[1] C. Tang et al., “Inhibition of dectin-1 signaling ameliorates colitis by inducing lactobacillus-mediated regulatory T cell expansion in the intestine,” Cell Host Microbe, vol. 18, no. 2, pp. 183–197, 2015.
[2] J. A. Sanford and R. L. Gallo, “Functions of the skin microbiota in health and disease,” Semin. Immunol., vol. 25, no. 5, pp. 370–377, 2013.
[3] E. Kernbauer, Y. Ding, and K. Cadwell, “An enteric virus can replace the beneficial function of commensal bacteria,” Nature, vol. 516, no. 7529, pp. 94–98, Nov. 2014.
[4] B. S. Ramakrishna, “Role of the gut microbiota in human nutrition and metabolism,” J. Gastroenterol. Hepatol., vol. 28, pp. 9–17, 2013.
[5] A. Mosca, M. Leclerc, and J. P. Hugot, “Gut Microbiota Diversity and Human Diseases: Should We Reintroduce Key Predators in Our Ecosystem?,” Front. Microbiol., vol. 7, no. MAR, pp. 1–12, Mar. 2016.
[6] C. A. Lozupone, J. I. Stombaugh, J. I. Gordon, J. K. Jansson, and R. Knight, “Diversity, stability and resilience of the human gut microbiota,” Nature, vol. 489, no. 7415, pp. 220–230, 2012.
[7] K. Atarashi et al., “Induction of colonic regulatory T cells by indigenous Clostridium species,” Science (80-. )., vol. 331, no. 6015, pp. 337–341, 2011.
[8] Y. Furusawa et al., “Commensal microbe-derived butyrate induces the differentiation of colonic regulatory T cells,” Nature, vol. 504, no. 7480, pp. 446–450, 2013.
[9] P. M. Smith et al., “The Microbial Metabolites, Short-Chain Fatty Acids, Regulate Colonic Treg Cell Homeostasis,” Science (80-. )., vol. 341, no. 6145, pp. 569–573, Aug. 2013.
[10] I. Kimura et al., “The gut microbiota suppresses insulin-mediated fat accumulation via the short-chain fatty acid receptor GPR43,” Nat. Commun., vol. 4, no. May, pp. 1–12, 2013.
[11] I. I. Ivanov et al., “Induction of Intestinal Th17 Cells by Segmented Filamentous Bacteria,” Cell, vol. 139, no. 3, pp. 485–498, 2009.
[12] Y. Goto et al., “Segmented Filamentous Bacteria Antigens Presented by Intestinal Dendritic Cells Drive Mucosal Th17 Cell Differentiation,” Immunity, vol. 40, no. 4, pp. 594–607, Apr. 2014.
[13] T. Sano et al., “An IL-23R/IL-22 Circuit Regulates Epithelial Serum Amyloid A to Promote Local Effector Th17 Responses,” Cell, vol. 163, no. 2, pp. 381–393, 2015.
[14] Y. Goto, T. Obata, and K. Jun, “Innate lymphoid cells regulate intestinal epithelial cell glycosylation,” Science (80-. )., vol. 345, no. 6202, pp. 1310–1323, 2014.
[15] T. Kawashima et al., “Double-Stranded RNA of Intestinal Commensal but Not Pathogenic Bacteria Triggers Production of Protective Interferon-β,” Immunity, vol. 38, no. 6, pp. 1187–1197, 2013.
[16] K. Khazaie et al., “Abating colon cancer polyposis by Lactobacillus acidophilus deficient in lipoteichoic acid,” Proc. Natl. Acad. Sci., vol. 109, no. 26, pp. 10462–10467, 2012.
[17] M. Mohamadzadeh et al., “Regulation of induced colonic inflammation by Lactobacillus acidophilus deficient in lipoteichoic acid,” Proc. Natl. Acad. Sci., vol. 108, no. Supplement_1, pp. 4623–4630, Mar. 2011.
[18] S. Yang, G. Reid, J. R. G. Challis, S. O. Kim, G. B. Gloor, and A. D. Bocking, “Is There a Role for Probiotics in the Prevention of Preterm Birth?,” Front. Immunol., vol. 6, no. February, pp. 1–8, 2015.
[19] Y. Sun et al., “Stress-induced corticotropin-releasing hormone-mediated NLRP6 inflammasome inhibition and transmissible enteritis in mice,” Gastroenterology, vol. 144, no. 7, pp. 1478–1487, 2013.
[20] A. Evrensel and M. E. Ceylan, “The gut-brain axis: The missing link in depression,” Clin. Psychopharmacol. Neurosci., vol. 13, no. 3, pp. 239– 244, 2015.
[21] H. Jiang et al., “Altered fecal microbiota composition in patients with major depressive disorder,” Brain. Behav. Immun., vol. 48, pp. 186–194, 2015.
[22] T. Higuchi, H. Hayashi, and K. Abe, “Exchange of glutamate and gammaaminobutyrate in a Lactobacillus strain.,” J. Bacteriol., vol. 179, no. 10, pp. 3362–4, May 1997.
[23] E. Barrett, R. P. Ross, P. W. O’Toole, G. F. Fitzgerald, and C. Stanton, “γAminobutyric acid production by culturable bacteria from the human intestine,” J. Appl. Microbiol., vol. 113, no. 2, pp. 411–417, 2012.
[24] J. K. Kolls, P. B. McCray, and Y. R. Chan, “Cytokine-mediated regulation of antimicrobial proteins,” Nat. Rev. Immunol., vol. 8, no. 11, pp. 829–835, Nov. 2008.
[25] L. R. Muniz, C. Knosp, and G. Yeretssian, “Intestinal antimicrobial peptides during homeostasis, infection, and disease,” Front. Immunol., vol. 3, no. OCT, pp. 1–13, 2012.
[26] K. Suzuki et al., “Aberrant expansion of segmented filamentous bacteria in IgA-deficient gut,” Proc. Natl. Acad. Sci., vol. 101, no. 7, pp. 1981– 1986, 2004.
[27] K. Masahata et al., “Generation of colonic IgA-secreting cells in the caecal patch,” Nat. Commun., vol. 5, p. 3704, 2014.
[28] L. M. Loonen et al., “REG3γ-deficient mice have altered mucus distribution and increased mucosal inflammatory responses to the microbiota and enteric pathogens in the ileum,” Mucosal Immunol., vol. 7, no. 4, pp. 939–47, Dec. 2013.
[29] N. H. Salzman et al., “Enteric defensins are essential regulators of intestinal microbial ecology,” Nat. Immunol., vol. 11, no. 1, pp. 76–83, 2010.
[30] J. Wehkamp et al., “Reduced Paneth cell -defensins in ileal Crohn’s disease,” Proc. Natl. Acad. Sci., vol. 102, no. 50, pp. 18129–18134, Dec. 2005.
[31] L. N. Y. Chow et al., “Human cathelicidin LL-37-derived peptide IG-19 confers protection in a murine model of collagen-induced arthritis,” Mol. Immunol., vol. 57, no. 2, pp. 86–92, 2014.
[32] R. Dziarski and D. Gupta, “The peptidoglycan recognition proteins (PGRPs),” Genome Biol., vol. 7, no. 8, p. 232, 2006.
[33] S. Saha et al., “Peptidoglycan recognition proteins protect mice from experimental colitis by promoting normal gut flora and preventing induction of interferon-γ,” Cell Host Microbe, vol. 8, no. 2, pp. 147–162, 2010.
[34] P. G. Sohnle, M. J. Hunter, B. Hahn, and W. J. Chazin, “Zinc-Reversible Antimicrobial Activity of Recombinant Calprotectin (Migration Inhibitory Factor–Related Proteins 8 and 14),” J. Infect. Dis., vol. 182, no. 4, pp. 1272–1275, 2000.
[35] V. E. Diaz-Ochoa, S. Jellbauer, S. Klaus, and M. Raffatellu, “Transition metal ions at the crossroads of mucosal immunity and microbial pathogenesis,” Front. Cell. Infect. Microbiol., vol. 4, no. January, pp. 1–10, 2014.
[36] S. Mukherjee and L. V. Hooper, “Antimicrobial Defense of the Intestine,” Immunity, vol. 42, no. 1, pp. 28–39, 2015.
[37] Y. Zhang, W. Lu, and M. Hong, “The membrane-bound structure and topology of a human α-defensin indicate a dimer pore mechanism for membrane disruption,” Biochemistry, vol. 49, no. 45, pp. 9770–9782, 2010.
[38] S. Mukherjee et al., “Antibacterial membrane attack by a pore-forming intestinal C-type lectin,” Nature, vol. 505, no. 7481, pp. 103–107, 2014.
[39] Y. Lai and R. L. Gallo, “AMPed up immunity: how antimicrobial peptides have multiple roles in immune defense,” Trends Immunol., vol. 30, no. 3, pp. 131–141, 2009.
[40] B. R. E. A. Dixon, J. N. Radin, M. B. Piazuelo, D. C. Contreras, and H. M. S. Algood, “IL-17a and IL-22 Induce Expression of Antimicrobials in Gastrointestinal Epithelial Cells and May Contribute to Epithelial Cell Defense against Helicobacter pylori,” PLoS One, vol. 11, no. 2, p. e0148514, Feb. 2016.
[41] H. F. Farin et al., “Paneth cell extrusion and release of antimicrobial products is directly controlled by immune cell–derived IFN-γ,” J. Exp. Med., vol. 211, no. 7, pp. 1393–1405, 2014.
[42] M. Bando et al., “Interleukin-1α regulates antimicrobial peptide expression in human keratinocytes,” Immunol. Cell Biol., vol. 85, no. 7, pp. 532–537, 2007.
[43] C. L. Zindl et al., “IL-22-producing neutrophils contribute to antimicrobial defense and restitution of colonic epithelial integrity during colitis,” Proc. Natl. Acad. Sci., vol. 110, no. 31, pp. 12768–12773, 2013.
[44] S. C. Liang et al., “Interleukin (IL)-22 and IL-17 are coexpressed by Th17 cells and cooperatively enhance expression of antimicrobial peptides,” J. Exp. Med., vol. 203, no. 10, pp. 2271–2279, 2006.
[45] A. Li et al., “IL-22 Up-Regulates β-Defensin-2 Expression in Human Alveolar Epithelium via STAT3 but Not NF-κB Signaling Pathway,” Inflammation, vol. 38, no. 3, pp. 1191–1200, 2015.
[46] X. Song et al., “IL-17RE is the functional receptor for IL-17C and mediates mucosal immunity to infection with intestinal pathogens,” Nat. Immunol., vol. 12, no. 12, pp. 1151–1158, 2011.
[47] T. A. N. Pham et al., “Epithelial IL-22RA1-mediated fucosylation promotes intestinal colonization resistance to an opportunistic pathogen,” Cell Host Microbe, vol. 16, no. 4, pp. 504–516, 2014.
[48] S. L. Sanos et al., “RORγt and commensal microflora are required for the differentiation of mucosal interleukin 22-producing NKp46+cells,” Nat. Immunol., vol. 10, no. 1, pp. 83–91, 2009.
[49] J. B. Cowland, O. E. Sorensen, M. Sehested, and N. Borregaard, “Neutrophil Gelatinase-Associated Lipocalin Is Up-Regulated in Human Epithelial Cells by IL-1 , but Not by TNF- ,” J. Immunol., vol. 171, no. 12, pp. 6630–6639, 2003.
[50] J. H. Cox et al., “Opposing consequences of IL-23 signaling mediated by innate and adaptive cells in chemically induced colitis in mice,” Mucosal Immunol., vol. 5, no. 1, pp. 99–109, 2012.
[51] M. Raetz et al., “Parasite-induced TH1 cells and intestinal dysbiosis cooperate in IFN-γ-dependent elimination of Paneth cells,” Nat. Immunol., vol. 14, no. 2, pp. 136–142, Feb. 2013.
[52] H. Ishigame et al., “Differential Roles of Interleukin-17A and -17F in Host Defense against Mucoepithelial Bacterial Infection and Allergic Responses,” Immunity, vol. 30, no. 1, pp. 108–119, 2009.
[53] W. Jin and C. Dong, “IL-17 cytokines in immunity and inflammation,” Emerg. Microbes Infect., vol. 2, no. 000, p. 0, 2013.
[54] Y. Iwakura, H. Ishigame, S. Saijo, and S. Nakae, “Functional Specialization of Interleukin-17 Family Members,” Immunity, vol. 34, no. 2, pp. 149–162, 2011.
[55] M. Bosmann et al., “MyD88-dependent production of IL-17F is modulated by the anaphylatoxin C5a via the Akt signaling pathway,” FASEB J., vol. 25, no. 12, pp. 4222–4232, 2011.
[56] Y. K. Kim, J. S. Shin, and M. H. Nahm, “NOD-like receptors in infection, immunity, and diseases,” Yonsei Med. J., vol. 57, no. 1, pp. 5–14, 2016.
[57] O. Takeuchi and S. Akira, “Pattern Recognition Receptors and Inflammation,” Cell, vol. 140, no. 6, pp. 805–820, Mar. 2010.
[58] D. Ramanan, M. S. Tang, R. Bowcutt, P. Loke, and K. Cadwell, “Bacterial sensor Nod2 prevents inflammation of the small intestine by restricting the expansion of the commensal bacteroides vulgatus,” Immunity, vol. 41, no. 2, pp. 311–324, 2014.
[59] T. Petnicki-Ocwieja et al., “Nod2 is required for the regulation of commensal microbiota in the intestine,” Proc. Natl. Acad. Sci., vol. 106, no. 37, pp. 15813–15818, Sep. 2009.
[60] E. Elinav et al., “NLRP6 inflammasome regulates colonic microbial ecology and risk for colitis,” Cell, vol. 145, no. 5, pp. 745–757, 2011.
[61] M. A. Kinnebrew, C. Ubeda, L. A. Zenewicz, N. Smith, R. A. Flavell, and E. G. Pamer, “Bacterial Flagellin Stimulates Toll-Like Receptor 5– Dependent Defense against Vancomycin-Resistant Enterococcus Infection,” J. Infect. Dis., vol. 201, no. 4, pp. 534–543, 2010.
[62] N. K. Crellin, S. Trifari, C. D. Kaplan, N. Satoh-Takayama, J. P. Di Santo, and H. Spits, “Regulation of cytokine secretion in human CD127+LTi-like innate lymphoid cells by toll-like receptor 2,” Immunity, vol. 33, no. 5, pp. 752–764, 2010.
[63] D. Artis, “Epithelial-cell recognition of commensal bacteria and maintenance of immune homeostasis in the gut,” Nat. Rev. Immunol., vol. 8, no. 6, pp. 411–420, 2008.
[64] C. A. Thaiss, N. Zmora, M. Levy, and E. Elinav, “The microbiome and innate immunity,” Nature, vol. 535, no. 7610, pp. 65–74, Jul. 2016.
[65] A. Everard et al., “Intestinal epithelial MyD88 is a sensor switching host metabolism towards obesity according to nutritional status,” Nat. Commun., vol. 5, pp. 1–12, 2014.
[66] C. G. Figdor, Y. van Kooyk, and G. J. Adema, “C-TYPE LECTIN RECEPTORS ON DENDRITIC CELLS AND LANGERHANS CELLS,” Nat. Rev. Immunol., vol. 2, no. 2, pp. 77–84, Feb. 2002.
[67] S. Saijo and Y. Iwakura, “Dectin-1 and Dectin-2 in innate immunity against fungi,” Int. Immunol., vol. 23, no. 8, pp. 467–472, 2011.
[68] A. Yonekawa et al., “Dectin-2 is a direct receptor for mannose-capped lipoarabinomannan of mycobacteria,” Immunity, vol. 41, no. 3, pp. 402– 413, 2014.
[69] S. Saijo et al., “Dectin-2 recognition of α-mannans and induction of Th17 cell differentiation is essential for host defense against candida albicans,” Immunity, vol. 32, no. 5, pp. 681–691, 2010.
[70] M. J. Marakalala, L. M. Graham, and G. D. Brown, “The Role of Syk/CARD9-Coupled C-Type Lectin Receptors in Immunity to Mycobacterium tuberculosis Infections,” Clin. Dev. Immunol., vol. 2010, pp. 1–9, 2010.
[71] G. D. Brown et al., “Dectin-1 Is A Major β-Glucan Receptor On Macrophages,” J. Exp. Med., vol. 196, no. 3, pp. 407–412, 2002.
[72] P. R. Taylor et al., “The β-Glucan Receptor, Dectin-1, Is Predominantly Expressed on the Surface of Cells of the Monocyte/Macrophage and Neutrophil Lineages,” J. Immunol., vol. 169, no. 7, pp. 3876–3882, Oct. 2002.
[73] S. LeibundGut-Landmann et al., “Syk- and CARD9-dependent coupling of innate immunity to the induction of T helper cells that produce interleukin 17,” Nat. Immunol., vol. 8, no. 6, pp. 630–638, 2007.
[74] G. D. Brown, “Dectin-1 : A signalling non-TLR pattern-recognition receptor,” Nat. Rev. Immunol., vol. 6, no. 1, pp. 33–43, 2006.
[75] S. Saijo et al., “Dectin-1 is required for host defense against Pneumocystis carinii but not against Candida albicans,” Nat. Immunol., vol. 8, no. 1, pp. 39–46, 2007.
[76] P. R. Taylor et al., “Dectin-1 is required for β-glucan recognition and control of fungal infection,” Nat. Immunol., vol. 8, no. 1, pp. 31–38, Jan. 2007.
[77] S. Batbayar, D.-H. Lee, and H.-W. Kim, “Immunomodulation of Fungal βGlucan in Host Defense Signaling by Dectin-1,” Biomol. Ther., vol. 20, no. 5, pp. 433–445, Sep. 2012.
[78] S. Nakae et al., “Antigen-specific T cell sensitization is impaired in Il-17- deficient mice, causing suppression of allergic cellular and humoral responses,” Immunity, vol. 17, no. 3, pp. 375–387, 2002.
[79] F. Obermeier, N. Dunger, L. Deml, H. Herfarth, J. Schölmerich, and W. Falk, “CpG motifs of bacterial DNA exacerbate colitis of dextran sulfate sodium-treated mice,” Eur. J. Immunol., vol. 32, no. 7, p. 2084, Jul. 2002.
[80] D. M. Reid, N. A. Gow, and G. D. Brown, “Pattern recognition: recent insights from Dectin-1,” Curr. Opin. Immunol., vol. 21, no. 1, pp. 30–37, 2009.
[81] M. Merad, P. Sathe, J. Helft, J. Miller, and A. Mortha, “The Dendritic Cell Lineage: Ontogeny and Function of Dendritic Cells and Their Subsets in the Steady State and the Inflamed Setting,” Annu. Rev. Immunol., vol. 31, no. 1, pp. 563–604, Mar. 2013.
[82] S. Nuding et al., “Antibacterial activity of human defensins on anaerobic intestinal bacterial species: a major role of HBD-3,” Microbes Infect., vol. 11, no. 3, pp. 384–393, 2009.
[83] L. W. Peterson and D. Artis, “Intestinal epithelial cells: Regulators of barrier function and immune homeostasis,” Nat. Rev. Immunol., vol. 14, no. 3, pp. 141–153, 2014.
[84] N. Holmes, “CD45: all is not yet crystal clear,” Immunology, vol. 117, no. 2, pp. 145–155, Feb. 2006.
[85] S. W. Rossi, W. E. Jenkinson, G. Anderson, and E. J. Jenkinson, “Clonal analysis reveals a common progenitor for thymic cortical and medullary epithelium,” Nature, vol. 441, no. 7096, pp. 988–991, Jun. 2006.
[86] D. Viemann et al., “Myeloid-related proteins 8 and 14 induce a specific inflammatory response in human microvascular endothelial cells,” Blood, vol. 105, no. 7, pp. 2955–2962, 2005.
[87] D. Pilling, T. Fan, D. Huang, B. Kaul, and R. H. Gomer, “Identification of markers that distinguish monocyte-derived fibrocytes from monocytes, macrophages, and fibroblasts,” PLoS One, vol. 4, no. 10, pp. 31–33, 2009.
[88] B. D. Corbin et al., “Metal chelation and inhibition of bacterial growth in tissue abscesses,” Science (80-. )., vol. 319, no. 5865, pp. 962–965, 2008.
[89] T. Vogl et al., “Mrp8 and Mrp14 are endogenous activators of Toll-like receptor 4, promoting lethal, endotoxin-induced shock,” Nat. Med., vol. 13, no. 9, pp. 1042–1049, 2007.
[90] K. Xu and C. L. Geczy, “IFN- and TNF Regulate Macrophage Expression of the Chemotactic S100 Protein S100A8,” J. Immunol., vol. 164, no. 9, pp. 4916–4923, 2000.
[91] M. E. Wildenberg and G. R. van den Brink, “A major advance in ex vivo intestinal organ culture,” Gut, vol. 61, no. 7, pp. 961–962, Jul. 2012.
[92] M. K. Dame et al., “Human colonic crypts in culture: segregation of immunochemical markers in normal versus adenoma-derived,” Lab. Investig., vol. 94, no. 2, pp. 222–234, Feb. 2014.
[93] S. H. LANG, J. SMITH, C. HYDE, C. MACINTOSH, M. STOWER, and N. J. MAITLAND, “DIFFERENTIATION OF PROSTATE EPITHELIAL CELL CULTURES BY MATRIGEL/ STROMAL CELL GLANDULAR RECONSTRUCTION,” Vitr. Cell. Dev. Biol. - Anim., vol. 42, no. 8, p. 273, 2006.
[94] I. D. Iliev et al., “Interactions between commensal fungi and the C-type lectin receptor dectin-1 influence colitis,” Science (80-. )., vol. 336, no. 6086, pp. 1314–1317, 2012.
[95] M. Kanagawa, T. Satoh, A. Ikeda, Y. Adachi, N. Ohno, and Y. Yamaguchi, “Structural Insights into Recognition of Triple-helical -Glucans by an Insect Fungal Receptor,” J. Biol. Chem., vol. 286, no. 33, pp. 29158–29165, Aug. 2011.
[96] H. Saitô, T. Ohki, and T. Sasaki, “A 13C nuclear magnetic resonance study of gel-forming (1 goes to 3)-beta-d-glucans. Evidence of the presence of single-helical conformation in a resilient gel of a curdlan-type polysaccharide 13140 from Alcaligenes faecalis var. myxogenes IFO 13140.,” Biochemistry, vol. 16, no. 5, pp. 908–14, Mar. 1977.
[97] K. R. Phillips, J. Pik, H. G. Lawford, B. Lavers, A. Kligerman, and G. R. Lawford, “Production of curdlan-type polysaccharide by Alcaligenes faecalis in batch and continuous culture.,” Can. J. Microbiol., vol. 29, no. 10, pp. 1331–8, Oct. 1983.
[98] M. Matsushita, “Curdlan, a (1 → 3)-β-d-glucan from Alcaligenes faecalis var. myxogenes IFO13140, activates the alternative complement pathway by heat treatment,” Immunol. Lett., vol. 26, no. 1, pp. 95–97, 1990.
[99] S. Rose, A. Misharin, and H. Perlman, “A novel Ly6C/Ly6G-based strategy to analyze the mouse splenic myeloid compartment,” Cytom. Part A, vol. 81A, no. 4, pp. 343–350, Apr. 2012.
[100] B. A. Wevers et al., “Fungal engagement of the C-type lectin mincle suppresses dectin-1-induced antifungal immunity,” Cell Host Microbe, vol. 15, no. 4, pp. 494–505, 2014.
[101] P. K. Kump et al., “Alteration of Intestinal Dysbiosis by Fecal Microbiota Transplantation Does not Induce Remission in Patients with Chronic Active Ulcerative Colitis,” Inflamm. Bowel Dis., vol. 19, no. 10, pp. 2155– 2165, 2013.
[102] T. E. Kehl-Fie et al., “Nutrient metal sequestration by calprotectin inhibits bacterial superoxide defense, enhancing neutrophil killing of Staphylococcus aureus,” Cell Host Microbe, vol. 10, no. 2, pp. 158–164, 2011.
[103] Y. Chen et al., “Robust bioengineered 3D functional human intestinal epithelium,” Sci. Rep., vol. 5, pp. 1–11, 2015.
[104] P. S. Thiagarajan et al., “Vimentin is an endogenous ligand for the pattern recognition receptor Dectin-1,” Cardiovasc. Res., vol. 99, no. 3, pp. 494– 504, 2013.
[105] D. Mucida et al., “Reciprocal TH17 and regulatory T cell differentiation mediated by retinoic acid,” Science (80-. )., vol. 317, no. 5835, pp. 256– 260, 2007.
[106] J. A. Hall et al., “Essential role for retinoic acid in the promotion of CD4+T cell effector responses via retinoic acid receptor alpha,” Immunity, vol. 34, no. 3, pp. 435–447, 2011.
[107] R. Reifen, T. Nur, K. Ghebermeskel, G. Zaiger, R. Urizky, and M. Pines, “Vitamin A deficiency exacerbates inflammation in a rat model of colitis through activation of nuclear factor-kappaB and collagen formation.,” J. Nutr., vol. 132, no. 9, pp. 2743–7, 2002.
[108] S. Devkota et al., “Dietary-fat-induced taurocholic acid promotes pathobiont expansion and colitis in Il10-/-mice,” Nature, vol. 487, no 7405, pp. 104–108, 2012.