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Volumn 8, Issue 10, 2016, Pages

Properties of gluten intolerance: Gluten structure, evolution, pathogenicity and detoxification capabilities

Author keywords

Avenin; Celiac disease; Gliadin; Gluten; Gluten intolerance; Glutenin; Hordein; NCGS; Secalin; Wheat allergy

Indexed keywords

AVENIN; GLIADIN; GLUTEN; GLUTENIN; HORDEIN; PROLAMIN; PEPTIDE;

EID: 84992052017     PISSN: None     EISSN: 20726643     Source Type: Journal    
DOI: 10.3390/nu8100644     Document Type: Review
Times cited : (187)

References (146)
  • 1
    • 0016856833 scopus 로고
    • Cell-mediated immunity to gliadin within the small-intestinal mucosa in coeliac disease
    • Ferguson, A.; MacDonald, T.T.; McClure, J.P.; Holden, R.J. Cell-mediated immunity to gliadin within the small-intestinal mucosa in coeliac disease. Lancet 1975, 1, 895–897.
    • (1975) Lancet , vol.1 , pp. 895-897
    • Ferguson, A.1    Macdonald, T.T.2    McClure, J.P.3    Holden, R.J.4
  • 2
    • 84924420674 scopus 로고    scopus 로고
    • Non coeliac gluten sensitivity—A new disease with gluten intolerance
    • Czaja-Bulsa, G. Non coeliac gluten sensitivity—A new disease with gluten intolerance. Clin. Nutr. 2015, 34, 189–194.
    • (2015) Clin. Nutr. , vol.34 , pp. 189-194
    • Czaja-Bulsa, G.1
  • 4
    • 84929999407 scopus 로고    scopus 로고
    • World perspective and celiac disease epidemiology
    • Catassi, C.; Gatti, S.; Lionetti, E. World perspective and celiac disease epidemiology. Dig. Dis. 2015, 33, 141–146.
    • (2015) Dig. Dis. , vol.33 , pp. 141-146
    • Catassi, C.1    Gatti, S.2    Lionetti, E.3
  • 8
    • 33745493934 scopus 로고    scopus 로고
    • Recent advances in coeliac disease
    • Van Heel, D.A.; West, J. Recent advances in coeliac disease. Gut 2006, 55, 1037–1046.
    • (2006) Gut , vol.55 , pp. 1037-1046
    • Van Heel, D.A.1    West, J.2
  • 9
    • 0034508690 scopus 로고    scopus 로고
    • Human zonulin, a potential modulator of intestinal tight junctions
    • Wang, W.; Uzzau, S.; Goldblum, S.E.; Fasano, A. Human zonulin, a potential modulator of intestinal tight junctions. J. Cell Sci. 2000, 113, 4435–4440.
    • (2000) J. Cell Sci , vol.113 , pp. 4435-4440
    • Wang, W.1    Uzzau, S.2    Goldblum, S.E.3    Fasano, A.4
  • 10
    • 0034235978 scopus 로고    scopus 로고
    • Current concepts of celiac disease pathogenesis
    • Schuppan, D. Current concepts of celiac disease pathogenesis. Gastroenterology 2000, 119, 234–242.
    • (2000) Gastroenterology , vol.119 , pp. 234-242
    • Schuppan, D.1
  • 16
    • 0036010140 scopus 로고    scopus 로고
    • Cereal seed storage proteins: Structures, properties and role in grain utilization
    • Shewry, P.R.; Halford, N.G. Cereal seed storage proteins: Structures, properties and role in grain utilization. J. Exp. Bot. 2002, 53, 947–958.
    • (2002) J. Exp. Bot , vol.53 , pp. 947-958
    • Shewry, P.R.1    Halford, N.G.2
  • 17
    • 0022419276 scopus 로고
    • Molecular evolution of the seed storage proteins of barley, rye and wheat
    • Kreis, M.; Forde, B.G.; Rahman, S.; Miflin, B.J.; Shewry, P.R. Molecular evolution of the seed storage proteins of barley, rye and wheat. J. Mol. Biol. 1985, 183, 499–502.
    • (1985) J. Mol. Biol. , vol.183 , pp. 499-502
    • Kreis, M.1    Forde, B.G.2    Rahman, S.3    Miflin, B.J.4    Shewry, P.R.5
  • 18
    • 33748885488 scopus 로고    scopus 로고
    • Chemistry of gluten proteins
    • Wieser, H. Chemistry of gluten proteins. Food Microbiol. 2007, 24, 115–119.
    • (2007) Food Microbiol , vol.24 , pp. 115-119
    • Wieser, H.1
  • 19
    • 0034952137 scopus 로고    scopus 로고
    • Application of polymer science to properties of gluten
    • Singh, H.; MacRitchie, F. Application of polymer science to properties of gluten. J. Cereal Sci. 2001, 33, 231–243.
    • (2001) J. Cereal Sci , vol.33 , pp. 231-243
    • Singh, H.1    Macritchie, F.2
  • 20
    • 14644397227 scopus 로고    scopus 로고
    • Characterization of B-and C-type low molecular weight glutenin subunits by electrospray ionization mass spectrometry and matrix-assisted laser desorption/ionization mass spectrometry
    • Muccilli, V.; Cunsolo, V.; Saletti, R.; Foti, S.; Masci, S.; Lafiandra, D. Characterization of B-and C-type low molecular weight glutenin subunits by electrospray ionization mass spectrometry and matrix-assisted laser desorption/ionization mass spectrometry. Proteomics 2005, 5, 719–728.
    • (2005) Proteomics , vol.5 , pp. 719-728
    • Muccilli, V.1    Cunsolo, V.2    Saletti, R.3    Foti, S.4    Masci, S.5    Lafiandra, D.6
  • 21
    • 80053195300 scopus 로고    scopus 로고
    • Characterization of proteins from grain of different bread and durum wheat genotypes
    • Zilic, S.; Barac, M.; Pesic, M.; Dodig, D.; Ignjatovic-Micic, D. Characterization of proteins from grain of different bread and durum wheat genotypes. Int. J. Mol. Sci. 2011, 12, 5878–5894.
    • (2011) Int. J. Mol. Sci. , vol.12 , pp. 5878-5894
    • Zilic, S.1    Barac, M.2    Pesic, M.3    Dodig, D.4    Ignjatovic-Micic, D.5
  • 22
    • 0015690724 scopus 로고
    • Electrofocusing of grain proteins from wheat genotypes
    • Wrigley, C.W.; Shepherd, K.W. Electrofocusing of grain proteins from wheat genotypes. Ann. N. Y. Acad. Sci. 1973, 209, 154–162.
    • (1973) Ann. N. Y. Acad. Sci , vol.209 , pp. 154-162
    • Wrigley, C.W.1    Shepherd, K.W.2
  • 23
    • 38149045956 scopus 로고    scopus 로고
    • Mass spectrometry analysis of gliadins in celiac disease
    • Ferranti, P.; Mamone, G.; Picariello, G.; Addeo, F. Mass spectrometry analysis of gliadins in celiac disease. J. Mass Spectrom. 2007, 42, 1531–1548.
    • (2007) J. Mass Spectrom , vol.42 , pp. 1531-1548
    • Ferranti, P.1    Mamone, G.2    Picariello, G.3    Addeo, F.4
  • 24
    • 0022032067 scopus 로고
    • Conformational study of a glutamine-and proline-rich cereal seed protein
    • Tatham, A.S.; Drake, A.F.; Shewry, P.R. A conformational study of a glutamine-and proline-rich cereal seed protein, C hordein. Biochem. J. 1985, 226, 557–562.
    • (1985) C Hordein. Biochem. J , vol.226 , pp. 557-562
    • Tatham, A.S.1    Drake, A.F.2    Shewry, P.3
  • 25
    • 0000971643 scopus 로고
    • The effect of heat on wheat gluten and the involvement of sulphydryl-disulphide interchange reactions
    • Schofield, J.D.; Bottomley, R.C.; Timms, M.F.; Booth, M.R. The effect of heat on wheat gluten and the involvement of sulphydryl-disulphide interchange reactions. J. Cereal Sci. 1983, 1, 241–253.
    • (1983) J. Cereal Sci , vol.1 , pp. 241-253
    • Schofield, J.D.1    Bottomley, R.C.2    Timms, M.F.3    Booth, M.R.4
  • 26
    • 78049292696 scopus 로고    scopus 로고
    • Elimination reactions and formation of covalent cross-links in gliadin during heating at alkaline pH
    • Rombouts, I.; Lagrain, B.; Brijs, K.; Delcour, J.A. _-Elimination reactions and formation of covalent cross-links in gliadin during heating at alkaline pH. J. Cereal Sci. 2010, 52, 362–367.
    • (2010) J. Cereal Sci. , vol.52 , pp. 362-367
    • Rombouts, I.1    Lagrain, B.2    Brijs, K.3    Delcour, J.A.4
  • 28
    • 84897459662 scopus 로고    scopus 로고
    • Biochemical and functional properties of wheat gliadins: A review
    • Barak, S.; Mudgil, D.; Khatkar, B.S. Biochemical and functional properties of wheat gliadins: A review. Crit. Rev. Food Sci. Nutr. 2015, 55, 357–368.
    • (2015) Crit. Rev. Food Sci. Nutr. , vol.55 , pp. 357-368
    • Barak, S.1    Mudgil, D.2    Khatkar, B.S.3
  • 29
    • 0012171761 scopus 로고    scopus 로고
    • T. Understanding the structure and properties of gluten: An overview
    • Wheat Gluten; Shewry, P.R., Tatham, A.S., Eds.;,: Cambrige, UK
    • Hamer, R.J.; van Vliet, T. Understanding the structure and properties of gluten: An overview. In Wheat Gluten; Shewry, P.R., Tatham, A.S., Eds.; Royal Society of Chemistry: Cambrige, UK, 2000; pp. 125–131.
    • (2000) Royal Society of Chemistry , pp. 125-131
    • Hamer, R.J.1    Vliet, V.2
  • 30
    • 84930044537 scopus 로고    scopus 로고
    • Diversification of the celiac disease alpha-gliadin complex in wheat: A 33-mer peptide with six overlapping epitopes, evolved following polyploidization
    • Ozuna, C.V.; Iehisa, J.C.; Gimenez, M.J.; Alvarez, J.B.; Sousa, C.; Barro, F. Diversification of the celiac disease alpha-gliadin complex in wheat: A 33-mer peptide with six overlapping epitopes, evolved following polyploidization. Plant J. 2015, 82, 794–805.
    • (2015) Plant J , vol.82 , pp. 794-805
    • Ozuna, C.V.1    Iehisa, J.C.2    Gimenez, M.J.3    Alvarez, J.B.4    Sousa, C.5    Barro, F.6
  • 31
    • 0025083155 scopus 로고
    • Conformational studies of peptides corresponding to the coeliac-activating regions of wheat alpha-gliadin
    • Tatham, A.S.; Marsh, M.N.; Wieser, H.; Shewry, P.R. Conformational studies of peptides corresponding to the coeliac-activating regions of wheat alpha-gliadin. Biochem. J. 1990, 270, 313–318.
    • (1990) Biochem. J , vol.270 , pp. 313-318
    • Tatham, A.S.1    Marsh, M.N.2    Wieser, H.3    Shewry, P.R.4
  • 33
    • 84943523260 scopus 로고    scopus 로고
    • Molecular assembly of wheat gliadins into nanostructures: A small-angle X-ray scattering study of gliadins in distilled water over a wide concentration range
    • Sato, N.; Matsumiya, A.; Higashino, Y.; Funaki, S.; Kitao, Y.; Oba, Y.; Inoue, R.; Arisaka, F.; Sugiyama, M.; Urade, R. Molecular assembly of wheat gliadins into nanostructures: A small-angle X-ray scattering study of gliadins in distilled water over a wide concentration range. J. Agric. Food Chem. 2015, 63, 8715–8721.
    • (2015) J. Agric. Food Chem , vol.63 , pp. 8715-8721
    • Sato, N.1    Matsumiya, A.2    Higashino, Y.3    Funaki, S.4    Kitao, Y.5    Oba, Y.6    Inoue, R.7    Arisaka, F.8    Sugiyama, M.9    Urade, R.10
  • 34
    • 84958268069 scopus 로고    scopus 로고
    • Self-organization of gliadin in aqueous media under physiological digestive pHs
    • Herrera, M.G.; Veuthey, T.V.; Dodero, V.I. Self-organization of gliadin in aqueous media under physiological digestive pHs. Colloids Surf. B Biointerfaces 2016, 141, 565–575.
    • (2016) Colloids Surf. B Biointerfaces , vol.141 , pp. 565-575
    • Herrera, M.G.1    Veuthey, T.V.2    Dodero, V.I.3
  • 36
    • 0029328357 scopus 로고
    • Seed storage proteins: Structures and biosynthesis
    • Shewry, P.R.; Napier, J.A.; Tatham, A.S. Seed storage proteins: Structures and biosynthesis. Plant Cell 1995, 7, 945–956.
    • (1995) Plant Cell , vol.7 , pp. 945-956
    • Shewry, P.R.1    Napier, J.A.2    Tatham, A.S.3
  • 38
    • 0002828525 scopus 로고
    • Chromosomal location of genes controlling seed proteins in species related to wheat
    • Lawrence, G.J.; Shepherd, K.W. Chromosomal location of genes controlling seed proteins in species related to wheat. Theor. Appl. Genet. 1981, 59, 25–31.
    • (1981) Theor. Appl. Genet. , vol.59 , pp. 25-31
    • Lawrence, G.J.1    Shepherd, K.W.2
  • 39
    • 0037208926 scopus 로고    scopus 로고
    • The high molecular weight subunits of wheat glutenin and their role in determining wheat processing properties
    • Shewry, P.R.; Halford, N.G.; Tatham, A.S.; Popineau, Y.; Lafiandra, D.; Belton, P.S. The high molecular weight subunits of wheat glutenin and their role in determining wheat processing properties. Adv. Food Nutr. Res. 2003, 45, 219–302.
    • (2003) Adv. Food Nutr. Res. , vol.45 , pp. 219-302
    • Shewry, P.R.1    Halford, N.G.2    Tatham, A.S.3    Popineau, Y.4    Lafiandra, D.5    Belton, P.S.6
  • 40
    • 0000061644 scopus 로고
    • Two-dimensional fractionation of the endosperm proteins of bread wheat (Triticum aestivum): Biochemical and genetic studies
    • Payne, P.I.; Holt, L.M.; Jarvis, G.; Jackson, E.A. Two-dimensional fractionation of the endosperm proteins of bread wheat (Triticum aestivum): Biochemical and genetic studies. Cereal Chem. 1985, 62, 319–326.
    • (1985) Cereal Chem. , vol.62 , pp. 319-326
    • Payne, P.I.1    Holt, L.M.2    Jarvis, G.3    Jackson, E.A.4
  • 41
    • 1542321059 scopus 로고    scopus 로고
    • Expression of epitope-tagged LMW glutenin subunits in the starchy endosperm of transgenic wheat and their incorporation into glutenin polymers
    • Tosi, P.; D’Ovidio, R.; Napier, J.A.; Bekes, F.; Shewry, P.R. Expression of epitope-tagged LMW glutenin subunits in the starchy endosperm of transgenic wheat and their incorporation into glutenin polymers. Theor. Appl. Genet. 2004, 108, 468–476.
    • (2004) Theor. Appl. Genet. , vol.108 , pp. 468-476
    • Tosi, P.1    D’Ovidio, R.2    Napier, J.A.3    Bekes, F.4    Shewry, P.R.5
  • 42
    • 0002459318 scopus 로고    scopus 로고
    • Evidence for the presence of only one cysteine residue in the D-type low molecular weight subunits of wheat glutenin
    • Masci, S.; Egorov, T.A.; Ronchi, C.; Kuzmicky, D.D.; Kasarda, D.D.; Lafiandra, D. Evidence for the presence of only one cysteine residue in the D-type low molecular weight subunits of wheat glutenin. J. Cereal Sci. 1999, 29, 17–25.
    • (1999) J. Cereal Sci , vol.29 , pp. 17-25
    • Masci, S.1    Egorov, T.A.2    Ronchi, C.3    Kuzmicky, D.D.4    Kasarda, D.D.5    Lafiandra, D.6
  • 43
  • 44
    • 0002204477 scopus 로고
    • Linkage of the hordein loci Hor1 and Hor2 with the powdery mildew resistance loci Ml-k and Ml-a on Barley chromosome 5
    • Jensen, J.; Jorgensen, J.H.; Jensen, H.P.; Giese, H.; Doll, H. Linkage of the hordein loci Hor1 and Hor2 with the powdery mildew resistance loci Ml-k and Ml-a on Barley chromosome 5. Theor. Appl. Genet. 1980, 58, 27–31.
    • (1980) Theor. Appl. Genet. , vol.58 , pp. 27-31
    • Jensen, J.1    Jorgensen, J.H.2    Jensen, H.P.3    Giese, H.4    Doll, H.5
  • 45
    • 0002569055 scopus 로고
    • Short tandem repeats shared by B-and C-hordein cDNAs suggest a common evolutionary origin for two groups of cereal storage protein genes
    • Forde, B.G.; Kreis, M.; Williamson, M.S.; Fry, R.P.; Pywell, J.; Shewry, P.R.; Bunce, N.; Miflin, B.J. Short tandem repeats shared by B-and C-hordein cDNAs suggest a common evolutionary origin for two groups of cereal storage protein genes. EMBO J. 1985, 4, 9–15.
    • (1985) EMBO J , vol.4 , pp. 9-15
    • Forde, B.G.1    Kreis, M.2    Williamson, M.S.3    Fry, R.P.4    Pywell, J.5    Shewry, P.R.6    Bunce, N.7    Miflin, B.J.8
  • 46
    • 84877668833 scopus 로고    scopus 로고
    • The B-hordein prolamin family of barley
    • Anderson, O.D. The B-hordein prolamin family of barley. Genome 2013, 56, 179–185.
    • (2013) Genome , vol.56 , pp. 179-185
    • Anderson, O.D.1
  • 47
    • 0027330386 scopus 로고
    • A role for gamma 3 hordein in the transport and targeting of prolamin polypeptides to the vacuole of developing barley endosperm
    • Rechinger, K.B.; Simpson, D.J.; Svendsen, I.; Cameron-Mills, V. A role for gamma 3 hordein in the transport and targeting of prolamin polypeptides to the vacuole of developing barley endosperm. Plant J. 1993, 4, 841–853.
    • (1993) Plant J , vol.4 , pp. 841-853
    • Rechinger, K.B.1    Simpson, D.J.2    Svendsen, I.3    Cameron-Mills, V.4
  • 48
    • 0000983002 scopus 로고
    • Exploring disulphide bond formation in a low molecular weight subunit of glutenin using a baculovirus expression system
    • Thompson, S.; Bishop, D.H.L.; Tatham, A.S.; Shewry, P.R. Exploring disulphide bond formation in a low molecular weight subunit of glutenin using a baculovirus expression system. Gluten Proteins 1994, 345–355.
    • (1994) Gluten Proteins , pp. 345-355
    • Thompson, S.1    Bishop, D.H.L.2    Tatham, A.S.3    Shewry, P.R.4
  • 49
    • 0019824260 scopus 로고
    • The polymorphism and structural homology of storage polypeptides (Hordein) coded by the Hor-2 locus in barley (Hordeum vulgare L.). Biochem
    • Faulks, A.J.; Shewry, P.R.; Miflin, B.J. The polymorphism and structural homology of storage polypeptides (hordein) coded by the Hor-2 locus in barley (Hordeum vulgare L.). Biochem. Genet. 1981, 19, 841–858.
    • (1981) Genet , vol.19 , pp. 841-858
    • Faulks, A.J.1    Shewry, P.R.2    Miflin, B.J.3
  • 51
    • 0026794955 scopus 로고
    • Small-angle X-ray-scattering studies of the C hordeins of barley (Hordeum vulgare)
    • I’Anson, K.J.; Morris, V.J.; Shewry, P.R.; Tatham, A.S. Small-angle X-ray-scattering studies of the C hordeins of barley (Hordeum vulgare). Biochem. J. 1992, 287, 183–185.
    • (1992) Biochem. J. , vol.287 , pp. 183-185
    • I’Anson, K.J.1    Morris, V.J.2    Shewry, P.R.3    Tatham, A.S.4
  • 52
    • 0007564053 scopus 로고
    • Protein body formation in the developing barley endosperm
    • Cameron-Mills, V.; von Wettstein, D. Protein body formation in the developing barley endosperm. Carlsberg Res. Commun. 1980, 45, 577–594.
    • (1980) Carlsberg Res. Commun. , vol.45 , pp. 577-594
    • Cameron-Mills, V.1    Von Wettstein, D.2
  • 54
    • 0026526122 scopus 로고
    • Restriction fragment analysis of the secalin loci of rye
    • Hull, G.; Sabelli, P.A.; Shewry, P.R. Restriction fragment analysis of the secalin loci of rye. Biochem. Genet. 1992, 30, 85–97.
    • (1992) Biochem. Genet. , vol.30 , pp. 85-97
    • Hull, G.1    Sabelli, P.A.2    Shewry, P.R.3
  • 55
    • 84908587313 scopus 로고    scopus 로고
    • Variation of high-molecular-weight secalin subunit composition in Rye (Secale cereale L.) inbred lines
    • Salmanowicz, B.P.; Langner, M.; Kubicka-Matusiewicz, H. Variation of high-molecular-weight secalin subunit composition in Rye (Secale cereale L.) inbred lines. J. Agric. Food Chem. 2014, 62, 10535–10541.
    • (2014) J. Agric. Food Chem. , vol.62 , pp. 10535-10541
    • Salmanowicz, B.P.1    Langner, M.2    Kubicka-Matusiewicz, H.3
  • 57
    • 0000854747 scopus 로고
    • Linkage mapping of genes for resistance to leaf, stem and stripe rusts and omega-secalins on the short arm of rye chromosome 1R
    • Singh, N.K.; Shepherd, K.W.; McIntosh, R.A. Linkage mapping of genes for resistance to leaf, stem and stripe rusts and omega-secalins on the short arm of rye chromosome 1R. Theor. Appl. Genet. 1990, 80, 609–616.
    • (1990) Theor. Appl. Genet. , vol.80 , pp. 609-616
    • Singh, N.K.1    Shepherd, K.W.2    McIntosh, R.A.3
  • 58
    • 0030460180 scopus 로고    scopus 로고
    • The Sec-1 locus on the short arm of chromosome 1R of rye (Secale cereale)
    • Clarke, B.C.; Mukai, Y.; Appels, R. The Sec-1 locus on the short arm of chromosome 1R of rye (Secale cereale). Chromosoma 1996, 105, 269–275.
    • (1996) Chromosoma , vol.105 , pp. 269-275
    • Clarke, B.C.1    Mukai, Y.2    Appels, R.3
  • 59
    • 13844311574 scopus 로고    scopus 로고
    • High-resolution physical mapping of the secalin-1 locus of rye on extended DNA fibers. Cytogenet
    • Yamamoto, M.; Mukai, Y. High-resolution physical mapping of the secalin-1 locus of rye on extended DNA fibers. Cytogenet. Genome Res. 2005, 109, 79–82.
    • (2005) Genome Res , vol.109 , pp. 79-82
    • Yamamoto, M.1    Mukai, Y.2
  • 60
    • 78649776880 scopus 로고    scopus 로고
    • Characterization of !-secalin genes from rye, triticale, and a wheat 1BL/1RS translocation line
    • Jiang, Q.T.; Wei, Y.M.; Andre, L.; Lu, Z.X.; Pu, Z.E.; Peng, Y.Y.; Zheng, Y.L. Characterization of !-secalin genes from rye, triticale, and a wheat 1BL/1RS translocation line. J. Appl. Genet. 2010, 51, 403–411.
    • (2010) J. Appl. Genet. , vol.51 , pp. 403-411
    • Jiang, Q.T.1    Wei, Y.M.2    Andre, L.3    Lu, Z.X.4    Pu, Z.E.5    Peng, Y.Y.6    Zheng, Y.L.7
  • 61
    • 84885077358 scopus 로고    scopus 로고
    • The genotypic and phenotypic interaction of wheat and rye storage proteins in primary triticale
    • Dennett, A.L.; Cooper, K.V.; Trethowan, R.M. The genotypic and phenotypic interaction of wheat and rye storage proteins in primary triticale. Euphytica 2013, 194, 235–242.
    • (2013) Euphytica , vol.194 , pp. 235-242
    • Dennett, A.L.1    Cooper, K.V.2    Trethowan, R.M.3
  • 63
    • 0024720616 scopus 로고
    • Analysis of avenin proteins and the expression of their mRNAs in developing oat seeds
    • Chesnut, R.S.; Shotwell, M.A.; Boyer, S.K.; Larkins, B.A. Analysis of avenin proteins and the expression of their mRNAs in developing oat seeds. Plant Cell 1989, 1, 913–924.
    • (1989) Plant Cell , vol.1 , pp. 913-924
    • Chesnut, R.S.1    Shotwell, M.A.2    Boyer, S.K.3    Larkins, B.A.4
  • 64
    • 0029140485 scopus 로고
    • Reversed-phase high-performance liquid chromatography of oat proteins: Application of cultivar comparison and analysis of the effect of wet processing
    • Lapvetelainen, A.; Bietz, J.; Huebner, F. Reversed-phase high-performance liquid chromatography of oat proteins: Application of cultivar comparison and analysis of the effect of wet processing. Cereal Chem. 1995, 72, 259–264.
    • (1995) Cereal Chem , vol.72 , pp. 259-264
    • Lapvetelainen, A.1    Bietz, J.2    Huebner, F.3
  • 65
    • 0027963588 scopus 로고
    • The complete amino acid sequence and disulphide bond arrangement of oat alcohol-soluble avenin-3
    • Egorov, T.A.; Musolyamov, A.K.; Andersen, J.S.; Roepstorff, P. The complete amino acid sequence and disulphide bond arrangement of oat alcohol-soluble avenin-3. Eur. J. Biochem. 1994, 224, 631–638.
    • (1994) Eur. J. Biochem , vol.224 , pp. 631-638
    • Egorov, T.A.1    Musolyamov, A.K.2    Andersen, J.S.3    Roepstorff, P.4
  • 67
    • 0001356151 scopus 로고
    • Immunolocalization of avenin and globulin storage proteins in developing endosperm of Avena sativa L
    • Lending, C.R.; Chesnut, R.S.; Shaw, K.L.; Larkins, B.A. Immunolocalization of avenin and globulin storage proteins in developing endosperm of Avena sativa L. Planta 1989, 178, 315–324.
    • (1989) Planta , vol.178 , pp. 315-324
    • Lending, C.R.1    Chesnut, R.S.2    Shaw, K.L.3    Larkins, B.A.4
  • 70
    • 16244391425 scopus 로고    scopus 로고
    • Neurologic presentation of celiac disease
    • Bushara, K.O. Neurologic presentation of celiac disease. Gastroenterology 2005, 128, S92–S97.
    • (2005) Gastroenterology , vol.128 , pp. S92-S97
    • Bushara, K.O.1
  • 73
    • 0035725287 scopus 로고    scopus 로고
    • Rye gamma-70 and gamma-35 secalins and barley gamma-3 hordein cross-react with omega-5 gliadin, a major allergen in wheat-dependent, exercise-induced anaphylaxis
    • Palosuo, K.; Alenius, H.; Varjonen, E.; Kalkkinen, N.; Reunala, T. Rye gamma-70 and gamma-35 secalins and barley gamma-3 hordein cross-react with omega-5 gliadin, a major allergen in wheat-dependent, exercise-induced anaphylaxis. Clin. Exp. Allergy 2001, 31, 466–473.
    • (2001) Clin. Exp. Allergy , vol.31 , pp. 466-473
    • Palosuo, K.1    Alenius, H.2    Varjonen, E.3    Kalkkinen, N.4    Reunala, T.5
  • 74
    • 45949121835 scopus 로고
    • Immunochemical relationships of the prolamin storage proteins of barley, wheat, rye and oat
    • Festenstein, G.W.; Hay, F.C.; Shewry, P.R. Immunochemical relationships of the prolamin storage proteins of barley, wheat, rye and oat. Biochim. Biophys. Acta 1987, 912, 371–383.
    • (1987) Biochim. Biophys. Acta , vol.912 , pp. 371-383
    • Festenstein, G.W.1    Hay, F.C.2    Shewry, P.R.3
  • 77
    • 84888364673 scopus 로고    scopus 로고
    • Oats in the diet of children with celiac disease: Preliminary results of a double-blind, randomized, placebo-controlled multicenter Italian study
    • Gatti, S.; Caporelli, N.; Galeazzi, T.; Francavilla, R.; Barbato, M.; Roggero, P.; Malamisura, B.; Iacono, G.; Budelli, A.; Gesuita, R., et al. Oats in the diet of children with celiac disease: Preliminary results of a double-blind, randomized, placebo-controlled multicenter Italian study. Nutrients 2013, 5, 4653–4664.
    • (2013) Nutrients , vol.5 , pp. 4653-4664
    • Gatti, S.1    Caporelli, N.2    Galeazzi, T.3    Francavilla, R.4    Barbato, M.5    Roggero, P.6    Malamisura, B.7    Iacono, G.8    Budelli, A.9    Gesuita, R.10
  • 78
    • 0029899086 scopus 로고    scopus 로고
    • Relation between gliadin structure and coeliac toxicity
    • Wieser, H. Relation between gliadin structure and coeliac toxicity. Acta Paediatr. 1996, 85, 3–9.
    • (1996) Acta Paediatr , vol.85 , pp. 3-9
    • Wieser, H.1
  • 79
    • 84920159588 scopus 로고    scopus 로고
    • Ingestion of oats and barley in patients with celiac disease mobilizes cross-reactive T cells activated by avenin peptides and immuno-dominant hordein peptides
    • Hardy, M.Y.; Tye-Din, J.A.; Stewart, J.A.; Schmitz, F.; Dudek, N.L.; Hanchapola, I.; Purcell, A.W.; Anderson, R.P. Ingestion of oats and barley in patients with celiac disease mobilizes cross-reactive T cells activated by avenin peptides and immuno-dominant hordein peptides. J. Autoimmun. 2015, 56, 56–65.
    • (2015) J. Autoimmun , vol.56 , pp. 56-65
    • Hardy, M.Y.1    Tye-Din, J.A.2    Stewart, J.A.3    Schmitz, F.4    Dudek, N.L.5    Hanchapola, I.6    Purcell, A.W.7    Anderson, R.P.8
  • 81
  • 82
    • 20444446016 scopus 로고    scopus 로고
    • The immune recognition of gluten in coeliac disease. Clin. Exp
    • Ciccocioppo, R.; Di Sabatino, A.; Corazza, G.R. The immune recognition of gluten in coeliac disease. Clin. Exp. Immunol. 2005, 140, 408–416.
    • (2005) Immunol , vol.140 , pp. 408-416
    • Ciccocioppo, R.1    Di Sabatino, A.2    Corazza, G.R.3
  • 84
    • 84992136239 scopus 로고    scopus 로고
    • Endocytosis and transcytosis of gliadin peptides
    • Barone, M.V.; Zimmer, K.P. Endocytosis and transcytosis of gliadin peptides. Mol. Cell. Pediatr. 2016, 3, 8.
    • (2016) Mol. Cell. Pediatr. , vol.3 , pp. 8
    • Barone, M.V.1    Zimmer, K.P.2
  • 85
    • 84886689192 scopus 로고    scopus 로고
    • Circular dichroism and electron microscopy studies in vitro of 33-mer gliadin peptide revealed secondary structure transition and supramolecular organization
    • Herrera, M.G.; Zamarreno, F.; Costabel, M.; Ritacco, H.; Hutten, A.; Sewald, N.; Dodero, V.I. Circular dichroism and electron microscopy studies in vitro of 33-mer gliadin peptide revealed secondary structure transition and supramolecular organization. Biopolymers 2014, 101, 96–106.
    • (2014) Biopolymers , vol.101 , pp. 96-106
    • Herrera, M.G.1    Zamarreno, F.2    Costabel, M.3    Ritacco, H.4    Hutten, A.5    Sewald, N.6    Dodero, V.I.7
  • 87
    • 84865462532 scopus 로고    scopus 로고
    • Interactions among secretory immunoglobulin A, CD71, and transglutaminase-2 affect permeability of intestinal epithelial cells to gliadin peptides
    • Lebreton, C.; Menard, S.; Abed, J.; Moura, I.C.; Coppo, R.; Dugave, C.; Monteiro, R.C.; Fricot, A.; Traore, M.G.; Griffin, M., et al. Interactions among secretory immunoglobulin A, CD71, and transglutaminase-2 affect permeability of intestinal epithelial cells to gliadin peptides. Gastroenterology 2012, 143, 698–707.
    • (2012) Gastroenterology , vol.143 , pp. 698-707
    • Lebreton, C.1    Menard, S.2    Abed, J.3    Moura, I.C.4    Coppo, R.5    Dugave, C.6    Monteiro, R.C.7    Fricot, A.8    Traore, M.G.9    Griffin, M.10
  • 88
    • 77956337677 scopus 로고    scopus 로고
    • Visualization of transepithelial passage of the immunogenic 33-residue peptide from alpha-2 gliadin in gluten-sensitive macaques
    • Mazumdar, K.; Alvarez, X.; Borda, J.T.; Dufour, J.; Martin, E.; Bethune, M.T.; Khosla, C.; Sestak, K. Visualization of transepithelial passage of the immunogenic 33-residue peptide from alpha-2 gliadin in gluten-sensitive macaques. PLoS ONE 2010, 5, e10228.
    • (2010) Plos ONE , vol.5
    • Mazumdar, K.1    Alvarez, X.2    Borda, J.T.3    Dufour, J.4    Martin, E.5    Bethune, M.T.6    Khosla, C.7    Sestak, K.8
  • 89
    • 17144416534 scopus 로고    scopus 로고
    • No evidence of cross-reactivity of human antibodies to a 33-mer peptide of the alpha-gliadin component of gluten with Bordetella pertussis pertactin
    • He, Q.; Viljanen, M.K.; Hinkkanen, A.E.; Arvilommi, H.; Mertsola, J.; Viander, M. No evidence of cross-reactivity of human antibodies to a 33-mer peptide of the alpha-gliadin component of gluten with Bordetella pertussis pertactin. Vaccine 2005, 23, 3336–3340.
    • (2005) Vaccine , vol.23 , pp. 3336-3340
    • He, Q.1    Viljanen, M.K.2    Hinkkanen, A.E.3    Arvilommi, H.4    Mertsola, J.5    Viander, M.6
  • 92
    • 0034066695 scopus 로고    scopus 로고
    • In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope
    • Anderson, R.P.; Degano, P.; Godkin, A.J.; Jewell, D.P.; Hill, A.V. In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope. Nat. Med. 2000, 6, 337–342.
    • (2000) Nat. Med. , vol.6 , pp. 337-342
    • Anderson, R.P.1    Degano, P.2    Godkin, A.J.3    Jewell, D.P.4    Hill, A.V.5
  • 94
    • 29144484021 scopus 로고    scopus 로고
    • A systematic approach for comprehensive T-cell epitope discovery using peptide libraries
    • Beissbarth, T.; Tye-Din, J.A.; Smyth, G.K.; Speed, T.P.; Anderson, R.P. A systematic approach for comprehensive T-cell epitope discovery using peptide libraries. Bioinformatics 2005, 21 (Suppl. 1), i29–i37.
    • (2005) Bioinformatics , vol.21 , pp. i29-i37
    • Beissbarth, T.1    Tye-Din, J.A.2    Smyth, G.K.3    Speed, T.P.4    Anderson, R.P.5
  • 95
    • 84861120545 scopus 로고    scopus 로고
    • Repertoire of gluten peptides active in celiac disease patients: Perspectives for translational therapeutic applications
    • Camarca, A.; Del Mastro, A.; Gianfrani, C. Repertoire of gluten peptides active in celiac disease patients: Perspectives for translational therapeutic applications. Endocr. Metab. Immune Disord. Drug Targets 2012, 12, 207–219.
    • (2012) Endocr. Metab. Immune Disord. Drug Targets , vol.12 , pp. 207-219
    • Camarca, A.1    Del Mastro, A.2    Gianfrani, C.3
  • 97
    • 84943601269 scopus 로고    scopus 로고
    • Food allergy: Common causes, diagnosis, and treatment
    • Patel, B.Y.; Volcheck, G.W. Food allergy: Common causes, diagnosis, and treatment. Mayo Clin. Proc. 2015, 90, 1411–1419.
    • (2015) Mayo Clin. Proc. , vol.90 , pp. 1411-1419
    • Patel, B.Y.1    Volcheck, G.W.2
  • 98
    • 11344286028 scopus 로고    scopus 로고
    • Oral tolerance and its relation to food hypersensitivities
    • Chehade, M.; Mayer, L. Oral tolerance and its relation to food hypersensitivities. J. Allergy Clin. Immunol. 2005, 115, 3–12.
    • (2005) J. Allergy Clin. Immunol. , vol.115 , pp. 3-12
    • Chehade, M.1    Mayer, L.2
  • 99
    • 84944172687 scopus 로고    scopus 로고
    • Common food allergens and their IgE-binding epitopes
    • Matsuo, H.; Yokooji, T.; Taogoshi, T. Common food allergens and their IgE-binding epitopes. Allergol. Int. 2015, 64, 332–343.
    • (2015) Allergol. Int. , vol.64 , pp. 332-343
    • Matsuo, H.1    Yokooji, T.2    Taogoshi, T.3
  • 100
    • 54849430360 scopus 로고    scopus 로고
    • Allergens to wheat and related cereals
    • Tatham, A.S.; Shewry, P.R. Allergens to wheat and related cereals. Clin. Exp. Allergy 2008, 38, 1712–1726.
    • (2008) Clin. Exp. Allergy , vol.38 , pp. 1712-1726
    • Tatham, A.S.1    Shewry, P.R.2
  • 101
    • 48349136221 scopus 로고    scopus 로고
    • The role of wheat omega-5 gliadin IgE antibodies as a diagnostic tool for wheat allergy in childhood
    • Beyer, K.; Chung, D.; Schulz, G.; Mishoe, M.; Niggemann, B.; Wahn, U.; Sampson, H.A. The role of wheat omega-5 gliadin IgE antibodies as a diagnostic tool for wheat allergy in childhood. J. Allergy Clin. Immunol. 2008, 122, 419–421.
    • (2008) J. Allergy Clin. Immunol , vol.122 , pp. 419-421
    • Beyer, K.1    Chung, D.2    Schulz, G.3    Mishoe, M.4    Niggemann, B.5    Wahn, U.6    Sampson, H.A.7
  • 102
    • 12444344811 scopus 로고    scopus 로고
    • IgE-binding abilities of pentapeptides, QQPFP and PQQPF, in wheat gliadin
    • Tanabe, S. IgE-binding abilities of pentapeptides, QQPFP and PQQPF, in wheat gliadin. J. Nutr. Sci. Vitaminol. (Tokyo) 2004, 50, 367–370.
    • (2004) J. Nutr. Sci. Vitaminol. (Tokyo) , vol.50 , pp. 367-370
    • Tanabe, S.1
  • 104
    • 84901301250 scopus 로고    scopus 로고
    • An Italian prospective multicenter survey on patients suspected of having non-celiac gluten sensitivity
    • The Study Group for Non-Celiac Gluten Sensitivity
    • Volta, U.; Bardella, M.T.; Calabro, A.; Troncone, R.; Corazza, G.R.; The Study Group for Non-Celiac Gluten Sensitivity. An Italian prospective multicenter survey on patients suspected of having non-celiac gluten sensitivity. BMC Med. 2014, 12, 85.
    • (2014) BMC Med , vol.12 , pp. 85
    • Volta, U.1    Bardella, M.T.2    Calabro, A.3    Troncone, R.4    Corazza, G.R.5
  • 111
    • 84870833287 scopus 로고    scopus 로고
    • Non-celiac wheat sensitivity: Separating the wheat from the chat
    • Sanders, D.S.; Aziz, I. Non-celiac wheat sensitivity: Separating the wheat from the chat! Am. J. Gastroenterol. 2012, 107, 1908–1912.
    • (2012) Am. J. Gastroenterol , vol.107 , pp. 1908-1912
    • Sanders, D.S.1    Aziz, I.2
  • 112
    • 84949604600 scopus 로고    scopus 로고
    • The overlap between irritable bowel syndrome and non-celiac gluten sensitivity: A clinical dilemma
    • Makharia, A.; Catassi, C.; Makharia, G.K. The overlap between irritable bowel syndrome and non-celiac gluten sensitivity: A clinical dilemma. Nutrients 2015, 7, 10417–10426.
    • (2015) Nutrients , vol.7 , pp. 10417-10426
    • Makharia, A.1    Catassi, C.2    Makharia, G.K.3
  • 113
    • 84946920250 scopus 로고    scopus 로고
    • Celiac disease genomic, environmental, microbiome, and metabolomic (CDGEMM) study design: Approach to the future of personalized prevention of celiac disease
    • Leonard, M.M.; Camhi, S.; Huedo-Medina, T.B.; Fasano, A. Celiac disease genomic, environmental, microbiome, and metabolomic (CDGEMM) study design: Approach to the future of personalized prevention of celiac disease. Nutrients 2015, 7, 9325–9336.
    • (2015) Nutrients , vol.7 , pp. 9325-9336
    • Leonard, M.M.1    Camhi, S.2    Huedo-Medina, T.B.3    Fasano, A.4
  • 114
    • 84962079721 scopus 로고    scopus 로고
    • The microbiome as a possible target to prevent celiac disease
    • Leonard, M.M.; Fasano, A. The microbiome as a possible target to prevent celiac disease. Expert Rev. Gastroenterol. Hepatol. 2016, 10, 555–556.
    • (2016) Expert Rev. Gastroenterol. Hepatol. , vol.10 , pp. 555-556
    • Leonard, M.M.1    Fasano, A.2
  • 116
    • 84887835185 scopus 로고    scopus 로고
    • Gluten-free diet in children: An approach to a nutritionally adequate and balanced diet
    • Penagini, F.; Dilillo, D.; Meneghin, F.; Mameli, C.; Fabiano, V.; Zuccotti, G.V. Gluten-free diet in children: An approach to a nutritionally adequate and balanced diet. Nutrients 2013, 5, 4553–4565.
    • (2013) Nutrients , vol.5 , pp. 4553-4565
    • Penagini, F.1    Dilillo, D.2    Meneghin, F.3    Mameli, C.4    Fabiano, V.5    Zuccotti, G.V.6
  • 117
    • 79952015315 scopus 로고    scopus 로고
    • The gluten-free diet: Safety and nutritional quality
    • Saturni, L.; Ferretti, G.; Bacchetti, T. The gluten-free diet: Safety and nutritional quality. Nutrients 2010, 2, 16–34.
    • (2010) Nutrients , vol.2 , pp. 16-34
    • Saturni, L.1    Ferretti, G.2    Bacchetti, T.3
  • 119
    • 62849114219 scopus 로고    scopus 로고
    • Clinical trial: B vitamins improve health in patients with coeliac disease living on a gluten-free diet. Aliment. Pharmacol
    • Hallert, C.; Svensson, M.; Tholstrup, J.; Hultberg, B. Clinical trial: B vitamins improve health in patients with coeliac disease living on a gluten-free diet. Aliment. Pharmacol. Ther. 2009, 29, 811–816.
    • (2009) Ther , vol.29 , pp. 811-816
    • Hallert, C.1    Svensson, M.2    Tholstrup, J.3    Hultberg, B.4
  • 121
    • 84887582602 scopus 로고    scopus 로고
    • Appropriate nutrient supplementation in celiac disease
    • Caruso, R.; Pallone, F.; Stasi, E.; Romeo, S.; Monteleone, G. Appropriate nutrient supplementation in celiac disease. Ann. Med. 2013, 45, 522–531.
    • (2013) Ann. Med , vol.45 , pp. 522-531
    • Caruso, R.1    Pallone, F.2    Stasi, E.3    Romeo, S.4    Monteleone, G.5
  • 123
    • 84893320042 scopus 로고    scopus 로고
    • Cereal-based gluten-free food: How to reconcile nutritional and technological properties of wheat proteins with safety for celiac disease patients
    • Lamacchia, C.; Camarca, A.; Picascia, S.; Di Luccia, A.; Gianfrani, C. Cereal-based gluten-free food: How to reconcile nutritional and technological properties of wheat proteins with safety for celiac disease patients. Nutrients 2014, 6, 575–590.
    • (2014) Nutrients , vol.6 , pp. 575-590
    • Lamacchia, C.1    Camarca, A.2    Picascia, S.3    Di Luccia, A.4    Gianfrani, C.5
  • 125
    • 84868699661 scopus 로고    scopus 로고
    • Novel therapeutic/integrative approaches for celiac disease and dermatitis herpetiformis
    • Fasano, A. Novel therapeutic/integrative approaches for celiac disease and dermatitis herpetiformis. Clin. Dev. Immunol. 2012, 2012, 959061.
    • (2012) Clin. Dev. Immunol. , vol.2012
    • Fasano, A.1
  • 126
    • 84952945695 scopus 로고    scopus 로고
    • Plant proteases involved in regulated cell death
    • Zamyatnin, A.A., Jr. Plant proteases involved in regulated cell death. Biochemistry 2015, 80, 1701–1715.
    • (2015) Biochemistry , vol.80 , pp. 1701-1715
    • Zamyatnin, A.A.1
  • 127
    • 79953294138 scopus 로고    scopus 로고
    • Fungal proteases and their pathophysiological effects
    • Yike, I. Fungal proteases and their pathophysiological effects. Mycopathologia 2011, 171, 299–323.
    • (2011) Mycopathologia , vol.171 , pp. 299-323
    • Yike, I.1
  • 128
    • 80053333971 scopus 로고    scopus 로고
    • Papain-like proteases of Staphylococcus aureus
    • Kantyka, T.; Shaw, L.N.; Potempa, J. Papain-like proteases of Staphylococcus aureus. Adv. Exp. Med. Biol. 2011, 712, 1–14.
    • (2011) Adv. Exp. Med. Biol , vol.712 , pp. 1-14
    • Kantyka, T.1    Shaw, L.N.2    Potempa, J.3
  • 129
    • 84855362153 scopus 로고    scopus 로고
    • Oral enzyme therapy for celiac sprue
    • Bethune, M.T.; Khosla, C. Oral enzyme therapy for celiac sprue. Methods Enzymol. 2012, 502, 241–271.
    • (2012) Methods Enzymol , vol.502 , pp. 241-271
    • Bethune, M.T.1    Khosla, C.2
  • 130
    • 85047688442 scopus 로고    scopus 로고
    • Detoxification of gluten by means of enzymatic treatment
    • Wieser, H.; Koehler, P. Detoxification of gluten by means of enzymatic treatment. J. AOAC Int. 2012, 95, 356–363.
    • (2012) J. AOAC Int , vol.95 , pp. 356-363
    • Wieser, H.1    Koehler, P.2
  • 131
    • 84974703341 scopus 로고    scopus 로고
    • Prospects of Developing Medicinal Therapeutic strategies and pharmaceutical design for effective gluten intolerance treatment
    • Savvateeva, L.V.; Zamyatnin, A.A. Prospects of Developing Medicinal Therapeutic strategies and pharmaceutical design for effective gluten intolerance treatment. Curr. Pharm. Des. 2016, 22, 2439–2449.
    • (2016) Curr. Pharm. Des. , vol.22 , pp. 2439-2449
    • Savvateeva, L.V.1    Zamyatnin, A.A.2
  • 133
    • 33745455375 scopus 로고    scopus 로고
    • Heterologous expression, purification, refolding, and structural-functional characterization of EP-B2, a self-activating barley cysteine endoprotease
    • Bethune, M.T.; Strop, P.; Tang, Y.; Sollid, L.M.; Khosla, C. Heterologous expression, purification, refolding, and structural-functional characterization of EP-B2, a self-activating barley cysteine endoprotease. Chem. Biol. 2006, 13, 637–647.
    • (2006) Chem. Biol. , vol.13 , pp. 637-647
    • Bethune, M.T.1    Strop, P.2    Tang, Y.3    Sollid, L.M.4    Khosla, C.5
  • 137
    • 76049115164 scopus 로고    scopus 로고
    • The effects of ALV003 pre-digestion of gluten on immune response and symptoms in celiac disease in vivo. Clin
    • Tye-Din, J.A.; Anderson, R.P.; Ffrench, R.A.; Brown, G.J.; Hodsman, P.; Siegel, M.; Botwick, W.; Shreeniwas, R. The effects of ALV003 pre-digestion of gluten on immune response and symptoms in celiac disease in vivo. Clin. Immunol. 2010, 134, 289–295.
    • (2010) Immunol , vol.134 , pp. 289-295
    • Tye-Din, J.A.1    Anderson, R.P.2    Ffrench, R.A.3    Brown, G.J.4    Hodsman, P.5    Siegel, M.6    Botwick, W.7    Shreeniwas, R.8
  • 139
    • 84855503091 scopus 로고    scopus 로고
    • Transformation of the US bread wheat ‘Butte 86‘and silencing of omega-5 gliadin genes
    • Altenbach, S.B.; Allen, P.V. Transformation of the US bread wheat ‘Butte 86‘and silencing of omega-5 gliadin genes. GM Crops 2011, 2, 66–73.
    • (2011) GM Crops , vol.2 , pp. 66-73
    • Altenbach, S.B.1    Allen, P.V.2
  • 140
    • 78049267205 scopus 로고    scopus 로고
    • Effective shutdown in the expression of celiac disease-related wheat gliadin T-cell epitopes by RNA interference
    • Gil-Humanes, J.; Piston, F.; Tollefsen, S.; Sollid, L.M.; Barro, F. Effective shutdown in the expression of celiac disease-related wheat gliadin T-cell epitopes by RNA interference. Proc. Natl. Acad. Sci. USA 2010, 107, 17023–17028.
    • (2010) Proc. Natl. Acad. Sci. USA , vol.107 , pp. 17023-17028
    • Gil-Humanes, J.1    Piston, F.2    Tollefsen, S.3    Sollid, L.M.4    Barro, F.5
  • 143
    • 0035019083 scopus 로고    scopus 로고
    • Cells from celiac disease lesions recognize gliadin epitopes deamidated in situ by endogenous tissue transglutaminase
    • Molberg, O.; McAdam, S.; Lundin, K.E.; Kristiansen, C.; Arentz-Hansen, H.; Kett, K.; Sollid, L.M. T cells from celiac disease lesions recognize gliadin epitopes deamidated in situ by endogenous tissue transglutaminase. Eur. J. Immunol. 2001, 31, 1317–1323.
    • (2001) Eur. J. Immunol , vol.31 , pp. 1317-1323
    • Molberg, O.1    McAdam, S.2    Lundin, K.E.3    Kristiansen, C.4    Arentz-Hansen, H.5    Kett, K.6    Sollid, L.7
  • 145
    • 34547852241 scopus 로고    scopus 로고
    • The safety, tolerance, pharmacokinetic and pharmacodynamic effects of single doses of AT-1001 in coeliac disease subjects: A proof of concept study
    • Paterson, B.M.; Lammers, K.M.; Arrieta, M.C.; Fasano, A.; Meddings, J.B. The safety, tolerance, pharmacokinetic and pharmacodynamic effects of single doses of AT-1001 in coeliac disease subjects: A proof of concept study. Aliment. Pharmacol. Ther. 2007, 26, 757–766.
    • (2007) Aliment. Pharmacol. Ther. , vol.26 , pp. 757-766
    • Paterson, B.M.1    Lammers, K.M.2    Arrieta, M.C.3    Fasano, A.4    Meddings, J.B.5
  • 146
    • 17644401678 scopus 로고    scopus 로고
    • Peptide-based therapeutic vaccines for allergic and autoimmune diseases
    • Larche, M.; Wraith, D.C. Peptide-based therapeutic vaccines for allergic and autoimmune diseases. Nat. Med. 2005, 11, S69–S76.
    • (2005) Nat. Med. , vol.11 , pp. S69-S76
    • Larche, M.1    Wraith, D.C.2


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