheum. , vol.34 , pp. 501-537
    • Sherer, Y.1    Gorstein, A.2    Fritzler, M.J.3    Shoenfeld, Y.4
  • 59
    • 0028154125 scopus 로고
    • Antigen recognition by an antibody light chain
    • Sun M., Li L., Gao Q.S., and Paul S. Antigen recognition by an antibody light chain. J. Biol. Chem. 269 (1994) 734-738
    • (1994) J. Biol. Chem. , vol.269 , pp. 734-738
    • Sun, M.1    Li, L.2    Gao, Q.S.3    Paul, S.4
  • 60
    • 0031583480 scopus 로고    scopus 로고
    • Cleavage specificity of a proteolytic antibody light chain and effects of the heavy chain variable domain
    • Sun M., Gao Q.S., Kirnarskiy L., Rees A., and Paul S. Cleavage specificity of a proteolytic antibody light chain and effects of the heavy chain variable domain. J. Mol. Biol. 271 (1997) 374-385
    • (1997) J. Mol. Biol. , vol.271 , pp. 374-385
    • Sun, M.1    Gao, Q.S.2    Kirnarskiy, L.3    Rees, A.4    Paul, S.5
  • 64
    • 0030598850 scopus 로고    scopus 로고
    • Efficient vasoactive intestinal polypeptide hydrolyzing autoantibody light chains selected by phage display
    • Tyutyulkova S., Gao Q.S., Thompson A., Rennard S., and Paul S. Efficient vasoactive intestinal polypeptide hydrolyzing autoantibody light chains selected by phage display. Biochim. Biophys. Acta 1316 (1996) 217-223
    • (1996) Biochim. Biophys. Acta , vol.1316 , pp. 217-223
    • Tyutyulkova, S.1    Gao, Q.S.2    Thompson, A.3    Rennard, S.4    Paul, S.5
  • 65
    • 0030066393 scopus 로고    scopus 로고
    • Human endogenous retroviruses: nature, occurrence, and clinical implications in human disease
    • Urnovitz H.B., and Murphy W.H. Human endogenous retroviruses: nature, occurrence, and clinical implications in human disease. Clin. Microbiol. Rev. 9 (1996) 72-99
    • (1996) Clin. Microbiol. Rev. , vol.9 , pp. 72-99
    • Urnovitz, H.B.1    Murphy, W.H.2
  • 67
    • 0017328803 scopus 로고
    • Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substrates
    • Zimmerman M., Ashe B., Yurewicz E.C., and Patel G. Sensitive assays for trypsin, elastase, and chymotrypsin using new fluorogenic substrates. Anal. Biochem. 78 (1977) 47-51
    • (1977) Anal. Biochem. , vol.78 , pp. 47-51
    • Zimmerman, M.1    Ashe, B.2    Yurewicz, E.C.3    Patel, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.