메뉴 건너뛰기




Volumn 55, Issue 8, 2011, Pages 1266-1270

Immunological evaluation of the alcohol-soluble protein fraction from gluten-free grains in relation to celiac disease

Author keywords

Celiac disease; Organ culture; Pseudocereals; T cells; Transgenic mice

Indexed keywords

ALCOHOL DERIVATIVE; GAMMA INTERFERON; GLUTEN; PLANT EXTRACT; VEGETABLE PROTEIN;

EID: 79961065186     PISSN: 16134125     EISSN: 16134133     Source Type: Journal    
DOI: 10.1002/mnfr.201100132     Document Type: Article
Times cited : (59)

References (22)
  • 1
    • 0038509007 scopus 로고    scopus 로고
    • Prevalence of celiac disease among children in Finland
    • Maki, M., Mustalahti, K., Kokkonen, J., Kulmala, P. et al., Prevalence of celiac disease among children in Finland. N. Engl. J. Med. 2003, 348, 2517-2524.
    • (2003) N. Engl. J. Med. , vol.348 , pp. 2517-2524
    • Maki, M.1    Mustalahti, K.2    Kokkonen, J.3    Kulmala, P.4
  • 2
    • 0036715684 scopus 로고    scopus 로고
    • Coeliac disease: dissecting a complex inflammatory disorder
    • Sollid, L. M., Coeliac disease: dissecting a complex inflammatory disorder. Nat. Rev. Immunol. 2002; 2, 647-655.
    • (2002) Nat. Rev. Immunol. , vol.2 , pp. 647-655
    • Sollid, L.M.1
  • 3
    • 0031660029 scopus 로고    scopus 로고
    • Gluten induces an intestinal cytokine response strongly dominated by interferon gamma in patients with celiac disease
    • Nilsen, E. M., Jahnsen, F. L., Lundin, K. E., Johansen, E. et al., Gluten induces an intestinal cytokine response strongly dominated by interferon gamma in patients with celiac disease. Gastroenterology 1998, 115, 551-563.
    • (1998) Gastroenterology , vol.115 , pp. 551-563
    • Nilsen, E.M.1    Jahnsen, F.L.2    Lundin, K.E.3    Johansen, E.4
  • 4
    • 0031779478 scopus 로고    scopus 로고
    • Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease
    • Molberg, O., McAdam, S. N., Korner, R., Quarsten, H. et al., Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease. Nat. Med. 1998, 4, 713-717.
    • (1998) Nat. Med. , vol.4 , pp. 713-717
    • Molberg, O.1    McAdam, S.N.2    Korner, R.3    Quarsten, H.4
  • 5
    • 0037018095 scopus 로고    scopus 로고
    • Specificity of tissue transglutaminase explains cereal toxicity in celiac disease
    • Vader, L. W., de Ru, A., van der Wal, Y., Kooy, Y. M. et al., Specificity of tissue transglutaminase explains cereal toxicity in celiac disease. J. Exp. Med. 2002, 195, 643-649.
    • (2002) J. Exp. Med. , vol.195 , pp. 643-649
    • Vader, L.W.1    de Ru, A.2    van der Wal, Y.3    Kooy, Y.M.4
  • 8
    • 29144480200 scopus 로고    scopus 로고
    • Identification of immunodominant epitopes of alpha-gliadin in HLA-DQ8 transgenic mice following oral immunization
    • Senger, S., Maurano, F., Mazzeo, M. F., Gaita, M. et al., Identification of immunodominant epitopes of alpha-gliadin in HLA-DQ8 transgenic mice following oral immunization. J. Immunol. 2005, 175, 8087-8095.
    • (2005) J. Immunol. , vol.175 , pp. 8087-8095
    • Senger, S.1    Maurano, F.2    Mazzeo, M.F.3    Gaita, M.4
  • 9
    • 0029823313 scopus 로고    scopus 로고
    • Both α and β chain polymorphisms determine the specificity of the disease-associated HLA-DQ2 molecules, with β chain residues being most influential
    • Johansen, B. H., Jensen, T., Thorpe, C. J., Vartdal, F. et al., Both α and β chain polymorphisms determine the specificity of the disease-associated HLA-DQ2 molecules, with β chain residues being most influential. Immunogenetics 1996, 45, 142-150.
    • (1996) Immunogenetics , vol.45 , pp. 142-150
    • Johansen, B.H.1    Jensen, T.2    Thorpe, C.J.3    Vartdal, F.4
  • 11
    • 0033854413 scopus 로고    scopus 로고
    • Structure of celiac disease-associated HLA-DQ8 and non-associated HLADQ9 alleles in complex with two disease-specific epitopes
    • Moustakas, A. K., van de Wal, Y., Routsias, J., Kooy, Y. M. et al., Structure of celiac disease-associated HLA-DQ8 and non-associated HLADQ9 alleles in complex with two disease-specific epitopes. Int. Immunol. 2000, 12, 1157-1166.
    • (2000) Int. Immunol. , vol.12 , pp. 1157-1166
    • Moustakas, A.K.1    van de Wal, Y.2    Routsias, J.3    Kooy, Y.M.4
  • 12
    • 78650730980 scopus 로고    scopus 로고
    • A universal approach to eliminate antigenic properties of alpha-gliadin peptides in celiac disease
    • doi:10.1371/journal.pone.0015637.
    • Mitea, C., Salentijn, E. M. J., van Veelen, P., Goryunova, S. V. et al., A universal approach to eliminate antigenic properties of alpha-gliadin peptides in celiac disease. PLoS ONE 2010, 5, e15637. doi:10.1371/journal.pone.0015637.
    • (2010) PLoS ONE , vol.5
    • Mitea, C.1    Salentijn, E.M.J.2    van Veelen, P.3    Goryunova, S.V.4
  • 13
    • 77955634105 scopus 로고    scopus 로고
    • Comprehensive, quantitative mapping of T cell epitopes in gluten in celiac disease
    • Tye-Din, J. A., Stewart, J. A., Dromey, J. A., Beissbarth, T. et al., Comprehensive, quantitative mapping of T cell epitopes in gluten in celiac disease. Sci. Transl. Med. 2010, 41, 41-51.
    • (2010) Sci. Transl. Med. , vol.41 , pp. 41-51
    • Tye-Din, J.A.1    Stewart, J.A.2    Dromey, J.A.3    Beissbarth, T.4
  • 14
    • 0036271172 scopus 로고    scopus 로고
    • Characterisation of pseudocereal and cereal proteins by protein and amino acid analyses
    • Gorinstein, S., Pawelzik, E., Delgado-Licon, E., Haruenkit, R. et al., Characterisation of pseudocereal and cereal proteins by protein and amino acid analyses. J. Food Sci. Technol. 2002, 82, 886-891.
    • (2002) J. Food Sci. Technol. , vol.82 , pp. 886-891
    • Gorinstein, S.1    Pawelzik, E.2    Delgado-Licon, E.3    Haruenkit, R.4
  • 15
    • 84857106328 scopus 로고    scopus 로고
    • Effect of nitrogen fertilizer on nitrogen assimilation and seed quality of amaranth (Amaranthus spp.) and quinoa (Chenopodium quinoa Willd). Doctoral Dissertation, Faculty of Agricultural Sciences Georg-August-University of Göttingen, Göttingen Germany, November .
    • Thanapornpoonpong, S., Effect of nitrogen fertilizer on nitrogen assimilation and seed quality of amaranth (Amaranthus spp.) and quinoa (Chenopodium quinoa Willd). Doctoral Dissertation, Faculty of Agricultural Sciences Georg-August-University of Göttingen, Göttingen Germany, November 2004.
    • (2004)
    • Thanapornpoonpong, S.1
  • 16
    • 0007632759 scopus 로고
    • Amino acid composition of the cereal Tef and related species of Eragrostis (Gramineae)
    • Lester, R. N., Bekele, E., Amino acid composition of the cereal Tef and related species of Eragrostis (Gramineae). Cereal Chem. 1981, 58, 113-115.
    • (1981) Cereal Chem. , vol.58 , pp. 113-115
    • Lester, R.N.1    Bekele, E.2
  • 17
    • 0000573572 scopus 로고
    • High performance liquid chromatography of gliadins from different wheat varieties: amino acid composition and N-terminal amino acid sequences of components
    • Wieser, H., Modl, A., Seilmeier, W., Belitz, H.-D., High performance liquid chromatography of gliadins from different wheat varieties: amino acid composition and N-terminal amino acid sequences of components. Z. Lebens. Unters. Forsch. 1987, 185, 371-378.
    • (1987) Z. Lebens. Unters. Forsch. , vol.185 , pp. 371-378
    • Wieser, H.1    Modl, A.2    Seilmeier, W.3    Belitz, H.-D.4
  • 18
    • 0031891459 scopus 로고    scopus 로고
    • Majority of gliadin-specific T-cell clones from celiac small intestinal mucosa produce interferon-gamma and interleukin-4
    • Troncone, R., Gianfrani, C., Mazzarella, G., Greco, L. et al., Majority of gliadin-specific T-cell clones from celiac small intestinal mucosa produce interferon-gamma and interleukin-4. Dig. Dis. Sci. 1998, 43, 156-161.
    • (1998) Dig. Dis. Sci. , vol.43 , pp. 156-161
    • Troncone, R.1    Gianfrani, C.2    Mazzarella, G.3    Greco, L.4
  • 19
    • 1642447710 scopus 로고    scopus 로고
    • Structural basis for HLA-DQ2 mediated presentation of gluten epitopes in celiac disease
    • Kim, C. Y., Quarsten, H., Bergseng, E., Khosla, C., Sollid, L. M., Structural basis for HLA-DQ2 mediated presentation of gluten epitopes in celiac disease. Proc. Natl. Acad. Sci. USA 2004, 101, 4175-4179.
    • (2004) Proc. Natl. Acad. Sci. USA , vol.101 , pp. 4175-4179
    • Kim, C.Y.1    Quarsten, H.2    Bergseng, E.3    Khosla, C.4    Sollid, L.M.5
  • 20
    • 73249118020 scopus 로고    scopus 로고
    • A deregulated immune response to gliadin causes a decreased villus height in DQ8 transgenic mice
    • D'Arienzo, R., Stefanile, R., Maurano, F., Luongo, D. et al., A deregulated immune response to gliadin causes a decreased villus height in DQ8 transgenic mice. Eur. J. Immunol. 2009, 39, 3552-3561.
    • (2009) Eur. J. Immunol. , vol.39 , pp. 3552-3561
    • D'Arienzo, R.1    Stefanile, R.2    Maurano, F.3    Luongo, D.4
  • 21
    • 0038501062 scopus 로고    scopus 로고
    • Association between innate response to gliadin and activation of pathogenic T cells in coeliac disease
    • Maiuri, L., Ciacci, C., Ricciardelli, I., Vacca, L. et al., Association between innate response to gliadin and activation of pathogenic T cells in coeliac disease. Lancet 2003, 362, 30-37.
    • (2003) Lancet , vol.362 , pp. 30-37
    • Maiuri, L.1    Ciacci, C.2    Ricciardelli, I.3    Vacca, L.4
  • 22
    • 0037214515 scopus 로고    scopus 로고
    • An immunodominant DQ8 restricted gliadin peptide activates small intestinal immune response in in vitro cultured mucosa from HLA-DQ8 positive but not HLA-DQ8 negative coeliac patients
    • Mazzarella, G., Maglio, M., Paparo, F., Nardone, G. et al., An immunodominant DQ8 restricted gliadin peptide activates small intestinal immune response in in vitro cultured mucosa from HLA-DQ8 positive but not HLA-DQ8 negative coeliac patients. Gut 2003, 52, 57-62.
    • (2003) Gut , vol.52 , pp. 57-62
    • Mazzarella, G.1    Maglio, M.2    Paparo, F.3    Nardone, G.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.