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Volumn 151, Issue 4, 2016, Pages 670-683

Duodenal Bacteria From Patients With Celiac Disease and Healthy Subjects Distinctly Affect Gluten Breakdown and Immunogenicity

Author keywords

Celiac Disease; Gluten Metabolism; Intestinal Inflammation; Intestinal Microbiota

Indexed keywords

ELASTASE; GLUTEN; HLA DQ2 ANTIGEN; PEPTIDE;

EID: 84989908021     PISSN: 00165085     EISSN: 15280012     Source Type: Journal    
DOI: 10.1053/j.gastro.2016.06.041     Document Type: Article
Times cited : (179)

References (51)
  • 1
    • 84893397242 scopus 로고    scopus 로고
    • US perspective on gluten-related diseases
    • 1 Leonard, M.M., Vasagar, B., US perspective on gluten-related diseases. Clin Exp Gastroenterol 7 (2014), 25–37.
    • (2014) Clin Exp Gastroenterol , vol.7 , pp. 25-37
    • Leonard, M.M.1    Vasagar, B.2
  • 2
    • 84871135111 scopus 로고    scopus 로고
    • The Oslo definitions for coeliac disease and related terms
    • 2 Ludvigsson, J.F., Leffler, D.A., Bai, J.C., et al. The Oslo definitions for coeliac disease and related terms. Gut 62 (2013), 43–52.
    • (2013) Gut , vol.62 , pp. 43-52
    • Ludvigsson, J.F.1    Leffler, D.A.2    Bai, J.C.3
  • 3
    • 0037183929 scopus 로고    scopus 로고
    • Structural basis for gluten intolerance in celiac sprue
    • 3 Shan, L., Molberg, O., Parrot, I., et al. Structural basis for gluten intolerance in celiac sprue. Science 297 (2002), 2275–2279.
    • (2002) Science , vol.297 , pp. 2275-2279
    • Shan, L.1    Molberg, O.2    Parrot, I.3
  • 4
    • 84945550142 scopus 로고    scopus 로고
    • Consistency in polyclonal T-cell responses to gluten between children and adults with celiac disease
    • 4 Hardy, M.Y., Girardin, A., Pizzey, C., et al. Consistency in polyclonal T-cell responses to gluten between children and adults with celiac disease. Gastroenterology 149 (2015), 1541–1552 e2.
    • (2015) Gastroenterology , vol.149 , pp. 1541-1552 e2
    • Hardy, M.Y.1    Girardin, A.2    Pizzey, C.3
  • 5
    • 0030838044 scopus 로고    scopus 로고
    • Identification of tissue transglutaminase as the autoantigen of celiac disease
    • 5 Dieterich, W., Ehnis, T., Bauer, M., et al. Identification of tissue transglutaminase as the autoantigen of celiac disease. Nat Med 3 (1997), 797–801.
    • (1997) Nat Med , vol.3 , pp. 797-801
    • Dieterich, W.1    Ehnis, T.2    Bauer, M.3
  • 6
    • 1642447710 scopus 로고    scopus 로고
    • Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease
    • 6 Kim, C.Y., Quarsten, H., Bergseng, E., et al. Structural basis for HLA-DQ2-mediated presentation of gluten epitopes in celiac disease. Proc Natl Acad Sci U S A 101 (2004), 4175–4179.
    • (2004) Proc Natl Acad Sci U S A , vol.101 , pp. 4175-4179
    • Kim, C.Y.1    Quarsten, H.2    Bergseng, E.3
  • 7
    • 84940890004 scopus 로고    scopus 로고
    • Novel players in coeliac disease pathogenesis: role of the gut microbiota
    • 7 Verdu, E.F., Galipeau, H.J., Jabri, B., Novel players in coeliac disease pathogenesis: role of the gut microbiota. Nat Rev Gastroenterol Hepatol 12 (2015), 497–506.
    • (2015) Nat Rev Gastroenterol Hepatol , vol.12 , pp. 497-506
    • Verdu, E.F.1    Galipeau, H.J.2    Jabri, B.3
  • 8
    • 37249066238 scopus 로고    scopus 로고
    • Imbalance in the composition of the duodenal microbiota of children with coeliac disease
    • 8 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 56 (2007), 1669–1674.
    • (2007) J Med Microbiol , vol.56 , pp. 1669-1674
    • Nadal, I.1    Donat, E.2    Ribes-Koninckx, C.3
  • 9
    • 84925223549 scopus 로고    scopus 로고
    • Altered duodenal microbiota composition in celiac disease patients suffering from persistent symptoms on a long-term gluten-free diet
    • 9 Wacklin, P., Laurikka, P., Lindfors, K., et al. Altered duodenal microbiota composition in celiac disease patients suffering from persistent symptoms on a long-term gluten-free diet. Am J Gastroenterol 109 (2014), 1933–1941.
    • (2014) Am J Gastroenterol , vol.109 , pp. 1933-1941
    • Wacklin, P.1    Laurikka, P.2    Lindfors, K.3
  • 10
    • 84962708324 scopus 로고    scopus 로고
    • Metagenomics reveals dysbiosis and a potentially pathogenic N flavescens strain in duodenum of adult celiac patients
    • 10 D'Argenio, V., Casaburi, G., Precone, V., et al. Metagenomics reveals dysbiosis and a potentially pathogenic N flavescens strain in duodenum of adult celiac patients. Am J Gastroenterol 111 (2016), 879–890.
    • (2016) Am J Gastroenterol , vol.111 , pp. 879-890
    • D'Argenio, V.1    Casaburi, G.2    Precone, V.3
  • 11
    • 84899950452 scopus 로고    scopus 로고
    • Diversity of the cultivable human gut microbiome involved in gluten metabolism: isolation of microorganisms with potential interest for coeliac disease
    • 11 Caminero, A., Herran, A.R., Nistal, E., et al. Diversity of the cultivable human gut microbiome involved in gluten metabolism: isolation of microorganisms with potential interest for coeliac disease. FEMS Microbiol Ecol 88 (2014), 309–319.
    • (2014) FEMS Microbiol Ecol , vol.88 , pp. 309-319
    • Caminero, A.1    Herran, A.R.2    Nistal, E.3
  • 12
    • 84882573472 scopus 로고    scopus 로고
    • The cultivable human oral gluten-degrading microbiome and its potential implications in coeliac disease and gluten sensitivity
    • 12 Fernandez-Feo, M., Wei, G., Blumenkranz, G., et al. The cultivable human oral gluten-degrading microbiome and its potential implications in coeliac disease and gluten sensitivity. Clin Microbiol Infect 19 (2013), E386–E394.
    • (2013) Clin Microbiol Infect , vol.19 , pp. E386-E394
    • Fernandez-Feo, M.1    Wei, G.2    Blumenkranz, G.3
  • 13
    • 84855362153 scopus 로고    scopus 로고
    • Oral enzyme therapy for celiac sprue
    • 13 Bethune, M.T., Khosla, C., Oral enzyme therapy for celiac sprue. Methods Enzymol 502 (2012), 241–271.
    • (2012) Methods Enzymol , vol.502 , pp. 241-271
    • Bethune, M.T.1    Khosla, C.2
  • 14
    • 68149091349 scopus 로고    scopus 로고
    • Innate and adaptive immunity cooperate flexibly to maintain host-microbiota mutualism
    • 14 Slack, E., Hapfelmeier, S., Stecher, B., et al. Innate and adaptive immunity cooperate flexibly to maintain host-microbiota mutualism. Science 325 (2009), 617–620.
    • (2009) Science , vol.325 , pp. 617-620
    • Slack, E.1    Hapfelmeier, S.2    Stecher, B.3
  • 15
    • 84945271830 scopus 로고    scopus 로고
    • Intestinal microbiota modulates gluten-induced immunopathology in humanized mice
    • 15 Galipeau, H.J., McCarville, J.L., Huebener, S., et al. Intestinal microbiota modulates gluten-induced immunopathology in humanized mice. Am J Pathol 185 (2015), 2969–2982.
    • (2015) Am J Pathol , vol.185 , pp. 2969-2982
    • Galipeau, H.J.1    McCarville, J.L.2    Huebener, S.3
  • 16
    • 0032803862 scopus 로고    scopus 로고
    • Phylogeny of the defined murine microbiota: altered Schaedler flora
    • 16 Dewhirst, F.E., Chien, C.C., Paster, B.J., et al. Phylogeny of the defined murine microbiota: altered Schaedler flora. Appl Environ Microbiol 65 (1999), 3287–3292.
    • (1999) Appl Environ Microbiol , vol.65 , pp. 3287-3292
    • Dewhirst, F.E.1    Chien, C.C.2    Paster, B.J.3
  • 17
    • 84989903287 scopus 로고    scopus 로고
    • Role of human Microbiota in Gluten Metabolism. Molecular Biology and Biotechnology
    • Universidad de Leon Leon, Spain
    • 17 Herran, A.R., Role of human Microbiota in Gluten Metabolism. Molecular Biology and Biotechnology. 2015, Universidad de Leon, Leon, Spain.
    • (2015)
    • Herran, A.R.1
  • 18
    • 84962853158 scopus 로고    scopus 로고
    • Study of duodenal bacterial communities by 16s rRNA gene analysis in adults with active celiac disease versus non celiac disease controls
    • 18 Nistal, E., Caminero, A., Herran, A.R., et al. Study of duodenal bacterial communities by 16s rRNA gene analysis in adults with active celiac disease versus non celiac disease controls. J Appl Microbiol 120 (2016), 1691–1700.
    • (2016) J Appl Microbiol , vol.120 , pp. 1691-1700
    • Nistal, E.1    Caminero, A.2    Herran, A.R.3
  • 19
    • 84866054288 scopus 로고    scopus 로고
    • Intestinal Staphylococcus spp. and virulent features associated with coeliac disease
    • 19 Sanchez, E., Ribes-Koninckx, C., Calabuig, M., et al. Intestinal Staphylococcus spp. and virulent features associated with coeliac disease. J Clin Pathol 65 (2012), 830–834.
    • (2012) J Clin Pathol , vol.65 , pp. 830-834
    • Sanchez, E.1    Ribes-Koninckx, C.2    Calabuig, M.3
  • 20
    • 84876497585 scopus 로고    scopus 로고
    • Composition and diversity of the duodenal mucosa-associated microbiome in children with untreated coeliac disease
    • 20 de Meij, T.G., Budding, A.E., Grasman, M.E., et al. Composition and diversity of the duodenal mucosa-associated microbiome in children with untreated coeliac disease. Scand J Gastroenterol 48 (2013), 530–536.
    • (2013) Scand J Gastroenterol , vol.48 , pp. 530-536
    • de Meij, T.G.1    Budding, A.E.2    Grasman, M.E.3
  • 21
    • 84944163068 scopus 로고    scopus 로고
    • Differences in gluten metabolism among healthy volunteers, coeliac disease patients and first-degree relatives
    • 21 Caminero, A., Nistal, E., Herran, A.R., et al. Differences in gluten metabolism among healthy volunteers, coeliac disease patients and first-degree relatives. Br J Nutr 114 (2015), 1157–1167.
    • (2015) Br J Nutr , vol.114 , pp. 1157-1167
    • Caminero, A.1    Nistal, E.2    Herran, A.R.3
  • 22
    • 84862844110 scopus 로고    scopus 로고
    • Differences in faecal bacteria populations and faecal bacteria metabolism in healthy adults and celiac disease patients
    • 22 Nistal, E., Caminero, A., Vivas, S., et al. Differences in faecal bacteria populations and faecal bacteria metabolism in healthy adults and celiac disease patients. Biochimie 94 (2012), 1724–1729.
    • (2012) Biochimie , vol.94 , pp. 1724-1729
    • Nistal, E.1    Caminero, A.2    Vivas, S.3
  • 23
    • 84903610377 scopus 로고    scopus 로고
    • The loss of topography in the microbial communities of the upper respiratory tract in the elderly
    • 23 Whelan, F.J., Verschoor, C.P., Stearns, J.C., et al. The loss of topography in the microbial communities of the upper respiratory tract in the elderly. Ann Am Thorac Soc 11 (2014), 513–521.
    • (2014) Ann Am Thorac Soc , vol.11 , pp. 513-521
    • Whelan, F.J.1    Verschoor, C.P.2    Stearns, J.C.3
  • 24
    • 84857011001 scopus 로고    scopus 로고
    • PANDAseq: paired-end assembler for illumina sequences
    • 24 Masella, A.P., Bartram, A.K., Truszkowski, J.M., et al. PANDAseq: paired-end assembler for illumina sequences. BMC Bioinform, 13, 2012, 31.
    • (2012) BMC Bioinform , vol.13 , pp. 31
    • Masella, A.P.1    Bartram, A.K.2    Truszkowski, J.M.3
  • 25
    • 79952404932 scopus 로고    scopus 로고
    • Identification and quantification of abundant species from pyrosequences of 16S rRNA by Consensus Alignment
    • 25 Ye, Y., Identification and quantification of abundant species from pyrosequences of 16S rRNA by Consensus Alignment. Proceedings (IEEE Int Conf Bioinformatics Biomed) 2010 (2011), 153–157.
    • (2011) Proceedings (IEEE Int Conf Bioinformatics Biomed) , vol.2010 , pp. 153-157
    • Ye, Y.1
  • 26
    • 48449083018 scopus 로고    scopus 로고
    • Toward the assessment of food toxicity for celiac patients: characterization of monoclonal antibodies to a main immunogenic gluten peptide
    • 26 Moron, B., Bethune, M.T., Comino, I., et al. Toward the assessment of food toxicity for celiac patients: characterization of monoclonal antibodies to a main immunogenic gluten peptide. PLoS One, 3, 2008, e2294.
    • (2008) PLoS One , vol.3 , pp. e2294
    • Moron, B.1    Bethune, M.T.2    Comino, I.3
  • 27
    • 78149423735 scopus 로고    scopus 로고
    • Discovery of a novel and rich source of gluten-degrading microbial enzymes in the oral cavity
    • 27 Helmerhorst, E.J., Zamakhchari, M., Schuppan, D., et al. Discovery of a novel and rich source of gluten-degrading microbial enzymes in the oral cavity. PLoS One, 5, 2010, e13264.
    • (2010) PLoS One , vol.5 , pp. e13264
    • Helmerhorst, E.J.1    Zamakhchari, M.2    Schuppan, D.3
  • 28
    • 84860677608 scopus 로고    scopus 로고
    • A gluten metabolism study in healthy individuals shows the presence of faecal glutenasic activity
    • 28 Caminero, A., Nistal, E., Arias, L., et al. A gluten metabolism study in healthy individuals shows the presence of faecal glutenasic activity. Eur J Nutr 51 (2012), 293–299.
    • (2012) Eur J Nutr , vol.51 , pp. 293-299
    • Caminero, A.1    Nistal, E.2    Arias, L.3
  • 29
    • 84869792678 scopus 로고    scopus 로고
    • Dereplicating nonribosomal peptides using an informatic search algorithm for natural products (iSNAP) discovery
    • 29 Ibrahim, A., Yang, L., Johnston, C., et al. Dereplicating nonribosomal peptides using an informatic search algorithm for natural products (iSNAP) discovery. Proc Natl Acad Sci U S A 109 (2012), 19196–19201.
    • (2012) Proc Natl Acad Sci U S A , vol.109 , pp. 19196-19201
    • Ibrahim, A.1    Yang, L.2    Johnston, C.3
  • 30
    • 77955634105 scopus 로고    scopus 로고
    • Comprehensive, quantitative mapping of T cell epitopes in gluten in celiac disease
    • 30 Tye-Din, J.A., Stewart, J.A., Dromey, J.A., et al. Comprehensive, quantitative mapping of T cell epitopes in gluten in celiac disease. Sci Transl Med, 2, 2010, 41ra51.
    • (2010) Sci Transl Med , vol.2 , pp. 41ra51
    • Tye-Din, J.A.1    Stewart, J.A.2    Dromey, J.A.3
  • 31
    • 68149094492 scopus 로고    scopus 로고
    • Host responses to intestinal microbial antigens in gluten-sensitive mice
    • 31 Natividad, J.M., Huang, X., Slack, E., et al. Host responses to intestinal microbial antigens in gluten-sensitive mice. PLoS One, 4, 2009, e6472.
    • (2009) PLoS One , vol.4 , pp. e6472
    • Natividad, J.M.1    Huang, X.2    Slack, E.3
  • 32
    • 84908102589 scopus 로고    scopus 로고
    • Effect of Rothia mucilaginosa enzymes on gliadin (gluten) structure, deamidation, and immunogenic epitopes relevant to celiac disease
    • 32 Tian, N., Wei, G., Schuppan, D., et al. Effect of Rothia mucilaginosa enzymes on gliadin (gluten) structure, deamidation, and immunogenic epitopes relevant to celiac disease. Am J Physiol Gastrointest Liver Physiol 307 (2014), G769–G776.
    • (2014) Am J Physiol Gastrointest Liver Physiol , vol.307 , pp. G769-G776
    • Tian, N.1    Wei, G.2    Schuppan, D.3
  • 33
    • 33644504829 scopus 로고    scopus 로고
    • An ordered, nonredundant library of Pseudomonas aeruginosa strain PA14 transposon insertion mutants
    • 33 Liberati, N.T., Urbach, J.M., Miyata, S., et al. An ordered, nonredundant library of Pseudomonas aeruginosa strain PA14 transposon insertion mutants. Proc Natl Acad Sci U S A 103 (2006), 2833–2838.
    • (2006) Proc Natl Acad Sci U S A , vol.103 , pp. 2833-2838
    • Liberati, N.T.1    Urbach, J.M.2    Miyata, S.3
  • 34
    • 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
    • 34 Anderson, R.P., Degano, P., Godkin, A.J., et al. In vivo antigen challenge in celiac disease identifies a single transglutaminase-modified peptide as the dominant A-gliadin T-cell epitope. Nat Med 6 (2000), 337–342.
    • (2000) Nat Med , vol.6 , pp. 337-342
    • Anderson, R.P.1    Degano, P.2    Godkin, A.J.3
  • 35
    • 84856018986 scopus 로고    scopus 로고
    • Paracellular versus transcellular intestinal permeability to gliadin peptides in active celiac disease
    • 35 Menard, S., Lebreton, C., Schumann, M., et al. Paracellular versus transcellular intestinal permeability to gliadin peptides in active celiac disease. Am J Pathol 180 (2012), 608–615.
    • (2012) Am J Pathol , vol.180 , pp. 608-615
    • Menard, S.1    Lebreton, C.2    Schumann, M.3
  • 36
    • 0029035765 scopus 로고
    • Common virulence factors for bacterial pathogenicity in plants and animals
    • 36 Rahme, L.G., Stevens, E.J., Wolfort, S.F., et al. Common virulence factors for bacterial pathogenicity in plants and animals. Science 268 (1995), 1899–1902.
    • (1995) Science , vol.268 , pp. 1899-1902
    • Rahme, L.G.1    Stevens, E.J.2    Wolfort, S.F.3
  • 37
    • 81755189040 scopus 로고    scopus 로고
    • Deciphering the Xcp Pseudomonas aeruginosa type II secretion machinery through multiple interactions with substrates
    • 37 Douzi, B., Ball, G., Cambillau, C., et al. Deciphering the Xcp Pseudomonas aeruginosa type II secretion machinery through multiple interactions with substrates. J Biol Chem 286 (2011), 40792–40801.
    • (2011) J Biol Chem , vol.286 , pp. 40792-40801
    • Douzi, B.1    Ball, G.2    Cambillau, C.3
  • 38
    • 32944466887 scopus 로고    scopus 로고
    • Ecological and evolutionary forces shaping microbial diversity in the human intestine
    • 38 Ley, R.E., Peterson, D.A., Gordon, J.I., Ecological and evolutionary forces shaping microbial diversity in the human intestine. Cell 124 (2006), 837–848.
    • (2006) Cell , vol.124 , pp. 837-848
    • Ley, R.E.1    Peterson, D.A.2    Gordon, J.I.3
  • 39
    • 35348961403 scopus 로고    scopus 로고
    • An ecological and evolutionary perspective on human-microbe mutualism and disease
    • 39 Dethlefsen, L., McFall-Ngai, M., Relman, D.A., An ecological and evolutionary perspective on human-microbe mutualism and disease. Nature 449 (2007), 811–818.
    • (2007) Nature , vol.449 , pp. 811-818
    • Dethlefsen, L.1    McFall-Ngai, M.2    Relman, D.A.3
  • 40
    • 84907000772 scopus 로고    scopus 로고
    • Commensal bacteria protect against food allergen sensitization
    • 40 Stefka, A.T., Feehley, T., Tripathi, P., et al. Commensal bacteria protect against food allergen sensitization. Proc Natl Acad Sci U S A 111 (2014), 13145–13150.
    • (2014) Proc Natl Acad Sci U S A , vol.111 , pp. 13145-13150
    • Stefka, A.T.1    Feehley, T.2    Tripathi, P.3
  • 41
    • 79960818162 scopus 로고    scopus 로고
    • Unraveling the ties between celiac disease and intestinal microbiota
    • 41 Sanz, Y., De Pama, G., Laparra, M., Unraveling the ties between celiac disease and intestinal microbiota. Int Rev Immunol 30 (2011), 207–218.
    • (2011) Int Rev Immunol , vol.30 , pp. 207-218
    • Sanz, Y.1    De Pama, G.2    Laparra, M.3
  • 42
    • 84984820359 scopus 로고    scopus 로고
    • Adverse effects of wheat gluten
    • 42 Koning, F., Adverse effects of wheat gluten. Ann Nutr Metab 67:Suppl 2 (2015), 8–14.
    • (2015) Ann Nutr Metab , vol.67 , pp. 8-14
    • Koning, F.1
  • 43
    • 84901236224 scopus 로고    scopus 로고
    • Glutenase ALV003 attenuates gluten-induced mucosal injury in patients with celiac disease
    • 43 Lahdeaho, M.L., Kaukinen, K., Laurila, K., et al. Glutenase ALV003 attenuates gluten-induced mucosal injury in patients with celiac disease. Gastroenterology 146 (2014), 1649–1658.
    • (2014) Gastroenterology , vol.146 , pp. 1649-1658
    • Lahdeaho, M.L.1    Kaukinen, K.2    Laurila, K.3
  • 44
    • 84885642584 scopus 로고    scopus 로고
    • Consumption of gluten with gluten-degrading enzyme by celiac patients: a pilot-study
    • 44 Tack, G.J., van de Water, J.M., Bruins, M.J., et al. Consumption of gluten with gluten-degrading enzyme by celiac patients: a pilot-study. World J Gastroenterol 19 (2013), 5837–5847.
    • (2013) World J Gastroenterol , vol.19 , pp. 5837-5847
    • Tack, G.J.1    van de Water, J.M.2    Bruins, M.J.3
  • 45
    • 7444226234 scopus 로고    scopus 로고
    • Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue
    • 45 Shan, L., Marti, T., Sollid, L.M., et al. Comparative biochemical analysis of three bacterial prolyl endopeptidases: implications for coeliac sprue. Biochem J 383 (2004), 311–318.
    • (2004) Biochem J , vol.383 , pp. 311-318
    • Shan, L.1    Marti, T.2    Sollid, L.M.3
  • 46
    • 84930763366 scopus 로고    scopus 로고
    • Identification of pseudolysin (lasB) as an Aciduric gluten-degrading enzyme with high therapeutic potential for celiac disease
    • 46 Wei, G., Tian, N., Valery, A.C., et al. Identification of pseudolysin (lasB) as an Aciduric gluten-degrading enzyme with high therapeutic potential for celiac disease. Am J Gastroenterol 110 (2015), 899–908.
    • (2015) Am J Gastroenterol , vol.110 , pp. 899-908
    • Wei, G.1    Tian, N.2    Valery, A.C.3
  • 47
    • 84870278199 scopus 로고    scopus 로고
    • TgpA, a protein with a eukaryotic-like transglutaminase domain, plays a critical role in the viability of Pseudomonas aeruginosa
    • 47 Milani, A., Vecchietti, D., Rusmini, R., et al. TgpA, a protein with a eukaryotic-like transglutaminase domain, plays a critical role in the viability of Pseudomonas aeruginosa. PLoS One, 7, 2012, e50323.
    • (2012) PLoS One , vol.7 , pp. e50323
    • Milani, A.1    Vecchietti, D.2    Rusmini, R.3
  • 48
    • 79956301429 scopus 로고    scopus 로고
    • Novel inhibitors of the Pseudomonas aeruginosa virulence factor LasB: a potential therapeutic approach for the attenuation of virulence mechanisms in pseudomonal infection
    • 48 Cathcart, G.R., Quinn, D., Greer, B., et al. Novel inhibitors of the Pseudomonas aeruginosa virulence factor LasB: a potential therapeutic approach for the attenuation of virulence mechanisms in pseudomonal infection. Antimicrob Agents Chemother 55 (2011), 2670–2678.
    • (2011) Antimicrob Agents Chemother , vol.55 , pp. 2670-2678
    • Cathcart, G.R.1    Quinn, D.2    Greer, B.3
  • 49
    • 84911422299 scopus 로고    scopus 로고
    • Lactobacillus paracasei CBA L74 interferes with gliadin peptides entrance in Caco-2 cells
    • 49 Sarno, M., Lania, G., Cuomo, M., et al. Lactobacillus paracasei CBA L74 interferes with gliadin peptides entrance in Caco-2 cells. Int J Food Sci Nutr 65 (2014), 953–959.
    • (2014) Int J Food Sci Nutr , vol.65 , pp. 953-959
    • Sarno, M.1    Lania, G.2    Cuomo, M.3
  • 50
    • 47149083075 scopus 로고    scopus 로고
    • Adjuvant effect of Lactobacillus casei in a mouse model of gluten sensitivity
    • 50 D'Arienzo, R., Maurano, F., Luongo, D., et al. Adjuvant effect of Lactobacillus casei in a mouse model of gluten sensitivity. Immunol Lett 119 (2008), 78–83.
    • (2008) Immunol Lett , vol.119 , pp. 78-83
    • D'Arienzo, R.1    Maurano, F.2    Luongo, D.3
  • 51
    • 84899919523 scopus 로고    scopus 로고
    • Novel role of the serine protease inhibitor elafin in gluten-related disorders
    • 51 Galipeau, H.J., Wiepjes, M., Motta, J.P., et al. Novel role of the serine protease inhibitor elafin in gluten-related disorders. Am J Gastroenterol 109 (2014), 748–756.
    • (2014) Am J Gastroenterol , vol.109 , pp. 748-756
    • Galipeau, H.J.1    Wiepjes, M.2    Motta, J.P.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.