메뉴 건너뛰기




Volumn 56, Issue , 2017, Pages 54-65

Interactions between gut bacteria and bile in health and disease

Author keywords

Bile acid inducible (BAI); Bile salt hydrolase (BSH); Lactobacillus; Microbiome; Microbiota

Indexed keywords

BILE ACID; BILE ACID INDUCIBLE ENZYME; BILE SALT; CELL RECEPTOR; FARNESOID X RECEPTOR; HYDROLASE; MICROBIAL ENZYME; PROTEIN TGR5; UNCLASSIFIED DRUG; VITAMIN D RECEPTOR; AMIDASE; BACTERIAL PROTEIN; BAIH PROTEIN, EUBACTERIUM; CALCITRIOL RECEPTOR; CHOLOYLGLYCINE HYDROLASE; FARNESOID X-ACTIVATED RECEPTOR; G PROTEIN COUPLED RECEPTOR; GPBAR1 PROTEIN, HUMAN; OXIDOREDUCTASE;

EID: 85020901911     PISSN: 00982997     EISSN: 18729452     Source Type: Journal    
DOI: 10.1016/j.mam.2017.06.002     Document Type: Review
Times cited : (378)

References (174)
  • 1
    • 84984637680 scopus 로고    scopus 로고
    • Clostridium difficile colitis: pathogenesis and host defence
    • Abt, M.C., McKenney, P.T., Pamer, E.G., Clostridium difficile colitis: pathogenesis and host defence. Nat. Rev. Microbiol. 14:10 (2016), 609–620.
    • (2016) Nat. Rev. Microbiol. , vol.14 , Issue.10 , pp. 609-620
    • Abt, M.C.1    McKenney, P.T.2    Pamer, E.G.3
  • 2
    • 64349115740 scopus 로고    scopus 로고
    • Bile Acid sulfation: a pathway of bile acid elimination and detoxification
    • Alnouti, Y., Bile Acid sulfation: a pathway of bile acid elimination and detoxification. Toxicol. Sci. 108:2 (2009), 225–246.
    • (2009) Toxicol. Sci. , vol.108 , Issue.2 , pp. 225-246
    • Alnouti, Y.1
  • 4
    • 0029446407 scopus 로고
    • A sting in the (N-terminal) tail
    • Artymiuk, P.J., A sting in the (N-terminal) tail. Nat. Struct. Biol. 2:12 (1995), 1035–1037.
    • (1995) Nat. Struct. Biol. , vol.2 , Issue.12 , pp. 1035-1037
    • Artymiuk, P.J.1
  • 6
    • 0028942320 scopus 로고
    • Comparison of Lactobacillus strains with respect to bile salt hydrolase activity, colonization of the gastrointestinal tract, and growth rate of the murine host
    • Bateup, J.M., McConnell, M.A., Jenkinson, H.F., Tannock, G.W., Comparison of Lactobacillus strains with respect to bile salt hydrolase activity, colonization of the gastrointestinal tract, and growth rate of the murine host. Appl. Environ. Microbiol. 61:3 (1995), 1147–1149.
    • (1995) Appl. Environ. Microbiol. , vol.61 , Issue.3 , pp. 1147-1149
    • Bateup, J.M.1    McConnell, M.A.2    Jenkinson, H.F.3    Tannock, G.W.4
  • 7
    • 20444493331 scopus 로고    scopus 로고
    • The interaction between bacteria and bile
    • Begley, M., Gahan, C.G., Hill, C., The interaction between bacteria and bile. FEMS Microbiol. Rev. 29:4 (2005), 625–651.
    • (2005) FEMS Microbiol. Rev. , vol.29 , Issue.4 , pp. 625-651
    • Begley, M.1    Gahan, C.G.2    Hill, C.3
  • 8
    • 33644941373 scopus 로고    scopus 로고
    • Bile salt hydrolase activity in probiotics
    • Begley, M., Hill, C., Gahan, C.G.M., Bile salt hydrolase activity in probiotics. Appl. Environ. Microbiol. 72:3 (2006), 1729–1738.
    • (2006) Appl. Environ. Microbiol. , vol.72 , Issue.3 , pp. 1729-1738
    • Begley, M.1    Hill, C.2    Gahan, C.G.M.3
  • 9
    • 12844275386 scopus 로고    scopus 로고
    • Contribution of three bile-associated loci, bsh, pva, and btlB, to gastrointestinal persistence and bile tolerance of Listeria monocytogenes
    • Begley, M., Sleator, R.D., Gahan, C.G., Hill, C., Contribution of three bile-associated loci, bsh, pva, and btlB, to gastrointestinal persistence and bile tolerance of Listeria monocytogenes. Infect. Immun. 73:2 (2005), 894–904.
    • (2005) Infect. Immun. , vol.73 , Issue.2 , pp. 894-904
    • Begley, M.1    Sleator, R.D.2    Gahan, C.G.3    Hill, C.4
  • 10
    • 0344896641 scopus 로고    scopus 로고
    • Cloning and characterization of the NAD-dependent 7alpha-Hydroxysteroid dehydrogenase from Bacteroides fragilis
    • Bennett, M.J., McKnight, S.L., Coleman, J.P., Cloning and characterization of the NAD-dependent 7alpha-Hydroxysteroid dehydrogenase from Bacteroides fragilis. Curr. Microbiol. 47:6 (2003), 475–484.
    • (2003) Curr. Microbiol. , vol.47 , Issue.6 , pp. 475-484
    • Bennett, M.J.1    McKnight, S.L.2    Coleman, J.P.3
  • 11
    • 0032892176 scopus 로고    scopus 로고
    • Removal of cholesterol from extrahepatic sources by oxidative mechanisms
    • Bjorkhem, I., Diczfalusy, U., Lutjohann, D., Removal of cholesterol from extrahepatic sources by oxidative mechanisms. Curr. Opin. Lipidol. 10:2 (1999), 161–165.
    • (1999) Curr. Opin. Lipidol. , vol.10 , Issue.2 , pp. 161-165
    • Bjorkhem, I.1    Diczfalusy, U.2    Lutjohann, D.3
  • 12
    • 0036137674 scopus 로고    scopus 로고
    • Nuclear xeno-sensors as receptors for cholestatic bile acids: the second line of defense
    • Bock, H.H., Lammert, F., Nuclear xeno-sensors as receptors for cholestatic bile acids: the second line of defense. Hepatology 35:1 (2002), 232–234.
    • (2002) Hepatology , vol.35 , Issue.1 , pp. 232-234
    • Bock, H.H.1    Lammert, F.2
  • 13
    • 0017669303 scopus 로고
    • Isolation and characterization of human fecal bacteria capable of 21-dehydroxylating corticoids
    • Bokkenheuser, V.D., Winter, J., Dehazya, P., Kelly, W.G., Isolation and characterization of human fecal bacteria capable of 21-dehydroxylating corticoids. Appl. Environ. Microbiol. 34:5 (1977), 571–575.
    • (1977) Appl. Environ. Microbiol. , vol.34 , Issue.5 , pp. 571-575
    • Bokkenheuser, V.D.1    Winter, J.2    Dehazya, P.3    Kelly, W.G.4
  • 14
    • 0028972449 scopus 로고
    • A protein catalytic framework with an N-terminal nucleophile is capable of self-activation
    • Brannigan, J.A., Dodson, G., Duggleby, H.J., Moody, P.C., Smith, J.L., Tomchick, D.R., Murzin, A.G., A protein catalytic framework with an N-terminal nucleophile is capable of self-activation. Nature 378:6555 (1995), 416–419.
    • (1995) Nature , vol.378 , Issue.6555 , pp. 416-419
    • Brannigan, J.A.1    Dodson, G.2    Duggleby, H.J.3    Moody, P.C.4    Smith, J.L.5    Tomchick, D.R.6    Murzin, A.G.7
  • 15
    • 84857672076 scopus 로고    scopus 로고
    • In vitro characterization and safety of the probiotic strain Lactobacillus reuteri cardioviva NCIMB 30242
    • Branton, W., Jones, M., Tomaro-Duchesneau, C., Martoni, C., Prakash, S., In vitro characterization and safety of the probiotic strain Lactobacillus reuteri cardioviva NCIMB 30242. Int. J. Probiotics Prebiotics, 6(1), 2011, 1.
    • (2011) Int. J. Probiotics Prebiotics , vol.6 , Issue.1 , pp. 1
    • Branton, W.1    Jones, M.2    Tomaro-Duchesneau, C.3    Martoni, C.4    Prakash, S.5
  • 16
    • 79954593169 scopus 로고    scopus 로고
    • Biocatalytic process optimization based on mechanistic modeling of cholic acid oxidation with cofactor regeneration
    • Braun, M., Link, H., Liu, L., Schmid, R.D., Weuster-Botz, D., Biocatalytic process optimization based on mechanistic modeling of cholic acid oxidation with cofactor regeneration. Biotechnol. Bioeng. 108:6 (2011), 1307–1317.
    • (2011) Biotechnol. Bioeng. , vol.108 , Issue.6 , pp. 1307-1317
    • Braun, M.1    Link, H.2    Liu, L.3    Schmid, R.D.4    Weuster-Botz, D.5
  • 19
    • 0025914556 scopus 로고
    • Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis
    • Cali, J.J., Hsieh, C.L., Francke, U., Russell, D.W., Mutations in the bile acid biosynthetic enzyme sterol 27-hydroxylase underlie cerebrotendinous xanthomatosis. J. Biol. Chem. 266:12 (1991), 7779–7783.
    • (1991) J. Biol. Chem. , vol.266 , Issue.12 , pp. 7779-7783
    • Cali, J.J.1    Hsieh, C.L.2    Francke, U.3    Russell, D.W.4
  • 20
    • 84871106689 scopus 로고    scopus 로고
    • Molecular cloning, characterization and comparison of bile salt hydrolases from Lactobacillus johnsonii PF01
    • Chae, J.P., Valeriano, V.D., Kim, G.B., Kang, D.K., Molecular cloning, characterization and comparison of bile salt hydrolases from Lactobacillus johnsonii PF01. J. Appl. Microbiol. 114:1 (2013), 121–133.
    • (2013) J. Appl. Microbiol. , vol.114 , Issue.1 , pp. 121-133
    • Chae, J.P.1    Valeriano, V.D.2    Kim, G.B.3    Kang, D.K.4
  • 21
    • 30144431977 scopus 로고    scopus 로고
    • Vitamin D receptor regulation of the steroid/bile acid sulfotransferase SULT2A1
    • Chatterjee, B., Echchgadda, I., Song, C.S., Vitamin D receptor regulation of the steroid/bile acid sulfotransferase SULT2A1. Methods Enzym. 400 (2005), 165–191.
    • (2005) Methods Enzym. , vol.400 , pp. 165-191
    • Chatterjee, B.1    Echchgadda, I.2    Song, C.S.3
  • 22
    • 70349430938 scopus 로고    scopus 로고
    • Bile acids: regulation of synthesis
    • Chiang, J.Y., Bile acids: regulation of synthesis. J. lipid Res. 50:10 (2009), 1955–1966.
    • (2009) J. lipid Res. , vol.50 , Issue.10 , pp. 1955-1966
    • Chiang, J.Y.1
  • 23
    • 84891710536 scopus 로고    scopus 로고
    • Bile acid metabolism and signaling
    • Chiang, J.Y., Bile acid metabolism and signaling. Compr. Physiol. 3:3 (2013), 1191–1212.
    • (2013) Compr. Physiol. , vol.3 , Issue.3 , pp. 1191-1212
    • Chiang, J.Y.1
  • 25
    • 0029041833 scopus 로고
    • Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens
    • Coleman, J.P., Hudson, L.L., Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens. Appl. Environ. Microbiol. 61:7 (1995), 2514–2520.
    • (1995) Appl. Environ. Microbiol. , vol.61 , Issue.7 , pp. 2514-2520
    • Coleman, J.P.1    Hudson, L.L.2
  • 26
    • 0023256008 scopus 로고
    • Molecular cloning of bile acid 7-dehydroxylase from Eubacterium sp. strain VPI 12708
    • Coleman, J.P., White, W.B., Hylemon, P.B., Molecular cloning of bile acid 7-dehydroxylase from Eubacterium sp. strain VPI 12708. J. Bacteriol. 169:4 (1987), 1516–1521.
    • (1987) J. Bacteriol. , vol.169 , Issue.4 , pp. 1516-1521
    • Coleman, J.P.1    White, W.B.2    Hylemon, P.B.3
  • 27
    • 0033091804 scopus 로고    scopus 로고
    • Bile salt hydrolase activity of three strains of Lactobacillus acidophilus1
    • Corzo, G., Gilliland, S.E., Bile salt hydrolase activity of three strains of Lactobacillus acidophilus1. J. Dairy Sci. 82:3 (1999), 472–480.
    • (1999) J. Dairy Sci. , vol.82 , Issue.3 , pp. 472-480
    • Corzo, G.1    Gilliland, S.E.2
  • 29
    • 84940978957 scopus 로고    scopus 로고
    • Preliminary probiotic and technological characterization of Pediococcus pentosaceus strain KID7 and in vivo assessment of its cholesterol-lowering activity
    • Damodharan, K., Lee, Y.S., Palaniyandi, S.A., Yang, S.H., Suh, J.W., Preliminary probiotic and technological characterization of Pediococcus pentosaceus strain KID7 and in vivo assessment of its cholesterol-lowering activity. Front. Microbiol., 6, 2015, 768.
    • (2015) Front. Microbiol. , vol.6 , pp. 768
    • Damodharan, K.1    Lee, Y.S.2    Palaniyandi, S.A.3    Yang, S.H.4    Suh, J.W.5
  • 30
    • 0029657766 scopus 로고    scopus 로고
    • Expression and characterization of a C24 bile acid 7 alpha-dehydratase from Eubacterium sp. strain VPI 12708 in Escherichia coli
    • Dawson, J.A., Mallonee, D.H., Bjorkhem, I., Hylemon, P.B., Expression and characterization of a C24 bile acid 7 alpha-dehydratase from Eubacterium sp. strain VPI 12708 in Escherichia coli. J. Lipid Res. 37:6 (1996), 1258–1267.
    • (1996) J. Lipid Res. , vol.37 , Issue.6 , pp. 1258-1267
    • Dawson, J.A.1    Mallonee, D.H.2    Bjorkhem, I.3    Hylemon, P.B.4
  • 34
    • 0031892684 scopus 로고    scopus 로고
    • Cholesterol lowering in pigs through enhanced bacterial bile salt hydrolase activity
    • De Smet, I., De Boever, P., Verstraete, W., Cholesterol lowering in pigs through enhanced bacterial bile salt hydrolase activity. Br. J. Nutr. 79:2 (1998), 185–194.
    • (1998) Br. J. Nutr. , vol.79 , Issue.2 , pp. 185-194
    • De Smet, I.1    De Boever, P.2    Verstraete, W.3
  • 36
    • 0036268762 scopus 로고    scopus 로고
    • Characterization of cholylglycine hydrolase from a bile-adapted strain of Xanthomonas maltophilia and its application for quantitative hydrolysis of conjugated bile salts
    • Dean, M., Cervellati, C., Casanova, E., Squerzanti, M., Lanzara, V., Medici, A., Polverino de Laureto, P., Bergamini, C.M., Characterization of cholylglycine hydrolase from a bile-adapted strain of Xanthomonas maltophilia and its application for quantitative hydrolysis of conjugated bile salts. Appl. Environ. Microbiol. 68:6 (2002), 3126–3128.
    • (2002) Appl. Environ. Microbiol. , vol.68 , Issue.6 , pp. 3126-3128
    • Dean, M.1    Cervellati, C.2    Casanova, E.3    Squerzanti, M.4    Lanzara, V.5    Medici, A.6    Polverino de Laureto, P.7    Bergamini, C.M.8
  • 37
    • 84898023722 scopus 로고    scopus 로고
    • Microbiota modification with probiotics induces hepatic bile acid synthesis via downregulation of the Fxr-Fgf15 axis in mice
    • Degirolamo, C., Rainaldi, S., Bovenga, F., Murzilli, S., Moschetta, A., Microbiota modification with probiotics induces hepatic bile acid synthesis via downregulation of the Fxr-Fgf15 axis in mice. Cell Rep. 7:1 (2014), 12–18.
    • (2014) Cell Rep. , vol.7 , Issue.1 , pp. 12-18
    • Degirolamo, C.1    Rainaldi, S.2    Bovenga, F.3    Murzilli, S.4    Moschetta, A.5
  • 38
    • 33846032324 scopus 로고    scopus 로고
    • A bile salt hydrolase of Brucella abortus contributes to the establishment of a successful infection through the oral route in mice
    • Delpino, M.V., Marchesini, M.I., Estein, S.M., Comerci, D.J., Cassataro, J., Fossati, C.A., Baldi, P.C., A bile salt hydrolase of Brucella abortus contributes to the establishment of a successful infection through the oral route in mice. Infect. Immun. 75:1 (2007), 299–305.
    • (2007) Infect. Immun. , vol.75 , Issue.1 , pp. 299-305
    • Delpino, M.V.1    Marchesini, M.I.2    Estein, S.M.3    Comerci, D.J.4    Cassataro, J.5    Fossati, C.A.6    Baldi, P.C.7
  • 40
    • 0037040184 scopus 로고    scopus 로고
    • Control of cholesterol turnover in the mouse
    • Dietschy, J.M., Turley, S.D., Control of cholesterol turnover in the mouse. J. Biol. Chem. 277:6 (2002), 3801–3804.
    • (2002) J. Biol. Chem. , vol.277 , Issue.6 , pp. 3801-3804
    • Dietschy, J.M.1    Turley, S.D.2
  • 45
    • 0036037505 scopus 로고    scopus 로고
    • Listeria monocytogenes bile salt hydrolase is a PrfA-regulated virulence factor involved in the intestinal and hepatic phases of listeriosis
    • Dussurget, O., Cabanes, D., Dehoux, P., Lecuit, M., Buchrieser, C., Glaser, P., Cossart, P., Listeria monocytogenes bile salt hydrolase is a PrfA-regulated virulence factor involved in the intestinal and hepatic phases of listeriosis. Mol. Microbiol. 45:4 (2002), 1095–1106.
    • (2002) Mol. Microbiol. , vol.45 , Issue.4 , pp. 1095-1106
    • Dussurget, O.1    Cabanes, D.2    Dehoux, P.3    Lecuit, M.4    Buchrieser, C.5    Glaser, P.6    Cossart, P.7
  • 46
    • 0021984234 scopus 로고
    • 12 beta-dehydrogenation of bile acids by Clostridium paraputrificum, C. tertium, and C. difficile and epimerization at carbon-12 of deoxycholic acid by cocultivation with 12 alpha-dehydrogenating Eubacterium lentum
    • Edenharder, R., Schneider, J., 12 beta-dehydrogenation of bile acids by Clostridium paraputrificum, C. tertium, and C. difficile and epimerization at carbon-12 of deoxycholic acid by cocultivation with 12 alpha-dehydrogenating Eubacterium lentum. Appl. Environ. Microbiol. 49:4 (1985), 964–968.
    • (1985) Appl. Environ. Microbiol. , vol.49 , Issue.4 , pp. 964-968
    • Edenharder, R.1    Schneider, J.2
  • 47
    • 0035217635 scopus 로고    scopus 로고
    • Genes encoding bile salt hydrolases and conjugated bile salt transporters in Lactobacillus johnsonii 100-100 and other Lactobacillus species
    • Elkins, C.A., Moser, S.A., Savage, D.C., Genes encoding bile salt hydrolases and conjugated bile salt transporters in Lactobacillus johnsonii 100-100 and other Lactobacillus species. Microbiology 147:12 (2001), 3403–3412.
    • (2001) Microbiology , vol.147 , Issue.12 , pp. 3403-3412
    • Elkins, C.A.1    Moser, S.A.2    Savage, D.C.3
  • 48
    • 0014811430 scopus 로고
    • Steroids in germfree and conventional rats. Distribution and excretion of labelled pregnenolone and corticosterone in male and female rats
    • Eriksson, H., Gustafsson, J.A., Steroids in germfree and conventional rats. Distribution and excretion of labelled pregnenolone and corticosterone in male and female rats. Eur. J. Biochem. 15:1 (1970), 132–139.
    • (1970) Eur. J. Biochem. , vol.15 , Issue.1 , pp. 132-139
    • Eriksson, H.1    Gustafsson, J.A.2
  • 49
    • 0020694594 scopus 로고
    • Cooperative formation of omega-muricholic acid by intestinal microorganisms
    • Eyssen, H., De Pauw, G., Stragier, J., Verhulst, A., Cooperative formation of omega-muricholic acid by intestinal microorganisms. Appl. Environ. Microbiol. 45:1 (1983), 141–147.
    • (1983) Appl. Environ. Microbiol. , vol.45 , Issue.1 , pp. 141-147
    • Eyssen, H.1    De Pauw, G.2    Stragier, J.3    Verhulst, A.4
  • 50
    • 0021873492 scopus 로고
    • Influence of microbial bile salt desulfation upon the fecal excretion of bile salts in gnotobiotic rats
    • Eyssen, H., Van Eldere, J., Parmentier, G., Huijghebaert, S., Mertens, J., Influence of microbial bile salt desulfation upon the fecal excretion of bile salts in gnotobiotic rats. J. Steroid Biochem. 22:4 (1985), 547–554.
    • (1985) J. Steroid Biochem. , vol.22 , Issue.4 , pp. 547-554
    • Eyssen, H.1    Van Eldere, J.2    Parmentier, G.3    Huijghebaert, S.4    Mertens, J.5
  • 51
    • 0033050648 scopus 로고    scopus 로고
    • Formation of hyodeoxycholic acid from muricholic acid and hyocholic acid by an unidentified gram-positive rod termed HDCA-1 isolated from rat intestinal microflora
    • Eyssen, H.J., De Pauw, G., Van Eldere, J., Formation of hyodeoxycholic acid from muricholic acid and hyocholic acid by an unidentified gram-positive rod termed HDCA-1 isolated from rat intestinal microflora. Appl. Environ. Microbiol. 65:7 (1999), 3158–3163.
    • (1999) Appl. Environ. Microbiol. , vol.65 , Issue.7 , pp. 3158-3163
    • Eyssen, H.J.1    De Pauw, G.2    Van Eldere, J.3
  • 53
    • 69949083658 scopus 로고    scopus 로고
    • Allelic variation of bile salt hydrolase genes in Lactobacillus salivarius does not determine bile resistance levels
    • Fang, F., Li, Y., Bumann, M., Raftis, E.J., Casey, P.G., Cooney, J.C., Walsh, M.A., O'Toole, P.W., Allelic variation of bile salt hydrolase genes in Lactobacillus salivarius does not determine bile resistance levels. J. Bacteriol. 191:18 (2009), 5743–5757.
    • (2009) J. Bacteriol. , vol.191 , Issue.18 , pp. 5743-5757
    • Fang, F.1    Li, Y.2    Bumann, M.3    Raftis, E.J.4    Casey, P.G.5    Cooney, J.C.6    Walsh, M.A.7    O'Toole, P.W.8
  • 54
    • 84875814163 scopus 로고    scopus 로고
    • In search of sustainable chemical processes: cloning, recombinant expression, and functional characterization of the 7alpha- and 7beta-hydroxysteroid dehydrogenases from Clostridium absonum
    • Ferrandi, E.E., Bertolesi, G.M., Polentini, F., Negri, A., Riva, S., Monti, D., In search of sustainable chemical processes: cloning, recombinant expression, and functional characterization of the 7alpha- and 7beta-hydroxysteroid dehydrogenases from Clostridium absonum. Appl. Microbiol. Biotechnol. 95:5 (2012), 1221–1233.
    • (2012) Appl. Microbiol. Biotechnol. , vol.95 , Issue.5 , pp. 1221-1233
    • Ferrandi, E.E.1    Bertolesi, G.M.2    Polentini, F.3    Negri, A.4    Riva, S.5    Monti, D.6
  • 55
    • 84878518519 scopus 로고    scopus 로고
    • Bile acid recognition by the Clostridium difficile germinant receptor, CspC, is important for establishing infection
    • Francis, M.B., Allen, C.A., Shrestha, R., Sorg, J.A., Bile acid recognition by the Clostridium difficile germinant receptor, CspC, is important for establishing infection. PLoS Pathog., 9(5), 2013, e1003356.
    • (2013) PLoS Pathog. , vol.9 , Issue.5 , pp. e1003356
    • Francis, M.B.1    Allen, C.A.2    Shrestha, R.3    Sorg, J.A.4
  • 56
    • 0035004396 scopus 로고    scopus 로고
    • Bile salt hydrolase activity of enterococci isolated from food: screening and quantitative determination
    • Franz, C.M.A.P., Specht, I., Haberer, P., Holzapfel, W.H., Bile salt hydrolase activity of enterococci isolated from food: screening and quantitative determination. J. Food Prot. 64:5 (2001), 725–729.
    • (2001) J. Food Prot. , vol.64 , Issue.5 , pp. 725-729
    • Franz, C.M.A.P.1    Specht, I.2    Haberer, P.3    Holzapfel, W.H.4
  • 57
    • 84903524994 scopus 로고    scopus 로고
    • Metabolism of cholesterol and bile acids by the gut microbiota
    • Gerard, P., Metabolism of cholesterol and bile acids by the gut microbiota. Pathogens 3:1 (2013), 14–24.
    • (2013) Pathogens , vol.3 , Issue.1 , pp. 14-24
    • Gerard, P.1
  • 59
    • 0021924550 scopus 로고
    • Assimilation of cholesterol by Lactobacillus acidophilus
    • Gilliland, S.E., Nelson, C.R., Maxwell, C., Assimilation of cholesterol by Lactobacillus acidophilus. Appl. Environ. Microbiol. 49:2 (1985), 377–381.
    • (1985) Appl. Environ. Microbiol. , vol.49 , Issue.2 , pp. 377-381
    • Gilliland, S.E.1    Nelson, C.R.2    Maxwell, C.3
  • 60
    • 55549142166 scopus 로고    scopus 로고
    • 7alpha- and 12alpha-Hydroxysteroid dehydrogenases from Acinetobacter calcoaceticus lwoffii: a new integrated chemo-enzymatic route to ursodeoxycholic acid
    • Giovannini, P.P., Grandini, A., Perrone, D., Pedrini, P., Fantin, G., Fogagnolo, M., 7alpha- and 12alpha-Hydroxysteroid dehydrogenases from Acinetobacter calcoaceticus lwoffii: a new integrated chemo-enzymatic route to ursodeoxycholic acid. Steroids 73:14 (2008), 1385–1390.
    • (2008) Steroids , vol.73 , Issue.14 , pp. 1385-1390
    • Giovannini, P.P.1    Grandini, A.2    Perrone, D.3    Pedrini, P.4    Fantin, G.5    Fogagnolo, M.6
  • 61
    • 84994876898 scopus 로고    scopus 로고
    • An intestinal microbiota–farnesoid X receptor Axis modulates metabolic disease
    • Gonzalez, F.J., Jiang, C., Patterson, A.D., An intestinal microbiota–farnesoid X receptor Axis modulates metabolic disease. Gastroenterology 151:5 (2016), 845–859.
    • (2016) Gastroenterology , vol.151 , Issue.5 , pp. 845-859
    • Gonzalez, F.J.1    Jiang, C.2    Patterson, A.D.3
  • 62
    • 0024058679 scopus 로고
    • Purification and characterization of bile salt hydrolase from Clostridium perfringens
    • Gopal-Srivastava, R., Hylemon, P.B., Purification and characterization of bile salt hydrolase from Clostridium perfringens. J. Lipid Res. 29:8 (1988), 1079–1085.
    • (1988) J. Lipid Res. , vol.29 , Issue.8 , pp. 1079-1085
    • Gopal-Srivastava, R.1    Hylemon, P.B.2
  • 63
    • 84999780423 scopus 로고    scopus 로고
    • Unconjugated bile acids influence expression of circadian genes: a potential mechanism for microbe-host crosstalk
    • Govindarajan, K., MacSharry, J., Casey, P.G., Shanahan, F., Joyce, S.A., Gahan, C.G., Unconjugated bile acids influence expression of circadian genes: a potential mechanism for microbe-host crosstalk. PLoS One, 11(12), 2016, e0167319.
    • (2016) PLoS One , vol.11 , Issue.12 , pp. e0167319
    • Govindarajan, K.1    MacSharry, J.2    Casey, P.G.3    Shanahan, F.4    Joyce, S.A.5    Gahan, C.G.6
  • 64
    • 0017355635 scopus 로고
    • Hydrolysis of steroid glucuronides with beta-glucuronidase preparations from bovine liver, Helix pomatia, and E. coli
    • Graef, V., Furuya, E., Nishikaze, O., Hydrolysis of steroid glucuronides with beta-glucuronidase preparations from bovine liver, Helix pomatia, and E. coli. Clin. Chem. 23:3 (1977), 532–535.
    • (1977) Clin. Chem. , vol.23 , Issue.3 , pp. 532-535
    • Graef, V.1    Furuya, E.2    Nishikaze, O.3
  • 65
    • 0029063548 scopus 로고
    • Purification and characterization of conjugated bile salt hydrolase from Bifidobacterium longum BB536
    • Grill, J., Schneider, F., Crociani, J., Ballongue, J., Purification and characterization of conjugated bile salt hydrolase from Bifidobacterium longum BB536. Appl. Environ. Microbiol. 61:7 (1995), 2577–2582.
    • (1995) Appl. Environ. Microbiol. , vol.61 , Issue.7 , pp. 2577-2582
    • Grill, J.1    Schneider, F.2    Crociani, J.3    Ballongue, J.4
  • 66
    • 0033785297 scopus 로고    scopus 로고
    • Isolation and characterization of a Lactobacillus amylovorus mutant depleted in conjugated bile salt hydrolase activity: relation between activity and bile salt resistance
    • Grill, J.P., Cayuela, C., Antoine, J.M., Schneider, F., Isolation and characterization of a Lactobacillus amylovorus mutant depleted in conjugated bile salt hydrolase activity: relation between activity and bile salt resistance. J. Appl. Microbiol. 89:4 (2000), 553–563.
    • (2000) J. Appl. Microbiol. , vol.89 , Issue.4 , pp. 553-563
    • Grill, J.P.1    Cayuela, C.2    Antoine, J.M.3    Schneider, F.4
  • 67
    • 0029022606 scopus 로고
    • Bifidobacteria and probiotic effects: action of Bifidobacterium species on conjugated bile salts
    • Grill, J.P., Manginot-Durr, C., Schneider, F., Ballongue, J., Bifidobacteria and probiotic effects: action of Bifidobacterium species on conjugated bile salts. Curr. Microbiol. 31:1 (1995), 23–27.
    • (1995) Curr. Microbiol. , vol.31 , Issue.1 , pp. 23-27
    • Grill, J.P.1    Manginot-Durr, C.2    Schneider, F.3    Ballongue, J.4
  • 68
  • 69
    • 84898540132 scopus 로고    scopus 로고
    • Cloning and analysis of bile salt hydrolase genes from Lactobacillus plantarum CGMCC No. 8198
    • Gu, X.C., Luo, X.G., Wang, C.X., Ma, D.Y., Wang, Y., He, Y.Y., Li, W., Zhou, H., Zhang, T.C., Cloning and analysis of bile salt hydrolase genes from Lactobacillus plantarum CGMCC No. 8198. Biotechnol. Lett. 36:5 (2014), 975–983.
    • (2014) Biotechnol. Lett. , vol.36 , Issue.5 , pp. 975-983
    • Gu, X.C.1    Luo, X.G.2    Wang, C.X.3    Ma, D.Y.4    Wang, Y.5    He, Y.Y.6    Li, W.7    Zhou, H.8    Zhang, T.C.9
  • 70
    • 33846078026 scopus 로고    scopus 로고
    • Relationship of dietary antimicrobial drug administration with broiler performance, decreased population levels of Lactobacillus salivarius, and reduced bile salt deconjugation in the ileum of broiler chickens
    • Guban, J., Korver, D.R., Allison, G.E., Tannock, G.W., Relationship of dietary antimicrobial drug administration with broiler performance, decreased population levels of Lactobacillus salivarius, and reduced bile salt deconjugation in the ileum of broiler chickens. Poult. Sci. 85:12 (2006), 2186–2194.
    • (2006) Poult. Sci. , vol.85 , Issue.12 , pp. 2186-2194
    • Guban, J.1    Korver, D.R.2    Allison, G.E.3    Tannock, G.W.4
  • 71
    • 63849295015 scopus 로고    scopus 로고
    • The enterohepatic circulation of bile acids in mammals: form and functions
    • Hofmann, A.F., The enterohepatic circulation of bile acids in mammals: form and functions. Front. Biosci. 14 (2009), 2584–2598.
    • (2009) Front. Biosci. , vol.14 , pp. 2584-2598
    • Hofmann, A.F.1
  • 72
    • 50249180215 scopus 로고    scopus 로고
    • Bile acids: chemistry, pathochemistry, biology, pathobiology, and therapeutics
    • Hofmann, A.F., Hagey, L.R., Bile acids: chemistry, pathochemistry, biology, pathobiology, and therapeutics. Cell. Mol. life Sci. CMLS 65:16 (2008), 2461–2483.
    • (2008) Cell. Mol. life Sci. CMLS , vol.65 , Issue.16 , pp. 2461-2483
    • Hofmann, A.F.1    Hagey, L.R.2
  • 73
    • 0020029418 scopus 로고
    • Isolation of a bile salt sulfatase-producing Clostridium strain from rat intestinal microflora
    • Huijghebaert, S.M., Mertens, J.A., Eyssen, H.J., Isolation of a bile salt sulfatase-producing Clostridium strain from rat intestinal microflora. Appl. Environ. Microbiol. 43:1 (1982), 185–192.
    • (1982) Appl. Environ. Microbiol. , vol.43 , Issue.1 , pp. 185-192
    • Huijghebaert, S.M.1    Mertens, J.A.2    Eyssen, H.J.3
  • 76
    • 84906948414 scopus 로고    scopus 로고
    • Identification and characterization of bile salt hydrolase genes from the genome of Lactobacillus fermentum MTCC 8711
    • Jayashree, S., Pooja, S., Pushpanathan, M., Rajendhran, J., Gunasekaran, P., Identification and characterization of bile salt hydrolase genes from the genome of Lactobacillus fermentum MTCC 8711. Appl. Biochem. Biotechnol. 174:2 (2014), 855–866.
    • (2014) Appl. Biochem. Biotechnol. , vol.174 , Issue.2 , pp. 855-866
    • Jayashree, S.1    Pooja, S.2    Pushpanathan, M.3    Rajendhran, J.4    Gunasekaran, P.5
  • 77
    • 51649086648 scopus 로고    scopus 로고
    • Functional and comparative metagenomic analysis of bile salt hydrolase activity in the human gut microbiome
    • Jones, B.V., Begley, M., Hill, C., Gahan, C.G.M., Marchesi, J.R., Functional and comparative metagenomic analysis of bile salt hydrolase activity in the human gut microbiome. Proc. Natl. Acad. Sci. 105:36 (2008), 13580–13585.
    • (2008) Proc. Natl. Acad. Sci. , vol.105 , Issue.36 , pp. 13580-13585
    • Jones, B.V.1    Begley, M.2    Hill, C.3    Gahan, C.G.M.4    Marchesi, J.R.5
  • 78
    • 84868636856 scopus 로고    scopus 로고
    • Cholesterol lowering and inhibition of sterol absorption by Lactobacillus reuteri NCIMB 30242: a randomized controlled trial
    • Jones, M., Martoni, C., Prakash, S., Cholesterol lowering and inhibition of sterol absorption by Lactobacillus reuteri NCIMB 30242: a randomized controlled trial. Eur. J. Clin. Nutr. 66:11 (2012), 1234–1241.
    • (2012) Eur. J. Clin. Nutr. , vol.66 , Issue.11 , pp. 1234-1241
    • Jones, M.1    Martoni, C.2    Prakash, S.3
  • 79
    • 84863604437 scopus 로고    scopus 로고
    • Cholesterol-lowering efficacy of a microencapsulated bile salt hydrolase-active Lactobacillus reuteri NCIMB 30242 yoghurt formulation in hypercholesterolaemic adults
    • Jones, M.L., Martoni, C.J., Parent, M., Prakash, S., Cholesterol-lowering efficacy of a microencapsulated bile salt hydrolase-active Lactobacillus reuteri NCIMB 30242 yoghurt formulation in hypercholesterolaemic adults. Br. J. Nutr. 107:10 (2012), 1505–1513.
    • (2012) Br. J. Nutr. , vol.107 , Issue.10 , pp. 1505-1513
    • Jones, M.L.1    Martoni, C.J.2    Parent, M.3    Prakash, S.4
  • 80
    • 84861407924 scopus 로고    scopus 로고
    • Evaluation of clinical safety and tolerance of a Lactobacillus reuteri NCIMB 30242 supplement capsule: a randomized control trial
    • Jones, M.L., Martoni, C.J., Di Pietro, E., Simon, R.R., Prakash, S., Evaluation of clinical safety and tolerance of a Lactobacillus reuteri NCIMB 30242 supplement capsule: a randomized control trial. Regul. Toxicol. Pharmacol. 63:2 (2012), 313–320.
    • (2012) Regul. Toxicol. Pharmacol. , vol.63 , Issue.2 , pp. 313-320
    • Jones, M.L.1    Martoni, C.J.2    Di Pietro, E.3    Simon, R.R.4    Prakash, S.5
  • 81
    • 84874911481 scopus 로고    scopus 로고
    • Cholesterol lowering with bile salt hydrolase-active probiotic bacteria, mechanism of action, clinical evidence, and future direction for heart health applications
    • Jones, M.L., Tomaro-Duchesneau, C., Martoni, C.J., Prakash, S., Cholesterol lowering with bile salt hydrolase-active probiotic bacteria, mechanism of action, clinical evidence, and future direction for heart health applications. Expert. Opin. Biol. Ther. 13:5 (2013), 631–642.
    • (2013) Expert. Opin. Biol. Ther. , vol.13 , Issue.5 , pp. 631-642
    • Jones, M.L.1    Tomaro-Duchesneau, C.2    Martoni, C.J.3    Prakash, S.4
  • 82
    • 84894049857 scopus 로고    scopus 로고
    • The gut microbiota and the metabolic health of the host
    • Joyce, S.A., Gahan, C.G., The gut microbiota and the metabolic health of the host. Curr. Opin. Gastroenterol. 30:2 (2014), 120–127.
    • (2014) Curr. Opin. Gastroenterol. , vol.30 , Issue.2 , pp. 120-127
    • Joyce, S.A.1    Gahan, C.G.2
  • 83
    • 84959882996 scopus 로고    scopus 로고
    • Bile acid modifications at the microbe-host interface: potential for nutraceutical and pharmaceutical interventions in host health
    • Joyce, S.A., Gahan, C.G., Bile acid modifications at the microbe-host interface: potential for nutraceutical and pharmaceutical interventions in host health. Annu. Rev. Food. Sci. Technol. 7 (2016), 313–333.
    • (2016) Annu. Rev. Food. Sci. Technol. , vol.7 , pp. 313-333
    • Joyce, S.A.1    Gahan, C.G.2
  • 85
    • 84922021716 scopus 로고    scopus 로고
    • Bacterial bile salt hydrolase in host metabolism: potential for influencing gastrointestinal microbe-host crosstalk
    • Joyce, S.A., Shanahan, F., Hill, C., Gahan, C.G., Bacterial bile salt hydrolase in host metabolism: potential for influencing gastrointestinal microbe-host crosstalk. Gut Microbes 5:5 (2014), 669–674.
    • (2014) Gut Microbes , vol.5 , Issue.5 , pp. 669-674
    • Joyce, S.A.1    Shanahan, F.2    Hill, C.3    Gahan, C.G.4
  • 86
    • 38849090693 scopus 로고    scopus 로고
    • Clostridium scindens baiCD and baiH genes encode stereo-specific 7alpha/7beta-hydroxy-3-oxo-delta4-cholenoic acid oxidoreductases
    • Kang, D.J., Ridlon, J.M., Moore, D.R. 2nd, Barnes, S., Hylemon, P.B., Clostridium scindens baiCD and baiH genes encode stereo-specific 7alpha/7beta-hydroxy-3-oxo-delta4-cholenoic acid oxidoreductases. Biochim. Biophys. Acta 1781:1–2 (2008), 16–25.
    • (2008) Biochim. Biophys. Acta , vol.1781 , Issue.1-2 , pp. 16-25
    • Kang, D.J.1    Ridlon, J.M.2    Moore, D.R.3    Barnes, S.4    Hylemon, P.B.5
  • 88
    • 0024847957 scopus 로고
    • Purification and characterization of a new hydrolase for conjugated bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus
    • Kawamoto, K., Horibe, I., Uchida, K., Purification and characterization of a new hydrolase for conjugated bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus. J. Biochem. 106:6 (1989), 1049–1053.
    • (1989) J. Biochem. , vol.106 , Issue.6 , pp. 1049-1053
    • Kawamoto, K.1    Horibe, I.2    Uchida, K.3
  • 89
    • 0017100043 scopus 로고
    • The biosynthesis of ethyl esters of lithocholic acid and isolithocholic acid by rat intestinal microflora
    • Kelsey, M.I., Sexton, S.A., The biosynthesis of ethyl esters of lithocholic acid and isolithocholic acid by rat intestinal microflora. J. Steroid Biochem. 7:9 (1976), 641–647.
    • (1976) J. Steroid Biochem. , vol.7 , Issue.9 , pp. 641-647
    • Kelsey, M.I.1    Sexton, S.A.2
  • 90
    • 84962053001 scopus 로고    scopus 로고
    • Protective effects of Lactobacillus rhamnosus GG against dyslipidemia in high-fat diet-induced obese mice
    • Kim, B., Park, K.Y., Ji, Y., Park, S., Holzapfel, W., Hyun, C.K., Protective effects of Lactobacillus rhamnosus GG against dyslipidemia in high-fat diet-induced obese mice. Biochem. Biophys. Res. Commun. 473:2 (2016), 530–536.
    • (2016) Biochem. Biophys. Res. Commun. , vol.473 , Issue.2 , pp. 530-536
    • Kim, B.1    Park, K.Y.2    Ji, Y.3    Park, S.4    Holzapfel, W.5    Hyun, C.K.6
  • 91
    • 4644360530 scopus 로고    scopus 로고
    • Cloning and characterization of the bile salt hydrolase genes (bsh) from Bifidobacterium bifidum strains
    • Kim, G.-B., Miyamoto, C.M., Meighen, E.A., Lee, B.H., Cloning and characterization of the bile salt hydrolase genes (bsh) from Bifidobacterium bifidum strains. Appl. Environ. Microbiol. 70:9 (2004), 5603–5612.
    • (2004) Appl. Environ. Microbiol. , vol.70 , Issue.9 , pp. 5603-5612
    • Kim, G.-B.1    Miyamoto, C.M.2    Meighen, E.A.3    Lee, B.H.4
  • 92
    • 23844544377 scopus 로고    scopus 로고
    • Cloning and characterization of a bile salt hydrolase (bsh) from Bifidobacterium adolescentis
    • Kim, G.B., Brochet, M., Lee, B.H., Cloning and characterization of a bile salt hydrolase (bsh) from Bifidobacterium adolescentis. Biotechnol. Lett. 27:12 (2005), 817–822.
    • (2005) Biotechnol. Lett. , vol.27 , Issue.12 , pp. 817-822
    • Kim, G.B.1    Brochet, M.2    Lee, B.H.3
  • 93
    • 2142651752 scopus 로고    scopus 로고
    • Purification and characterization of three different types of bile salt hydrolases from Bifidobacterium strains
    • Kim, G.B., Yi, S.H., Lee, B.H., Purification and characterization of three different types of bile salt hydrolases from Bifidobacterium strains. J. Dairy Sci. 87:2 (2004), 258–266.
    • (2004) J. Dairy Sci. , vol.87 , Issue.2 , pp. 258-266
    • Kim, G.B.1    Yi, S.H.2    Lee, B.H.3
  • 94
    • 84857787967 scopus 로고    scopus 로고
    • Hydroxysteroid dehydrogenases (HSDs) in bacteria: a bioinformatic perspective
    • Kisiela, M., Skarka, A., Ebert, B., Maser, E., Hydroxysteroid dehydrogenases (HSDs) in bacteria: a bioinformatic perspective. J. Steroid Biochem. Mol. Biol. 129:1–2 (2012), 31–46.
    • (2012) J. Steroid Biochem. Mol. Biol. , vol.129 , Issue.1-2 , pp. 31-46
    • Kisiela, M.1    Skarka, A.2    Ebert, B.3    Maser, E.4
  • 97
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E., Henrick, K., Inference of macromolecular assemblies from crystalline state. J. Mol. Biol. 372:3 (2007), 774–797.
    • (2007) J. Mol. Biol. , vol.372 , Issue.3 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 98
    • 33845963604 scopus 로고    scopus 로고
    • Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase
    • Kumar, R.S., Brannigan, J.A., Prabhune, A.A., Pundle, A.V., Dodson, G.G., Dodson, E.J., Suresh, C.G., Structural and functional analysis of a conjugated bile salt hydrolase from Bifidobacterium longum reveals an evolutionary relationship with penicillin V acylase. J. Biol. Chem. 281:43 (2006), 32516–32525.
    • (2006) J. Biol. Chem. , vol.281 , Issue.43 , pp. 32516-32525
    • Kumar, R.S.1    Brannigan, J.A.2    Prabhune, A.A.3    Pundle, A.V.4    Dodson, G.G.5    Dodson, E.J.6    Suresh, C.G.7
  • 99
    • 49449092314 scopus 로고    scopus 로고
    • Functional analysis of four bile salt hydrolase and penicillin acylase family members in Lactobacillus plantarum WCFS1
    • Lambert, J.M., Bongers, R.S., de Vos, W.M., Kleerebezem, M., Functional analysis of four bile salt hydrolase and penicillin acylase family members in Lactobacillus plantarum WCFS1. Appl. Environ. Microbiol. 74:15 (2008), 4719–4726.
    • (2008) Appl. Environ. Microbiol. , vol.74 , Issue.15 , pp. 4719-4726
    • Lambert, J.M.1    Bongers, R.S.2    de Vos, W.M.3    Kleerebezem, M.4
  • 100
    • 51149085146 scopus 로고    scopus 로고
    • Improved annotation of conjugated bile acid hydrolase superfamily members in Gram-positive bacteria
    • Lambert, J.M., Siezen, R.J., de Vos, W.M., Kleerebezem, M., Improved annotation of conjugated bile acid hydrolase superfamily members in Gram-positive bacteria. Microbiology 154:8 (2008), 2492–2500.
    • (2008) Microbiology , vol.154 , Issue.8 , pp. 2492-2500
    • Lambert, J.M.1    Siezen, R.J.2    de Vos, W.M.3    Kleerebezem, M.4
  • 103
    • 2442678019 scopus 로고    scopus 로고
    • Epimerization of chenodeoxycholic acid to ursodeoxycholic acid by Clostridium baratii isolated from human feces
    • Lepercq, P., Gerard, P., Beguet, F., Raibaud, P., Grill, J.P., Relano, P., Cayuela, C., Juste, C., Epimerization of chenodeoxycholic acid to ursodeoxycholic acid by Clostridium baratii isolated from human feces. FEMS Microbiol. Lett. 235:1 (2004), 65–72.
    • (2004) FEMS Microbiol. Lett. , vol.235 , Issue.1 , pp. 65-72
    • Lepercq, P.1    Gerard, P.2    Beguet, F.3    Raibaud, P.4    Grill, J.P.5    Relano, P.6    Cayuela, C.7    Juste, C.8
  • 104
    • 85027957031 scopus 로고    scopus 로고
    • Bile acid sensitivity and in vivo virulence of clinical Clostridium difficile isolates
    • Lewis, B.B., Carter, R.A., Pamer, E.G., Bile acid sensitivity and in vivo virulence of clinical Clostridium difficile isolates. Anaerobe 41 (2016), 32–36.
    • (2016) Anaerobe , vol.41 , pp. 32-36
    • Lewis, B.B.1    Carter, R.A.2    Pamer, E.G.3
  • 106
    • 84872741573 scopus 로고    scopus 로고
    • Nuclear receptors in bile acid metabolism
    • Li, T., Chiang, J.Y., Nuclear receptors in bile acid metabolism. Drug Metab. Rev. 45:1 (2013), 145–155.
    • (2013) Drug Metab. Rev. , vol.45 , Issue.1 , pp. 145-155
    • Li, T.1    Chiang, J.Y.2
  • 107
    • 84905257719 scopus 로고    scopus 로고
    • Bile acid signaling in metabolic disease and drug therapy
    • Li, T., Chiang, J.Y., Bile acid signaling in metabolic disease and drug therapy. Pharmacol. Rev. 66:4 (2014), 948–983.
    • (2014) Pharmacol. Rev. , vol.66 , Issue.4 , pp. 948-983
    • Li, T.1    Chiang, J.Y.2
  • 108
    • 12344257016 scopus 로고    scopus 로고
    • Bile salt deconjugation ability, bile salt hydrolase activity and cholesterol co-precipitation ability of lactobacilli strains
    • Liong, M.T., Shah, N.P., Bile salt deconjugation ability, bile salt hydrolase activity and cholesterol co-precipitation ability of lactobacilli strains. Int. Dairy J. 15:4 (2005), 391–398.
    • (2005) Int. Dairy J. , vol.15 , Issue.4 , pp. 391-398
    • Liong, M.T.1    Shah, N.P.2
  • 109
    • 84876139394 scopus 로고    scopus 로고
    • Conserved shifts in the gut microbiota due to gastric bypass reduce host weight and adiposity
    • 178ra141
    • Liou, A.P., Paziuk, M., Luevano, J.M. Jr., Machineni, S., Turnbaugh, P.J., Kaplan, L.M., Conserved shifts in the gut microbiota due to gastric bypass reduce host weight and adiposity. Sci. Transl. Med., 5(178), 2013 178ra141.
    • (2013) Sci. Transl. Med. , vol.5 , Issue.178
    • Liou, A.P.1    Paziuk, M.2    Luevano, J.M.3    Machineni, S.4    Turnbaugh, P.J.5    Kaplan, L.M.6
  • 110
    • 0025348851 scopus 로고
    • Characterization and purification of bile salt hydrolase from Lactobacillus sp. strain 100-100
    • Lundeen, S.G., Savage, D.C., Characterization and purification of bile salt hydrolase from Lactobacillus sp. strain 100-100. J. Bacteriol. 172:8 (1990), 4171–4177.
    • (1990) J. Bacteriol. , vol.172 , Issue.8 , pp. 4171-4177
    • Lundeen, S.G.1    Savage, D.C.2
  • 112
    • 0019518952 scopus 로고
    • Formation of urso- and ursodeoxy-cholic acids from primary bile acids by Clostridium absonum
    • Macdonald, I.A., Hutchison, D.M., Forrest, T.P., Formation of urso- and ursodeoxy-cholic acids from primary bile acids by Clostridium absonum. J. Lipid Res. 22:3 (1981), 458–466.
    • (1981) J. Lipid Res. , vol.22 , Issue.3 , pp. 458-466
    • Macdonald, I.A.1    Hutchison, D.M.2    Forrest, T.P.3
  • 113
    • 0026532069 scopus 로고
    • The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase
    • Mallonee, D.H., Adams, J.L., Hylemon, P.B., The bile acid-inducible baiB gene from Eubacterium sp. strain VPI 12708 encodes a bile acid-coenzyme A ligase. J. Bacteriol. 174:7 (1992), 2065–2071.
    • (1992) J. Bacteriol. , vol.174 , Issue.7 , pp. 2065-2071
    • Mallonee, D.H.1    Adams, J.L.2    Hylemon, P.B.3
  • 114
    • 0030447221 scopus 로고    scopus 로고
    • Sequencing and expression of a gene encoding a bile acid transporter from Eubacterium sp. strain VPI 12708
    • Mallonee, D.H., Hylemon, P.B., Sequencing and expression of a gene encoding a bile acid transporter from Eubacterium sp. strain VPI 12708. J. Bacteriol. 178:24 (1996), 7053–7058.
    • (1996) J. Bacteriol. , vol.178 , Issue.24 , pp. 7053-7058
    • Mallonee, D.H.1    Hylemon, P.B.2
  • 115
    • 0025606274 scopus 로고
    • Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708
    • Mallonee, D.H., White, W.B., Hylemon, P.B., Cloning and sequencing of a bile acid-inducible operon from Eubacterium sp. strain VPI 12708. J. Bacteriol. 172:12 (1990), 7011–7019.
    • (1990) J. Bacteriol. , vol.172 , Issue.12 , pp. 7011-7019
    • Mallonee, D.H.1    White, W.B.2    Hylemon, P.B.3
  • 116
    • 0021368274 scopus 로고
    • 7 alpha-Dehydroxylation of bile acids by resting cells of a Eubacterium lentum-like intestinal anaerobe, strain c-25
    • Masuda, N., Oda, H., Hirano, S., Masuda, M., Tanaka, H., 7 alpha-Dehydroxylation of bile acids by resting cells of a Eubacterium lentum-like intestinal anaerobe, strain c-25. Appl. Environ. Microbiol. 47:4 (1984), 735–739.
    • (1984) Appl. Environ. Microbiol. , vol.47 , Issue.4 , pp. 735-739
    • Masuda, N.1    Oda, H.2    Hirano, S.3    Masuda, M.4    Tanaka, H.5
  • 117
    • 84925486076 scopus 로고    scopus 로고
    • The gut microbiota and inflammatory bowel disease
    • Matsuoka, K., Kanai, T., The gut microbiota and inflammatory bowel disease. Semin. Immunopathol. 37:1 (2015), 47–55.
    • (2015) Semin. Immunopathol. , vol.37 , Issue.1 , pp. 47-55
    • Matsuoka, K.1    Kanai, T.2
  • 118
    • 23744451686 scopus 로고    scopus 로고
    • Genetic analysis of two bile salt hydrolase activities in Lactobacillus acidophilus NCFM
    • McAuliffe, O., Cano, R.J., Klaenhammer, T.R., Genetic analysis of two bile salt hydrolase activities in Lactobacillus acidophilus NCFM. Appl. Environ. Microbiol. 71:8 (2005), 4925–4929.
    • (2005) Appl. Environ. Microbiol. , vol.71 , Issue.8 , pp. 4925-4929
    • McAuliffe, O.1    Cano, R.J.2    Klaenhammer, T.R.3
  • 119
    • 33845267470 scopus 로고    scopus 로고
    • The role of cytochrome P450 enzymes in endogenous signalling pathways and environmental carcinogenesis
    • Nebert, D.W., Dalton, T.P., The role of cytochrome P450 enzymes in endogenous signalling pathways and environmental carcinogenesis. Nat. Rev. Cancer 6:12 (2006), 947–960.
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.12 , pp. 947-960
    • Nebert, D.W.1    Dalton, T.P.2
  • 122
    • 0034495297 scopus 로고    scopus 로고
    • Structural comparison of Ntn-hydrolases
    • Oinonen, C., Rouvinen, J., Structural comparison of Ntn-hydrolases. Protein Sci. 9:12 (2000), 2329–2337.
    • (2000) Protein Sci. , vol.9 , Issue.12 , pp. 2329-2337
    • Oinonen, C.1    Rouvinen, J.2
  • 123
    • 78649340112 scopus 로고    scopus 로고
    • Lactobacillus gasseri [corrected] CHO-220 and inulin reduced plasma total cholesterol and low-density lipoprotein cholesterol via alteration of lipid transporters
    • Ooi, L.G., Ahmad, R., Yuen, K.H., Liong, M.T., Lactobacillus gasseri [corrected] CHO-220 and inulin reduced plasma total cholesterol and low-density lipoprotein cholesterol via alteration of lipid transporters. J. Dairy Sci. 93:11 (2010), 5048–5058.
    • (2010) J. Dairy Sci. , vol.93 , Issue.11 , pp. 5048-5058
    • Ooi, L.G.1    Ahmad, R.2    Yuen, K.H.3    Liong, M.T.4
  • 124
    • 84901717147 scopus 로고    scopus 로고
    • An improved method for specificity annotation shows a distinct evolutionary divergence among the microbial enzymes of the cholylglycine hydrolase family
    • Panigrahi, P., Sule, M., Sharma, R., Ramasamy, S., Suresh, C.G., An improved method for specificity annotation shows a distinct evolutionary divergence among the microbial enzymes of the cholylglycine hydrolase family. Microbiology 160:6 (2014), 1162–1174.
    • (2014) Microbiology , vol.160 , Issue.6 , pp. 1162-1174
    • Panigrahi, P.1    Sule, M.2    Sharma, R.3    Ramasamy, S.4    Suresh, C.G.5
  • 127
    • 32144453839 scopus 로고    scopus 로고
    • Xanthomonas maltophilia CBS 897.97 as a source of new 7β- and 7α-hydroxysteroid dehydrogenases and cholylglycine hydrolase: improved biotransformations of bile acids
    • Pedrini, P., Andreotti, E., Guerrini, A., Dean, M., Fantin, G., Giovannini, P.P., Xanthomonas maltophilia CBS 897.97 as a source of new 7β- and 7α-hydroxysteroid dehydrogenases and cholylglycine hydrolase: improved biotransformations of bile acids. Steroids 71:3 (2006), 189–198.
    • (2006) Steroids , vol.71 , Issue.3 , pp. 189-198
    • Pedrini, P.1    Andreotti, E.2    Guerrini, A.3    Dean, M.4    Fantin, G.5    Giovannini, P.P.6
  • 128
    • 84997334774 scopus 로고    scopus 로고
    • Short bowel syndrome (SBS)-associated alterations within the gut-liver axis evolve early and persist long-term in the piglet model of short bowel syndrome
    • Pereira-Fantini, P.M., Bines, J.E., Lapthorne, S., Fouhy, F., Scurr, M., Cotter, P.D., Gahan, C.G., Joyce, S.A., Short bowel syndrome (SBS)-associated alterations within the gut-liver axis evolve early and persist long-term in the piglet model of short bowel syndrome. J. Gastroenterol. Hepatol. 31:12 (2016), 1946–1955.
    • (2016) J. Gastroenterol. Hepatol. , vol.31 , Issue.12 , pp. 1946-1955
    • Pereira-Fantini, P.M.1    Bines, J.E.2    Lapthorne, S.3    Fouhy, F.4    Scurr, M.5    Cotter, P.D.6    Gahan, C.G.7    Joyce, S.A.8
  • 130
    • 0036731780 scopus 로고    scopus 로고
    • Cholesterol assimilation by lactic acid bacteria and bifidobacteria isolated from the human gut
    • Pereira, D.I., Gibson, G.R., Cholesterol assimilation by lactic acid bacteria and bifidobacteria isolated from the human gut. Appl. Environ. Microbiol. 68:9 (2002), 4689–4693.
    • (2002) Appl. Environ. Microbiol. , vol.68 , Issue.9 , pp. 4689-4693
    • Pereira, D.I.1    Gibson, G.R.2
  • 131
    • 80955151991 scopus 로고    scopus 로고
    • All 4 bile salt hydrolase proteins are responsible for the hydrolysis activity in Lactobacillus plantarum ST-III
    • Ren, J., Sun, K., Wu, Z., Yao, J., Guo, B., All 4 bile salt hydrolase proteins are responsible for the hydrolysis activity in Lactobacillus plantarum ST-III. J. Food Sci. 76:9 (2011), M622–M628.
    • (2011) J. Food Sci. , vol.76 , Issue.9 , pp. M622-M628
    • Ren, J.1    Sun, K.2    Wu, Z.3    Yao, J.4    Guo, B.5
  • 132
    • 84455192400 scopus 로고    scopus 로고
    • Identification and characterization of two bile acid coenzyme A transferases from Clostridium scindens, a bile acid 7alpha-dehydroxylating intestinal bacterium
    • Ridlon, J.M., Hylemon, P.B., Identification and characterization of two bile acid coenzyme A transferases from Clostridium scindens, a bile acid 7alpha-dehydroxylating intestinal bacterium. J. Lipid Res. 53:1 (2012), 66–76.
    • (2012) J. Lipid Res. , vol.53 , Issue.1 , pp. 66-76
    • Ridlon, J.M.1    Hylemon, P.B.2
  • 133
    • 33244467651 scopus 로고    scopus 로고
    • Bile salt biotransformations by human intestinal bacteria
    • Ridlon, J.M., Kang, D.J., Hylemon, P.B., Bile salt biotransformations by human intestinal bacteria. J. Lipid Res. 47:2 (2006), 241–259.
    • (2006) J. Lipid Res. , vol.47 , Issue.2 , pp. 241-259
    • Ridlon, J.M.1    Kang, D.J.2    Hylemon, P.B.3
  • 134
    • 77951768945 scopus 로고    scopus 로고
    • Isolation and characterization of a bile acid inducible 7alpha-dehydroxylating operon in Clostridium hylemonae TN271
    • Ridlon, J.M., Kang, D.J., Hylemon, P.B., Isolation and characterization of a bile acid inducible 7alpha-dehydroxylating operon in Clostridium hylemonae TN271. Anaerobe 16:2 (2010), 137–146.
    • (2010) Anaerobe , vol.16 , Issue.2 , pp. 137-146
    • Ridlon, J.M.1    Kang, D.J.2    Hylemon, P.B.3
  • 135
    • 33645116164 scopus 로고    scopus 로고
    • Cytochrome P450 pharmacogenetics and cancer
    • Rodriguez-Antona, C., Ingelman-Sundberg, M., Cytochrome P450 pharmacogenetics and cancer. Oncogene 25:11 (2006), 1679–1691.
    • (2006) Oncogene , vol.25 , Issue.11 , pp. 1679-1691
    • Rodriguez-Antona, C.1    Ingelman-Sundberg, M.2
  • 136
    • 17144405290 scopus 로고    scopus 로고
    • Conjugated bile acid hydrolase is a tetrameric N-Terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product
    • Rossocha, M., Schultz-Heienbrok, R., von Moeller, H., Coleman, J.P., Saenger, W., Conjugated bile acid hydrolase is a tetrameric N-Terminal thiol hydrolase with specific recognition of its cholyl but not of its tauryl product. Biochemistry 44:15 (2005), 5739–5748.
    • (2005) Biochemistry , vol.44 , Issue.15 , pp. 5739-5748
    • Rossocha, M.1    Schultz-Heienbrok, R.2    von Moeller, H.3    Coleman, J.P.4    Saenger, W.5
  • 137
    • 84872742547 scopus 로고    scopus 로고
    • Regulation of the cytosolic sulfotransferases by nuclear receptors
    • Runge-Morris, M., Kocarek, T.A., Falany, C.N., Regulation of the cytosolic sulfotransferases by nuclear receptors. Drug Metab. Rev. 45:1 (2013), 15–33.
    • (2013) Drug Metab. Rev. , vol.45 , Issue.1 , pp. 15-33
    • Runge-Morris, M.1    Kocarek, T.A.2    Falany, C.N.3
  • 140
  • 141
    • 0000447259 scopus 로고
    • Dietary glycine and taurine on bile acid conjugation in man; bile acids and steroids 75
    • Sjovall, J., Dietary glycine and taurine on bile acid conjugation in man; bile acids and steroids 75. Proc. Soc. Exp. Biol. Med. 100:4 (1959), 676–678.
    • (1959) Proc. Soc. Exp. Biol. Med. , vol.100 , Issue.4 , pp. 676-678
    • Sjovall, J.1
  • 142
    • 0028254682 scopus 로고    scopus 로고
    • In vitro study of bile salt hydrolase (BSH) activity of BSH isogenic Lactobacillus plantarum 80 strains and estimation of cholesterol lowering through enhanced BSH activity
    • Smet, I.D., Hoorde, L.V., Saeyer, N.D., Woestyne, M.V., Verstraete, W., In vitro study of bile salt hydrolase (BSH) activity of BSH isogenic Lactobacillus plantarum 80 strains and estimation of cholesterol lowering through enhanced BSH activity. Microb. Ecol. Health Dis., 7(6), 2011.
    • (2011) Microb. Ecol. Health Dis. , vol.7 , Issue.6
    • Smet, I.D.1    Hoorde, L.V.2    Saeyer, N.D.3    Woestyne, M.V.4    Verstraete, W.5
  • 143
    • 84897621880 scopus 로고    scopus 로고
    • Discovery of bile salt hydrolase inhibitors using an efficient high-throughput screening system
    • Smith, K., Zeng, X., Lin, J., Discovery of bile salt hydrolase inhibitors using an efficient high-throughput screening system. PLoS One, 9(1), 2014, e85344.
    • (2014) PLoS One , vol.9 , Issue.1 , pp. e85344
    • Smith, K.1    Zeng, X.2    Lin, J.3
  • 144
    • 77957337708 scopus 로고    scopus 로고
    • Inhibiting the initiation of Clostridium difficile spore germination using analogs of chenodeoxycholic acid, a bile acid
    • Sorg, J.A., Sonenshein, A.L., Inhibiting the initiation of Clostridium difficile spore germination using analogs of chenodeoxycholic acid, a bile acid. J. Bacteriol. 192:19 (2010), 4983–4990.
    • (2010) J. Bacteriol. , vol.192 , Issue.19 , pp. 4983-4990
    • Sorg, J.A.1    Sonenshein, A.L.2
  • 145
    • 67649890953 scopus 로고    scopus 로고
    • Brevibacillus sp: a novel thermophilic source for the production of bile salt hydrolase
    • Sridevi, N., Prabhune, A.A., Brevibacillus sp: a novel thermophilic source for the production of bile salt hydrolase. Appl. Biochem. Biotech. 157:2 (2009), 254–262.
    • (2009) Appl. Biochem. Biotech. , vol.157 , Issue.2 , pp. 254-262
    • Sridevi, N.1    Prabhune, A.A.2
  • 146
    • 61449163738 scopus 로고    scopus 로고
    • Characterization of the smallest dimeric bile salt hydrolase from a thermophile Brevibacillus sp
    • Sridevi, N., Srivastava, S., Khan, B.M., Prabhune, A.A., Characterization of the smallest dimeric bile salt hydrolase from a thermophile Brevibacillus sp. Extremophiles 13:2 (2009), 363–370.
    • (2009) Extremophiles , vol.13 , Issue.2 , pp. 363-370
    • Sridevi, N.1    Srivastava, S.2    Khan, B.M.3    Prabhune, A.A.4
  • 147
    • 0017110325 scopus 로고
    • Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis
    • Stellwag, E.J., Hylemon, P.B., Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis. Biochim. Biophys. Acta 452:1 (1976), 165–176.
    • (1976) Biochim. Biophys. Acta , vol.452 , Issue.1 , pp. 165-176
    • Stellwag, E.J.1    Hylemon, P.B.2
  • 149
    • 84910003335 scopus 로고    scopus 로고
    • Metabolic surgery: action via hormonal milieu changes, changes in bile acids or gut microbiota? A summary of the literature
    • Sweeney, T.E., Morton, J.M., Metabolic surgery: action via hormonal milieu changes, changes in bile acids or gut microbiota? A summary of the literature. Best. Pract. Res. Clin. Gastroenterol. 28:4 (2014), 727–740.
    • (2014) Best. Pract. Res. Clin. Gastroenterol. , vol.28 , Issue.4 , pp. 727-740
    • Sweeney, T.E.1    Morton, J.M.2
  • 150
    • 84952637577 scopus 로고    scopus 로고
    • Absence of the intestinal microbiota exacerbates hepatobiliary disease in a murine model of primary sclerosing cholangitis
    • Tabibian, J.H., O'Hara, S.P., Trussoni, C.E., Tietz, P.S., Splinter, P.L., Mounajjed, T., Hagey, L.R., LaRusso, N.F., Absence of the intestinal microbiota exacerbates hepatobiliary disease in a murine model of primary sclerosing cholangitis. Hepatology 63:1 (2016), 185–196.
    • (2016) Hepatology , vol.63 , Issue.1 , pp. 185-196
    • Tabibian, J.H.1    O'Hara, S.P.2    Trussoni, C.E.3    Tietz, P.S.4    Splinter, P.L.5    Mounajjed, T.6    Hagey, L.R.7    LaRusso, N.F.8
  • 151
    • 0034048222 scopus 로고    scopus 로고
    • Bile salt hydrolase of Bifidobacterium longum—biochemical and genetic characterization
    • Tanaka, H., Hashiba, H., Kok, J., Mierau, I., Bile salt hydrolase of Bifidobacterium longum—biochemical and genetic characterization. Appl. Environ. Microbiol. 66:6 (2000), 2502–2512.
    • (2000) Appl. Environ. Microbiol. , vol.66 , Issue.6 , pp. 2502-2512
    • Tanaka, H.1    Hashiba, H.2    Kok, J.3    Mierau, I.4
  • 152
    • 0024374964 scopus 로고
    • Lactobacilli and bile salt hydrolase in the murine intestinal tract
    • Tannock, G.W., Dashkevicz, M.P., Feighner, S.D., Lactobacilli and bile salt hydrolase in the murine intestinal tract. Appl. Environ. Microbiol. 55:7 (1989), 1848–1851.
    • (1989) Appl. Environ. Microbiol. , vol.55 , Issue.7 , pp. 1848-1851
    • Tannock, G.W.1    Dashkevicz, M.P.2    Feighner, S.D.3
  • 153
    • 0032150419 scopus 로고    scopus 로고
    • Purification and properties of a novel sulfatase from Pseudomonas testosteroni that hydrolyzed 3 beta-hydroxy-5-cholenoic acid 3-sulfate
    • Tazuke, Y., Matsuda, K., Adachi, K., Tsukada, Y., Purification and properties of a novel sulfatase from Pseudomonas testosteroni that hydrolyzed 3 beta-hydroxy-5-cholenoic acid 3-sulfate. Biosci. Biotechnol. Biochem. 62:9 (1998), 1739–1744.
    • (1998) Biosci. Biotechnol. Biochem. , vol.62 , Issue.9 , pp. 1739-1744
    • Tazuke, Y.1    Matsuda, K.2    Adachi, K.3    Tsukada, Y.4
  • 156
    • 84927538688 scopus 로고    scopus 로고
    • Cholesterol assimilation by Lactobacillus probiotic bacteria: an in vitro investigation
    • Tomaro-Duchesneau, C., Cholesterol assimilation by Lactobacillus probiotic bacteria: an in vitro investigation. Biomed. Res. Int., 2014, 2014, 380316.
    • (2014) Biomed. Res. Int. , vol.2014 , pp. 380316
    • Tomaro-Duchesneau, C.1
  • 158
    • 84857669243 scopus 로고    scopus 로고
    • Probiotic ferulic acid esterase active Lactobacillus fermentum NCIMB 5221 APA microcapsules for oral delivery: preparation and in vitro characterization
    • Tomaro-Duchesneau, C., Saha, S., Malhotra, M., Coussa-Charley, M., Kahouli, I., Jones, M.L., Labbé, A., Prakash, S., Probiotic ferulic acid esterase active Lactobacillus fermentum NCIMB 5221 APA microcapsules for oral delivery: preparation and in vitro characterization. Pharmaceuticals 5:2 (2012), 236–248.
    • (2012) Pharmaceuticals , vol.5 , Issue.2 , pp. 236-248
    • Tomaro-Duchesneau, C.1    Saha, S.2    Malhotra, M.3    Coussa-Charley, M.4    Kahouli, I.5    Jones, M.L.6    Labbé, A.7    Prakash, S.8
  • 159
    • 0025039774 scopus 로고
    • Influence of intestinal bacterial desulfation on the enterohepatic circulation of dehydroepiandrosterone sulfate
    • Van Eldere, J., Mertens, J., Eyssen, H., Influence of intestinal bacterial desulfation on the enterohepatic circulation of dehydroepiandrosterone sulfate. J. Steroid Biochem. 36:5 (1990), 451–456.
    • (1990) J. Steroid Biochem. , vol.36 , Issue.5 , pp. 451-456
    • Van Eldere, J.1    Mertens, J.2    Eyssen, H.3
  • 160
    • 84975784398 scopus 로고    scopus 로고
    • The role of bile acids in metabolic regulation
    • Vitek, L., Haluzik, M., The role of bile acids in metabolic regulation. J. Endocrinol. 228:3 (2016), R85–R96.
    • (2016) J. Endocrinol. , vol.228 , Issue.3 , pp. R85-R96
    • Vitek, L.1    Haluzik, M.2
  • 161
    • 33747063863 scopus 로고    scopus 로고
    • Lactobacillus spp. with in vitro probiotic properties from human faeces and traditional fermented products
    • Vizoso Pinto, M.G., Franz, C.M.A.P., Schillinger, U., Holzapfel, W.H., Lactobacillus spp. with in vitro probiotic properties from human faeces and traditional fermented products. Int. J. Food Microbiol. 109:3 (2006), 205–214.
    • (2006) Int. J. Food Microbiol. , vol.109 , Issue.3 , pp. 205-214
    • Vizoso Pinto, M.G.1    Franz, C.M.A.P.2    Schillinger, U.3    Holzapfel, W.H.4
  • 162
    • 84882568778 scopus 로고    scopus 로고
    • Glycine metabolism in animals and humans: implications for nutrition and health
    • Wang, W., Wu, Z., Dai, Z., Yang, Y., Wang, J., Wu, G., Glycine metabolism in animals and humans: implications for nutrition and health. Amino Acids 45:3 (2013), 463–477.
    • (2013) Amino Acids , vol.45 , Issue.3 , pp. 463-477
    • Wang, W.1    Wu, Z.2    Dai, Z.3    Yang, Y.4    Wang, J.5    Wu, G.6
  • 163
    • 84871016728 scopus 로고    scopus 로고
    • Identification and characterization of a bile salt hydrolase from Lactobacillus salivarius for development of novel alternatives to antibiotic growth promoters
    • Wang, Z., Zeng, X., Mo, Y., Smith, K., Guo, Y., Lin, J., Identification and characterization of a bile salt hydrolase from Lactobacillus salivarius for development of novel alternatives to antibiotic growth promoters. Appl. Environ. Microbiol. 78:24 (2012), 8795–8802.
    • (2012) Appl. Environ. Microbiol. , vol.78 , Issue.24 , pp. 8795-8802
    • Wang, Z.1    Zeng, X.2    Mo, Y.3    Smith, K.4    Guo, Y.5    Lin, J.6
  • 166
    • 84958576368 scopus 로고    scopus 로고
    • Changes in colonic bile acid composition following fecal microbiota transplantation are sufficient to control Clostridium difficile germination and growth
    • Weingarden, A.R., Dosa, P.I., DeWinter, E., Steer, C.J., Shaughnessy, M.K., Johnson, J.R., Khoruts, A., Sadowsky, M.J., Changes in colonic bile acid composition following fecal microbiota transplantation are sufficient to control Clostridium difficile germination and growth. PLoS One, 11(1), 2016, e0147210.
    • (2016) PLoS One , vol.11 , Issue.1 , pp. e0147210
    • Weingarden, A.R.1    Dosa, P.I.2    DeWinter, E.3    Steer, C.J.4    Shaughnessy, M.K.5    Johnson, J.R.6    Khoruts, A.7    Sadowsky, M.J.8
  • 167
    • 0034010274 scopus 로고    scopus 로고
    • Identification and characterization of a bile acid 7alpha-dehydroxylation operon in Clostridium sp. strain TO-931, a highly active 7alpha-dehydroxylating strain isolated from human feces
    • Wells, J.E., Hylemon, P.B., Identification and characterization of a bile acid 7alpha-dehydroxylation operon in Clostridium sp. strain TO-931, a highly active 7alpha-dehydroxylating strain isolated from human feces. Appl. Environ. Microbiol. 66:3 (2000), 1107–1113.
    • (2000) Appl. Environ. Microbiol. , vol.66 , Issue.3 , pp. 1107-1113
    • Wells, J.E.1    Hylemon, P.B.2
  • 168
    • 10344266990 scopus 로고    scopus 로고
    • Cloning of the bile salt hydrolase (bsh) gene from Enterococcus faecium FAIR-E 345 and chromosomal location of bsh genes in food enterococci
    • Wijaya, A., Hermann, A., Abriouel, H., Specht, I., Yousif, N.M.K., Holzapfel, W.H., Franz, C.M.A.P., Cloning of the bile salt hydrolase (bsh) gene from Enterococcus faecium FAIR-E 345 and chromosomal location of bsh genes in food enterococci. J. Food Prot. 67:12 (2004), 2772–2778.
    • (2004) J. Food Prot. , vol.67 , Issue.12 , pp. 2772-2778
    • Wijaya, A.1    Hermann, A.2    Abriouel, H.3    Specht, I.4    Yousif, N.M.K.5    Holzapfel, W.H.6    Franz, C.M.A.P.7
  • 170
    • 84969135865 scopus 로고    scopus 로고
    • Crystal structure of bile salt hydrolase from Lactobacillus salivarius
    • Xu, F., Guo, F., Hu, X.-J., Lin, J., Crystal structure of bile salt hydrolase from Lactobacillus salivarius. Acta Crystallogr. Sect. F. 72:5 (2016), 376–381.
    • (2016) Acta Crystallogr. Sect. F. , vol.72 , Issue.5 , pp. 376-381
    • Xu, F.1    Guo, F.2    Hu, X.-J.3    Lin, J.4
  • 174
    • 84901365815 scopus 로고    scopus 로고
    • Bile acids are nutrient signaling hormones
    • Zhou, H., Hylemon, P.B., Bile acids are nutrient signaling hormones. Steroids 86 (2014), 62–68.
    • (2014) Steroids , vol.86 , pp. 62-68
    • Zhou, H.1    Hylemon, P.B.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.