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Volumn 44, Issue 6, 2007, Pages 1178-1189

Molecular characterization of a disease associated conformational epitope on GAD65 recognised by a human monoclonal antibody b96.11

Author keywords

Antigen antibody interactions; Antigens peptides epitopes; Autoantibodies; Autoimmunity; Diabetes; GAD65; Homology modelling; Phage display; Protein protein docking; Type 1 diabetes

Indexed keywords

AMINO ACID; EPITOPE; GLUTAMATE DECARBOXYLASE 65; GLUTAMATE DECARBOXYLASE 67; HUMAN MONOCLONAL ANTIBODY; HUMAN MONOCLONAL ANTIBODY B96.11; IMMUNOGLOBULIN F(AB) FRAGMENT; PHENYLALANINE; UNCLASSIFIED DRUG;

EID: 33748790946     PISSN: 01615890     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.molimm.2006.06.025     Document Type: Article
Times cited : (16)

References (56)
  • 1
    • 0031558798 scopus 로고    scopus 로고
    • Standard conformations for the canonical structures of immunoglobulins
    • Al-Lazikani B., Lesk A.M., and Chothia C. Standard conformations for the canonical structures of immunoglobulins. J. Mol. Biol. 273 (1997) 927-948
    • (1997) J. Mol. Biol. , vol.273 , pp. 927-948
    • Al-Lazikani, B.1    Lesk, A.M.2    Chothia, C.3
  • 3
    • 0033964008 scopus 로고    scopus 로고
    • Maturation of the humoral autoimmune response to epitopes of GAD in preclinical childhood type 1 diabetes
    • Bonifacio E., Lampasona V., Bernasconi L., and Ziegler A.G. Maturation of the humoral autoimmune response to epitopes of GAD in preclinical childhood type 1 diabetes. Diabetes 49 (2000) 202-208
    • (2000) Diabetes , vol.49 , pp. 202-208
    • Bonifacio, E.1    Lampasona, V.2    Bernasconi, L.3    Ziegler, A.G.4
  • 4
    • 0038302757 scopus 로고    scopus 로고
    • Biochemical filtering of a protein-protein docking simulation identifies the structure of a complex between a recombinant antibody fragment and alpha-bungarotoxin
    • Bracci L., Pini A., Bernini A., Lelli B., Ricci C., Scarselli M., Niccolai N., and Neri P. Biochemical filtering of a protein-protein docking simulation identifies the structure of a complex between a recombinant antibody fragment and alpha-bungarotoxin. Biochem. J. 371 (2003) 423-427
    • (2003) Biochem. J. , vol.371 , pp. 423-427
    • Bracci, L.1    Pini, A.2    Bernini, A.3    Lelli, B.4    Ricci, C.5    Scarselli, M.6    Niccolai, N.7    Neri, P.8
  • 5
    • 14744273934 scopus 로고    scopus 로고
    • Structural model of human GAD65: prediction and interpretation of biochemical and immunogenic features
    • Capitani G., De Biase D., Gut H., Ahmed S., and Grutter M.G. Structural model of human GAD65: prediction and interpretation of biochemical and immunogenic features. Proteins 59 (2005) 7-14
    • (2005) Proteins , vol.59 , pp. 7-14
    • Capitani, G.1    De Biase, D.2    Gut, H.3    Ahmed, S.4    Grutter, M.G.5
  • 6
    • 0031869580 scopus 로고    scopus 로고
    • Structural characteristics of brain glutamate decarboxylase in relation to its interaction and activation
    • Chen C.H., Wu S.J., and Martin D.L. Structural characteristics of brain glutamate decarboxylase in relation to its interaction and activation. Arch. Biochem. Biophys. 349 (1998) 175-182
    • (1998) Arch. Biochem. Biophys. , vol.349 , pp. 175-182
    • Chen, C.H.1    Wu, S.J.2    Martin, D.L.3
  • 7
    • 0038185277 scopus 로고    scopus 로고
    • A novel shape complementarity scoring function for protein-protein docking
    • Chen R., and Weng Z. A novel shape complementarity scoring function for protein-protein docking. Proteins 51 (2003) 397-408
    • (2003) Proteins , vol.51 , pp. 397-408
    • Chen, R.1    Weng, Z.2
  • 8
    • 0023278330 scopus 로고
    • Canonical structures for the hypervariable regions of immunoglobulins
    • Chothia C., and Lesk A.M. Canonical structures for the hypervariable regions of immunoglobulins. J. Mol. Biol. 196 (1987) 901-917
    • (1987) J. Mol. Biol. , vol.196 , pp. 901-917
    • Chothia, C.1    Lesk, A.M.2
  • 9
    • 3242877815 scopus 로고    scopus 로고
    • ClusPro: a fully automated algorithm for protein-protein docking
    • Comeau S.R., Gatchell D.W., Vajda S., and Camacho C.J. ClusPro: a fully automated algorithm for protein-protein docking. Nucl. Acids Res. 32 (2004) 96-99
    • (2004) Nucl. Acids Res. , vol.32 , pp. 96-99
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 10
    • 0345832301 scopus 로고    scopus 로고
    • ClusPro: an automated docking and discrimination method for the prediction of protein complexes
    • Comeau S.R., Gatchell D.W., Vajda S., and Camacho C.J. ClusPro: an automated docking and discrimination method for the prediction of protein complexes. Bioinformatics 20 (2004) 45-50
    • (2004) Bioinformatics , vol.20 , pp. 45-50
    • Comeau, S.R.1    Gatchell, D.W.2    Vajda, S.3    Camacho, C.J.4
  • 11
    • 21644472422 scopus 로고    scopus 로고
    • Performance of the first protein docking server ClusPro in CAPRI rounds 3-5
    • Comeau S.R., Vajda S., and Camacho C.J. Performance of the first protein docking server ClusPro in CAPRI rounds 3-5. Proteins 60 (2005) 239-244
    • (2005) Proteins , vol.60 , pp. 239-244
    • Comeau, S.R.1    Vajda, S.2    Camacho, C.J.3
  • 12
    • 0034658591 scopus 로고    scopus 로고
    • Modelling studies on the binding of substrate and inhibitor to the active site of human sorbitol dehydrogenase
    • Darmanin C., and El-Kabbani O. Modelling studies on the binding of substrate and inhibitor to the active site of human sorbitol dehydrogenase. Bioorg. Med. Chem. Lett. 10 (2000) 1101-1104
    • (2000) Bioorg. Med. Chem. Lett. , vol.10 , pp. 1101-1104
    • Darmanin, C.1    El-Kabbani, O.2
  • 13
    • 0035904883 scopus 로고    scopus 로고
    • Modelling studies of the active site of human sorbitol dehydrogenase: an approach to structure-based inhibitor design of the enzyme
    • Darmanin C., and El-Kabbani O. Modelling studies of the active site of human sorbitol dehydrogenase: an approach to structure-based inhibitor design of the enzyme. Bioorg. Med. Chem. Lett. 11 (2001) 3133-3136
    • (2001) Bioorg. Med. Chem. Lett. , vol.11 , pp. 3133-3136
    • Darmanin, C.1    El-Kabbani, O.2
  • 14
    • 0032863205 scopus 로고    scopus 로고
    • Multiple alignment and sorting of peptides derived from phage-displayed random peptide libraries with polyclonal sera allows discrimination of relevant phagotopes
    • Davies J.M., Scealy M., Cai Y.P., Whisstock J., Mackay I.R., and Rowley M.J. Multiple alignment and sorting of peptides derived from phage-displayed random peptide libraries with polyclonal sera allows discrimination of relevant phagotopes. Mol. Immunol. 36 (1999) 659-667
    • (1999) Mol. Immunol. , vol.36 , pp. 659-667
    • Davies, J.M.1    Scealy, M.2    Cai, Y.P.3    Whisstock, J.4    Mackay, I.R.5    Rowley, M.J.6
  • 15
    • 0030028799 scopus 로고    scopus 로고
    • Glutamic acid decarboxylase autoantibodies in stiff-man syndrome and insulin-dependent diabetes mellitus exhibit similarities and differences in epitope recognition
    • Daw K., Ujihara N., Atkinson M., and Powers A.C. Glutamic acid decarboxylase autoantibodies in stiff-man syndrome and insulin-dependent diabetes mellitus exhibit similarities and differences in epitope recognition. J. Immunol. 156 (1996) 818-825
    • (1996) J. Immunol. , vol.156 , pp. 818-825
    • Daw, K.1    Ujihara, N.2    Atkinson, M.3    Powers, A.C.4
  • 16
    • 0031887368 scopus 로고    scopus 로고
    • Effects of substitutions in the binding surface of an antibody on antigen affinity
    • Dougan D.A., Malby R.L., Gruen L.C., Kortt A.A., and Hudson P.J. Effects of substitutions in the binding surface of an antibody on antigen affinity. Protein Eng. 11 (1998) 65-74
    • (1998) Protein Eng. , vol.11 , pp. 65-74
    • Dougan, D.A.1    Malby, R.L.2    Gruen, L.C.3    Kortt, A.A.4    Hudson, P.J.5
  • 17
    • 0029793724 scopus 로고    scopus 로고
    • Diagnostic sensitivity of immunodominant epitopes of glutamic acid decarboxylase (GAD65) autoantibodies in childhood IDDM
    • Falorni A., Ackefors M., Carlberg C., Daniels T., Persson B., Robertson J., and Lernmark A. Diagnostic sensitivity of immunodominant epitopes of glutamic acid decarboxylase (GAD65) autoantibodies in childhood IDDM. Diabetologia 39 (1996) 1091-1098
    • (1996) Diabetologia , vol.39 , pp. 1091-1098
    • Falorni, A.1    Ackefors, M.2    Carlberg, C.3    Daniels, T.4    Persson, B.5    Robertson, J.6    Lernmark, A.7
  • 19
    • 0040949714 scopus 로고    scopus 로고
    • Molecular and structural basis of the specificity of a neutralizing acetylcholine receptor-mimicking antibody, using combined mutational and molecular modeling analyses
    • Germain N., Merienne K., Zinn-Justin S., Boulain J.C., Ducancel F., and Menez A. Molecular and structural basis of the specificity of a neutralizing acetylcholine receptor-mimicking antibody, using combined mutational and molecular modeling analyses. J. Biol. Chem. 275 (2000) 21578-21586
    • (2000) J. Biol. Chem. , vol.275 , pp. 21578-21586
    • Germain, N.1    Merienne, K.2    Zinn-Justin, S.3    Boulain, J.C.4    Ducancel, F.5    Menez, A.6
  • 20
  • 21
    • 0036606483 scopus 로고    scopus 로고
    • Principles of docking: an overview of search algorithms and a guide to scoring functions
    • Halperin I., Ma B., Wolfson H., and Nussinov R. Principles of docking: an overview of search algorithms and a guide to scoring functions. Proteins 47 (2002) 409
    • (2002) Proteins , vol.47 , pp. 409
    • Halperin, I.1    Ma, B.2    Wolfson, H.3    Nussinov, R.4
  • 23
    • 0033555271 scopus 로고    scopus 로고
    • On the importance of being aromatic at an antibody-protein antigen interface: mutagenesis of the extracellular interferon gamma receptor and recognition by the neutralizing antibody A6
    • Hofstadter K., Stuart F., Jiang L., Vrijbloed J.W., and Robinson J.A. On the importance of being aromatic at an antibody-protein antigen interface: mutagenesis of the extracellular interferon gamma receptor and recognition by the neutralizing antibody A6. J. Mol. Biol. 285 (1999) 805-815
    • (1999) J. Mol. Biol. , vol.285 , pp. 805-815
    • Hofstadter, K.1    Stuart, F.2    Jiang, L.3    Vrijbloed, J.W.4    Robinson, J.A.5
  • 24
    • 1842559613 scopus 로고    scopus 로고
    • GAD65 antibody isotypes and epitope recognition during the prediabetic process in siblings of children with type I diabetes
    • Hoppu S., Ronkainen M.S., Kulmala P., Akerblom H.K., and Knip M. GAD65 antibody isotypes and epitope recognition during the prediabetic process in siblings of children with type I diabetes. Clin. Exp. Immunol. 136 (2004) 120-128
    • (2004) Clin. Exp. Immunol. , vol.136 , pp. 120-128
    • Hoppu, S.1    Ronkainen, M.S.2    Kulmala, P.3    Akerblom, H.K.4    Knip, M.5
  • 25
    • 0026675750 scopus 로고
    • High resolution functional analysis of antibody-antigen interactions
    • Jin L., Fendly B.M., and Wells J.A. High resolution functional analysis of antibody-antigen interactions. J. Mol. Biol. 226 (1992) 851-865
    • (1992) J. Mol. Biol. , vol.226 , pp. 851-865
    • Jin, L.1    Fendly, B.M.2    Wells, J.A.3
  • 26
    • 0028232762 scopus 로고
    • Higher autoantibody levels and recognition of a linear NH2-terminal epitope in the autoantigen GAD65, distinguish stiff-man syndrome from insulin-dependent diabetes mellitus
    • Kim J., Namchuk M., Bugawan T., Fu Q., Jaffe M., Shi Y., Aanstoot H.J., Turck C.W., Erlich H., Lennon V., and Baekkeskov S. Higher autoantibody levels and recognition of a linear NH2-terminal epitope in the autoantigen GAD65, distinguish stiff-man syndrome from insulin-dependent diabetes mellitus. J. Exp. Med. 180 (1994) 595-606
    • (1994) J. Exp. Med. , vol.180 , pp. 595-606
    • Kim, J.1    Namchuk, M.2    Bugawan, T.3    Fu, Q.4    Jaffe, M.5    Shi, Y.6    Aanstoot, H.J.7    Turck, C.W.8    Erlich, H.9    Lennon, V.10    Baekkeskov, S.11
  • 27
    • 0029683483 scopus 로고    scopus 로고
    • Glutamic acid decarboxylase-gene to antigen to disease
    • Lernmark A. Glutamic acid decarboxylase-gene to antigen to disease. J. Intern. Med. 240 (1996) 259-277
    • (1996) J. Intern. Med. , vol.240 , pp. 259-277
    • Lernmark, A.1
  • 28
    • 28444486947 scopus 로고    scopus 로고
    • Immunomodulation with human recombinant autoantigens
    • Lernmark A., and Agardh C.D. Immunomodulation with human recombinant autoantigens. Trends Immunol. 26 (2005) 608-612
    • (2005) Trends Immunol. , vol.26 , pp. 608-612
    • Lernmark, A.1    Agardh, C.D.2
  • 29
    • 0026751404 scopus 로고
    • X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase
    • McPhalen C.A., Vincent M.G., and Jansonius J.N. X-ray structure refinement and comparison of three forms of mitochondrial aspartate aminotransferase. J. Mol. Biol. 225 (1992) 495-517
    • (1992) J. Mol. Biol. , vol.225 , pp. 495-517
    • McPhalen, C.A.1    Vincent, M.G.2    Jansonius, J.N.3
  • 30
    • 0034426867 scopus 로고    scopus 로고
    • Antibody modeling: implications for engineering and design
    • Morea V., Lesk A.M., and Tramontano A. Antibody modeling: implications for engineering and design. Methods 20 (2000) 267-279
    • (2000) Methods , vol.20 , pp. 267-279
    • Morea, V.1    Lesk, A.M.2    Tramontano, A.3
  • 32
    • 0032536197 scopus 로고    scopus 로고
    • Conformations of the third hypervariable region in the VH domain of immunoglobulins
    • Morea V., Tramontano A., Rustici M., Chothia C., and Lesk A.M. Conformations of the third hypervariable region in the VH domain of immunoglobulins. J. Mol. Biol. 275 (1998) 269-294
    • (1998) J. Mol. Biol. , vol.275 , pp. 269-294
    • Morea, V.1    Tramontano, A.2    Rustici, M.3    Chothia, C.4    Lesk, A.M.5
  • 33
    • 0034292407 scopus 로고    scopus 로고
    • Conformational epitopes on the diabetes autoantigen GAD65 identified by peptide phage display and molecular modeling
    • Myers M.A., Davies J.M., Tong J.C., Whisstock J., Scealy M., Mackay I.R., and Rowley M.J. Conformational epitopes on the diabetes autoantigen GAD65 identified by peptide phage display and molecular modeling. J. Immunol. 165 (2000) 3830-3838
    • (2000) J. Immunol. , vol.165 , pp. 3830-3838
    • Myers, M.A.1    Davies, J.M.2    Tong, J.C.3    Whisstock, J.4    Scealy, M.5    Mackay, I.R.6    Rowley, M.J.7
  • 37
    • 0031863617 scopus 로고    scopus 로고
    • Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase
    • Qu K., Martin D.L., and Lawrence C.E. Motifs and structural fold of the cofactor binding site of human glutamate decarboxylase. Protein Sci. 7 (1998) 1092-1105
    • (1998) Protein Sci. , vol.7 , pp. 1092-1105
    • Qu, K.1    Martin, D.L.2    Lawrence, C.E.3
  • 39
    • 0027510420 scopus 로고
    • Autoreactive epitopes defined by diabetes-associated human monoclonal antibodies are localized in the middle and C-terminal domains of the smaller form of glutamate decarboxylase
    • Richter W., Shi Y., and Baekkeskov S. Autoreactive epitopes defined by diabetes-associated human monoclonal antibodies are localized in the middle and C-terminal domains of the smaller form of glutamate decarboxylase. Proc. Natl. Acad. Sci. U.S.A. 90 (1993) 2832-2836
    • (1993) Proc. Natl. Acad. Sci. U.S.A. , vol.90 , pp. 2832-2836
    • Richter, W.1    Shi, Y.2    Baekkeskov, S.3
  • 40
    • 1842452699 scopus 로고    scopus 로고
    • Antibodies to GAD65 epitopes at diagnosis and over the first 10 years of clinical type 1 diabetes mellitus
    • Ronkainen M.S., Savola K., and Knip M. Antibodies to GAD65 epitopes at diagnosis and over the first 10 years of clinical type 1 diabetes mellitus. Scand. J. Immunol. 59 (2004) 334-340
    • (2004) Scand. J. Immunol. , vol.59 , pp. 334-340
    • Ronkainen, M.S.1    Savola, K.2    Knip, M.3
  • 41
    • 7044241282 scopus 로고    scopus 로고
    • Phage display for epitope determination: a paradigm for identifying receptor-ligand interactions
    • Rowley M.J., O'Connor K., and Wijeyewickrema L. Phage display for epitope determination: a paradigm for identifying receptor-ligand interactions. Biotechnol. Annu. Rev. 10 (2004) 151-188
    • (2004) Biotechnol. Annu. Rev. , vol.10 , pp. 151-188
    • Rowley, M.J.1    O'Connor, K.2    Wijeyewickrema, L.3
  • 44
    • 20344405720 scopus 로고    scopus 로고
    • 3D-epitope-explorer (3DEX): localization of conformational epitopes within three-dimensional structures of proteins
    • Schreiber A., Humbert M., Benz A., and Dietrich U. 3D-epitope-explorer (3DEX): localization of conformational epitopes within three-dimensional structures of proteins. J. Comput. Chem. 26 (2005) 879-887
    • (2005) J. Comput. Chem. , vol.26 , pp. 879-887
    • Schreiber, A.1    Humbert, M.2    Benz, A.3    Dietrich, U.4
  • 45
    • 27344449197 scopus 로고    scopus 로고
    • Progress in modeling of protein structures and interactions
    • Schueler-Furman O., Wang C., Bradley P., Misura K., and Baker D. Progress in modeling of protein structures and interactions. Science 310 (2005) 638-642
    • (2005) Science , vol.310 , pp. 638-642
    • Schueler-Furman, O.1    Wang, C.2    Bradley, P.3    Misura, K.4    Baker, D.5
  • 47
    • 0032530578 scopus 로고    scopus 로고
    • Clustering of low-energy conformations near the native structures of small proteins
    • Shortle D., Simons K.T., and Baker D. Clustering of low-energy conformations near the native structures of small proteins. Proc. Natl. Acad. Sci. U.S.A. 95 (1998) 11158-11162
    • (1998) Proc. Natl. Acad. Sci. U.S.A. , vol.95 , pp. 11158-11162
    • Shortle, D.1    Simons, K.T.2    Baker, D.3
  • 48
    • 0032415715 scopus 로고    scopus 로고
    • Autoantigenic reactivity of diabetes sera with a hybrid glutamic acid decarboxylase GAD67-65 molecule GAD67(1-101)/GAD65(96-585)
    • Teoh K.L., Fida S., Rowley M.J., and Mackay I.R. Autoantigenic reactivity of diabetes sera with a hybrid glutamic acid decarboxylase GAD67-65 molecule GAD67(1-101)/GAD65(96-585). Autoimmunity 28 (1998) 259-266
    • (1998) Autoimmunity , vol.28 , pp. 259-266
    • Teoh, K.L.1    Fida, S.2    Rowley, M.J.3    Mackay, I.R.4
  • 49
    • 0027968068 scopus 로고
    • CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice
    • Thompson J.D., Higgins D.G., and Gibson T.J. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucl. Acids Res. 22 (1994) 4673-4680
    • (1994) Nucl. Acids Res. , vol.22 , pp. 4673-4680
    • Thompson, J.D.1    Higgins, D.G.2    Gibson, T.J.3
  • 51
    • 0030838447 scopus 로고    scopus 로고
    • Human B cells secreting immunoglobulin G to glutamic acid decarboxylase-65 from a nondiabetic patient with multiple autoantibodies and Graves' disease: a comparison with those present in type 1 diabetes
    • Tremble J., Morgenthaler N.G., Vlug A., Powers A.C., Christie M.R., Scherbaum W.A., and Banga J.P. Human B cells secreting immunoglobulin G to glutamic acid decarboxylase-65 from a nondiabetic patient with multiple autoantibodies and Graves' disease: a comparison with those present in type 1 diabetes. J. Clin. Endocrinol. Metab. 82 (1997) 2664-2670
    • (1997) J. Clin. Endocrinol. Metab. , vol.82 , pp. 2664-2670
    • Tremble, J.1    Morgenthaler, N.G.2    Vlug, A.3    Powers, A.C.4    Christie, M.R.5    Scherbaum, W.A.6    Banga, J.P.7
  • 52
    • 0029988383 scopus 로고    scopus 로고
    • Protein-protein interfaces: architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences
    • Tsai C.J., Lin S.L., Wolfson H.J., and Nussinov R. Protein-protein interfaces: architectures and interactions in protein-protein interfaces and in protein cores. Their similarities and differences. Crit. Rev. Biochem. Mol. Biol. 31 (1996) 127-152
    • (1996) Crit. Rev. Biochem. Mol. Biol. , vol.31 , pp. 127-152
    • Tsai, C.J.1    Lin, S.L.2    Wolfson, H.J.3    Nussinov, R.4
  • 53
    • 0027500697 scopus 로고
    • Antibodies to glutamic acid decarboxylase reveal latent autoimmune diabetes mellitus in adults with a non-insulin-dependent onset of disease
    • Tuomi T., Groop L.C., Zimmet P.Z., Rowley M.J., Knowles W., and Mackay I.R. Antibodies to glutamic acid decarboxylase reveal latent autoimmune diabetes mellitus in adults with a non-insulin-dependent onset of disease. Diabetes 42 (1993) 359-362
    • (1993) Diabetes , vol.42 , pp. 359-362
    • Tuomi, T.1    Groop, L.C.2    Zimmet, P.Z.3    Rowley, M.J.4    Knowles, W.5    Mackay, I.R.6
  • 54
    • 1242270553 scopus 로고    scopus 로고
    • Protein-protein docking: is the glass half-full or half-empty?
    • Vajda S., and Camacho C.J. Protein-protein docking: is the glass half-full or half-empty?. Trends Biotechnol. 22 (2004) 110-116
    • (2004) Trends Biotechnol. , vol.22 , pp. 110-116
    • Vajda, S.1    Camacho, C.J.2
  • 55
    • 0029610794 scopus 로고
    • Canonical structure repertoire of the antigen-binding site of immunoglobulins suggests strong geometrical restrictions associated to the mechanism of immune recognition
    • Vargas-Madrazo E., Lara-Ochoa F., and Almagro J.C. Canonical structure repertoire of the antigen-binding site of immunoglobulins suggests strong geometrical restrictions associated to the mechanism of immune recognition. J. Mol. Biol. 254 (1995) 497-504
    • (1995) J. Mol. Biol. , vol.254 , pp. 497-504
    • Vargas-Madrazo, E.1    Lara-Ochoa, F.2    Almagro, J.C.3
  • 56
    • 0036568230 scopus 로고    scopus 로고
    • Modifications to canonical structure sequence patterns: analysis for L1 and L3
    • Vargas-Madrazo E., and Paz-Garcia E. Modifications to canonical structure sequence patterns: analysis for L1 and L3. Proteins 47 (2002) 250-254
    • (2002) Proteins , vol.47 , pp. 250-254
    • Vargas-Madrazo, E.1    Paz-Garcia, E.2


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