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Volumn 31, Issue 3, 2008, Pages 228-232

GAD65 as a prototypic autoantigen

Author keywords

Antigenicity; Autoepitopes; Epitope structure; Glutamic acid decarboxylase; Type 1 diabetes

Indexed keywords

AUTOANTIGEN; EPITOPE; GLUTAMATE DECARBOXYLASE 65; GLUTAMATE DECARBOXYLASE 67;

EID: 56349160583     PISSN: 08968411     EISSN: 10959157     Source Type: Journal    
DOI: 10.1016/j.jaut.2008.04.013     Document Type: Article
Times cited : (23)

References (46)
  • 2
    • 0037264546 scopus 로고    scopus 로고
    • The autoantibody repertoire: searching for order
    • Plotz P.H. The autoantibody repertoire: searching for order. Nat Rev Immunol 3 (2003) 73-78
    • (2003) Nat Rev Immunol , vol.3 , pp. 73-78
    • Plotz, P.H.1
  • 3
    • 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
  • 4
    • 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
  • 5
    • 33746718136 scopus 로고    scopus 로고
    • Latent autoimmune diabetes in adults (LADA) - more than a name
    • Groop L., Tuomi T., Rowley M., Zimmet P., and Mackay I.R. Latent autoimmune diabetes in adults (LADA) - more than a name. Diabetologia 49 (2006) 1996-1998
    • (2006) Diabetologia , vol.49 , pp. 1996-1998
    • Groop, L.1    Tuomi, T.2    Rowley, M.3    Zimmet, P.4    Mackay, I.R.5
  • 6
    • 0025039679 scopus 로고
    • Identification of the 64K autoantigen in insulin-dependent diabetes as the GABA-synthesizing enzyme glutamic acid decarboxylase
    • Baekkeskov S., Aanstoot H.J., Christgau S., Reetz A., Solimena M., Cascalho M., et al. Identification of the 64K autoantigen in insulin-dependent diabetes as the GABA-synthesizing enzyme glutamic acid decarboxylase. Nature 347 (1990) 151-156
    • (1990) Nature , vol.347 , pp. 151-156
    • Baekkeskov, S.1    Aanstoot, H.J.2    Christgau, S.3    Reetz, A.4    Solimena, M.5    Cascalho, M.6
  • 7
    • 0028237147 scopus 로고
    • Antibodies to glutamic acid decarboxylase as predictors of insulin-dependent diabetes mellitus before clinical onset of disease
    • Tuomilehto J., Zimmet P., Mackay I.R., Koskela P., Vidgren G., Toivanen L., et al. Antibodies to glutamic acid decarboxylase as predictors of insulin-dependent diabetes mellitus before clinical onset of disease. Lancet 343 (1994) 1383-1385
    • (1994) Lancet , vol.343 , pp. 1383-1385
    • Tuomilehto, J.1    Zimmet, P.2    Mackay, I.R.3    Koskela, P.4    Vidgren, G.5    Toivanen, L.6
  • 8
    • 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
  • 9
    • 34247249781 scopus 로고    scopus 로고
    • GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop
    • Fenalti G., Law R.H., Buckle A.M., Langendorf C., Tuck K., Rosado C.J., et al. GABA production by glutamic acid decarboxylase is regulated by a dynamic catalytic loop. Nat Struct Mol Biol 14 (2007) 280-286
    • (2007) Nat Struct Mol Biol , vol.14 , pp. 280-286
    • Fenalti, G.1    Law, R.H.2    Buckle, A.M.3    Langendorf, C.4    Tuck, K.5    Rosado, C.J.6
  • 10
    • 0033574642 scopus 로고    scopus 로고
    • High-resolution autoreactive epitope mapping and structural modeling of the 65 kDa form of human glutamic acid decarboxylase
    • Schwartz H.L., Chandonia J.M., Kash S.F., Kanaani J., Tunnell E., Domingo A., et al. High-resolution autoreactive epitope mapping and structural modeling of the 65 kDa form of human glutamic acid decarboxylase. J Mol Biol 287 (1999) 983-999
    • (1999) J Mol Biol , vol.287 , pp. 983-999
    • Schwartz, H.L.1    Chandonia, J.M.2    Kash, S.F.3    Kanaani, J.4    Tunnell, E.5    Domingo, A.6
  • 11
    • 33646695933 scopus 로고    scopus 로고
    • Characterisation of an autoreactive conformational epitope on GAD65 recognised by the human monoclonal antibody b78 using a combination of phage display, in vitro mutagenesis and molecular modelling
    • O'Connor K.H., Banga J.P., Darmanin C., El-Kabbani O., Mackay I.R., and Rowley M.J. Characterisation of an autoreactive conformational epitope on GAD65 recognised by the human monoclonal antibody b78 using a combination of phage display, in vitro mutagenesis and molecular modelling. J Autoimmun 26 (2006) 172-181
    • (2006) J Autoimmun , vol.26 , pp. 172-181
    • O'Connor, K.H.1    Banga, J.P.2    Darmanin, C.3    El-Kabbani, O.4    Mackay, I.R.5    Rowley, M.J.6
  • 12
    • 48449102723 scopus 로고    scopus 로고
    • COOH terminal clustering of autoantibody and T cell determinants on the structure of GAD65 provide insights into the molecular basis of autoreactivity
    • Fenalti G., Hampe C.S., Law R.H., Arafat Y., Banga J.P., Mackay I.R., et al. COOH terminal clustering of autoantibody and T cell determinants on the structure of GAD65 provide insights into the molecular basis of autoreactivity. Diabetes 57 (2008) 1293-1301
    • (2008) Diabetes , vol.57 , pp. 1293-1301
    • Fenalti, G.1    Hampe, C.S.2    Law, R.H.3    Arafat, Y.4    Banga, J.P.5    Mackay, I.R.6
  • 13
    • 0030695027 scopus 로고    scopus 로고
    • Prediction of IDDM in the general population: strategies based on combinations of autoantibody markers
    • Bingley P.J., Bonifacio E., Williams A.J., Genovese S., Bottazzo G.F., and Gale E.A. Prediction of IDDM in the general population: strategies based on combinations of autoantibody markers. Diabetes 46 (1997) 1701-1710
    • (1997) Diabetes , vol.46 , pp. 1701-1710
    • Bingley, P.J.1    Bonifacio, E.2    Williams, A.J.3    Genovese, S.4    Bottazzo, G.F.5    Gale, E.A.6
  • 14
    • 0026673880 scopus 로고
    • Human monoclonal islet cell antibodies from a patient with insulin-dependent diabetes mellitus reveal glutamate decarboxylase as the target antigen
    • Richter W., Endl J., Eiermann T.H., Brandt M., Kientsch-Engel R., Thivolet C., et al. Human monoclonal islet cell antibodies from a patient with insulin-dependent diabetes mellitus reveal glutamate decarboxylase as the target antigen. Proc Natl Acad Sci U S A 89 (1992) 8467-8471
    • (1992) Proc Natl Acad Sci U S A , vol.89 , pp. 8467-8471
    • Richter, W.1    Endl, J.2    Eiermann, T.H.3    Brandt, M.4    Kientsch-Engel, R.5    Thivolet, C.6
  • 15
    • 0029931076 scopus 로고    scopus 로고
    • Four IgG anti-islet human monoclonal antibodies isolated from a type 1 diabetes patient recognize distinct epitopes of glutamic acid decarboxylase 65 and are somatically mutated
    • Madec A.M., Rousset F., Ho S., Robert F., Thivolet C., Orgiazzi J., et al. Four IgG anti-islet human monoclonal antibodies isolated from a type 1 diabetes patient recognize distinct epitopes of glutamic acid decarboxylase 65 and are somatically mutated. J Immunol 156 (1996) 3541-3549
    • (1996) J Immunol , vol.156 , pp. 3541-3549
    • Madec, A.M.1    Rousset, F.2    Ho, S.3    Robert, F.4    Thivolet, C.5    Orgiazzi, J.6
  • 16
    • 0030470633 scopus 로고    scopus 로고
    • Immune reactivity of diabetes-associated human monoclonal autoantibodies defines multiple epitopes and detects two domain boundaries in glutamate decarboxylase
    • Syren K., Lindsay L., Stoehrer B., Jury K., Luhder F., Baekkeskov S., et al. Immune reactivity of diabetes-associated human monoclonal autoantibodies defines multiple epitopes and detects two domain boundaries in glutamate decarboxylase. J Immunol 157 (1996) 5208-5214
    • (1996) J Immunol , vol.157 , pp. 5208-5214
    • Syren, K.1    Lindsay, L.2    Stoehrer, B.3    Jury, K.4    Luhder, F.5    Baekkeskov, S.6
  • 17
    • 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., et al. 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
  • 18
    • 0027433010 scopus 로고
    • Cytoplasmic islet cell antibodies recognize distinct islet antigens in IDDM but not in stiff man syndrome
    • Richter W., Seissler J., Northemann W., Wolfahrt S., Meinck H.M., and Scherbaum W.A. Cytoplasmic islet cell antibodies recognize distinct islet antigens in IDDM but not in stiff man syndrome. Diabetes 42 (1993) 1642-1648
    • (1993) Diabetes , vol.42 , pp. 1642-1648
    • Richter, W.1    Seissler, J.2    Northemann, W.3    Wolfahrt, S.4    Meinck, H.M.5    Scherbaum, W.A.6
  • 19
    • 10744229400 scopus 로고    scopus 로고
    • Recombinant Fabs of human monoclonal antibodies specific to the middle epitope of GAD65 inhibit type 1 diabetes-specific GAD65Abs
    • Padoa C.J., Banga J.P., Madec A.M., Ziegler M., Schlosser M., Ortqvist E., et al. Recombinant Fabs of human monoclonal antibodies specific to the middle epitope of GAD65 inhibit type 1 diabetes-specific GAD65Abs. Diabetes 52 (2003) 2689-2695
    • (2003) Diabetes , vol.52 , pp. 2689-2695
    • Padoa, C.J.1    Banga, J.P.2    Madec, A.M.3    Ziegler, M.4    Schlosser, M.5    Ortqvist, E.6
  • 20
    • 28344449503 scopus 로고    scopus 로고
    • Analysis of GAD65 autoantibodies in Stiff-Person syndrome patients
    • Raju R., Foote J., Banga J.P., Hall T.R., Padoa C.J., Dalakas M.C., et al. Analysis of GAD65 autoantibodies in Stiff-Person syndrome patients. J Immunol 175 (2005) 7755-7762
    • (2005) J Immunol , vol.175 , pp. 7755-7762
    • Raju, R.1    Foote, J.2    Banga, J.P.3    Hall, T.R.4    Padoa, C.J.5    Dalakas, M.C.6
  • 21
    • 0037408360 scopus 로고    scopus 로고
    • Diabetes Antibody Standardization Program: first assay proficiency evaluation
    • Bingley P.J., Bonifacio E., and Mueller P.W. Diabetes Antibody Standardization Program: first assay proficiency evaluation. Diabetes 52 (2003) 1128-1136
    • (2003) Diabetes , vol.52 , pp. 1128-1136
    • Bingley, P.J.1    Bonifacio, E.2    Mueller, P.W.3
  • 22
    • 33748790946 scopus 로고    scopus 로고
    • Molecular characterization of a disease associated conformational epitope on GAD65 recognised by a human monoclonal antibody b96.11
    • Fenalti G., Hampe C.S., O'Connor K., Banga J.P., Mackay I.R., Rowley M.J., et al. Molecular characterization of a disease associated conformational epitope on GAD65 recognised by a human monoclonal antibody b96.11. Mol Immunol 44 (2007) 1178-1189
    • (2007) Mol Immunol , vol.44 , pp. 1178-1189
    • Fenalti, G.1    Hampe, C.S.2    O'Connor, K.3    Banga, J.P.4    Mackay, I.R.5    Rowley, M.J.6
  • 23
    • 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., et al. 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
  • 24
    • 33847629171 scopus 로고    scopus 로고
    • Translational mini-review series on type 1 diabetes: systematic analysis of T cell epitopes in autoimmune diabetes
    • Di Lorenzo T.P., Peakman M., and Roep B.O. Translational mini-review series on type 1 diabetes: systematic analysis of T cell epitopes in autoimmune diabetes. Clin Exp Immunol 148 (2007) 1-16
    • (2007) Clin Exp Immunol , vol.148 , pp. 1-16
    • Di Lorenzo, T.P.1    Peakman, M.2    Roep, B.O.3
  • 25
    • 0036673437 scopus 로고    scopus 로고
    • GAD65 antibody epitope patterns of type 1.5 diabetic patients are consistent with slow-onset autoimmune diabetes
    • Hampe C.S., Kockum I., Landin-Olsson M., Torn C., Ortqvist E., Persson B., et al. GAD65 antibody epitope patterns of type 1.5 diabetic patients are consistent with slow-onset autoimmune diabetes. Diabetes Care 25 (2002) 1481-1482
    • (2002) Diabetes Care , vol.25 , pp. 1481-1482
    • Hampe, C.S.1    Kockum, I.2    Landin-Olsson, M.3    Torn, C.4    Ortqvist, E.5    Persson, B.6
  • 26
    • 0242351804 scopus 로고    scopus 로고
    • Unique epitopes of glutamic acid decarboxylase autoantibodies in slowly progressive type 1 diabetes
    • Kobayashi T., Tanaka S., Okubo M., Nakanishi K., Murase T., and Lernmark A. Unique epitopes of glutamic acid decarboxylase autoantibodies in slowly progressive type 1 diabetes. J Clin Endocrinol Metab 88 (2003) 4768-4775
    • (2003) J Clin Endocrinol Metab , vol.88 , pp. 4768-4775
    • Kobayashi, T.1    Tanaka, S.2    Okubo, M.3    Nakanishi, K.4    Murase, T.5    Lernmark, A.6
  • 27
    • 33847615573 scopus 로고    scopus 로고
    • Longitudinal changes in epitope recognition of autoantibodies against glutamate decarboxylase 65 (GAD65Ab) in prediabetic adults developing diabetes
    • Hampe C.S., Hall T.R., Agren A., and Rolandsson O. Longitudinal changes in epitope recognition of autoantibodies against glutamate decarboxylase 65 (GAD65Ab) in prediabetic adults developing diabetes. Clin Exp Immunol 148 (2007) 72-78
    • (2007) Clin Exp Immunol , vol.148 , pp. 72-78
    • Hampe, C.S.1    Hall, T.R.2    Agren, A.3    Rolandsson, O.4
  • 28
    • 33846952847 scopus 로고    scopus 로고
    • Association of amino-terminal-specific antiglutamate decarboxylase (GAD65) autoantibodies with beta-cell functional reserve and a milder clinical phenotype in patients with GAD65 antibodies and ketosis-prone diabetes mellitus
    • Hampe C.S., Nalini R., Maldonado M.R., Hall T.R., Garza G., Iyer D., et al. Association of amino-terminal-specific antiglutamate decarboxylase (GAD65) autoantibodies with beta-cell functional reserve and a milder clinical phenotype in patients with GAD65 antibodies and ketosis-prone diabetes mellitus. J Clin Endocrinol Metab 92 (2007) 462-467
    • (2007) J Clin Endocrinol Metab , vol.92 , pp. 462-467
    • Hampe, C.S.1    Nalini, R.2    Maldonado, M.R.3    Hall, T.R.4    Garza, G.5    Iyer, D.6
  • 29
    • 20044386159 scopus 로고    scopus 로고
    • Dynamic changes of GAD65 autoantibody epitope specificities in individuals at risk of developing type 1 diabetes
    • Schlosser M., Banga J.P., Madec A.M., Binder K.A., Strebelow M., Rjasanowski I., et al. Dynamic changes of GAD65 autoantibody epitope specificities in individuals at risk of developing type 1 diabetes. Diabetologia 48 (2005) 922-930
    • (2005) Diabetologia , vol.48 , pp. 922-930
    • Schlosser, M.1    Banga, J.P.2    Madec, A.M.3    Binder, K.A.4    Strebelow, M.5    Rjasanowski, I.6
  • 30
    • 24744468198 scopus 로고    scopus 로고
    • A peptide of glutamic acid decarboxylase 65 can recruit and expand a diabetogenic T cell clone, BDC2.5, in the pancreas
    • Dai Y.D., Jensen K.P., Lehuen A., Masteller E.L., Bluestone J.A., Wilson D.B., et al. A peptide of glutamic acid decarboxylase 65 can recruit and expand a diabetogenic T cell clone, BDC2.5, in the pancreas. J Immunol 175 (2005) 3621-3627
    • (2005) J Immunol , vol.175 , pp. 3621-3627
    • Dai, Y.D.1    Jensen, K.P.2    Lehuen, A.3    Masteller, E.L.4    Bluestone, J.A.5    Wilson, D.B.6
  • 31
    • 33644666732 scopus 로고    scopus 로고
    • Antigen processing by autoreactive B cells promotes determinant spreading
    • Dai Y.D., Carayanniotis G., and Sercarz E. Antigen processing by autoreactive B cells promotes determinant spreading. Cell Mol Immunol 2 (2005) 169-175
    • (2005) Cell Mol Immunol , vol.2 , pp. 169-175
    • Dai, Y.D.1    Carayanniotis, G.2    Sercarz, E.3
  • 32
    • 0031010513 scopus 로고    scopus 로고
    • Identification of immunogenic epitopes of GAD 65 presented by Ag7 in non-obese diabetic mice
    • Chao C.C., and McDevitt H.O. Identification of immunogenic epitopes of GAD 65 presented by Ag7 in non-obese diabetic mice. Immunogenetics 46 (1997) 29-34
    • (1997) Immunogenetics , vol.46 , pp. 29-34
    • Chao, C.C.1    McDevitt, H.O.2
  • 33
    • 0035852674 scopus 로고    scopus 로고
    • Identification and modulation of a naturally processed T cell epitope from the diabetes-associated autoantigen human glutamic acid decarboxylase 65 (hGAD65)
    • Nepom G.T., Lippolis J.D., White F.M., Masewicz S., Marto J.A., Herman A., et al. Identification and modulation of a naturally processed T cell epitope from the diabetes-associated autoantigen human glutamic acid decarboxylase 65 (hGAD65). Proc Natl Acad Sci U S A 98 (2001) 1763-1768
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 1763-1768
    • Nepom, G.T.1    Lippolis, J.D.2    White, F.M.3    Masewicz, S.4    Marto, J.A.5    Herman, A.6
  • 34
    • 0030759825 scopus 로고    scopus 로고
    • Identification of immunodominant T cell epitopes of human glutamic acid decarboxylase 65 by using HLA-DR(alpha1*0101,beta1*0401) transgenic mice
    • Patel S.D., Cope A.P., Congia M., Chen T.T., Kim E., Fugger L., et al. Identification of immunodominant T cell epitopes of human glutamic acid decarboxylase 65 by using HLA-DR(alpha1*0101,beta1*0401) transgenic mice. Proc Natl Acad Sci U S A 94 (1997) 8082-8087
    • (1997) Proc Natl Acad Sci U S A , vol.94 , pp. 8082-8087
    • Patel, S.D.1    Cope, A.P.2    Congia, M.3    Chen, T.T.4    Kim, E.5    Fugger, L.6
  • 35
    • 10544223741 scopus 로고    scopus 로고
    • Naturally processed T cell epitopes from human glutamic acid decarboxylase identified using mice transgenic for the type 1 diabetes-associated human MHC class II allele, DRB1*0401
    • Wicker L.S., Chen S.L., Nepom G.T., Elliott J.F., Freed D.C., Bansal A., et al. Naturally processed T cell epitopes from human glutamic acid decarboxylase identified using mice transgenic for the type 1 diabetes-associated human MHC class II allele, DRB1*0401. J Clin Invest 98 (1996) 2597-2603
    • (1996) J Clin Invest , vol.98 , pp. 2597-2603
    • Wicker, L.S.1    Chen, S.L.2    Nepom, G.T.3    Elliott, J.F.4    Freed, D.C.5    Bansal, A.6
  • 37
    • 8844259795 scopus 로고    scopus 로고
    • Autoimmune epitopes: autoepitopes
    • Mackay I.R., and Rowley M.J. Autoimmune epitopes: autoepitopes. Autoimmun Rev 3 (2004) 487-492
    • (2004) Autoimmun Rev , vol.3 , pp. 487-492
    • Mackay, I.R.1    Rowley, M.J.2
  • 38
    • 0347949511 scopus 로고    scopus 로고
    • Modulation of antigen presentation by autoreactive B cell clones specific for GAD65 from a type I diabetic patient
    • Banga J.P., Moore J.K., Duhindan N., Madec A.M., van Endert P.M., Orgiazzi J., et al. Modulation of antigen presentation by autoreactive B cell clones specific for GAD65 from a type I diabetic patient. Clin Exp Immunol 135 (2004) 74-84
    • (2004) Clin Exp Immunol , vol.135 , pp. 74-84
    • Banga, J.P.1    Moore, J.K.2    Duhindan, N.3    Madec, A.M.4    van Endert, P.M.5    Orgiazzi, J.6
  • 39
    • 0037100387 scopus 로고    scopus 로고
    • Suppressive effect of glutamic acid decarboxylase 65-specific autoimmune B lymphocytes on processing of T cell determinants located within the antibody epitope
    • Jaume J.C., Parry S.L., Madec A.M., Sonderstrup G., and Baekkeskov S. Suppressive effect of glutamic acid decarboxylase 65-specific autoimmune B lymphocytes on processing of T cell determinants located within the antibody epitope. J Immunol 169 (2002) 665-672
    • (2002) J Immunol , vol.169 , pp. 665-672
    • Jaume, J.C.1    Parry, S.L.2    Madec, A.M.3    Sonderstrup, G.4    Baekkeskov, S.5
  • 40
    • 34248213007 scopus 로고    scopus 로고
    • Antibody-enhanced cross-presentation of self antigen breaks T cell tolerance
    • Harbers S.O., Crocker A., Catalano G., D'Agati V., Jung S., Desai D.D., et al. Antibody-enhanced cross-presentation of self antigen breaks T cell tolerance. J Clin Invest 117 (2007) 1361-1369
    • (2007) J Clin Invest , vol.117 , pp. 1361-1369
    • Harbers, S.O.1    Crocker, A.2    Catalano, G.3    D'Agati, V.4    Jung, S.5    Desai, D.D.6
  • 41
    • 10844266513 scopus 로고    scopus 로고
    • Human autoantibodies modulate the T cell epitope repertoire but fail to unmask a pathogenic cryptic epitope
    • Quaratino S., Ruf J., Osman M., Guo J., McLachlan S., Rapoport B., et al. Human autoantibodies modulate the T cell epitope repertoire but fail to unmask a pathogenic cryptic epitope. J Immunol 174 (2005) 557-563
    • (2005) J Immunol , vol.174 , pp. 557-563
    • Quaratino, S.1    Ruf, J.2    Osman, M.3    Guo, J.4    McLachlan, S.5    Rapoport, B.6
  • 42
    • 4644225746 scopus 로고    scopus 로고
    • Investigation of the role of B-cells in type 1 diabetes in the NOD mouse
    • Wong F.S., Wen L., Tang M., Ramanathan M., Visintin I., Daugherty J., et al. Investigation of the role of B-cells in type 1 diabetes in the NOD mouse. Diabetes 53 (2004) 2581-2587
    • (2004) Diabetes , vol.53 , pp. 2581-2587
    • Wong, F.S.1    Wen, L.2    Tang, M.3    Ramanathan, M.4    Visintin, I.5    Daugherty, J.6
  • 43
    • 33748784872 scopus 로고    scopus 로고
    • Antigen three-dimensional structure guides the processing and presentation of helper T-cell epitopes
    • Carmicle S., Steede N.K., and Landry S.J. Antigen three-dimensional structure guides the processing and presentation of helper T-cell epitopes. Mol Immunol 44 (2007) 1159-1168
    • (2007) Mol Immunol , vol.44 , pp. 1159-1168
    • Carmicle, S.1    Steede, N.K.2    Landry, S.J.3
  • 44
    • 0035836680 scopus 로고    scopus 로고
    • Localization of CD4+ T cell epitope hotspots to exposed strands of HIV envelope glycoprotein suggests structural influences on antigen processing
    • Surman S., Lockey T.D., Slobod K.S., Jones B., Riberdy J.M., White S.W., et al. Localization of CD4+ T cell epitope hotspots to exposed strands of HIV envelope glycoprotein suggests structural influences on antigen processing. Proc Natl Acad Sci U S A 98 (2001) 4587-4592
    • (2001) Proc Natl Acad Sci U S A , vol.98 , pp. 4587-4592
    • Surman, S.1    Lockey, T.D.2    Slobod, K.S.3    Jones, B.4    Riberdy, J.M.5    White, S.W.6
  • 45
    • 33745152667 scopus 로고    scopus 로고
    • Mapping epitopes and antigenicity by site-directed masking
    • Paus D., and Winter G. Mapping epitopes and antigenicity by site-directed masking. Proc Natl Acad Sci U S A 103 (2006) 9172-9177
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 9172-9177
    • Paus, D.1    Winter, G.2
  • 46
    • 0141858715 scopus 로고    scopus 로고
    • The specificity of cross-reactivity: promiscuous antibody binding involves specific hydrogen bonds rather than nonspecific hydrophobic stickiness
    • James L.C., and Tawfik D.S. The specificity of cross-reactivity: promiscuous antibody binding involves specific hydrogen bonds rather than nonspecific hydrophobic stickiness. Protein Sci 12 (2003) 2183-2193
    • (2003) Protein Sci , vol.12 , pp. 2183-2193
    • James, L.C.1    Tawfik, D.S.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.