메뉴 건너뛰기




Volumn 8, Issue 4, 2013, Pages 445-457

Latest in vitro and in vivo models of celiac disease

Author keywords

Celiac; Gliadin; Gluten; in vitro; in vivo; Model; Monkey; Mouse; Rat; T cell; Therapy; Treatment

Indexed keywords

CHEMOKINE RECEPTOR CCR9; GAMMA INTERFERON; GLIADIN; GLUTEN; INTERLEUKIN 10; INTERLEUKIN 12; INTERLEUKIN 15; INTERLEUKIN 1BETA; INTERLEUKIN 6; INTERLEUKIN 8; LARAZOTIDE; MACROPHAGE INFLAMMATORY PROTEIN 3BETA; MAJOR HISTOCOMPATIBILITY ANTIGEN CLASS 2; NEXVAX2; SECONDARY LYMPHOID TISSUE CHEMOKINE; TUMOR NECROSIS FACTOR ALPHA; UNCLASSIFIED DRUG; VACCINE; VERCIRNON;

EID: 84875393818     PISSN: 17460441     EISSN: 1746045X     Source Type: Journal    
DOI: 10.1517/17460441.2013.761203     Document Type: Review
Times cited : (24)

References (114)
  • 1
    • 67649200339 scopus 로고    scopus 로고
    • Increased prevalence and mortality in undiagnosed celiac disease
    • Rubio-Tapia A, Kyle RA, Kaplan EL, et al. Increased prevalence and mortality in undiagnosed celiac disease. Gastroenterology 2009;137(1):88-93
    • (2009) Gastroenterology , vol.137 , Issue.1 , pp. 88-93
    • Rubio-Tapia, A.1    Kyle, R.A.2    Kaplan, E.L.3
  • 2
    • 33748323039 scopus 로고    scopus 로고
    • Mechanisms of disease: Immunopathogenesis of celiac disease
    • Jabri B, Sollid LM. Mechanisms of disease: immunopathogenesis of celiac disease. Nat Clin Pract Gastroenterol Hepatol 2006;3(9):516-25
    • (2006) Nat Clin Pract Gastroenterol Hepatol , vol.3 , Issue.9 , pp. 516-525
    • Jabri, B.1    Sollid, L.M.2
  • 3
    • 78751699186 scopus 로고    scopus 로고
    • Zonulin and Its Regulation of Intestinal Barrier Function: The Biological Door to Inflammation Autoimmunity and Cancer
    • Fasano A. Zonulin and its regulation of intestinal barrier function: the biological door to inflammation, autoimmunity, and cancer. Physiol Rev 2011;91(1):151-75
    • (2011) Physiol Rev , vol.91 , Issue.1 , pp. 151-175
    • Fasano, A.1
  • 4
    • 84857634950 scopus 로고    scopus 로고
    • T-cell Response to Gluten in Patients with HLA-DQ2.2 Reveals Requirement of Peptide-MHC Stability in Celiac Disease
    • Bodd M, Kim CY, Lundin KE, Sollid LM. T-cell response to gluten in patients with HLA-DQ2.2 reveals requirement of peptide-MHC stability in celiac disease. Gastroenterology 2012;142(3):552-61
    • (2012) Gastroenterology , vol.142 , Issue.3 , pp. 552-561
    • Bodd, M.1    Kim, C.Y.2    Lundin, K.E.3    Sollid, L.M.4
  • 5
    • 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 SN, Korner R, et al. Tissue transglutaminase selectively modifies gliadin peptides that are recognized by gut-derived T cells in celiac disease. Nat Med 1998;4(6):713-17
    • (1998) Nat Med , vol.4 , Issue.6 , pp. 713-717
    • Molberg, O.1    McAdam, S.N.2    Korner, R.3
  • 6
    • 79953057255 scopus 로고    scopus 로고
    • Integration of genetic and immunological insights into a model of celiac disease pathogenesis
    • Abadie V, Sollid LM, Barreiro LB, Jabri B. Integration of genetic and immunological insights into a model of celiac disease pathogenesis. Annu Rev Immunol 2011;29:493-525
    • (2011) Annu Rev Immunol , vol.29 , pp. 493-49525
    • Abadie, V.1    Sollid, L.M.2    Barreiro, L.B.3    Jabri, B.4
  • 7
    • 3343010394 scopus 로고    scopus 로고
    • Gliadin stimulates human monocytes to production of IL-8 and TNF-alpha through a mechanism involving NF-kappaB
    • Jelinkova L, Tuckova L, Cinova J, et al. Gliadin stimulates human monocytes to production of IL-8 and TNF-alpha through a mechanism involving NF-kappaB. FEBS Lett 2004;571(1-3):81-5
    • (2004) FEBS Lett , vol.571 , Issue.1-3 , pp. 81-85
    • Jelinkova, L.1    Tuckova, L.2    Cinova, J.3
  • 8
    • 27744526778 scopus 로고    scopus 로고
    • Gliadin fragments induce phenotypic and functional maturation of human dendritic cells
    • Palova-Jelinkova L, Rozkova D, Pecharova B, et al. Gliadin fragments induce phenotypic and functional maturation of human dendritic cells. J Immunol 2005;175(10):7038-45
    • (2005) J Immunol , vol.175 , Issue.10 , pp. 7038-7045
    • Palova-Jelinkova, L.1    Rozkova, D.2    Pecharova, B.3
  • 9
    • 79952218606 scopus 로고    scopus 로고
    • Gliadin-mediated Proliferation and Innate Immune Activation in Celiac Disease Are Due to Alterations in Vesicular Trafficking
    • Barone MV, Zanzi D, Maglio M, et al. Gliadin-mediated proliferation and innate immune activation in celiac disease are due to alterations in vesicular trafficking. PLoS ONE 2011;6(2):e17039
    • (2011) PLoS ONE , vol.6 , Issue.2
    • Barone, M.V.1    Zanzi, D.2    Maglio, M.3
  • 10
  • 11
    • 0037302604 scopus 로고    scopus 로고
    • Early effects of gliadin on enterocyte intracellular signalling involved in intestinal barrier function
    • Clemente MG, De Virgiliis S, Kang JS, et al. Early effects of gliadin on enterocyte intracellular signalling involved in intestinal barrier function. Gut 2003;52(2):218-23
    • (2003) Gut , vol.52 , Issue.2 , pp. 218-223
    • Clemente, M.G.1    De Virgiliis, S.2    Kang, J.S.3
  • 12
    • 79960844175 scopus 로고    scopus 로고
    • Impairment of Protein Trafficking by Direct Interaction of Gliadin Peptides with Actin
    • Reinke Y, Behrendt M, Schmidt S, et al. Impairment of protein trafficking by direct interaction of gliadin peptides with actin. Exp Cell Res 2011;317(15):2124-35
    • (2011) Exp Cell Res , vol.317 , Issue.15 , pp. 2124-2135
    • Reinke, Y.1    Behrendt, M.2    Schmidt, S.3
  • 13
    • 77749320438 scopus 로고    scopus 로고
    • Endocytotic segregation of gliadin peptide 31-49 in enterocytes
    • Zimmer KP, Fischer I, Mothes T, et al. Endocytotic segregation of gliadin peptide 31-49 in enterocytes. Gut 2010;59(3):300-10
    • (2010) Gut , vol.59 , Issue.3 , pp. 300-310
    • Zimmer, K.P.1    Fischer, I.2    Mothes, T.3
  • 14
    • 77957924395 scopus 로고    scopus 로고
    • Gliadin peptide p31-43 localises to endocytic vesicles and interferes with their maturation
    • Barone MV, Nanayakkara M, Paolella G, et al. Gliadin peptide P31-43 localises to endocytic vesicles and interferes with their maturation. PLoS ONE 2010;5(8):e12246
    • (2010) PLoS ONE , vol.5 , Issue.8
    • Barone, M.V.1    Nanayakkara, M.2    Paolella, G.3
  • 15
    • 84866688699 scopus 로고    scopus 로고
    • Gliadin peptides induce tissue transglutaminase activation and er-stress through ca(2+) mobilization in caco-2 cells
    • Caputo I, Secondo A, Lepretti M, et al. Gliadin Peptides Induce Tissue Transglutaminase Activation and ER-Stress through Ca(2+) Mobilization in Caco-2 cells. PLoS ONE 2012;7(9):e45209
    • (2012) PLoS ONE , vol.7 , Issue.9
    • Caputo, I.1    Secondo, A.2    Lepretti, M.3
  • 16
    • 61849116850 scopus 로고    scopus 로고
    • Specific duodenal and faecal bacterial groups associated with paediatric coeliac disease
    • Collado MC, Donat E, Ribes-Koninckx C, et al. Specific duodenal and faecal bacterial groups associated with paediatric coeliac disease. J Clin Pathol 2009;62(3):264-9
    • (2009) J Clin Pathol , vol.62 , Issue.3 , pp. 264-269
    • Collado, M.C.1    Donat, E.2    Ribes-Koninckx, C.3
  • 17
    • 37249066238 scopus 로고    scopus 로고
    • Imbalance in the composition of the duodenal microbiota of children with coeliac disease
    • Nadal I, Donat E, Ribes-Koninckx C, et al. Imbalance in the composition of the duodenal microbiota of children with coeliac disease. J Med Microbiol 2007;56(Pt 12):1669-74
    • (2007) J Med Microbiol , vol.56 , Issue.PART 12 , pp. 1669-1674
    • Nadal, I.1    Donat, E.2    Ribes-Koninckx, C.3
  • 18
    • 84866152531 scopus 로고    scopus 로고
    • Discerning the role of bacteroides fragilis in celiac disease pathogenesis
    • Sanchez E, Laparra JM, Sanz Y. Discerning the role of Bacteroides fragilis in celiac disease pathogenesis. Appl Environ Microbiol 2012;78(18):6507-15
    • (2012) Appl Environ Microbiol , vol.78 , Issue.18 , pp. 6507-6515
    • Sanchez, E.1    Laparra, J.M.2    Sanz, Y.3
  • 19
    • 24944583626 scopus 로고    scopus 로고
    • Chemokine receptor CCR7 guides T cell exit from peripheral tissues and entry into afferent lymphatics
    • Bromley SK, Thomas SY, Luster AD. Chemokine receptor CCR7 guides T cell exit from peripheral tissues and entry into afferent lymphatics. Nat Immunol 2005;6(9):895-901
    • (2005) Nat Immunol , vol.6 , Issue.9 , pp. 895-901
    • Bromley, S.K.1    Thomas, S.Y.2    Luster, A.D.3
  • 20
    • 84868314491 scopus 로고    scopus 로고
    • Modulation of phenotypic and functional maturation of dendritic cells by intestinal bacteria and gliadin: Relevance for celiac disease
    • De Palma G, Kamanova J, Cinova J, et al. Modulation of phenotypic and functional maturation of dendritic cells by intestinal bacteria and gliadin: relevance for celiac disease. J Leukoc Biol 2012;92(5):1043-54
    • (2012) J Leukoc Biol , vol.92 , Issue.5 , pp. 1043-1054
    • De Palma, G.1    Kamanova, J.2    Cinova, J.3
  • 21
    • 77951877329 scopus 로고    scopus 로고
    • Monocytes differentiated with il-15 support th17 and th1 responses to wheat gliadin: Implications for celiac disease
    • Harris KM, Fasano A, Mann DL. Monocytes differentiated with IL-15 support Th17 and Th1 responses to wheat gliadin: implications for celiac disease. Clin Immunol 2010;135(3):430-9
    • (2010) Clin Immunol , vol.135 , Issue.3 , pp. 430-439
    • Harris, K.M.1    Fasano, A.2    Mann, D.L.3
  • 22
    • 0030877557 scopus 로고    scopus 로고
    • Gliadin specific, HLA DQ2-restricted T cells are commonly found in small intestinal biopsies from coeliac disease patients, but not from controls
    • Molberg O, Kett K, Scott H, et al. Gliadin specific, HLA DQ2-restricted T cells are commonly found in small intestinal biopsies from coeliac disease patients, but not from controls. Scand J Immunol 1997;46(3):103-9
    • (1997) Scand J Immunol , vol.46 , Issue.3 , pp. 103-109
    • Molberg, O.1    Kett, K.2    Scott, H.3
  • 23
    • 0027319208 scopus 로고
    • Gliadin-specific, HLA-DQ(alpha 1&z.ast;0501, beta 1&z.ast;0201) restricted T cells isolated from the small intestinal mucosa of celiac disease patients
    • Lundin KE, Scott H, Hansen T, et al. Gliadin-specific, HLA-DQ(alpha 1&z.ast;0501, beta 1&z.ast;0201) restricted T cells isolated from the small intestinal mucosa of celiac disease patients. J Exp Med 1993;178(1):187-96
    • (1993) J Exp Med , vol.178 , Issue.1 , pp. 187-196
    • Lundin, K.E.1    Scott, H.2    Hansen, T.3
  • 24
    • 0142091358 scopus 로고    scopus 로고
    • The HLA-DQ2 gene dose effect in celiac disease is directly related to the magnitude and breadth of gluten-specific T cell responses
    • Vader W, Stepniak D, Kooy Y, et al. The HLA-DQ2 gene dose effect in celiac disease is directly related to the magnitude and breadth of gluten-specific T cell responses. Proc Natl Acad Sci USA 2003;100(21):12390-5
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.21 , pp. 12390-12395
    • Vader, W.1    Stepniak, D.2    Kooy, Y.3
  • 25
    • 33244472849 scopus 로고    scopus 로고
    • Inhibition of HLA-DQ2-mediated antigen presentation by analogues of a high affinity 33-residue peptide from alpha2-gliadin
    • Xia J, Siegel M, Bergseng E, et al. Inhibition of HLA-DQ2-mediated antigen presentation by analogues of a high affinity 33-residue peptide from alpha2-gliadin. J Am Chem Soc 2006;128(6):1859-67
    • (2006) J Am Chem Soc , vol.128 , Issue.6 , pp. 1859-1867
    • Xia, J.1    Siegel, M.2    Bergseng, E.3
  • 26
    • 84857313418 scopus 로고    scopus 로고
    • In vitro models for gluten toxicity: Relevance for celiac disease pathogenesis and development of novel treatment options
    • Lindfors K, Rauhavirta T, Stenman S, et al. In vitro models for gluten toxicity: relevance for celiac disease pathogenesis and development of novel treatment options. Exp Biol Med (Maywood) 2012;237(2):119-25
    • (2012) Exp Biol Med (Maywood) , vol.237 , Issue.2 , pp. 119-125
    • Lindfors, K.1    Rauhavirta, T.2    Stenman, S.3
  • 27
    • 0023849698 scopus 로고
    • In vitro (organ culture) studies of the toxicity of specific A-gliadin peptides in celiac disease
    • de Ritis G, Auricchio S, Jones HW, et al. In vitro (organ culture) studies of the toxicity of specific A-gliadin peptides in celiac disease. Gastroenterology 1988;94(1):41-9
    • (1988) Gastroenterology , vol.94 , Issue.1 , pp. 41-49
    • De Ritis, G.1    Auricchio, S.2    Jones, H.W.3
  • 28
    • 0021360452 scopus 로고
    • Are all gliadins toxic in coeliac disease? An in vitro study of alpha, beta, gamma, and w gliadins
    • Howdle PD, Ciclitira PJ, Simpson FG, Losowsky MS. Are all gliadins toxic in coeliac disease? An in vitro study of alpha, beta, gamma, and w gliadins. Scand J Gastroenterol 1984;19(1):41-7
    • (1984) Scand J Gastroenterol , vol.19 , Issue.1 , pp. 41-47
    • Howdle, P.D.1    Ciclitira, P.J.2    Simpson, F.G.3    Losowsky, M.S.4
  • 29
    • 84865462532 scopus 로고    scopus 로고
    • Interactions among secretory immunoglobulin a cd71 and transglutaminase-2 affect permeability of intestinal epithelial cells to gliadin peptides
    • e1-4
    • Lebreton C, Menard S, Abed J, et al. Interactions among secretory immunoglobulin A, CD71, and transglutaminase-2 affect permeability of intestinal epithelial cells to gliadin peptides. Gastroenterology 2012;143(3):698-707; e1-4
    • (2012) Gastroenterology , vol.143 , Issue.3 , pp. 698-707
    • Lebreton, C.1    Menard, S.2    Abed, J.3
  • 30
    • 79960062797 scopus 로고    scopus 로고
    • IL-15 interferes with suppressive activity of intestinal regulatory T cells expanded in Celiac disease
    • Zanzi D, Stefanile R, Santagata S, et al. IL-15 interferes with suppressive activity of intestinal regulatory T cells expanded in Celiac disease. Am J Gastroenterol 2011;106(7):1308-17
    • (2011) Am J Gastroenterol , vol.106 , Issue.7 , pp. 1308-1317
    • Zanzi, D.1    Stefanile, R.2    Santagata, S.3
  • 31
    • 77649308933 scopus 로고    scopus 로고
    • Long-term and acute effects of gliadin on small intestine of patients on potentially pathogenic networks in celiac disease
    • Castellanos-Rubio A, Santin I, Martin-Pagola A, et al. Long-term and acute effects of gliadin on small intestine of patients on potentially pathogenic networks in celiac disease. Autoimmunity 2010;43(2):131-9
    • (2010) Autoimmunity , vol.43 , Issue.2 , pp. 131-139
    • Castellanos-Rubio, A.1    Santin, I.2    Martin-Pagola, A.3
  • 32
    • 34548486891 scopus 로고    scopus 로고
    • Transamidation of wheat flour inhibits the response to gliadin of intestinal T cells in celiac disease
    • Gianfrani C, Siciliano RA, Facchiano AM, et al. Transamidation of wheat flour inhibits the response to gliadin of intestinal T cells in celiac disease. Gastroenterology 2007;133(3):780-9
    • (2007) Gastroenterology , vol.133 , Issue.3 , pp. 780-789
    • Gianfrani, C.1    Siciliano, R.A.2    Facchiano, A.M.3
  • 33
    • 84864370863 scopus 로고    scopus 로고
    • Variable activation of immune response by quinoa (Chenopodium quinoa Willd.) prolamins in celiac disease
    • Zevallos VF, Ellis HJ, Suligoj T, et al. Variable activation of immune response by quinoa (Chenopodium quinoa Willd.) prolamins in celiac disease. Am J Clin Nutr 2012;96(2):337-44
    • (2012) Am J Clin Nutr , vol.96 , Issue.2 , pp. 337-344
    • Zevallos, V.F.1    Ellis, H.J.2    Suligoj, T.3
  • 34
    • 80052882197 scopus 로고    scopus 로고
    • Immunogenicity of two oat varieties, in relation to their safety for celiac patients
    • Maglio M, Mazzarella G, Barone MV, et al. Immunogenicity of two oat varieties, in relation to their safety for celiac patients. Scand J Gastroenterol 2011;46(10):1194-205
    • (2011) Scand J Gastroenterol , vol.46 , Issue.10 , pp. 1194-1205
    • Maglio, M.1    Mazzarella, G.2    Barone, M.V.3
  • 35
    • 84869779522 scopus 로고    scopus 로고
    • Immunogenicity of monococcum wheat in celiac patients
    • Gianfrani C, Maglio M, Rotondi Aufiero V, et al. Immunogenicity of monococcum wheat in celiac patients. Am J Clin Nutr 2012;96(6):1339-45
    • (2012) Am J Clin Nutr , vol.96 , Issue.6 , pp. 1339-1345
    • Gianfrani, C.1    Maglio, M.2    Rotondi Aufiero, V.3
  • 36
    • 84930475429 scopus 로고    scopus 로고
    • Gluten-dependent antibodies in horses with inflammatory small bowel disease (ISBD)
    • van der Kolk JH, van Putten LA, Mulder CJ, et al. Gluten-dependent antibodies in horses with inflammatory small bowel disease (ISBD). Vet Q 2012;32(1):3-11
    • (2012) Vet Q , vol.32 , Issue.1 , pp. 3-11
    • Van Der Kolk, J.H.1    Van Putten, L.A.2    Mulder, C.J.3
  • 37
    • 0022088169 scopus 로고
    • Wheat-sensitive enteropathy in Irish setter dogs: Possible age-related brush border abnormalities
    • Batt RM, Carter MW, McLean L. Wheat-sensitive enteropathy in Irish setter dogs: possible age-related brush border abnormalities. Res Vet Sci 1985;39(1):80-3
    • (1985) Res Vet Sci , vol.39 , Issue.1 , pp. 80-83
    • Batt, R.M.1    Carter, M.W.2    McLean, L.3
  • 38
    • 0023132228 scopus 로고
    • Sequential morphologic and biochemical studies of naturally occurring wheat-sensitive enteropathy in Irish setter dogs
    • Batt RM, McLean L, Carter MW. Sequential morphologic and biochemical studies of naturally occurring wheat-sensitive enteropathy in Irish setter dogs. Dig Dis Sci 1987;32(2):184-94
    • (1987) Dig Dis Sci , vol.32 , Issue.2 , pp. 184-194
    • Batt, R.M.1    McLean, L.2    Carter, M.W.3
  • 39
    • 0026599068 scopus 로고
    • Dietary modulation of gluten sensitivity in a naturally occurring enteropathy of Irish setter dogs
    • Hall EJ, Batt RM. Dietary modulation of gluten sensitivity in a naturally occurring enteropathy of Irish setter dogs. Gut 1992;33(2):198-205
    • (1992) Gut , vol.33 , Issue.2 , pp. 198-205
    • Hall, E.J.1    Batt, R.M.2
  • 40
    • 0032408172 scopus 로고    scopus 로고
    • Genetic susceptibility to gluten sensitive enteropathy in Irish setter dogs is not linked to the major histocompatibility complex
    • Polvi A, Garden OA, Houlston RS, et al. Genetic susceptibility to gluten sensitive enteropathy in Irish setter dogs is not linked to the major histocompatibility complex. Tissue Antigens 1998;52(6):543-9
    • (1998) Tissue Antigens , vol.52 , Issue.6 , pp. 543-549
    • Polvi, A.1    Garden, O.A.2    Houlston, R.S.3
  • 41
    • 45449108449 scopus 로고    scopus 로고
    • A non-human primate model for gluten sensitivity
    • Bethune MT, Borda JT, Ribka E, et al. A non-human primate model for gluten sensitivity. PLoS ONE 2008;3(2):e1614
    • (2008) PLoS ONE , vol.3 , Issue.2
    • Bethune, M.T.1    Borda, J.T.2    Ribka, E.3
  • 42
    • 83455201302 scopus 로고    scopus 로고
    • Recognition of epidermal transglutaminase by IgA and tissue transglutaminase 2 antibodies in a rare case of Rhesus dermatitis
    • Sestak K, Mazumdar K, Midkiff CC, et al. Recognition of epidermal transglutaminase by IgA and tissue transglutaminase 2 antibodies in a rare case of Rhesus dermatitis. J Vis Exp 2011(58):3154
    • (2011) J Vis Exp , Issue.58 , pp. 3154
    • Sestak, K.1    Mazumdar, K.2    Midkiff, C.C.3
  • 43
    • 0037128650 scopus 로고    scopus 로고
    • Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis
    • Sardy M, Karpati S, Merkl B, et al. Epidermal transglutaminase (TGase 3) is the autoantigen of dermatitis herpetiformis. J Exp Med 2002;195(6):747-57
    • (2002) J Exp Med , vol.195 , Issue.6 , pp. 747-757
    • Sardy, M.1    Karpati, S.2    Merkl, B.3
  • 44
    • 9644294268 scopus 로고    scopus 로고
    • A new model for dermatitis herpetiformis that uses HLA-DQ8 transgenic NOD mice
    • Marietta E, Black K, Camilleri M, et al. A new model for dermatitis herpetiformis that uses HLA-DQ8 transgenic NOD mice. J Clin Invest 2004;114(8):1090-7
    • (2004) J Clin Invest , vol.114 , Issue.8 , pp. 1090-1097
    • Marietta, E.1    Black, K.2    Camilleri, M.3
  • 45
    • 46649111178 scopus 로고    scopus 로고
    • Transepithelial transport and enzymatic detoxification of gluten in gluten-sensitive rhesus macaques
    • Bethune MT, Ribka E, Khosla C, Sestak K. Transepithelial transport and enzymatic detoxification of gluten in gluten-sensitive rhesus macaques. PLoS ONE 2008;3(3):e1857
    • (2008) PLoS ONE , vol.3 , Issue.3
    • Bethune, M.T.1    Ribka, E.2    Khosla, C.3    Sestak, K.4
  • 46
    • 0029948833 scopus 로고    scopus 로고
    • Changes in jejunal mucosa after long-term feeding of germfree rats with gluten
    • Stepankova R, Tlaskalova-Hogenova H, Sinkora J, et al. Changes in jejunal mucosa after long-term feeding of germfree rats with gluten. Scand J Gastroenterol 1996;31(6):551-7
    • (1996) Scand J Gastroenterol , vol.31 , Issue.6 , pp. 551-557
    • Stepankova, R.1    Tlaskalova-Hogenova, H.2    Sinkora, J.3
  • 47
    • 84856777535 scopus 로고    scopus 로고
    • Bifidobacterium longum cect 7347 modulates immune responses in a gliadin-induced enteropathy animal model
    • Laparra JM, Olivares M, Gallina O, Sanz Y. Bifidobacterium longum CECT 7347 modulates immune responses in a gliadin-induced enteropathy animal model. PLoS ONE 2012;7(2):e30744
    • (2012) PLoS ONE , vol.7 , Issue.2
    • Laparra, J.M.1    Olivares, M.2    Gallina, O.3    Sanz, Y.4
  • 48
    • 84870390001 scopus 로고    scopus 로고
    • Oral administration of Bifidobacterium longum CECT 7347 modulates jejunal proteome in an in vivo gliadin-induced enteropathy animal model
    • Olivares M, Laparra M, Sanz Y. Oral administration of Bifidobacterium longum CECT 7347 modulates jejunal proteome in an in vivo gliadin-induced enteropathy animal model. J Proteomics 2012;77:310-20
    • (2012) J Proteomics , vol.77 , pp. 310-320
    • Olivares, M.1    Laparra, M.2    Sanz, Y.3
  • 49
    • 79251547709 scopus 로고    scopus 로고
    • Role of intestinal bacteria in gliadin-induced changes in intestinal mucosa: Study in germ-free rats
    • Cinova J, De Palma G, Stepankova R, et al. Role of intestinal bacteria in gliadin-induced changes in intestinal mucosa: study in germ-free rats. PLoS ONE 2011;6(1):e16169
    • (2011) PLoS ONE , vol.6 , Issue.1
    • Cinova, J.1    De Palma, G.2    Stepankova, R.3
  • 50
    • 70649097782 scopus 로고    scopus 로고
    • Gliadin-primed CD4 +CD45RBlowCD25-T cells drive gluten-dependent small intestinal damage after adoptive transfer into lymphopenic mice
    • Freitag TL, Rietdijk S, Junker Y, et al. Gliadin-primed CD4 +CD45RBlowCD25-T cells drive gluten-dependent small intestinal damage after adoptive transfer into lymphopenic mice. Gut 2009;58(12):1597-605
    • (2009) Gut , vol.58 , Issue.12 , pp. 1597-1605
    • Freitag, T.L.1    Rietdijk, S.2    Junker, Y.3
  • 51
    • 84859341173 scopus 로고    scopus 로고
    • Gluten induces coeliac-like disease in sensitised mice involving iga cd71 and transglutaminase 2 interactions that are prevented by probiotics
    • Papista C, Gerakopoulos V, Kourelis A, et al. Gluten induces coeliac-like disease in sensitised mice involving IgA, CD71 and transglutaminase 2 interactions that are prevented by probiotics. Lab Invest 2012;92(4):625-35
    • (2012) Lab Invest , vol.92 , Issue.4 , pp. 625-635
    • Papista, C.1    Gerakopoulos, V.2    Kourelis, A.3
  • 52
    • 0037111368 scopus 로고    scopus 로고
    • HLA-DQ determines the response to exogenous wheat proteins: A model of gluten sensitivity in transgenic knockout mice
    • Black KE, Murray JA, David CS. HLA-DQ determines the response to exogenous wheat proteins: a model of gluten sensitivity in transgenic knockout mice. J Immunol 2002;169(10):5595-600
    • (2002) J Immunol , vol.169 , Issue.10 , pp. 5595-5600
    • Black, K.E.1    Murray, J.A.2    David, C.S.3
  • 53
    • 70149093019 scopus 로고    scopus 로고
    • Induction of antigen-specific tolerance by oral administration of Lactococcus lactis delivered immunodominant DQ8-restricted gliadin peptide in sensitized nonobese diabetic Abo Dq8 transgenic mice
    • Huibregtse IL, Marietta EV, Rashtak S, et al. Induction of antigen-specific tolerance by oral administration of Lactococcus lactis delivered immunodominant DQ8-restricted gliadin peptide in sensitized nonobese diabetic Abo Dq8 transgenic mice. J Immunol 2009;183(4):2390-6
    • (2009) J Immunol , vol.183 , Issue.4 , pp. 2390-2396
    • Huibregtse, I.L.1    Marietta, E.V.2    Rashtak, S.3
  • 54
    • 57049132880 scopus 로고    scopus 로고
    • The role of HLA-DQ8 beta57 polymorphism in the anti-gluten T-cell response in coeliac disease
    • Hovhannisyan Z, Weiss A, Martin A, et al. The role of HLA-DQ8 beta57 polymorphism in the anti-gluten T-cell response in coeliac disease. Nature 2008;456(7221):534-8
    • (2008) Nature , vol.456 , Issue.7221 , pp. 534-5538
    • Hovhannisyan, Z.1    Weiss, A.2    Martin, A.3
  • 55
    • 79952389800 scopus 로고    scopus 로고
    • Co-adjuvant effects of retinoic acid and il-15 induce inflammatory immunity to dietary antigens
    • DePaolo RW, Abadie V, Tang F, et al. Co-adjuvant effects of retinoic acid and IL-15 induce inflammatory immunity to dietary antigens. Nature 2011;471(7337):220-4
    • (2011) Nature , vol.471 , Issue.7337 , pp. 220-224
    • Depaolo, R.W.1    Abadie, V.2    Tang, F.3
  • 56
    • 38349112856 scopus 로고    scopus 로고
    • Gliadin-dependent neuromuscular and epithelial secretory responses in gluten-sensitive HLA-DQ8 transgenic mice
    • Verdu EF, Huang X, Natividad J, et al. Gliadin-dependent neuromuscular and epithelial secretory responses in gluten-sensitive HLA-DQ8 transgenic mice. Am J Physiol Gastrointest Liver Physiol 2008;294(1):G217-25
    • (2008) Am J Physiol Gastrointest Liver Physiol , vol.294 , Issue.1
    • Verdu, E.F.1    Huang, X.2    Natividad, J.3
  • 57
    • 68149094492 scopus 로고    scopus 로고
    • Host responses to intestinal microbial antigens in gluten-sensitive mice
    • Natividad JM, Huang X, Slack E, et al. Host responses to intestinal microbial antigens in gluten-sensitive mice. PLoS ONE 2009;4(7):e6472
    • (2009) PLoS ONE , vol.4 , Issue.7
    • Natividad, J.M.1    Huang, X.2    Slack, E.3
  • 58
    • 80054738919 scopus 로고    scopus 로고
    • Sensitization to Gliadin Induces Moderate Enteropathy and Insulitis in Nonobese Diabetic-DQ8 Mice
    • Galipeau HJ, Rulli NE, Jury J, et al. Sensitization to Gliadin Induces Moderate Enteropathy and Insulitis in Nonobese Diabetic-DQ8 Mice. J Immunol 2011;187(8):4338-46
    • (2011) J Immunol , vol.187 , Issue.8 , pp. 4338-4346
    • Galipeau, H.J.1    Rulli, N.E.2    Jury, J.3
  • 59
    • 59849086162 scopus 로고    scopus 로고
    • Polymeric binders suppress gliadin-induced toxicity in the intestinal epithelium
    • Pinier M, Verdu EF, Nasser-Eddine M, et al. Polymeric binders suppress gliadin-induced toxicity in the intestinal epithelium. Gastroenterology 2009;136(1):288-98
    • (2009) Gastroenterology , vol.136 , Issue.1 , pp. 288-298
    • Pinier, M.1    Verdu, E.F.2    Nasser-Eddine, M.3
  • 60
    • 84856207904 scopus 로고    scopus 로고
    • The copolymer p(hema-co-ss) binds gluten and reduces immune response in gluten-sensitized mice and human tissues
    • e1-12
    • Pinier M, Fuhrmann G, Galipeau HJ, et al. The copolymer P(HEMA-co-SS) binds gluten and reduces immune response in gluten-sensitized mice and human tissues. Gastroenterology 2012;142(2):316-25; e1-12
    • (2012) Gastroenterology , vol.142 , Issue.2 , pp. 316-325
    • Pinier, M.1    Fuhrmann, G.2    Galipeau, H.J.3
  • 61
    • 84856714131 scopus 로고    scopus 로고
    • Increased bacterial translocation in gluten-sensitive mice is independent of small intestinal paracellular permeability defect
    • Silva MA, Jury J, Sanz Y, et al. Increased bacterial translocation in gluten-sensitive mice is independent of small intestinal paracellular permeability defect. Dig Dis Sci 2012;57(1):38-47
    • (2012) Dig Dis Sci , vol.57 , Issue.1 , pp. 38-47
    • Silva, M.A.1    Jury, J.2    Sanz, Y.3
  • 62
    • 47149083075 scopus 로고    scopus 로고
    • Adjuvant effect of Lactobacillus casei in a mouse model of gluten sensitivity
    • D'Arienzo R, Maurano F, Luongo D, et al. Adjuvant effect of Lactobacillus casei in a mouse model of gluten sensitivity. Immunol Lett 2008;119(1-2):78-83
    • (2008) Immunol Lett , vol.119 , Issue.1-2 , pp. 78-83
    • D'Arienzo, R.1    Maurano, F.2    Luongo, D.3
  • 63
    • 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, et al. A deregulated immune response to gliadin causes a decreased villus height in DQ8 transgenic mice. Eur J Immunol 2009;39(12):3552-61
    • (2009) Eur J Immunol , vol.39 , Issue.12 , pp. 3552-3561
    • D'Arienzo, R.1    Stefanile, R.2    Maurano, F.3
  • 64
    • 80052659382 scopus 로고    scopus 로고
    • Immunomodulatory effects of Lactobacillus casei administration in a mouse model of gliadin-sensitive enteropathy
    • D'Arienzo R, Stefanile R, Maurano F, et al. Immunomodulatory effects of Lactobacillus casei administration in a mouse model of gliadin-sensitive enteropathy. Scand J Immunol 2011;74(4):335-41
    • (2011) Scand J Immunol , vol.74 , Issue.4 , pp. 335-341
    • D'Arienzo, R.1    Stefanile, R.2    Maurano, F.3
  • 65
    • 70350020776 scopus 로고    scopus 로고
    • Modulation of the immune response by probiotic strains in a mouse model of gluten sensitivity
    • D'Arienzo R, Maurano F, Lavermicocca P, et al. Modulation of the immune response by probiotic strains in a mouse model of gluten sensitivity. Cytokine 2009;48(3):254-9
    • (2009) Cytokine , vol.48 , Issue.3 , pp. 254-259
    • D'Arienzo, R.1    Maurano, F.2    Lavermicocca, P.3
  • 66
    • 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 MF, et al. Identification of immunodominant epitopes of alpha-gliadin in HLA-DQ8 transgenic mice following oral immunization. J Immunol 2005;175(12):8087-95
    • (2005) J Immunol , vol.175 , Issue.12 , pp. 8087-8095
    • Senger, S.1    Maurano, F.2    Mazzeo, M.F.3
  • 67
    • 10744225587 scopus 로고    scopus 로고
    • Intranasal administration of a recombinant alpha-gliadin down-regulates the immune response to wheat gliadin in DQ8 transgenic mice
    • Senger S, Luongo D, Maurano F, et al. Intranasal administration of a recombinant alpha-gliadin down-regulates the immune response to wheat gliadin in DQ8 transgenic mice. Immunol Lett 2003;88(2):127-34
    • (2003) Immunol Lett , vol.88 , Issue.2 , pp. 127-134
    • Senger, S.1    Luongo, D.2    Maurano, F.3
  • 68
    • 80053263292 scopus 로고    scopus 로고
    • Conjugated linoleic acid protects against gliadin-induced depletion of intestinal defenses
    • Bergamo P, Gogliettino M, Palmieri G, et al. Conjugated linoleic acid protects against gliadin-induced depletion of intestinal defenses. Mol Nutr Food Res 2011;55(Suppl 2):S248-56
    • (2011) Mol Nutr Food Res , vol.55 , Issue.SUPPL. 2
    • Bergamo, P.1    Gogliettino, M.2    Palmieri, G.3
  • 69
    • 67649160603 scopus 로고    scopus 로고
    • Resistance to celiac disease in humanized HLA-DR3-DQ2-transgenic mice expressing specific anti-gliadin CD4 + T cells
    • de Kauwe AL, Chen Z, Anderson RP, et al. Resistance to celiac disease in humanized HLA-DR3-DQ2-transgenic mice expressing specific anti-gliadin CD4 + T cells. J Immunol 2009;182(12):7440-50
    • (2009) J Immunol , vol.182 , Issue.12 , pp. 7440-7450
    • De Kauwe, A.L.1    Chen, Z.2    Anderson, R.P.3
  • 70
    • 55549105057 scopus 로고    scopus 로고
    • Effects of gliadin stimulation on bone marrow-derived dendritic cells from HLA-DQ8 transgenic MICE
    • Ciccocioppo R, Rossi M, Pesce I, et al. Effects of gliadin stimulation on bone marrow-derived dendritic cells from HLA-DQ8 transgenic MICE. Dig Liver Dis 2008;40(12):927-35
    • (2008) Dig Liver Dis , vol.40 , Issue.12 , pp. 927-935
    • Ciccocioppo, R.1    Rossi, M.2    Pesce, I.3
  • 71
    • 0037255428 scopus 로고    scopus 로고
    • Characterization of HLA DR3/DQ2 transgenic mice: A potential humanized animal model for autoimmune disease studies
    • Chen D, Ueda R, Harding F, et al. Characterization of HLA DR3/DQ2 transgenic mice: a potential humanized animal model for autoimmune disease studies. Eur J Immunol 2003;33(1):172-82
    • (2003) Eur J Immunol , vol.33 , Issue.1 , pp. 172-182
    • Chen, D.1    Ueda, R.2    Harding, F.3
  • 72
    • 80051535925 scopus 로고    scopus 로고
    • Tolerance to ingested deamidated gliadin in mice is maintained by splenic type 1 regulatory t cells
    • 20 e1-2
    • Du Pre MF, Kozijn AE, van Berkel LA, et al. Tolerance to ingested deamidated gliadin in mice is maintained by splenic, type 1 regulatory T cells. Gastroenterology 2011;141(2):610-20; 20 e1-2
    • (2011) Gastroenterology , vol.141 , Issue.2 , pp. 610-620
    • Du Pre, M.F.1    Kozijn, A.E.2    Van Berkel, L.A.3
  • 73
    • 33947678875 scopus 로고    scopus 로고
    • Recognition of double-stranded RNA by TLR3 induces severe small intestinal injury in mice
    • Zhou R, Wei H, Sun R, Tian Z. Recognition of double-stranded RNA by TLR3 induces severe small intestinal injury in mice. J Immunol 2007;178(7):4548-56
    • (2007) J Immunol , vol.178 , Issue.7 , pp. 4548-4556
    • Zhou, R.1    Wei, H.2    Sun, R.3    Tian, Z.4
  • 74
    • 84856467615 scopus 로고    scopus 로고
    • Activation and inhibition of transglutaminase 2 in mice
    • Dafik L, Albertelli M, Stamnaes J, et al. Activation and inhibition of transglutaminase 2 in mice. PLoS ONE 2012;7(2):e30642
    • (2012) PLoS ONE , vol.7 , Issue.2
    • Dafik, L.1    Albertelli, M.2    Stamnaes, J.3
  • 75
    • 0036644327 scopus 로고    scopus 로고
    • IL-15-dependent activation-induced cell death-resistant Th1 type CD8 alpha beta +NK1.1+ T cells for the development of small intestinal inflammation
    • Ohta N, Hiroi T, Kweon MN, et al. IL-15-dependent activation-induced cell death-resistant Th1 type CD8 alpha beta +NK1.1+ T cells for the development of small intestinal inflammation. J Immunol 2002;169(1):460-8
    • (2002) J Immunol , vol.169 , Issue.1 , pp. 460-468
    • Ohta, N.1    Hiroi, T.2    Kweon, M.N.3
  • 76
    • 84857059940 scopus 로고    scopus 로고
    • Transgenic mice that overexpress human IL-15 in enterocytes recapitulate both B and T cell-mediated pathologic manifestations of celiac disease
    • Yokoyama S, Takada K, Hirasawa M, et al. Transgenic mice that overexpress human IL-15 in enterocytes recapitulate both B and T cell-mediated pathologic manifestations of celiac disease. J Clin Immunol 2011;31(6):1038-44
    • (2011) J Clin Immunol , vol.31 , Issue.6 , pp. 1038-1044
    • Yokoyama, S.1    Takada, K.2    Hirasawa, M.3
  • 77
    • 33846095469 scopus 로고    scopus 로고
    • A prospective, double-blind, placebo-controlled trial to establish a safe gluten threshold for patients with celiac disease
    • Catassi C, Fabiani E, Iacono G, et al. A prospective, double-blind, placebo-controlled trial to establish a safe gluten threshold for patients with celiac disease. Am J Clin Nutr 2007;85(1):160-6
    • (2007) Am J Clin Nutr , vol.85 , Issue.1 , pp. 160-166
    • Catassi, C.1    Fabiani, E.2    Iacono, G.3
  • 78
    • 42949120968 scopus 로고    scopus 로고
    • Systematic review: Tolerable amount of gluten for people with coeliac disease
    • Akobeng AK, Thomas AG. Systematic review: tolerable amount of gluten for people with coeliac disease. Aliment Pharmacol Ther 2008;27(11):1044-52
    • (2008) Aliment Pharmacol Ther , vol.27 , Issue.11 , pp. 1044-1052
    • Akobeng, A.K.1    Thomas, A.G.2
  • 79
    • 76049115164 scopus 로고    scopus 로고
    • The effects of alv003 pre-digestion of gluten on immune response and symptoms in celiac disease in vivo
    • Tye-Din JA, Anderson RP, Ffrench RA, et al. The effects of ALV003 pre-digestion of gluten on immune response and symptoms in celiac disease in vivo. Clin Immunol 2010;134(3):289-95
    • (2010) Clin Immunol , vol.134 , Issue.3 , pp. 289-295
    • Tye-Din, J.A.1    Anderson, R.P.2    Ffrench, R.A.3
  • 80
    • 36048968839 scopus 로고    scopus 로고
    • Celiac disease: In vitro and in vivo safety and palatability of wheat-free sorghum food products
    • Ciacci C, Maiuri L, Caporaso N, et al. Celiac disease: in vitro and in vivo safety and palatability of wheat-free sorghum food products. Clin Nutr 2007;26(6):799-805
    • (2007) Clin Nutr , vol.26 , Issue.6 , pp. 799-805
    • Ciacci, C.1    Maiuri, L.2    Caporaso, N.3
  • 81
    • 65249126893 scopus 로고    scopus 로고
    • Removing celiac disease-related gluten proteins from bread wheat while retaining technological properties: A study with Chinese Spring deletion lines
    • van den Broeck HC, van Herpen TW, Schuit C, et al. Removing celiac disease-related gluten proteins from bread wheat while retaining technological properties: a study with Chinese Spring deletion lines. BMC Plant Biol 2009;9:41
    • (2009) BMC Plant Biol , vol.9 , pp. 41
    • Van Den Broeck, H.C.1    Van Herpen, T.W.2    Schuit, C.3
  • 82
    • 24144461686 scopus 로고    scopus 로고
    • Natural variation in toxicity of wheat: Potential for selection of nontoxic varieties for celiac disease patients
    • Spaenij-Dekking L, Kooy-Winkelaar Y, van Veelen P, et al. Natural variation in toxicity of wheat: potential for selection of nontoxic varieties for celiac disease patients. Gastroenterology 2005;129(3):797-806
    • (2005) Gastroenterology , vol.129 , Issue.3 , pp. 797-806
    • Spaenij-Dekking, L.1    Kooy-Winkelaar, Y.2    Van Veelen, P.3
  • 83
    • 78649929787 scopus 로고    scopus 로고
    • Searching for wheat plants with low toxicity in celiac disease: Between direct toxicity and immunologic activation
    • Carroccio A, Di Prima L, Noto D, et al. Searching for wheat plants with low toxicity in celiac disease: between direct toxicity and immunologic activation. Dig Liver Dis 2011;43(1):34-9
    • (2011) Dig Liver Dis , vol.43 , Issue.1 , pp. 34-39
    • Carroccio, A.1    Di Prima, L.2    Noto, D.3
  • 84
    • 2342464831 scopus 로고    scopus 로고
    • Sourdough bread made from wheat and nontoxic flours and started with selected lactobacilli is tolerated in celiac sprue patients
    • Di Cagno R, De Angelis M, Auricchio S, et al. Sourdough bread made from wheat and nontoxic flours and started with selected lactobacilli is tolerated in celiac sprue patients. Appl Environ Microbiol 2004;70(2):1088-96
    • (2004) Appl Environ Microbiol , vol.70 , Issue.2 , pp. 1088-1096
    • Di Cagno, R.1    De Angelis, M.2    Auricchio, S.3
  • 85
    • 20744437428 scopus 로고    scopus 로고
    • Pasta made from durum wheat semolina fermented with selected lactobacilli as a tool for a potential decrease of the gluten intolerance
    • di Cagno R, de Angelis M, Alfonsi G, et al. Pasta made from durum wheat semolina fermented with selected lactobacilli as a tool for a potential decrease of the gluten intolerance. J Agric Food Chem 2005;53(11):4393-402
    • (2005) J Agric Food Chem , vol.53 , Issue.11 , pp. 4393-4402
    • Di Cagno, R.1    De Angelis, M.2    Alfonsi, G.3
  • 86
    • 78650242136 scopus 로고    scopus 로고
    • Safety for patients with celiac disease of baked goods made of wheat flour hydrolyzed during food processing
    • Greco L, Gobbetti M, Auricchio R, et al. Safety for patients with celiac disease of baked goods made of wheat flour hydrolyzed during food processing. Clin Gastroenterol Hepatol 2011;9(1):24-9
    • (2011) Clin Gastroenterol Hepatol , vol.9 , Issue.1 , pp. 24-29
    • Greco, L.1    Gobbetti, M.2    Auricchio, R.3
  • 87
    • 78650516167 scopus 로고    scopus 로고
    • Gluten-free sourdough wheat baked goods appear safe for young celiac patients: A pilot study
    • Di Cagno R, Barbato M, Di Camillo C, et al. Gluten-free sourdough wheat baked goods appear safe for young celiac patients: a pilot study. J Pediatr Gastroenterol Nutr 2010;51(6):777-83
    • (2010) J Pediatr Gastroenterol Nutr , vol.51 , Issue.6 , pp. 777-783
    • Di Cagno, R.1    Barbato, M.2    Di Camillo, C.3
  • 88
    • 84864937594 scopus 로고    scopus 로고
    • Reintroduction of gluten following flour transamidation in adult celiac patients: A randomized, controlled clinical study
    • Mazzarella G, Salvati VM, Iaquinto G, et al. Reintroduction of gluten following flour transamidation in adult celiac patients: a randomized, controlled clinical study. Clin Dev Immunol 2012;2012:329150
    • (2012) Clin Dev Immunol , vol.2012 , pp. 329150
    • Mazzarella, G.1    Salvati, V.M.2    Iaquinto, G.3
  • 89
    • 34547494627 scopus 로고    scopus 로고
    • Combination enzyme therapy for gastric digestion of dietary gluten in patients with celiac sprue
    • Gass J, Bethune MT, Siegel M, et al. Combination enzyme therapy for gastric digestion of dietary gluten in patients with celiac sprue. Gastroenterology 2007;133(2):472-80
    • (2007) Gastroenterology , vol.133 , Issue.2 , pp. 472-480
    • Gass, J.1    Bethune, M.T.2    Siegel, M.3
  • 90
    • 84856744117 scopus 로고    scopus 로고
    • Safety tolerability and activity of alv003: Results from two phase 1 single escalating-dose clinical trials
    • Siegel M, Garber ME, Spencer AG, et al. Safety, tolerability, and activity of ALV003: results from two phase 1 single, escalating-dose clinical trials. Dig Dis Sci 2012;57(2):440-50
    • (2012) Dig Dis Sci , vol.57 , Issue.2 , pp. 440-450
    • Siegel, M.1    Garber, M.E.2    Spencer, A.G.3
  • 91
    • 84862516437 scopus 로고    scopus 로고
    • ALV003, a novel glutenase, attenuates gluten-induced small intestinal mucosal injury in Celiac Disease patients: A randomized controlled phase 2A clinical trial
    • Lahdeaho M, Maki M, Kaukinen K, et al. ALV003, a novel glutenase, attenuates gluten-induced small intestinal mucosal injury in Celiac Disease patients: a randomized controlled phase 2A clinical trial. Gut 2011;60(A12)
    • (2011) Gut , vol.60
    • Lahdeaho, M.1    Maki, M.2    Kaukinen, K.3
  • 92
    • 33749440740 scopus 로고    scopus 로고
    • Highly efficient gluten degradation with a newly identified prolyl endoprotease: Implications for celiac disease
    • Stepniak D, Spaenij-Dekking L, Mitea C, et al. Highly efficient gluten degradation with a newly identified prolyl endoprotease: implications for celiac disease. Am J Physiol Gastrointest Liver Physiol 2006;291(4):G621-9
    • (2006) Am J Physiol Gastrointest Liver Physiol , vol.291 , Issue.4
    • Stepniak, D.1    Spaenij-Dekking, L.2    Mitea, C.3
  • 93
    • 38349083815 scopus 로고    scopus 로고
    • Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: Implications for coeliac disease
    • Mitea C, Havenaar R, Drijfhout JW, et al. Efficient degradation of gluten by a prolyl endoprotease in a gastrointestinal model: implications for coeliac disease. Gut 2008;57(1):25-32
    • (2008) Gut , vol.57 , Issue.1 , pp. 25-32
    • Mitea, C.1    Havenaar, R.2    Drijfhout, J.W.3
  • 95
    • 84875391866 scopus 로고    scopus 로고
    • DSM Food Specialties In: Clinicaltrials.gov [internet]. National Library Of Medicine (US); Bethesda (MD) cited 2012 Apr 16]
    • DSM Food Specialties. Effect of AN-PEP enzyme on gluten digestion. In: Clinicaltrials.gov [internet]. National Library of Medicine (US); Bethesda (MD): 2000. Available from: http://clinicaltrials.gov/show/NCT01335503 NLM Identifier: NCT01335503 [cited 2012 Apr 16]
    • (2000) Effect of AN-PEP Enzyme on Gluten Digestion
  • 96
    • 67651248240 scopus 로고    scopus 로고
    • A food-grade enzyme preparation with modest gluten detoxification properties
    • Ehren J, Moron B, Martin E, et al. A food-grade enzyme preparation with modest gluten detoxification properties. PLoS ONE 2009;4(7):e6313
    • (2009) PLoS ONE , vol.4 , Issue.7
    • Ehren, J.1    Moron, B.2    Martin, E.3
  • 97
    • 84872218376 scopus 로고    scopus 로고
    • Food-grade gluten degrading enzymes to treat dietary transgressions in coeliac adolescents
    • Korponay-Szabo IR, Tumpek J, Gyimesi J, et al. Food-grade gluten degrading enzymes to treat dietary transgressions in coeliac adolescents. J Pediatr Gastroenterol Nutr 2010;50:E68
    • (2010) J Pediatr Gastroenterol Nutr , vol.50
    • Korponay-Szabo, I.R.1    Tumpek, J.2    Gyimesi, J.3
  • 98
    • 79960605389 scopus 로고    scopus 로고
    • Influence of Bifidobacterium longum CECT 7347 and gliadin peptides on intestinal epithelial cell proteome
    • Olivares M, Laparra M, Sanz Y. Influence of Bifidobacterium longum CECT 7347 and gliadin peptides on intestinal epithelial cell proteome. J Agric Food Chem 2011;59(14):7666-71
    • (2011) J Agric Food Chem , vol.59 , Issue.14 , pp. 7666-7671
    • Olivares, M.1    Laparra, M.2    Sanz, Y.3
  • 99
    • 20144387754 scopus 로고    scopus 로고
    • Permeability, zonulin production, and enteropathy in dermatitis herpetiformis
    • Smecuol E, Sugai E, Niveloni S, et al. Permeability, zonulin production, and enteropathy in dermatitis herpetiformis. Clin Gastroenterol Hepatol 2005;3(4):335-41
    • (2005) Clin Gastroenterol Hepatol , vol.3 , Issue.4 , pp. 335-341
    • Smecuol, E.1    Sugai, E.2    Niveloni, S.3
  • 100
    • 0037105415 scopus 로고    scopus 로고
    • An enteric helminth infection protects against an allergic response to dietary antigen
    • Bashir ME, Andersen P, Fuss IJ, et al. An enteric helminth infection protects against an allergic response to dietary antigen. J Immunol 2002;169(6):3284-92
    • (2002) J Immunol , vol.169 , Issue.6 , pp. 3284-3292
    • Bashir, M.E.1    Andersen, P.2    Fuss, I.J.3
  • 101
    • 79952427391 scopus 로고    scopus 로고
    • Effect of hookworm infection on wheat challenge in celiac disease-a randomised double-blinded placebo controlled trial
    • Daveson AJ, Jones DM, Gaze S, et al. Effect of hookworm infection on wheat challenge in celiac disease-a randomised double-blinded placebo controlled trial. PLoS ONE 2011;6(3):e17366
    • (2011) PLoS ONE , vol.6 , Issue.3
    • Daveson, A.J.1    Jones, D.M.2    Gaze, S.3
  • 102
    • 80052868010 scopus 로고    scopus 로고
    • Suppression of inflammatory immune responses in celiac disease by experimental hookworm infection
    • McSorley HJ, Gaze S, Daveson J, et al. Suppression of inflammatory immune responses in celiac disease by experimental hookworm infection. PLoS ONE 2011;6(9):e24092
    • (2011) PLoS ONE , vol.6 , Issue.9
    • McSorley, H.J.1    Gaze, S.2    Daveson, J.3
  • 103
    • 84892833130 scopus 로고    scopus 로고
    • Are transglutaminase 2 inhibitors able to reduce gliadin-induced toxicity related to celiac disease? A proof-of-concept study
    • [Epub ahead of print]
    • Rauhavirta T, Oittinen M, Kivisto R, et al. Are transglutaminase 2 inhibitors able to reduce gliadin-induced toxicity related to celiac disease? A proof-of-concept study. J Clin Immunol 2012. [Epub ahead of print]
    • (2012) J Clin Immunol
    • Rauhavirta, T.1    Oittinen, M.2    Kivisto, R.3
  • 104
    • 84859805588 scopus 로고    scopus 로고
    • Larazotide acetate regulates epithelial tight junctions in vitro and in vivo
    • Gopalakrishnan S, Durai M, Kitchens K, et al. Larazotide acetate regulates epithelial tight junctions in vitro and in vivo. Peptides 2012;35(1):86-94
    • (2012) Peptides , vol.35 , Issue.1 , pp. 86-94
    • Gopalakrishnan, S.1    Durai, M.2    Kitchens, K.3
  • 105
    • 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 BM, Lammers KM, Arrieta MC, et al. 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(5):757-66
    • (2007) Aliment Pharmacol Ther , vol.26 , Issue.5 , pp. 757-766
    • Paterson, B.M.1    Lammers, K.M.2    Arrieta, M.C.3
  • 106
    • 84867101199 scopus 로고    scopus 로고
    • A randomized, double-blind study of larazotide acetate to prevent the activation of celiac disease during gluten challenge
    • Leffler DA, Kelly CP, Abdallah HZ, et al. A randomized, double-blind study of larazotide acetate to prevent the activation of celiac disease during gluten challenge. Am J Gastroenterol 2012;107(10):1554-62
    • (2012) Am J Gastroenterol , vol.107 , Issue.10 , pp. 1554-1562
    • Leffler, D.A.1    Kelly, C.P.2    Abdallah, H.Z.3
  • 107
    • 84875408592 scopus 로고    scopus 로고
    • Alba Therapeutics In: Clinicaltrials.gov [internet]. National Library Of Medicine (US); Bethesda (MD) cited 2012 Oct 31]
    • Alba Therapeutics. A double-blind Placebo-controlled study to evaluate larazotide acetate for the treatment of celiac disease. In: Clinicaltrials.gov [internet]. National Library of Medicine (US); Bethesda (MD): 2000. Available from: http://clinicaltrials.gov/ct2/show/NCT01396213?term=01396213&rank=1 NLMIdentifier: NCT01396213 [cited 2012 Oct 31]
    • (2000) A Double-blind Placebo-controlled Study to Evaluate Larazotide Acetate for the Treatment of Celiac Disease
  • 108
    • 84856013383 scopus 로고    scopus 로고
    • Ascorbate-dependent decrease of the mucosal immune inflammatory response to gliadin in coeliac disease patients
    • Bernardo D, Martinez-Abad B, Vallejo-Diez S, et al. Ascorbate-dependent decrease of the mucosal immune inflammatory response to gliadin in coeliac disease patients. Allergol Immunopathol (Madr) 2012;40(1):3-8
    • (2012) Allergol Immunopathol (Madr) , vol.40 , Issue.1 , pp. 3-8
    • Bernardo, D.1    Martinez-Abad, B.2    Vallejo-Diez, S.3
  • 109
    • 70349463158 scopus 로고    scopus 로고
    • Antibody-mediated blockade of IL-15 reverses the autoimmune intestinal damage in transgenic mice that overexpress IL-15 in enterocytes
    • Yokoyama S, Watanabe N, Sato N, et al. Antibody-mediated blockade of IL-15 reverses the autoimmune intestinal damage in transgenic mice that overexpress IL-15 in enterocytes. Proc Natl Acad Sci USA 2009;106(37):15849-54
    • (2009) Proc Natl Acad Sci USA , vol.106 , Issue.37 , pp. 15849-15854
    • Yokoyama, S.1    Watanabe, N.2    Sato, N.3
  • 110
    • 77953192176 scopus 로고    scopus 로고
    • IL-15 triggers an antiapoptotic pathway in human intraepithelial lymphocytes that is a potential new target in celiac disease-associated inflammation and lymphomagenesis
    • Malamut G, El Machhour R, Montcuquet N, et al. IL-15 triggers an antiapoptotic pathway in human intraepithelial lymphocytes that is a potential new target in celiac disease-associated inflammation and lymphomagenesis. J Clin Invest 2010;120(6):2131-43
    • (2010) J Clin Invest , vol.120 , Issue.6 , pp. 2131-2143
    • Malamut, G.1    El MacHhour, R.2    Montcuquet, N.3
  • 111
    • 72949112576 scopus 로고    scopus 로고
    • Immune Tolerance Induced by Peptide Immunotherapy in An HLA Dq2-Dependent Mouse Model of Gluten Immunity
    • Keech CL, Dromey J, Chen ZJ, et al. Immune Tolerance Induced By Peptide Immunotherapy in An HLA Dq2-Dependent Mouse Model of Gluten Immunity. Gastroenterology 2009;136(5):A57
    • (2009) Gastroenterology , vol.136 , Issue.5
    • Keech, C.L.1    Dromey, J.2    Chen, Z.J.3
  • 112
    • 84855280577 scopus 로고    scopus 로고
    • A Phase 1 study to determine safety, tolerability, and bioactivityof ® DQ2 Nexvax2 in HLA-+ volunteers with celiac diseas following a long-term, strict gluten-free diet
    • Brown GJ, Daveson J, Marjason JK, et al. A Phase 1 study to determine safety, tolerability, and bioactivityof ® DQ2 Nexvax2 in HLA-+ volunteers with celiac diseas following a long-term, strict gluten-free diet. Gastroenterology 2011;140:S437-8
    • (2011) Gastroenterology , vol.140
    • Brown, G.J.1    Daveson, J.2    Marjason, J.K.3
  • 113
    • 77957244016 scopus 로고    scopus 로고
    • Characterization of CCX282-B, an orally bioavailable antagonist of the CCR9 chemokine receptor, for treatment of inflammatory bowel disease
    • Walters MJ, Wang Y, Lai N, et al. Characterization of CCX282-B, an orally bioavailable antagonist of the CCR9 chemokine receptor, for treatment of inflammatory bowel disease. J Pharmacol Exp Ther 2010;335(1):61-9
    • (2010) J Pharmacol Exp Ther , vol.335 , Issue.1 , pp. 61-669
    • Walters, M.J.1    Wang, Y.2    Lai, N.3
  • 114
    • 84861980130 scopus 로고    scopus 로고
    • Interactions between the microbiota and the immune system
    • Hooper LV, Littman DR, Macpherson AJ. Interactions between the microbiota and the immune system. Science 2012;336(6086):1268-73
    • (2012) Science , vol.336 , Issue.6086 , pp. 1268-1273
    • Hooper, L.V.1    Littman, D.R.2    MacPherson, A.J.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.