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Volumn 29, Issue 4, 2005, Pages 625-651

The interaction between bacteria and bile

Author keywords

Bile salt hydrolase; Gastrointestinal persistence; Probiotic; Stress; Virulence

Indexed keywords

BILE ACID; BILE ACID CONJUGATE; BILE SALT; HYDROLASE; LIPOPOLYSACCHARIDE; MICROBIAL ENZYME;

EID: 20444493331     PISSN: 01686445     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.femsre.2004.09.003     Document Type: Review
Times cited : (1345)

References (259)
  • 1
    • 0000413318 scopus 로고    scopus 로고
    • Stress response in pathogenic bacteria
    • R. Chowdhury, G.K. Sahu, and J. Das Stress response in pathogenic bacteria J. Biosci. 21 1996 149 160
    • (1996) J. Biosci. , vol.21 , pp. 149-160
    • Chowdhury, R.1    Sahu, G.K.2    Das, J.3
  • 2
    • 0002310338 scopus 로고
    • Enterohepatic circulation
    • I.M. Arias J.L. Boyer N. Fausto W.B. Jackoby D.A. Schachter D.A. Shafritz Raven Press Ltd New York
    • M.C. Carey, and W.C. Duane Enterohepatic circulation I.M. Arias J.L. Boyer N. Fausto W.B. Jackoby D.A. Schachter D.A. Shafritz The Liver: Biology and Pathobiology 1994 Raven Press Ltd New York 719 738
    • (1994) The Liver: Biology and Pathobiology , pp. 719-738
    • Carey, M.C.1    Duane, W.C.2
  • 3
    • 0002966509 scopus 로고
    • Bile flow
    • I.M. Arias J.L. Boyer N. Fausto W.B. Jackoby D.A. Schachter D.A. Shafritz Raven Press Ltd New York
    • S. Erlinger Bile flow I.M. Arias J.L. Boyer N. Fausto W.B. Jackoby D.A. Schachter D.A. Shafritz The Liver: Biology and Pathobiology 1994 Raven Press Ltd New York 769 786
    • (1994) The Liver: Biology and Pathobiology , pp. 769-786
    • Erlinger, S.1
  • 4
    • 0033470181 scopus 로고    scopus 로고
    • Bile acids: The good, the bad, and the ugly
    • A.F. Hofmann Bile acids: the good, the bad, and the ugly News Physiol. Sci. 14 1999 24 29
    • (1999) News Physiol. Sci. , vol.14 , pp. 24-29
    • Hofmann, A.F.1
  • 5
    • 85011662950 scopus 로고    scopus 로고
    • Bile secretion and gallbladder function
    • L.R. Johnson Second ed. Lippincott-Raven Philadelphia
    • L.R. Johnson Bile secretion and gallbladder function L.R. Johnson Essential Medical Physiology Second ed. 1998 Lippincott-Raven Philadelphia 465 471
    • (1998) Essential Medical Physiology , pp. 465-471
    • Johnson, L.R.1
  • 6
    • 0003555028 scopus 로고
    • Diseases of the gallbladder and bile duct
    • R.T. Harrison Eleventh ed. Mc Graw-Hill New York
    • M.S. McPhee, and N.J. Greenberger Diseases of the gallbladder and bile duct R.T. Harrison Harrison's Principles of Internal Medicine Eleventh ed. 1987 Mc Graw-Hill New York 1358 1362
    • (1987) Harrison's Principles of Internal Medicine , pp. 1358-1362
    • McPhee, M.S.1    Greenberger, N.J.2
  • 7
    • 0002661606 scopus 로고
    • Bile acids
    • I.M. Arias J.L. Boyer N. Fausto W.B. Jackoby D.A. Schachter D.A. Shafritz Raven Press Ltd New York
    • A.F. Hofmann Bile acids I.M. Arias J.L. Boyer N. Fausto W.B. Jackoby D.A. Schachter D.A. Shafritz The Liver: Biology and Pathobiology 1994 Raven Press Ltd New York 677 718
    • (1994) The Liver: Biology and Pathobiology , pp. 677-718
    • Hofmann, A.F.1
  • 8
    • 0022466827 scopus 로고
    • Influence of the amino acid moiety on deconjugation of bile acid amidates by cholylglycine hydrolase or human fecal cultures
    • S.M. Huijghebaert, and A.F. Hofmann Influence of the amino acid moiety on deconjugation of bile acid amidates by cholylglycine hydrolase or human fecal cultures J. Lipid Res. 27 1986 742 752
    • (1986) J. Lipid Res. , vol.27 , pp. 742-752
    • Huijghebaert, S.M.1    Hofmann, A.F.2
  • 9
    • 0018191563 scopus 로고
    • Hepatic taurine concentration and dietary taurine as regulators of bile acid conjugation with taurine
    • W.G. Hardison Hepatic taurine concentration and dietary taurine as regulators of bile acid conjugation with taurine Gastroenterology 75 1978 71 75
    • (1978) Gastroenterology , vol.75 , pp. 71-75
    • Hardison, W.G.1
  • 10
    • 0000447259 scopus 로고
    • Dietary glycine and taurine on bile acid conjugation on man. Bile acids and steroids 75
    • J. Sjovall Dietary glycine and taurine on bile acid conjugation on man. Bile acids and steroids 75 Proc. Soc. Exp. Biol. Med. 100 1959 676 678
    • (1959) Proc. Soc. Exp. Biol. Med. , vol.100 , pp. 676-678
    • Sjovall, J.1
  • 12
    • 0021739393 scopus 로고
    • Physicochemical properties of bile acids and their relationship to biological properties: An overview of the problem
    • A.F. Hofmann, and A. Roda Physicochemical properties of bile acids and their relationship to biological properties: an overview of the problem J. Lipid Res. 25 1984 1477 1489
    • (1984) J. Lipid Res. , vol.25 , pp. 1477-1489
    • Hofmann, A.F.1    Roda, A.2
  • 13
    • 0025147694 scopus 로고
    • Physical chemistry of biliary lipids during bile formation
    • D.E. Cohen, and M.C. Carey Physical chemistry of biliary lipids during bile formation Hepatology 112 1990 143S 148S
    • (1990) Hepatology , vol.112
    • Cohen, D.E.1    Carey, M.C.2
  • 15
    • 0026446050 scopus 로고
    • Cloning and expression of a conjugated bile acid hydrolase gene from Lactobacillus plantarum by using a direct plate assay
    • H. Christiaens, R.J. Leer, P.H. Pouwels, and W. Verstraete Cloning and expression of a conjugated bile acid hydrolase gene from Lactobacillus plantarum by using a direct plate assay Appl. Environ. Microbiol. 58 1992 3792 3798
    • (1992) Appl. Environ. Microbiol. , vol.58 , pp. 3792-3798
    • Christiaens, H.1    Leer, R.J.2    Pouwels, P.H.3    Verstraete, W.4
  • 17
    • 0029063548 scopus 로고
    • Purification and characterization of conjugated bile salt hydrolase from Bifidobacterium longum BB536
    • J.P. Grill, F. Schneider, J. Crociani, and J. Ballongue Purification and characterization of conjugated bile salt hydrolase from Bifidobacterium longum BB536 Appl. Environ. Microbiol. 61 1995 2577 2582
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2577-2582
    • Grill, J.P.1    Schneider, F.2    Crociani, J.3    Ballongue, J.4
  • 18
    • 0025348851 scopus 로고
    • Characterization and purification of bile salt hydrolase from Lactobacillus sp. strain 100-100
    • S.G. Lundeen, and D.C. Savage Characterization and purification of bile salt hydrolase from Lactobacillus sp. strain 100-100 J. Bacteriol. 172 1990 4171 4177
    • (1990) J. Bacteriol. , vol.172 , pp. 4171-4177
    • Lundeen, S.G.1    Savage, D.C.2
  • 19
    • 0031038206 scopus 로고    scopus 로고
    • Assessment of fecal bacteria with bile acid 7α-dehydroxylation activity for the presence of bai-like genes
    • K.C. Doerner, F. Takamine, C.P. LaVoie, D.H. Mallonee, and P.B. Hylemon Assessment of fecal bacteria with bile acid 7α-dehydroxylation activity for the presence of bai-like genes Appl. Environ. Microbiol. 63 1997 1185 1188
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 1185-1188
    • Doerner, K.C.1    Takamine, F.2    Lavoie, C.P.3    Mallonee, D.H.4    Hylemon, P.B.5
  • 20
    • 0030447221 scopus 로고    scopus 로고
    • Sequencing and expression of a gene encoding a bile acid transporter from Eubacterium sp. strain VPI 12708
    • D.H. Mallonee, and P.B. Hylemon Sequencing and expression of a gene encoding a bile acid transporter from Eubacterium sp. strain VPI 12708 J. Bacteriol. 178 1996 7053 7058
    • (1996) J. Bacteriol. , vol.178 , pp. 7053-7058
    • Mallonee, D.H.1    Hylemon, P.B.2
  • 21
    • 0034010274 scopus 로고    scopus 로고
    • Identification and characterization of a bile acid 7α- dehydroxylation operon in Clostridium sp. strain TO-931, a highly active 7α-dehydroxylating strain isolated from human feces
    • J.E. Wells, and P.B. Hylemon Identification and characterization of a bile acid 7α-dehydroxylation operon in Clostridium sp. strain TO-931, a highly active 7α-dehydroxylating strain isolated from human feces Appl. Environ. Microbiol. 66 2000 1107 1113
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 1107-1113
    • Wells, J.E.1    Hylemon, P.B.2
  • 22
    • 0030769885 scopus 로고    scopus 로고
    • Biotransformations on steroid nucleus of bile acids
    • O. Bortolini, A. Medici, and S. Poli Biotransformations on steroid nucleus of bile acids Steroids 62 1997 564 577
    • (1997) Steroids , vol.62 , pp. 564-577
    • Bortolini, O.1    Medici, A.2    Poli, S.3
  • 23
    • 0022375571 scopus 로고
    • Biotransformation of bile acids by Clostridia
    • R.W. Owen Biotransformation of bile acids by Clostridia J. Med. Microbiol. 20 1985 233 238
    • (1985) J. Med. Microbiol. , vol.20 , pp. 233-238
    • Owen, R.W.1
  • 25
    • 0035366705 scopus 로고    scopus 로고
    • Bile acid hydrophobicity is correlated with induction of apoptosis and/or growth arrest in HCT116 cells
    • A.A. Powell, J.M. LaRue, and J.D. Martinez Bile acid hydrophobicity is correlated with induction of apoptosis and/or growth arrest in HCT116 cells Biochem. J. 356 2001 481 486
    • (2001) Biochem. J. , vol.356 , pp. 481-486
    • Powell, A.A.1    Larue, J.M.2    Martinez, J.D.3
  • 26
    • 0019734722 scopus 로고
    • Behaviour of digestive enzymes in the pancreatic juice and pancreas of rats fed on a low-protein diet than on a balanced diet
    • O. Kheroua, and J. Belleville Behaviour of digestive enzymes in the pancreatic juice and pancreas of rats fed on a low-protein diet than on a balanced diet Reprod. Nutr. Dev. 21 1981 901 917
    • (1981) Reprod. Nutr. Dev. , vol.21 , pp. 901-917
    • Kheroua, O.1    Belleville, J.2
  • 27
    • 0023894865 scopus 로고
    • The effect of protein-calorie malnutrition on the developing liver
    • K. Opleta, J.D. Butzner, E.A. Schaeffer, and D.G. Gall The effect of protein-calorie malnutrition on the developing liver Pediatr. Res. 23 1988 505 508
    • (1988) Pediatr. Res. , vol.23 , pp. 505-508
    • Opleta, K.1    Butzner, J.D.2    Schaeffer, E.A.3    Gall, D.G.4
  • 28
    • 0025934778 scopus 로고
    • Gallstones: Pathogenesis
    • G. Paumgartner, and T. Sauerbruch Gallstones: pathogenesis Lancet 338 1991 1117 1121
    • (1991) Lancet , vol.338 , pp. 1117-1121
    • Paumgartner, G.1    Sauerbruch, T.2
  • 30
    • 0019518216 scopus 로고
    • Effect of dietary chenodeoxycholic acid in intestinal carcinogenesis induced by 1,2 dimethylhydrazine in mice
    • M.S. Martin, E. Justrabo, J.F. Jeannin, A. Leclerc, and F. Martin Effect of dietary chenodeoxycholic acid in intestinal carcinogenesis induced by 1,2 dimethylhydrazine in mice Br. J. Cancer 43 1981 884 886
    • (1981) Br. J. Cancer , vol.43 , pp. 884-886
    • Martin, M.S.1    Justrabo, E.2    Jeannin, J.F.3    Leclerc, A.4    Martin, F.5
  • 32
    • 0029912668 scopus 로고    scopus 로고
    • Clinical uses of probiotics for stabilizing the gut mucosal barrier: Successful strains and future challenges
    • S. Salminen, E. Isolauri, and E. Salminen Clinical uses of probiotics for stabilizing the gut mucosal barrier: successful strains and future challenges Antonie Van Leeuwenhoek 70 1996 347 358
    • (1996) Antonie Van Leeuwenhoek , vol.70 , pp. 347-358
    • Salminen, S.1    Isolauri, E.2    Salminen, E.3
  • 33
    • 0029905444 scopus 로고    scopus 로고
    • Effects of submicellar bile salt concentrations on biological membrane permeability to low molecular weight non-ionic solutes
    • A. Albalak, M.L. Zeidel, S.D. Zucker, A.A. Jackson, and J.M. Donovan Effects of submicellar bile salt concentrations on biological membrane permeability to low molecular weight non-ionic solutes Biochemistry 35 1996 7936 7945
    • (1996) Biochemistry , vol.35 , pp. 7936-7945
    • Albalak, A.1    Zeidel, M.L.2    Zucker, S.D.3    Jackson, A.A.4    Donovan, J.M.5
  • 35
    • 0030061978 scopus 로고    scopus 로고
    • Tauroursodeoxycholic acid protects in vitro models of human colonic cancer cells from cytotoxic effects of hydrophobic bile acid
    • L.C. Shekels, J.E. Beste, and S.B. Ho Tauroursodeoxycholic acid protects in vitro models of human colonic cancer cells from cytotoxic effects of hydrophobic bile acid J. Lab. Clin. Med. 127 1996 57 66
    • (1996) J. Lab. Clin. Med. , vol.127 , pp. 57-66
    • Shekels, L.C.1    Beste, J.E.2    Ho, S.B.3
  • 36
    • 0036956818 scopus 로고    scopus 로고
    • Bile stress response in Listeria monocytogenes LO28: Adaptation, cross-protection and identification of genetic loci involved in bile resistance
    • M. Begley, C.G.M. Gahan, and C. Hill Bile stress response in Listeria monocytogenes LO28: adaptation, cross-protection and identification of genetic loci involved in bile resistance Appl. Environ. Microbiol. 68 2002 6005 6012
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 6005-6012
    • Begley, M.1    Gahan, C.G.M.2    Hill, C.3
  • 37
    • 0029885478 scopus 로고    scopus 로고
    • Defense against lethal treatments and de novo protein synthesis induced by NaCl in Enterococcus faecalis ATCC 19433
    • S. Flahaut, A. Benachour, J.C. Giard, P. Boutibonnes, and Y. Auffray Defense against lethal treatments and de novo protein synthesis induced by NaCl in Enterococcus faecalis ATCC 19433 Arch. Microbiol. 165 1996 317 324
    • (1996) Arch. Microbiol. , vol.165 , pp. 317-324
    • Flahaut, S.1    Benachour, A.2    Giard, J.C.3    Boutibonnes, P.4    Auffray, Y.5
  • 38
    • 0030015503 scopus 로고    scopus 로고
    • Comparison of bile salts and sodium doceyl sulfate stress responses in Enterococcus faecalis
    • S. Flahaut, J. Frere, P. Boutibonnes, and Y. Auffray Comparison of bile salts and sodium doceyl sulfate stress responses in Enterococcus faecalis Appl. Environ. Microbiol. 62 1996 2416 2420
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 2416-2420
    • Flahaut, S.1    Frere, J.2    Boutibonnes, P.3    Auffray, Y.4
  • 39
    • 0029978528 scopus 로고    scopus 로고
    • Relationship between stress response towards bile salts, acid and heat treatment in Enterococcus faecalis
    • S. Flahaut, A. Hartke, J.C. Giard, A. Benachour, P. Boutibonnes, and A. Auffray Relationship between stress response towards bile salts, acid and heat treatment in Enterococcus faecalis FEMS Microbiol. Lett. 138 1996 49 54
    • (1996) FEMS Microbiol. Lett. , vol.138 , pp. 49-54
    • Flahaut, S.1    Hartke, A.2    Giard, J.C.3    Benachour, A.4    Boutibonnes, P.5    Auffray, A.6
  • 40
    • 0030944438 scopus 로고    scopus 로고
    • Alkaline stress response in Enterococcus faecalis: Adaptation, cross-protection and changes in protein synthesis
    • S. Flahaut, A. Hartke, J.C. Giard, and Y. Auffray Alkaline stress response in Enterococcus faecalis: adaptation, cross-protection and changes in protein synthesis Appl. Environ. Microbiol. 63 1997 812 814
    • (1997) Appl. Environ. Microbiol. , vol.63 , pp. 812-814
    • Flahaut, S.1    Hartke, A.2    Giard, J.C.3    Auffray, Y.4
  • 41
    • 0035487189 scopus 로고    scopus 로고
    • Survival response and rearrangement of plasmid DNA of Lactococcus lactis during long-term starvation
    • W.S. Kim, J.H. Park, J. Ren, P. Su, and N.W. Dunn Survival response and rearrangement of plasmid DNA of Lactococcus lactis during long-term starvation Appl. Environ. Microbiol. 67 2001 4594 4602
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4594-4602
    • Kim, W.S.1    Park, J.H.2    Ren, J.3    Su, P.4    Dunn, N.W.5
  • 42
    • 0033402383 scopus 로고    scopus 로고
    • Acid adaptation induces cross-protection against some environmental stresses in Vibrio parahaemolyticus
    • T. Koga, F. Sakamoto, A. Yamoto, and K. Takumi Acid adaptation induces cross-protection against some environmental stresses in Vibrio parahaemolyticus J. Gen. Appl. Microbiol. 45 1999 155 161
    • (1999) J. Gen. Appl. Microbiol. , vol.45 , pp. 155-161
    • Koga, T.1    Sakamoto, F.2    Yamoto, A.3    Takumi, K.4
  • 43
    • 0036451387 scopus 로고    scopus 로고
    • Alkaline adaptation induces cross-protection against some environmental stresses and morphological change in Vibrio parahaemolyticus
    • T. Koga, T. Katagiri, H. Hori, and K. Takumi Alkaline adaptation induces cross-protection against some environmental stresses and morphological change in Vibrio parahaemolyticus Microbiol. Res. 157 2002 1 7
    • (2002) Microbiol. Res. , vol.157 , pp. 1-7
    • Koga, T.1    Katagiri, T.2    Hori, H.3    Takumi, K.4
  • 44
    • 0037479837 scopus 로고    scopus 로고
    • Susceptibility and adaptive response to bile salts in Propionibacterium freudenreichii: Physiological and proteomic analysis
    • P. Leverrier, D. Dimova, V. Pichereau, Y. Auffray, P. Boyaval, and G. Jan Susceptibility and adaptive response to bile salts in Propionibacterium freudenreichii: physiological and proteomic analysis Appl. Environ. Microbiol. 69 2003 3809 3818
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 3809-3818
    • Leverrier, P.1    Dimova, D.2    Pichereau, V.3    Auffray, Y.4    Boyaval, P.5    Jan, G.6
  • 45
    • 0031230432 scopus 로고    scopus 로고
    • Influence of bile on β-galactosidase activity and cell viability of Lactobacillus reuteri when subjected to freeze-drying
    • G.F. Valdez, G. Martos, M.P. Taranto, G.L. Lorca, G. Oliver, and A.P. Ruiz Holgado Influence of bile on β-galactosidase activity and cell viability of Lactobacillus reuteri when subjected to freeze-drying J. Dairy Sci. 80 1996 1955 1958
    • (1996) J. Dairy Sci. , vol.80 , pp. 1955-1958
    • Valdez, G.F.1    Martos, G.2    Taranto, M.P.3    Lorca, G.L.4    Oliver, G.5    Ruiz Holgado, A.P.6
  • 46
    • 0029878402 scopus 로고    scopus 로고
    • Influence of bile salts on β-glucuronidase activity of intestinal bacteria
    • T. Fujisawa, and M. Mori Influence of bile salts on β-glucuronidase activity of intestinal bacteria Lett. Appl. Microbiol. 22 1996 271 274
    • (1996) Lett. Appl. Microbiol. , vol.22 , pp. 271-274
    • Fujisawa, T.1    Mori, M.2
  • 47
    • 0027601549 scopus 로고
    • Influence of bile on cellular integrity and β-galactosidase activity of Lactobacillus acidoplilus
    • D.O. Noh, and S.E. Gilliland Influence of bile on cellular integrity and β-galactosidase activity of Lactobacillus acidoplilus J. Dairy Sci. 76 1993 1253 1259
    • (1993) J. Dairy Sci. , vol.76 , pp. 1253-1259
    • Noh, D.O.1    Gilliland, S.E.2
  • 48
    • 0019329516 scopus 로고
    • Membrane lipid composition and susceptibility to bile salt damage
    • R. Coleman, P.J. Lowe, and D. Billington Membrane lipid composition and susceptibility to bile salt damage Biochim. Biophys. Acta 588 1980 294 300
    • (1980) Biochim. Biophys. Acta , vol.588 , pp. 294-300
    • Coleman, R.1    Lowe, P.J.2    Billington, D.3
  • 49
    • 0029863204 scopus 로고    scopus 로고
    • Adsorption of mixtures of bile salt taurine conjugates to lecithin-cholesterol membranes: Implications for bile salt toxicity and cytoprotection
    • D.M. Heuman, R.S. Bajaj, and Q. Lin Adsorption of mixtures of bile salt taurine conjugates to lecithin-cholesterol membranes: implications for bile salt toxicity and cytoprotection J. Lipid Res. 37 1996 562 573
    • (1996) J. Lipid Res. , vol.37 , pp. 562-573
    • Heuman, D.M.1    Bajaj, R.S.2    Lin, Q.3
  • 50
    • 0034399006 scopus 로고    scopus 로고
    • Effect of bile on the β-galactosidase activity of dairy propionibacteria
    • G. Zarate, S. Gonzalez, A.P. Chaia, and G. Oliver Effect of bile on the β-galactosidase activity of dairy propionibacteria Lait 80 2000 267 276
    • (2000) Lait , vol.80 , pp. 267-276
    • Zarate, G.1    Gonzalez, S.2    Chaia, A.P.3    Oliver, G.4
  • 52
    • 0036325196 scopus 로고    scopus 로고
    • Adhesion to bile drain materials and physicochemical surface properties of Enterococcus faecalis strains grown in the presence of bile
    • K. Waar, H.C. van der Mei, J.M. Harmsen, J.E. Degener, and H.J. Busscher Adhesion to bile drain materials and physicochemical surface properties of Enterococcus faecalis strains grown in the presence of bile Appl. Environ. Microbiol. 68 2002 3855 3858
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 3855-3858
    • Waar, K.1    Van Der Mei, H.C.2    Harmsen, J.M.3    Degener, J.E.4    Busscher, H.J.5
  • 54
    • 0021023912 scopus 로고
    • Studies on the mechanism of bile salt-induced liposomal membrane damage
    • R. Schubert, H. Jaroni, J. Schoelmerich, and K.H. Schmidt Studies on the mechanism of bile salt-induced liposomal membrane damage Digestion 28 1983 181 190
    • (1983) Digestion , vol.28 , pp. 181-190
    • Schubert, R.1    Jaroni, H.2    Schoelmerich, J.3    Schmidt, K.H.4
  • 55
  • 56
    • 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
    • J.P. Grill, C. Cayuela, J.M. Antoine, and F. Schneider 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 2000 553 563
    • (2000) J. Appl. Microbiol. , vol.89 , pp. 553-563
    • Grill, J.P.1    Cayuela, C.2    Antoine, J.M.3    Schneider, F.4
  • 57
    • 0025837495 scopus 로고
    • Ion-pair high-performance liquid chromatography of bile salt conjugates: Application to pig bile
    • V. Legrand-Defretin, C. Juste, R. Henry, and T. Corring Ion-pair high-performance liquid chromatography of bile salt conjugates: application to pig bile Lipids 26 1991 578 583
    • (1991) Lipids , vol.26 , pp. 578-583
    • Legrand-Defretin, V.1    Juste, C.2    Henry, R.3    Corring, T.4
  • 59
    • 0034332737 scopus 로고    scopus 로고
    • Recovery of low-temperature stressed E. coli 0157:H7 and its susceptibility to crystal violet, bile salt, sodium chloride and ethanol
    • C.C. Chou, and S.J. Cheng Recovery of low-temperature stressed E. coli 0157:H7 and its susceptibility to crystal violet, bile salt, sodium chloride and ethanol Int. J. Food Microbiol. 61 2000 127 136
    • (2000) Int. J. Food Microbiol. , vol.61 , pp. 127-136
    • Chou, C.C.1    Cheng, S.J.2
  • 60
    • 0038439564 scopus 로고    scopus 로고
    • The effect of growth atmosphere on the ability of Listeria monocytogenes to survive exposure to acid, proteolytic enzymes and bile salts
    • T. King, T. Ferenci, and E.A. Szabo The effect of growth atmosphere on the ability of Listeria monocytogenes to survive exposure to acid, proteolytic enzymes and bile salts Int. J. Food Microbiol. 84 2002 133 143
    • (2002) Int. J. Food Microbiol. , vol.84 , pp. 133-143
    • King, T.1    Ferenci, T.2    Szabo, E.A.3
  • 61
    • 0344199899 scopus 로고    scopus 로고
    • Permeability and stability properties of membranes formed by lipids extracted from Lactobacillus acidophilus grown at different temperatures
    • M.L. Fernandez Murga, D. Bernick, G.F. de Valdez, and A.E. Disalvo Permeability and stability properties of membranes formed by lipids extracted from Lactobacillus acidophilus grown at different temperatures Arch. Biochem. Biophys. 364 1999 115 121
    • (1999) Arch. Biochem. Biophys. , vol.364 , pp. 115-121
    • Fernandez Murga, M.L.1    Bernick, D.2    De Valdez, G.F.3    Disalvo, A.E.4
  • 62
    • 0036194555 scopus 로고    scopus 로고
    • Enhancement of bile tolerance in Lactococci by Tween 80
    • H. Kimoto, S. Ohmomo, and T. Okamoto Enhancement of bile tolerance in Lactococci by Tween 80 J. Appl. Micro. 92 2002 41 46
    • (2002) J. Appl. Micro. , vol.92 , pp. 41-46
    • Kimoto, H.1    Ohmomo, S.2    Okamoto, T.3
  • 63
    • 0032604912 scopus 로고    scopus 로고
    • Isolation and characterization of acid- and bile-tolerant isolates from strains of Lactobacillus acidophilus
    • L. Chou, and B. Weimer Isolation and characterization of acid- and bile-tolerant isolates from strains of Lactobacillus acidophilus J. Dairy Sci. 82 1999 23 31
    • (1999) J. Dairy Sci. , vol.82 , pp. 23-31
    • Chou, L.1    Weimer, B.2
  • 65
    • 0033618443 scopus 로고    scopus 로고
    • Activation of the promoters of genes associated with DNA damage, oxidative stress, ER stress and protein malfolding by the bile salt, deoxycholate
    • H. Bernstein, C.M. Payne, C. Bernstein, J. Schneider, S.E. Beard, and C.L. Crowley Activation of the promoters of genes associated with DNA damage, oxidative stress, ER stress and protein malfolding by the bile salt, deoxycholate Toxicol. Lett. 108 1999 37 46
    • (1999) Toxicol. Lett. , vol.108 , pp. 37-46
    • Bernstein, H.1    Payne, C.M.2    Bernstein, C.3    Schneider, J.4    Beard, S.E.5    Crowley, C.L.6
  • 66
    • 0026327144 scopus 로고
    • Bile salt/acid induction of DNA damage in bacterial and mammalian cells: Implications for colon cancer
    • R.L. Kandell, and C. Bernstein Bile salt/acid induction of DNA damage in bacterial and mammalian cells: implications for colon cancer Nutr. Cancer 16 1991 227 238
    • (1991) Nutr. Cancer , vol.16 , pp. 227-238
    • Kandell, R.L.1    Bernstein, C.2
  • 67
    • 0031874147 scopus 로고    scopus 로고
    • The stress-response proteins poly(ADP-ribose) polymerase and NF-κB protect against bile salt-induced apoptosis
    • C.M. Payne, C. Crowley, D. Washo, H. Bernstein, C. Bernstein, and M. Briel The stress-response proteins poly(ADP-ribose) polymerase and NF-κB protect against bile salt-induced apoptosis Cell Death Diff. 5 1998 623 636
    • (1998) Cell Death Diff. , vol.5 , pp. 623-636
    • Payne, C.M.1    Crowley, C.2    Washo, D.3    Bernstein, H.4    Bernstein, C.5    Briel, M.6
  • 68
    • 0035010025 scopus 로고    scopus 로고
    • Characterization of the groESL operon in Listeria monocytogenes: Utilization of two reporter systems (gfp and hly) for evaluating in vivo expression
    • C.G.M. Gahan, J. O'Mahony, and C. Hill Characterization of the groESL operon in Listeria monocytogenes: utilization of two reporter systems (gfp and hly) for evaluating in vivo expression Infect. Immun. 69 2001 3924 3932
    • (2001) Infect. Immun. , vol.69 , pp. 3924-3932
    • Gahan, C.G.M.1    O'Mahony, J.2    Hill, C.3
  • 69
    • 0034630096 scopus 로고    scopus 로고
    • Identification of general stress genes in Enterococcus faecalis
    • A. Rincé, S. Flahaut, and Y. Auffray Identification of general stress genes in Enterococcus faecalis Int. J. Food Microbiol. 55 2000 87 91
    • (2000) Int. J. Food Microbiol. , vol.55 , pp. 87-91
    • Rincé, A.1    Flahaut, S.2    Auffray, Y.3
  • 70
    • 0034630225 scopus 로고    scopus 로고
    • Basic features of the bile stress response in three species of bifidobacteria: B. longum, B. adolescentis, and B. breve
    • G. Schmidt, and R. Zink Basic features of the bile stress response in three species of bifidobacteria: B. longum, B. adolescentis, and B. breve Int. J. Food Microbiol. 55 2000 41 45
    • (2000) Int. J. Food Microbiol. , vol.55 , pp. 41-45
    • Schmidt, G.1    Zink, R.2
  • 72
    • 0029123537 scopus 로고
    • Generation of hydroperoxides in isolated rat hepatocytes and hepatic mitochondria exposed to hydrophobic bile acids
    • R.J. Sokol, B.M. Winklhofer-Roob, M.W. Devereaux, and J.M. McKim Jr. Generation of hydroperoxides in isolated rat hepatocytes and hepatic mitochondria exposed to hydrophobic bile acids Gastroenterology 109 1995 1249 1256
    • (1995) Gastroenterology , vol.109 , pp. 1249-1256
    • Sokol, R.J.1    Winklhofer-Roob, B.M.2    Devereaux, M.W.3    McKim Jr., J.M.4
  • 74
    • 0025834236 scopus 로고
    • Premicellar taurocholate enhances ferrous iron uptake from all regions of rat small intestine
    • A. Sanyal, M.L. Shiffman, J.I. Hirsch, and E.W. Moore Premicellar taurocholate enhances ferrous iron uptake from all regions of rat small intestine Gastroenterology 101 1991 382 388
    • (1991) Gastroenterology , vol.101 , pp. 382-388
    • Sanyal, A.1    Shiffman, M.L.2    Hirsch, J.I.3    Moore, E.W.4
  • 75
  • 76
    • 0033003281 scopus 로고    scopus 로고
    • PhoP-PhoQ-regulated loci are required for enhanced bile resistance in Salmonella spp
    • J.C. Van Velkinburgh, and J.S. Gunn PhoP-PhoQ-regulated loci are required for enhanced bile resistance in Salmonella spp Infect. Immun. 67 1999 1614 1622
    • (1999) Infect. Immun. , vol.67 , pp. 1614-1622
    • Van Velkinburgh, J.C.1    Gunn, J.S.2
  • 77
    • 0036117936 scopus 로고    scopus 로고
    • Biofilm formation and interaction with the surfaces of gallstones by Salmonella spp
    • A.M. Prouty, W.H. Schwesinger, and J.S. Gunn Biofilm formation and interaction with the surfaces of gallstones by Salmonella spp Infect. Immun. 70 2002 2640 2649
    • (2002) Infect. Immun. , vol.70 , pp. 2640-2649
    • Prouty, A.M.1    Schwesinger, W.H.2    Gunn, J.S.3
  • 78
    • 0024470068 scopus 로고
    • Aerobic and anaerobic microbiology of biliary tract disease
    • I. Brook Aerobic and anaerobic microbiology of biliary tract disease J. Clin. Microbiol. 27 1989 2373 2375
    • (1989) J. Clin. Microbiol. , vol.27 , pp. 2373-2375
    • Brook, I.1
  • 80
    • 0031749711 scopus 로고    scopus 로고
    • Bacterial and parasitic cholangastrointestinal tractis
    • H.A. Carpenter Bacterial and parasitic cholangastrointestinal tractis Mayo Clin. Proc. 73 1998 473 478
    • (1998) Mayo Clin. Proc. , vol.73 , pp. 473-478
    • Carpenter, H.A.1
  • 81
    • 0037366596 scopus 로고    scopus 로고
    • Microbiology of choledochal bile in patients with choledocholithiasis admitted to a tertiary hospital
    • C. Flores, I. Maguilnik, E. Hadlich, and L.Z. Goldani Microbiology of choledochal bile in patients with choledocholithiasis admitted to a tertiary hospital J. Gastroenterol. Hepatol. 18 2003 333 336
    • (2003) J. Gastroenterol. Hepatol. , vol.18 , pp. 333-336
    • Flores, C.1    Maguilnik, I.2    Hadlich, E.3    Goldani, L.Z.4
  • 82
    • 0022504845 scopus 로고
    • Bacteria and helminth isolated from bile and faeces of zebu cattle slaughtered for human consumption in the Niger Delta areas of Nigeria
    • C.O. Onyekaba, and H.O. Njoku Bacteria and helminth isolated from bile and faeces of zebu cattle slaughtered for human consumption in the Niger Delta areas of Nigeria Ann. Trop. Med. Parasitol. 80 1986 421 424
    • (1986) Ann. Trop. Med. Parasitol. , vol.80 , pp. 421-424
    • Onyekaba, C.O.1    Njoku, H.O.2
  • 83
    • 2542509679 scopus 로고    scopus 로고
    • Effect of bacteriocin-producing lactobacilli on the survival of Escherichia coli and Listeria in a dynamic model of the stomach and the small intestine
    • M.G. Gänzle, C. Hertel, J.M.B.M. van der Vossen, and W.P. Hammes Effect of bacteriocin-producing lactobacilli on the survival of Escherichia coli and Listeria in a dynamic model of the stomach and the small intestine Int. J. Food Microbiol. 48 1999 21 35
    • (1999) Int. J. Food Microbiol. , vol.48 , pp. 21-35
    • Gänzle, M.G.1    Hertel, C.2    Van Der Vossen, J.M.B.M.3    Hammes, W.P.4
  • 85
    • 0032708203 scopus 로고    scopus 로고
    • The interaction of bile acids and Helicobacter pylori
    • Y. Hirai The interaction of bile acids and Helicobacter pylori Editorial. J. Gastroenterol. 34 1999 653 654
    • (1999) Editorial. J. Gastroenterol. , vol.34 , pp. 653-654
    • Hirai, Y.1
  • 86
    • 0025231696 scopus 로고
    • Helicobacter pylori is not identified in areas of gastric metaplasia of gallbladder
    • A.H. Arnaout, S.H. Abbas, and S. Shousha Helicobacter pylori is not identified in areas of gastric metaplasia of gallbladder J. Pathol. 160 1990 333 334
    • (1990) J. Pathol. , vol.160 , pp. 333-334
    • Arnaout, A.H.1    Abbas, S.H.2    Shousha, S.3
  • 87
    • 0025868472 scopus 로고
    • Sensitivity of Helicobacter pylori to different bile salts
    • M.L. Hänninen Sensitivity of Helicobacter pylori to different bile salts Eur. J. Clin. Microbiol. Infect. Dis. 10 1991 515 518
    • (1991) Eur. J. Clin. Microbiol. Infect. Dis. , vol.10 , pp. 515-518
    • Hänninen, M.L.1
  • 89
    • 0023813359 scopus 로고
    • Isolation of Campylobacter jejuni from the bile of a cholecystic patient
    • S. Drion, C. Wahlen, and P. Taziaux Isolation of Campylobacter jejuni from the bile of a cholecystic patient J. Clin. Microbiol. 26 1988 2193 2194
    • (1988) J. Clin. Microbiol. , vol.26 , pp. 2193-2194
    • Drion, S.1    Wahlen, C.2    Taziaux, P.3
  • 91
    • 0020020375 scopus 로고
    • Characterization of Campylobacter jejuni coli isolated from different sources
    • M.L. Hänninen characterization of Campylobacter jejuni coli isolated from different sources Acta Veterinaria Scandinavica 23 1982 88 98
    • (1982) Acta Veterinaria Scandinavica , vol.23 , pp. 88-98
    • Hänninen, M.L.1
  • 92
    • 0030103160 scopus 로고    scopus 로고
    • Experimental hepatitis induced by Campylobacter jejuni infection in Japanese quail (Coturnix coturnix japonica)
    • N. Misawa, T. Ohnishi, K. Uchida, M. Nakai, T. Nasu, K. Itoh, and E. Takahashi Experimental hepatitis induced by Campylobacter jejuni infection in Japanese quail (Coturnix coturnix japonica) J. Vet. Med. Sci. 58 1996 205 210
    • (1996) J. Vet. Med. Sci. , vol.58 , pp. 205-210
    • Misawa, N.1    Ohnishi, T.2    Uchida, K.3    Nakai, M.4    Nasu, T.5    Itoh, K.6    Takahashi, E.7
  • 95
    • 84982189058 scopus 로고
    • A review: Probiotics in man and animals
    • R. Fuller A review: probiotics in man and animals J. Appl. Bacteriol. 66 1989 365 378
    • (1989) J. Appl. Bacteriol. , vol.66 , pp. 365-378
    • Fuller, R.1
  • 96
    • 0021669414 scopus 로고
    • Importance of bile tolerance of Lactobacillus acidophilus used as a dietary adjunct
    • S.E. Gilliland, T.E. Stanley, and L.J. Bush Importance of bile tolerance of Lactobacillus acidophilus used as a dietary adjunct J. Dairy Sci. 67 1984 3045 3051
    • (1984) J. Dairy Sci. , vol.67 , pp. 3045-3051
    • Gilliland, S.E.1    Stanley, T.E.2    Bush, L.J.3
  • 103
    • 0037008125 scopus 로고    scopus 로고
    • A distinct physiological state of Lactococcus lactis cells that confers survival against a direct and prolonged exposure to severe stresses
    • W.S. Kim, J.H. Park, J.E. Tandianus, J. Ren, P. Su, and N.W. Dunn A distinct physiological state of Lactococcus lactis cells that confers survival against a direct and prolonged exposure to severe stresses FEMS Microbiol. Lett. 212 2002 203 208
    • (2002) FEMS Microbiol. Lett. , vol.212 , pp. 203-208
    • Kim, W.S.1    Park, J.H.2    Tandianus, J.E.3    Ren, J.4    Su, P.5    Dunn, N.W.6
  • 104
    • 0033451295 scopus 로고    scopus 로고
    • Lactococci as probiotic strains: Adhesion to human enterocyte-like Caco-2 cells and tolerance to low pH and bile
    • H. Kimoto, J. Kurisaki, N.M. Tsuji, S. Okmomo, and T. Okamoto Lactococci as probiotic strains: adhesion to human enterocyte-like Caco-2 cells and tolerance to low pH and bile Letts. Appl. Microbiol. 29 1999 313 316
    • (1999) Letts. Appl. Microbiol. , vol.29 , pp. 313-316
    • Kimoto, H.1    Kurisaki, J.2    Tsuji, N.M.3    Okmomo, S.4    Okamoto, T.5
  • 106
    • 0028365078 scopus 로고
    • Heterogeneity of bile salts resistance in the Lactobacillus isolates of a probiotic consortium
    • N. Chateau, A.M. Deschamps, and A. Hadj Sassi Heterogeneity of bile salts resistance in the Lactobacillus isolates of a probiotic consortium Letts. Appl. Microbiol. 18 1994 42 44
    • (1994) Letts. Appl. Microbiol. , vol.18 , pp. 42-44
    • Chateau, N.1    Deschamps, A.M.2    Hadj Sassi, A.3
  • 107
    • 0028525424 scopus 로고
    • Comparisons of freshly isolated strains of Lactobacillus acidophilus of human intestinal origin for ability to assimilate cholesterol during growth
    • L.M. Buck, and S.E. Gilliland Comparisons of freshly isolated strains of Lactobacillus acidophilus of human intestinal origin for ability to assimilate cholesterol during growth J. Dairy Sci. 77 1994 2925 2933
    • (1994) J. Dairy Sci. , vol.77 , pp. 2925-2933
    • Buck, L.M.1    Gilliland, S.E.2
  • 108
    • 0030365463 scopus 로고    scopus 로고
    • Bile tolerance, taurocholate deconjugation and cholesterol removal by Lactobacillus acidophilus and Bifidobacterium spp
    • A. Gopal, N.P. Shah, and H. Roginski Bile tolerance, taurocholate deconjugation and cholesterol removal by Lactobacillus acidophilus and Bifidobacterium spp Milchwissenschaft 51 1996 619 623
    • (1996) Milchwissenschaft , vol.51 , pp. 619-623
    • Gopal, A.1    Shah, N.P.2    Roginski, H.3
  • 109
    • 0029917828 scopus 로고    scopus 로고
    • Characterization of Lactobacillus acidophilus strains for use as dietary adjunct
    • P.K. Gupta, B.K. Mital, and S.K. Garg Characterization of Lactobacillus acidophilus strains for use as dietary adjunct Int. J. Food Microbiol. 29 1996 105 109
    • (1996) Int. J. Food Microbiol. , vol.29 , pp. 105-109
    • Gupta, P.K.1    Mital, B.K.2    Garg, S.K.3
  • 110
    • 0027582430 scopus 로고
    • Relationship among bile tolerance, bile salt deconjugation, and assimilation of cholesterol by Lactobacillus acidophilus
    • D.K. Walker, and S.E. Gilliland Relationship among bile tolerance, bile salt deconjugation, and assimilation of cholesterol by Lactobacillus acidophilus J. Dairy Sci. 76 1993 956 961
    • (1993) J. Dairy Sci. , vol.76 , pp. 956-961
    • Walker, D.K.1    Gilliland, S.E.2
  • 111
    • 0027130129 scopus 로고
    • Survival of bifidobacteria in the presence of bile salt
    • S.A. Ibrahim, and A. Bezhorovainy Survival of bifidobacteria in the presence of bile salt J. Sci. Food Agric. 62 1993 351 354
    • (1993) J. Sci. Food Agric. , vol.62 , pp. 351-354
    • Ibrahim, S.A.1    Bezhorovainy, A.2
  • 112
    • 0002248661 scopus 로고
    • Selection of bifidobacteria for use as dietary adjuncts in cultured dairy foods. III. Tolerance to simulated bile concentrations of human small intestines
    • P.A. Clark, and J.H. Martin Selection of bifidobacteria for use as dietary adjuncts in cultured dairy foods. III. Tolerance to simulated bile concentrations of human small intestines Cult. Dairy Prod. J. 29 1994 18 21
    • (1994) Cult. Dairy Prod. J. , vol.29 , pp. 18-21
    • Clark, P.A.1    Martin, J.H.2
  • 115
    • 0842266703 scopus 로고    scopus 로고
    • Extracellular replication of Listeria monocytogenes in the murine gallbladder
    • J. Hardy, K.P. Francis, M. DeBoer, P. Chu, K. Gibbs, and C.H. Contag Extracellular replication of Listeria monocytogenes in the murine gallbladder Science 303 2004 851 853
    • (2004) Science , vol.303 , pp. 851-853
    • Hardy, J.1    Francis, K.P.2    Deboer, M.3    Chu, P.4    Gibbs, K.5    Contag, C.H.6
  • 117
    • 2342646776 scopus 로고    scopus 로고
    • Screening of glutamate decarboxylase activity and bile salt resistance of human asymptomatic carriage, clinical, food, and environmental isolates of Listeria monocytogenes
    • M. Olier, S. Rousseaux, P. Piveteau, J.P. Lemaître, A. Rousset, and J. Guzzo Screening of glutamate decarboxylase activity and bile salt resistance of human asymptomatic carriage, clinical, food, and environmental isolates of Listeria monocytogenes Int. J. Food Microbiol. 93 2004 87 99
    • (2004) Int. J. Food Microbiol. , vol.93 , pp. 87-99
    • Olier, M.1    Rousseaux, S.2    Piveteau, P.3    Lemaître, J.P.4    Rousset, A.5    Guzzo, J.6
  • 119
    • 0020679147 scopus 로고
    • Clostridium perfringens and other anaerobes isolated from bile
    • Y. Sakaguchi, K. Murata, and M. Kimura Clostridium perfringens and other anaerobes isolated from bile J. Clin. Pathol. 36 1983 345 349
    • (1983) J. Clin. Pathol. , vol.36 , pp. 345-349
    • Sakaguchi, Y.1    Murata, K.2    Kimura, M.3
  • 120
  • 121
    • 0025118262 scopus 로고
    • Cholesterol-lowering activity of various undigested fractions of soybean protein in rats
    • M. Sugano, S. Goto, Y. Yamada, K. Yoshida, Y. Hashimoto, T. Matsuo, and M. Kimoto Cholesterol-lowering activity of various undigested fractions of soybean protein in rats J. Nutr. 120 1990 977 985
    • (1990) J. Nutr. , vol.120 , pp. 977-985
    • Sugano, M.1    Goto, S.2    Yamada, Y.3    Yoshida, K.4    Hashimoto, Y.5    Matsuo, T.6    Kimoto, M.7
  • 122
    • 0038515421 scopus 로고    scopus 로고
    • Increase of viability of entrapped cells of Lactobacillus delbrueckii spp. bulgaricus in artifical sesame oil emulsions
    • R.C. Hou, M.Y. Lin, M.M. Wang, and J.T. Tzen Increase of viability of entrapped cells of Lactobacillus delbrueckii spp. bulgaricus in artifical sesame oil emulsions J. Dairy Sci. 86 2003 424 428
    • (2003) J. Dairy Sci. , vol.86 , pp. 424-428
    • Hou, R.C.1    Lin, M.Y.2    Wang, M.M.3    Tzen, J.T.4
  • 123
    • 0025108915 scopus 로고
    • Thermotolerance of Listeria monocytogenes and Salmonella typhimurium after sublethal heat shock
    • V.K. Bunning, R.G. Crawford, J.T. Tierney, and J.T. Peeler Thermotolerance of Listeria monocytogenes and Salmonella typhimurium after sublethal heat shock Appl. Environ. Microbiol. 56 1990 3216 3219
    • (1990) Appl. Environ. Microbiol. , vol.56 , pp. 3216-3219
    • Bunning, V.K.1    Crawford, R.G.2    Tierney, J.T.3    Peeler, J.T.4
  • 124
    • 0029931088 scopus 로고    scopus 로고
    • Adaptive acid tolerance response in Listeria monocytogenes: Isolation of an acid-tolerant mutant which demonstrates increased virulence
    • B. O' Driscoll, C.G.M. Gahan, and C. Hill Adaptive acid tolerance response in Listeria monocytogenes: isolation of an acid-tolerant mutant which demonstrates increased virulence Appl. Environ. Microbiol. 62 1996 1693 1698
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 1693-1698
    • Driscoll, B.O.'.1    Gahan, C.G.M.2    Hill, C.3
  • 126
    • 0027233525 scopus 로고
    • Acid adaptation induces cross-protection against environmental stresses in Salmonella typhimurium
    • G.J. Leyer, and E.A. Johnson Acid adaptation induces cross-protection against environmental stresses in Salmonella typhimurium Appl. Environ. Microbiol. 59 1993 1842 1847
    • (1993) Appl. Environ. Microbiol. , vol.59 , pp. 1842-1847
    • Leyer, G.J.1    Johnson, E.A.2
  • 127
    • 0029761469 scopus 로고    scopus 로고
    • Resistance of Listeria monocytogenes to heat after adaptation to environmental stresses
    • Y. Lou, and A.E. Yousef Resistance of Listeria monocytogenes to heat after adaptation to environmental stresses J. Food Prot. 59 1996 465 471
    • (1996) J. Food Prot. , vol.59 , pp. 465-471
    • Lou, Y.1    Yousef, A.E.2
  • 128
    • 0034707086 scopus 로고    scopus 로고
    • Interaction of membrane proteins and lipids with solubilizing detergents
    • M. Le Maire, P. Champeil, and J.V. Møller Interaction of membrane proteins and lipids with solubilizing detergents Biochim. Biophys. Acta 1508 2000 86 111
    • (2000) Biochim. Biophys. Acta , vol.1508 , pp. 86-111
    • Le Maire, M.1    Champeil, P.2    Møller, J.V.3
  • 129
    • 1542373514 scopus 로고    scopus 로고
    • Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii
    • P. Leverrier, J.P.C. Vissers, A. Rouault, P. Boyaval, and G. Jan Mass spectrometry proteomic analysis of stress adaptation reveals both common and distinct response pathways in Propionibacterium freudenreichii Arch. Microbiol. 181 2004 215 230
    • (2004) Arch. Microbiol. , vol.181 , pp. 215-230
    • Leverrier, P.1    Vissers, J.P.C.2    Rouault, A.3    Boyaval, P.4    Jan, G.5
  • 133
    • 0033134782 scopus 로고    scopus 로고
    • Acid-adapted Listeria monocytogenes displays enhanced tolerance against the lantibiotics nisin and lacticin 3147
    • W. Van Schaik, C.G.M. Gahan, and C. Hill Acid-adapted Listeria monocytogenes displays enhanced tolerance against the lantibiotics nisin and lacticin 3147 J. Food Prot. 62 1999 536 539
    • (1999) J. Food Prot. , vol.62 , pp. 536-539
    • Van Schaik, W.1    Gahan, C.G.M.2    Hill, C.3
  • 134
    • 0347320637 scopus 로고    scopus 로고
    • Osmotic response in Lactobacillus casei ATCC393: Biochemical and biophysical characteristics of the membrane
    • M.C. Machado, C.S. López, H. Heras, and E.A. Rivas Osmotic response in Lactobacillus casei ATCC393: biochemical and biophysical characteristics of the membrane Arch. Biochem. Biophys. 422 2004 61 70
    • (2004) Arch. Biochem. Biophys. , vol.422 , pp. 61-70
    • MacHado, M.C.1    López, C.S.2    Heras, H.3    Rivas, E.A.4
  • 135
    • 0028827806 scopus 로고
    • Salmonella typhimurium TnphoA mutants with increased sensitivity to biological and chemical detergents
    • F.J. Lacroix, C. Ayoyne, C. Pinault, M.Y. Popoff, and P. Pardon Salmonella typhimurium TnphoA mutants with increased sensitivity to biological and chemical detergents Res. Microbiol. 146 1995 659 670
    • (1995) Res. Microbiol. , vol.146 , pp. 659-670
    • Lacroix, F.J.1    Ayoyne, C.2    Pinault, C.3    Popoff, M.Y.4    Pardon, P.5
  • 136
    • 0036182369 scopus 로고    scopus 로고
    • Salmonella enterica serovar Typhimurium resistance to bile: Identification and characterization of the tolQRA cluster
    • A.M. Prouty, J.C. Van Velkinburgh, and J.S. Gunn Salmonella enterica serovar Typhimurium resistance to bile: identification and characterization of the tolQRA cluster J. Bacteriol. 184 2002 1270 1276
    • (2002) J. Bacteriol. , vol.184 , pp. 1270-1276
    • Prouty, A.M.1    Van Velkinburgh, J.C.2    Gunn, J.S.3
  • 137
    • 0033941838 scopus 로고    scopus 로고
    • Mechanisms of bacterial resistance and response to bile
    • J.S. Gunn Mechanisms of bacterial resistance and response to bile Microbes Infect. 2 2000 907 913
    • (2000) Microbes Infect. , vol.2 , pp. 907-913
    • Gunn, J.S.1
  • 138
    • 0030045627 scopus 로고    scopus 로고
    • Salmonella typhimurium acrB-like gene: Identification and role in resistance to biliary salts and detergents and role in murine infection
    • F.J. Lacroix, A. Cloeckaert, O. Grepinet, C. Pinault, M.Y. Popoff, H. Waxin, and P. Pardon Salmonella typhimurium acrB-like gene: identification and role in resistance to biliary salts and detergents and role in murine infection FEMS Microbiol. Lett. 135 1996 161 167
    • (1996) FEMS Microbiol. Lett. , vol.135 , pp. 161-167
    • Lacroix, F.J.1    Cloeckaert, A.2    Grepinet, O.3    Pinault, C.4    Popoff, M.Y.5    Waxin, H.6    Pardon, P.7
  • 139
    • 0031720812 scopus 로고    scopus 로고
    • Multidrug efflux pump AcrAB of Salmonella typhimurium excretes only those beta lactam antibiotics containing lipophilic side chains
    • H. Nikaido, V. Basina, V. Nguyen, and E.Y. Rosenberg Multidrug efflux pump AcrAB of Salmonella typhimurium excretes only those beta lactam antibiotics containing lipophilic side chains J. Bacteriol. 180 1998 4686 4692
    • (1998) J. Bacteriol. , vol.180 , pp. 4686-4692
    • Nikaido, H.1    Basina, V.2    Nguyen, V.3    Rosenberg, E.Y.4
  • 140
    • 1942537625 scopus 로고    scopus 로고
    • Bile-salt-mediated induction of antimicrobial and bile resistance in Salmonella typhimurium
    • A.M. Prouty, I.E. Brodsky, S. Falkow, and J.S. Gunn Bile-salt-mediated induction of antimicrobial and bile resistance in Salmonella typhimurium Microbiology 150 2004 775 783
    • (2004) Microbiology , vol.150 , pp. 775-783
    • Prouty, A.M.1    Brodsky, I.E.2    Falkow, S.3    Gunn, J.S.4
  • 141
    • 0031278034 scopus 로고    scopus 로고
    • A family of Gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from Gram-negative bacteria
    • I.T. Paulsen, J.M. Park, P.S. Choi, and M.H. Saier A family of Gram-negative bacterial outer membrane factors that function in the export of proteins, carbohydrates, drugs and heavy metals from Gram-negative bacteria FEMS Microbiol. Lett. 156 1997 1 8
    • (1997) FEMS Microbiol. Lett. , vol.156 , pp. 1-8
    • Paulsen, I.T.1    Park, J.M.2    Choi, P.S.3    Saier, M.H.4
  • 142
    • 0042890353 scopus 로고    scopus 로고
    • Role for Salmonella enterica enterobacterial common antigen in bile resistance and virulence
    • F. Ramos-Morales, A.I. Prieto, C.R. Beuzón, D.W. Holden, and J. Casadesús Role for Salmonella enterica enterobacterial common antigen in bile resistance and virulence J. Bacteriol. 185 2003 5328 5332
    • (2003) J. Bacteriol. , vol.185 , pp. 5328-5332
    • Ramos-Morales, F.1    Prieto, A.I.2    Beuzón, C.R.3    Holden, D.W.4    Casadesús, J.5
  • 144
    • 0030942395 scopus 로고    scopus 로고
    • The Salmonella typhimurium mar locus: Molecular and genetic analyses and assessment of its role in virulence
    • M.C. Sulavik, M. Dazer, and P.F. Miller The Salmonella typhimurium mar locus: molecular and genetic analyses and assessment of its role in virulence J. Bacteriol. 179 1997 1857 1866
    • (1997) J. Bacteriol. , vol.179 , pp. 1857-1866
    • Sulavik, M.C.1    Dazer, M.2    Miller, P.F.3
  • 146
    • 0030934759 scopus 로고    scopus 로고
    • Active efflux of bile salts by Escherichia coli
    • D.G. Thanassi, L.W. Cheng, and H. Nikaido Active efflux of bile salts by Escherichia coli J. Bacteriol. 179 1997 2512 2518
    • (1997) J. Bacteriol. , vol.179 , pp. 2512-2518
    • Thanassi, D.G.1    Cheng, L.W.2    Nikaido, H.3
  • 147
    • 0017709211 scopus 로고
    • Bacteriophage-resistant mutants of Escherichia coli K-12. Location of receptors within the lipopolysaccharide
    • R.N. Picken, and I.R. Beacham Bacteriophage-resistant mutants of Escherichia coli K-12. Location of receptors within the lipopolysaccharide J. Gen. Microbiol. 102 1977 305 318
    • (1977) J. Gen. Microbiol. , vol.102 , pp. 305-318
    • Picken, R.N.1    Beacham, I.R.2
  • 148
    • 0036066806 scopus 로고    scopus 로고
    • The BaeSR two-component system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobiocin and deoxycholate
    • N. Baranova, and H. Nikaido The BaeSR two-component system activates transcription of the yegMNOB (mdtABCD) transporter gene cluster in Escherichia coli and increases its resistance to novobiocin and deoxycholate J. Bacteriol. 184 2002 4168 4176
    • (2002) J. Bacteriol. , vol.184 , pp. 4168-4176
    • Baranova, N.1    Nikaido, H.2
  • 149
    • 0035158943 scopus 로고    scopus 로고
    • Characterization of Vibrio cholerae 01 El tor galU and galE mutants: Influence on lipopolysaccharide structure, colonization, and biofilm formation
    • J. Nesper, C.M. Lauriano, K.E. Klose, D. Kapfjammer, A. Kraiss, and J. Reidl Characterization of Vibrio cholerae 01 El tor galU and galE mutants: influence on lipopolysaccharide structure, colonization, and biofilm formation Infect. Immun. 69 2001 435 445
    • (2001) Infect. Immun. , vol.69 , pp. 435-445
    • Nesper, J.1    Lauriano, C.M.2    Klose, K.E.3    Kapfjammer, D.4    Kraiss, A.5    Reidl, J.6
  • 150
    • 0036841443 scopus 로고    scopus 로고
    • Role of Vibrio cholerae 0139 surface polysaccharides in intestinal colonisation
    • J. Nesper, S. Schild, C.M. Lauriano, A. Kraiss, K.E. Klose, and J. Reidl Role of Vibrio cholerae 0139 surface polysaccharides in intestinal colonisation Infect. Immun. 70 2002 5990 5996
    • (2002) Infect. Immun. , vol.70 , pp. 5990-5996
    • Nesper, J.1    Schild, S.2    Lauriano, C.M.3    Kraiss, A.4    Klose, K.E.5    Reidl, J.6
  • 151
    • 0031983410 scopus 로고    scopus 로고
    • Isolation and characterization of a putative multidrug resistance pump from Vibrio cholerae
    • J.A. Colmer, J.A. Fralick, and A.N. Hamood Isolation and characterization of a putative multidrug resistance pump from Vibrio cholerae Mol. Microbiol. 27 1998 63 72
    • (1998) Mol. Microbiol. , vol.27 , pp. 63-72
    • Colmer, J.A.1    Fralick, J.A.2    Hamood, A.N.3
  • 152
    • 0034967448 scopus 로고    scopus 로고
    • Vibrio cholerae tolC is required for bile resistance and colonization
    • J.E. Bina, and J.J. Mekalanos Vibrio cholerae tolC is required for bile resistance and colonization Infect. Immun. 69 2001 4681 4685
    • (2001) Infect. Immun. , vol.69 , pp. 4681-4685
    • Bina, J.E.1    Mekalanos, J.J.2
  • 153
    • 0034730163 scopus 로고    scopus 로고
    • Altered expression of the ToxR-regulated porins OmpU and OmpT diminishes Vibrio cholerae bile resistance, virulence factor expression and intestinal colonization
    • D. Provenzano, and K.E. Klose Altered expression of the ToxR-regulated porins OmpU and OmpT diminishes Vibrio cholerae bile resistance, virulence factor expression and intestinal colonization Proc. Natl. Acad. Sci. USA 97 2000 10220 10224
    • (2000) Proc. Natl. Acad. Sci. USA , vol.97 , pp. 10220-10224
    • Provenzano, D.1    Klose, K.E.2
  • 155
    • 0034986996 scopus 로고    scopus 로고
    • Characterization of the role of the ToxR-modulated outer membrane porins OmpU and OmpT in Vibrio cholerae virulence
    • D. Provenzano, C.M. Lauriano, and K.E. Klose Characterization of the role of the ToxR-modulated outer membrane porins OmpU and OmpT in Vibrio cholerae virulence J. Bacteriol. 183 2001 3652 3662
    • (2001) J. Bacteriol. , vol.183 , pp. 3652-3662
    • Provenzano, D.1    Lauriano, C.M.2    Klose, K.E.3
  • 156
    • 0036635124 scopus 로고    scopus 로고
    • CmeABC functions as a multidrug efflux system in Campylobacter jejuni
    • J. Lin, L. Overbye Michel, and Q. Zhang CmeABC functions as a multidrug efflux system in Campylobacter jejuni Antimicrob. Agents Chemother. 46 2002 2124 2131
    • (2002) Antimicrob. Agents Chemother. , vol.46 , pp. 2124-2131
    • Lin, J.1    Overbye Michel, L.2    Zhang, Q.3
  • 157
    • 0042265519 scopus 로고    scopus 로고
    • Critical role of multidrug efflux pump CmeABC in bile resistance and in vivo colonization of Campylobacter jejuni
    • J. Lin, O. Sahin, L. Overbye Michel, and Q. Zhang Critical role of multidrug efflux pump CmeABC in bile resistance and in vivo colonization of Campylobacter jejuni Infect. Immun. 71 2003 4250 4259
    • (2003) Infect. Immun. , vol.71 , pp. 4250-4259
    • Lin, J.1    Sahin, O.2    Overbye Michel, L.3    Zhang, Q.4
  • 158
    • 0035142748 scopus 로고    scopus 로고
    • Identification and characterization of gsp65, an organic hydroperoxide resistance (ohr) gene encoding a general stress protein in Enterococcus faecalis
    • A. Rincé, J.C. Giard, V. Pichereau, S. Flahaut, and Y. Auffray Identification and characterization of gsp65, an organic hydroperoxide resistance (ohr) gene encoding a general stress protein in Enterococcus faecalis J. Bacteriol. 183 2001 1482 1489
    • (2001) J. Bacteriol. , vol.183 , pp. 1482-1489
    • Rincé, A.1    Giard, J.C.2    Pichereau, V.3    Flahaut, S.4    Auffray, Y.5
  • 160
    • 0036884874 scopus 로고    scopus 로고
    • Isolation and characterization of bile salts-sensitive mutants of Enterococcus faecalis
    • Y. Le Breton, A. Maze, A. Hartke, S. Lemarinier, Y. Auffray, and A. Rincé Isolation and characterization of bile salts-sensitive mutants of Enterococcus faecalis Curr. Microbiol. 45 2002 434 439
    • (2002) Curr. Microbiol. , vol.45 , pp. 434-439
    • Le Breton, Y.1    Maze, A.2    Hartke, A.3    Lemarinier, S.4    Auffray, Y.5    Rincé, A.6
  • 161
    • 0030864578 scopus 로고    scopus 로고
    • Stress proteins in Listeria monocytogenes
    • L. Phan-Thanh, and T. Gormon Stress proteins in Listeria monocytogenes Electrophoresis 18 1997 1464 1471
    • (1997) Electrophoresis , vol.18 , pp. 1464-1471
    • Phan-Thanh, L.1    Gormon, T.2
  • 162
    • 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., the European Listeria Genome Consortium, Buchreiser, C., Glaser, P. and Cossart, P. (2002) Listeria monocytogenes bile salt hydrolase is a prfA-regulated virulence factor involved in the intestinal and hepatic phases of listeriosis. Mol. Microbiol. 45, 1095-1106.
    • (2002) Mol. Microbiol. , vol.45 , pp. 1095-1106
    • Dussurget, O.1    Cabanes, D.2    Dehoux, P.3    Lecuit, M.4    Buchreiser, C.5    Glaser, P.6    Cossart, P.7
  • 164
    • 0037458177 scopus 로고    scopus 로고
    • Identification and disruption of btlA, a locus involved in bile tolerance and general stress resistance in Listeria monocytogenes
    • M. Begley, C. Hill, and C.G.M. Gahan Identification and disruption of btlA, a locus involved in bile tolerance and general stress resistance in Listeria monocytogenes FEMS Microbiol. Lett. 218 2003 31 38
    • (2003) FEMS Microbiol. Lett. , vol.218 , pp. 31-38
    • Begley, M.1    Hill, C.2    Gahan, C.G.M.3
  • 168
    • 0042060982 scopus 로고    scopus 로고
    • The virulence activator AphA links quorum sensing to pathogenesis and physiology in Vibrio cholerae by repressing the expression of a penicillin amidase gene on the small chromosome
    • G. Kovacikova, W. Lin, and K. Skorupsk The virulence activator AphA links quorum sensing to pathogenesis and physiology in Vibrio cholerae by repressing the expression of a penicillin amidase gene on the small chromosome J. Bacteriol. 185 2003 4825 4836
    • (2003) J. Bacteriol. , vol.185 , pp. 4825-4836
    • Kovacikova, G.1    Lin, W.2    Skorupsk, K.3
  • 169
    • 0026705620 scopus 로고
    • Carbon regulation and the role in nature of the Escherichia coli penicillin acylase (pac) gene
    • E. Merino, P. Balbás, F. Recillas, B. Becerril, F. Valle, and F. Bolivar Carbon regulation and the role in nature of the Escherichia coli penicillin acylase (pac) gene Mol. Microbiol. 6 1992 2175 2182
    • (1992) Mol. Microbiol. , vol.6 , pp. 2175-2182
    • Merino, E.1    Balbás, P.2    Recillas, F.3    Becerril, B.4    Valle, F.5    Bolivar, F.6
  • 170
    • 0033091804 scopus 로고    scopus 로고
    • Bile salt hydrolase activity of three strains of Lactobacillus acidophilus
    • G. Corzo, and S.E. Gilliland Bile salt hydrolase activity of three strains of Lactobacillus acidophilus J. Dairy Sci. 82 1999 472 480
    • (1999) J. Dairy Sci. , vol.82 , pp. 472-480
    • Corzo, G.1    Gilliland, S.E.2
  • 171
    • 0033088387 scopus 로고    scopus 로고
    • Measurement of bile salt hydrolase activity from Lactobacillus acidophilus based on disappearance of conjugated bile salts
    • G. Corzo, and S.E. Gilliland Measurement of bile salt hydrolase activity from Lactobacillus acidophilus based on disappearance of conjugated bile salts J. Dairy Sci. 82 1999 466 471
    • (1999) J. Dairy Sci. , vol.82 , pp. 466-471
    • Corzo, G.1    Gilliland, S.E.2
  • 172
    • 0017325626 scopus 로고
    • Deconjugation of bile acids by intestinal lactobacilli
    • S.E. Gilliland, and M.J. Speck Deconjugation of bile acids by intestinal lactobacilli Appl. Environ. Microbiol. 33 1977 15 18
    • (1977) Appl. Environ. Microbiol. , vol.33 , pp. 15-18
    • Gilliland, S.E.1    Speck, M.J.2
  • 173
    • 0024058679 scopus 로고
    • Purification and characterization of bile salt hydrolase from Clostridium perfringens
    • R. Gopal-Srivastava, and P.B. Hylemon Purification and characterization of bile salt hydrolase from Clostridium perfringens J. Lipid Res. 29 1988 1079 1085
    • (1988) J. Lipid Res. , vol.29 , pp. 1079-1085
    • Gopal-Srivastava, R.1    Hylemon, P.B.2
  • 175
    • 0024847957 scopus 로고
    • Purification and characterization of a new hydrolase for conjugated bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus
    • K. Kawamoto, I. Horibe, and K. Uchida Purification and characterization of a new hydrolase for conjugated bile acids, chenodeoxycholyltaurine hydrolase, from Bacteroides vulgatus J. Biochem. 106 1989 1049 1053
    • (1989) J. Biochem. , vol.106 , pp. 1049-1053
    • Kawamoto, K.1    Horibe, I.2    Uchida, K.3
  • 176
    • 0019473679 scopus 로고
    • Deconjugation of bile salts by Bacteroides and Clostridium
    • N. Masuda Deconjugation of bile salts by Bacteroides and Clostridium Microbiol. Immunol. 25 1981 1 11
    • (1981) Microbiol. Immunol. , vol.25 , pp. 1-11
    • Masuda, N.1
  • 177
    • 0017110325 scopus 로고
    • Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis
    • E.J. Stellwag, and P.B. Hylemon Purification and characterization of bile salt hydrolase from Bacteroides fragilis subsp. fragilis Biochim. Biophys. Acta 452 1976 165 176
    • (1976) Biochim. Biophys. Acta , vol.452 , pp. 165-176
    • Stellwag, E.J.1    Hylemon, P.B.2
  • 178
    • 0034048222 scopus 로고    scopus 로고
    • Bile salt hydrolase of Bifidobacterium longum - Biochemical and genetic characterization
    • H. Tanaka, H. Hashiba, J. Kok, and I. Mierau Bile salt hydrolase of Bifidobacterium longum - biochemical and genetic characterization Appl. Environ. Microbiol. 66 2000 2502 2512
    • (2000) Appl. Environ. Microbiol. , vol.66 , pp. 2502-2512
    • Tanaka, H.1    Hashiba, H.2    Kok, J.3    Mierau, I.4
  • 179
    • 0033403825 scopus 로고    scopus 로고
    • Localization and primary characterization of bile salt hydrolase from Lactobacillus reuteri
    • M.P. Taranto, and G. Font de Valdez Localization and primary characterization of bile salt hydrolase from Lactobacillus reuteri Biotechnol. Lett. 21 1999 935 938
    • (1999) Biotechnol. Lett. , vol.21 , pp. 935-938
    • Taranto, M.P.1    Font De Valdez, G.2
  • 180
    • 0028098796 scopus 로고
    • High concentrations of conjugated bile acids inhibit bacterial growth of Clostridium perfringens and induce its extracellular cholylglycine hydrolase
    • M. Kishinaka, A. Umeda, and S. Kuroki High concentrations of conjugated bile acids inhibit bacterial growth of Clostridium perfringens and induce its extracellular cholylglycine hydrolase Steroids 59 1994 485 489
    • (1994) Steroids , vol.59 , pp. 485-489
    • Kishinaka, M.1    Umeda, A.2    Kuroki, S.3
  • 181
    • 0026574594 scopus 로고
    • Multiple forms of bile salt hydrolase from Lactobacillus sp. strain 100-100
    • S.G. Lundeen, and D.C. Savage Multiple forms of bile salt hydrolase from Lactobacillus sp. strain 100-100 J. Bacteriol. 174 1992 7217 7220
    • (1992) J. Bacteriol. , vol.174 , pp. 7217-7220
    • Lundeen, S.G.1    Savage, D.C.2
  • 182
    • 0029041833 scopus 로고
    • Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens
    • J.P. Coleman, and L.L. Hudson Cloning and characterization of a conjugated bile acid hydrolase gene from Clostridium perfringens Appl. Environ. Microbiol. 61 1995 2514 2520
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 2514-2520
    • Coleman, J.P.1    Hudson, L.L.2
  • 183
    • 0028942320 scopus 로고
    • Comparison of Lactobacillus strains with respect to bile salt hydrolase activity, colonisation of the gastrointestinal tract, and growth rate of the murine host
    • J.M. Bateup, M.A. Mc Connell, H.F. Jenkinson, and G.W. Tannock Comparison of Lactobacillus strains with respect to bile salt hydrolase activity, colonisation of the gastrointestinal tract, and growth rate of the murine host Appl. Environ. Microbiol. 61 1995 1147 1149
    • (1995) Appl. Environ. Microbiol. , vol.61 , pp. 1147-1149
    • Bateup, J.M.1    Mc Connell, M.A.2    Jenkinson, H.F.3    Tannock, G.W.4
  • 184
    • 0024527116 scopus 로고
    • Development of a differential medium for bile salt hydrolase-active Lactobacillus spp
    • M.P. Dashkevicz, and S.D. Feighner Development of a differential medium for bile salt hydrolase-active Lactobacillus spp Appl. Environ. Microbiol. 55 1989 11 16
    • (1989) Appl. Environ. Microbiol. , vol.55 , pp. 11-16
    • Dashkevicz, M.P.1    Feighner, S.D.2
  • 185
    • 0032881357 scopus 로고    scopus 로고
    • Bile salt deconjugation by Lactobacillus plantarum 80 and its implication for bacterial toxicity
    • P. De Boever, and W. Verstraete Bile salt deconjugation by Lactobacillus plantarum 80 and its implication for bacterial toxicity J. Appl. Microbiol. 87 1999 345 352
    • (1999) J. Appl. Microbiol. , vol.87 , pp. 345-352
    • De Boever, P.1    Verstraete, W.2
  • 186
    • 0035217635 scopus 로고    scopus 로고
    • Genes encoding bile salt hydrolases and conjugated bile salt transporters in Lactobacillus johnsonni 100-100 and other Lactobacillus species
    • C.A. Elkins, S.A. Moser, and D.C. Savage Genes encoding bile salt hydrolases and conjugated bile salt transporters in Lactobacillus johnsonni 100-100 and other Lactobacillus species Microbiology 147 2001 3403 3412
    • (2001) Microbiology , vol.147 , pp. 3403-3412
    • Elkins, C.A.1    Moser, S.A.2    Savage, D.C.3
  • 187
    • 0031720810 scopus 로고    scopus 로고
    • Identification of genes encoding conjugated bile salt hydrolase and transport in Lactobacillus johnsonni 100-100
    • E.A. Elkins, and D.C. Savage Identification of genes encoding conjugated bile salt hydrolase and transport in Lactobacillus johnsonni 100-100 J. Bacteriol. 180 1998 4344 4349
    • (1998) J. Bacteriol. , vol.180 , pp. 4344-4349
    • Elkins, E.A.1    Savage, D.C.2
  • 188
  • 189
    • 0033773424 scopus 로고    scopus 로고
    • Bile toxicity to some bifidobacteria strains: Role of conjugated bile salt hydrolase and pH
    • J.P. Grill, S. Perrin, and F. Schneider Bile toxicity to some bifidobacteria strains: role of conjugated bile salt hydrolase and pH Can. J. Microbiol. 46 2000 878 884
    • (2000) Can. J. Microbiol. , vol.46 , pp. 878-884
    • Grill, J.P.1    Perrin, S.2    Schneider, F.3
  • 190
    • 0035004396 scopus 로고    scopus 로고
    • Bile salt hydrolase activity of Enterococci isolated from food: Screening and quantitative determination
    • C.M.A.P. Franz, I. Specht, P. Haberer, and W.H. Holzapfel Bile salt hydrolase activity of Enterococci isolated from food: screening and quantitative determination J. Food Prot. 64 2001 725 729
    • (2001) J. Food Prot. , vol.64 , pp. 725-729
    • Franz, C.M.A.P.1    Specht, I.2    Haberer, P.3    Holzapfel, W.H.4
  • 191
    • 0036947087 scopus 로고    scopus 로고
    • Quantitative determination of bile salt hydrolase activity in bacteria isolated from the small intestine of chickens
    • A. Knarreborg, R.M. Engberg, S.K. Jensen, and B.B. Jensen Quantitative determination of bile salt hydrolase activity in bacteria isolated from the small intestine of chickens Appl. Environ. Microbiol. 68 2002 6425 6428
    • (2002) Appl. Environ. Microbiol. , vol.68 , pp. 6425-6428
    • Knarreborg, A.1    Engberg, R.M.2    Jensen, S.K.3    Jensen, B.B.4
  • 193
    • 0020029418 scopus 로고
    • Isolation of a bile salt sulfatase-producing Clostridium strain from rat intestinal microflora
    • S.M. Huijghebaert, J.A. Mertens, and H.J. Eyssen Isolation of a bile salt sulfatase-producing Clostridium strain from rat intestinal microflora Appl. Environ. Microbiol. 43 1982 185 192
    • (1982) Appl. Environ. Microbiol. , vol.43 , pp. 185-192
    • Huijghebaert, S.M.1    Mertens, J.A.2    Eyssen, H.J.3
  • 194
    • 0032114156 scopus 로고    scopus 로고
    • Incorporation of cholesterol into the cellular membrane of Bifidobacterium longum
    • P.C. Dambekodi, and S.E. Gilliland Incorporation of cholesterol into the cellular membrane of Bifidobacterium longum J. Dairy Sci. 81 1998 1818 1824
    • (1998) J. Dairy Sci. , vol.81 , pp. 1818-1824
    • Dambekodi, P.C.1    Gilliland, S.E.2
  • 195
    • 0037710618 scopus 로고    scopus 로고
    • Bile salts and cholesterol induce changes in the lipid cell membrane of Lactobacillus reuteri
    • M.P. Taranto, M.L. Fernandez Murga, G. Lorca, and G.F. de Valdez Bile salts and cholesterol induce changes in the lipid cell membrane of Lactobacillus reuteri J. Appl. Microbiol. 95 2003 86 91
    • (2003) J. Appl. Microbiol. , vol.95 , pp. 86-91
    • Taranto, M.P.1    Fernandez Murga, M.L.2    Lorca, G.3    De Valdez, G.F.4
  • 196
    • 0030774042 scopus 로고    scopus 로고
    • Bile salt hydrolase plays a key role on cholesterol removal by Lactobacillus reuteri
    • M.P. Taranto, F. Sesma, A.P. Ruiz Holgado, and G.F. Valdez Bile salt hydrolase plays a key role on cholesterol removal by Lactobacillus reuteri Biotechnol. Lett. 19 1997 845 847
    • (1997) Biotechnol. Lett. , vol.19 , pp. 845-847
    • Taranto, M.P.1    Sesma, F.2    Ruiz Holgado, A.P.3    Valdez, G.F.4
  • 197
    • 0023239664 scopus 로고
    • Lipid intermolecular hydrogen bonding: Influence on structural organization and membrane function
    • J.M. Boggs Lipid intermolecular hydrogen bonding: influence on structural organization and membrane function Biochem. Biophys. Acta 906 1987 353 404
    • (1987) Biochem. Biophys. Acta , vol.906 , pp. 353-404
    • Boggs, J.M.1
  • 202
    • 0033069373 scopus 로고    scopus 로고
    • Bile tolerance, taurocholate deconjugation, and binding of cholesterol by Lactobacillus gasseri strains
    • USMAN (The United Graduate School of Agricultural Science), and A. Hosono Bile tolerance, taurocholate deconjugation, and binding of cholesterol by Lactobacillus gasseri strains J. Dairy Sci. 82 1999 243 248
    • (1999) J. Dairy Sci. , vol.82 , pp. 243-248
  • 203
    • 0035430951 scopus 로고    scopus 로고
    • Bile salt hydrolase activity and resistance to toxicity of conjugated bile salts are unrelated properties in Lactobacilli
    • S.A. Moser, and D.C. Savage Bile salt hydrolase activity and resistance to toxicity of conjugated bile salts are unrelated properties in Lactobacilli Appl. Environ. Microbiol. 67 2001 3476 3480
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 3476-3480
    • Moser, S.A.1    Savage, D.C.2
  • 204
    • 0037227360 scopus 로고    scopus 로고
    • Deconjugation of bile salts by Lactobacillus acidophilus isolates
    • Y.T. Ahn, G.B. Kim, Y.S. Lim, Y.J. Baek, and Y.U. Kim Deconjugation of bile salts by Lactobacillus acidophilus isolates Int. Dairy J. 13 2003 303 311
    • (2003) Int. Dairy J. , vol.13 , pp. 303-311
    • Ahn, Y.T.1    Kim, G.B.2    Lim, Y.S.3    Baek, Y.J.4    Kim, Y.U.5
  • 205
    • 0033251402 scopus 로고    scopus 로고
    • Screening of lactic acid bacteria for bile salt hydrolase activity
    • H. Tanaka, K. Doesburg, T. Iwasaki, and I. Mierau Screening of lactic acid bacteria for bile salt hydrolase activity J. Dairy Sci. 82 1999 2530 2535
    • (1999) J. Dairy Sci. , vol.82 , pp. 2530-2535
    • Tanaka, H.1    Doesburg, K.2    Iwasaki, T.3    Mierau, I.4
  • 207
    • 0028254682 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
    • I. De Smet, L. Van Hoorde, N. De Sayer, M. Vande Woestyne, and W. Verstraete 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 1994 315 329
    • (1994) Microb. Ecol. Health Dis. , vol.7 , pp. 315-329
    • De Smet, I.1    Van Hoorde, L.2    De Sayer, N.3    Vande Woestyne, M.4    Verstraete, W.5
  • 208
    • 0023096281 scopus 로고
    • Subtherapeutic levels of antibiotics in poultry feeds and their effects on weight gain, feed efficiency, and bacterial cholyltaurine hydrolase activity
    • S.D. Feighner, and M.P. Dashkevicz Subtherapeutic levels of antibiotics in poultry feeds and their effects on weight gain, feed efficiency, and bacterial cholyltaurine hydrolase activity Appl. Environ. Microbiol. 53 1987 331 336
    • (1987) Appl. Environ. Microbiol. , vol.53 , pp. 331-336
    • Feighner, S.D.1    Dashkevicz, M.P.2
  • 209
    • 0023953741 scopus 로고
    • Effect of dietary carbohydrates on bacterial cholyltaurine hydrolase in poultry intestinal homogenates
    • S.D. Feighner, and M.P. Dashkevicz Effect of dietary carbohydrates on bacterial cholyltaurine hydrolase in poultry intestinal homogenates Appl. Environ. Microbiol. 54 1988 337 342
    • (1988) Appl. Environ. Microbiol. , vol.54 , pp. 337-342
    • Feighner, S.D.1    Dashkevicz, M.P.2
  • 210
    • 0023414693 scopus 로고
    • Deconjugation of bile acids by human intestinal bacteria implanted in germ-free rats
    • T. Chikai, H. Nakao, and K. Uchida Deconjugation of bile acids by human intestinal bacteria implanted in germ-free rats Lipids 22 1987 669 671
    • (1987) Lipids , vol.22 , pp. 669-671
    • Chikai, T.1    Nakao, H.2    Uchida, K.3
  • 211
    • 0031892684 scopus 로고    scopus 로고
    • Cholesterol lowering in pigs through enhanced bacterial bile salt hydrolase activity
    • I. De Smet, P. De Boever, and W. Verstraete Cholesterol lowering in pigs through enhanced bacterial bile salt hydrolase activity Br. J. Nutr. 79 1998 185 194
    • (1998) Br. J. Nutr. , vol.79 , pp. 185-194
    • De Smet, I.1    De Boever, P.2    Verstraete, W.3
  • 212
    • 0032478228 scopus 로고    scopus 로고
    • Characterisation and selection of probiotic lactobacilli for a preliminary minipig feeding trial and their effect on serum cholesterol levels, faeces pH and faeces moisture content
    • M. du Toit, C.M. Franz, L.M. Dicks, U. Schillinger, P. Harberer, B. Warlies, F. Ahrens, and W.H. Holzapfel Characterisation and selection of probiotic lactobacilli for a preliminary minipig feeding trial and their effect on serum cholesterol levels, faeces pH and faeces moisture content Int. J. Food Microbiol. 40 1998 93 104
    • (1998) Int. J. Food Microbiol. , vol.40 , pp. 93-104
    • Du Toit, M.1    Franz, C.M.2    Dicks, L.M.3    Schillinger, U.4    Harberer, P.5    Warlies, B.6    Ahrens, F.7    Holzapfel, W.H.8
  • 213
    • 0041528244 scopus 로고    scopus 로고
    • An in vitro study of the probiotic potential of a bile-salt-hydrolyzing Lactobacillus fermentum strain, and determination of its cholesterol-lowering properties
    • D.I.A. Pereira, A.L. Mc Cartney, and G.R. Gibson An in vitro study of the probiotic potential of a bile-salt-hydrolyzing Lactobacillus fermentum strain, and determination of its cholesterol-lowering properties Appl. Environ. Microbiol. 69 2003 4743 4752
    • (2003) Appl. Environ. Microbiol. , vol.69 , pp. 4743-4752
    • Pereira, D.I.A.1    Mc Cartney, A.L.2    Gibson, G.R.3
  • 214
    • 0000540595 scopus 로고
    • Microecology of the gastrointestinal tract in relation to lactic acid bacteria
    • G.W. Tannock Microecology of the gastrointestinal tract in relation to lactic acid bacteria Int. Dairy J. 5 1995 1059 1070
    • (1995) Int. Dairy J. , vol.5 , pp. 1059-1070
    • Tannock, G.W.1
  • 215
    • 0002732598 scopus 로고
    • Biotransformation of bile acids and cholesterol by intestinal microflora
    • D.J. Hentges Academic Press New York
    • P.B. Hylemon, and T.L. Glass Biotransformation of bile acids and cholesterol by intestinal microflora D.J. Hentges Human Intestinal Microflora in Health and Disease 1983 Academic Press New York 189 213
    • (1983) Human Intestinal Microflora in Health and Disease , pp. 189-213
    • Hylemon, P.B.1    Glass, T.L.2
  • 216
    • 0029657766 scopus 로고    scopus 로고
    • Expression and characterization of a C24 bile acid 7α-dehydratase from Eubacterium sp. strain VPI 12708 in Escherichia coli
    • J.A. Dawson, D.H. Mallonee, I. Björkhem, and P.B. Hylemon Expression and characterization of a C24 bile acid 7α-dehydratase from Eubacterium sp. strain VPI 12708 in Escherichia coli J. Lipid Res. 37 1996 1258 1267
    • (1996) J. Lipid Res. , vol.37 , pp. 1258-1267
    • Dawson, J.A.1    Mallonee, D.H.2    Björkhem, I.3    Hylemon, P.B.4
  • 217
    • 0032895658 scopus 로고    scopus 로고
    • The bile-acid inducible baiF gene from Eubacterium sp. strain VPI 12708 a bile acid-coenzyme a hydrolase
    • G. Ye, D.H. Mallonee, J.E. Wells, I. Bjorkhem, and P.B. Hylemon The bile-acid inducible baiF gene from Eubacterium sp. strain VPI 12708 a bile acid-coenzyme A hydrolase J. Lipid Res. 40 1999 17 23
    • (1999) J. Lipid Res. , vol.40 , pp. 17-23
    • Ye, G.1    Mallonee, D.H.2    Wells, J.E.3    Bjorkhem, I.4    Hylemon, P.B.5
  • 218
    • 0028793304 scopus 로고
    • Deoxycholic acid influences cholesterol solubilization and microcrystal nucleation time in gallbladder bile
    • S.H. Hussaini, S.P. Pereira, G.M. Murphy, and R.W. Dowling Deoxycholic acid influences cholesterol solubilization and microcrystal nucleation time in gallbladder bile Hepatology 22 1995 1735 1744
    • (1995) Hepatology , vol.22 , pp. 1735-1744
    • Hussaini, S.H.1    Pereira, S.P.2    Murphy, G.M.3    Dowling, R.W.4
  • 220
    • 0029017084 scopus 로고
    • Increase of deoxycholic acid in supersaturated bile of patients with cholesterol gallstone disease and its correlation with de novo synthesis of cholesterol and bile acids in the liver, gallbladder emptying, and small intestine transit
    • J. Shoda, B.F. He, N. Tanaka, Y. Matsuzaki, T. Osuga, S. Yamamori, H. Miyazaki, and J. Sjovall Increase of deoxycholic acid in supersaturated bile of patients with cholesterol gallstone disease and its correlation with de novo synthesis of cholesterol and bile acids in the liver, gallbladder emptying, and small intestine transit Hepatology 21 1995 1291 1302
    • (1995) Hepatology , vol.21 , pp. 1291-1302
    • Shoda, J.1    He, B.F.2    Tanaka, N.3    Matsuzaki, Y.4    Osuga, T.5    Yamamori, S.6    Miyazaki, H.7    Sjovall, J.8
  • 221
    • 0027056677 scopus 로고
    • Communication modules in bacterial signalling proteins
    • J.S. Parkinson, and E.C. Kofoid Communication modules in bacterial signalling proteins Annu. Rev. Genetics 26 1992 71 112
    • (1992) Annu. Rev. Genetics , vol.26 , pp. 71-112
    • Parkinson, J.S.1    Kofoid, E.C.2
  • 222
    • 0037135593 scopus 로고    scopus 로고
    • Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli
    • P. De Wulf, A.M. McGuire, X. Liu, and E.C. Lin Genome-wide profiling of promoter recognition by the two-component response regulator CpxR-P in Escherichia coli J. Biol. Chem. 277 2002 26652 26661
    • (2002) J. Biol. Chem. , vol.277 , pp. 26652-26661
    • De Wulf, P.1    McGuire, A.M.2    Liu, X.3    Lin, E.C.4
  • 223
    • 0037384456 scopus 로고    scopus 로고
    • Signal detection and target gene induction by the CpxRA two-component system
    • P.A. DiGiuseppe, and T.J. Silhavy Signal detection and target gene induction by the CpxRA two-component system J. Bacteriol. 185 2003 2432 2440
    • (2003) J. Bacteriol. , vol.185 , pp. 2432-2440
    • Digiuseppe, P.A.1    Silhavy, T.J.2
  • 224
    • 0023430342 scopus 로고
    • Changes in the linking number of supercoiled DNA accompany growth transitions in Escherichia coli
    • V.L. Balke, and J.D. Gralla Changes in the linking number of supercoiled DNA accompany growth transitions in Escherichia coli J. Bacteriol. 169 1987 4499 4506
    • (1987) J. Bacteriol. , vol.169 , pp. 4499-4506
    • Balke, V.L.1    Gralla, J.D.2
  • 225
    • 0025968977 scopus 로고
    • DNA supercoiling and environmental regulation of gene expression in pathogenic bacteria
    • C.J. Dorman DNA supercoiling and environmental regulation of gene expression in pathogenic bacteria Infect. Immun. 59 1991 745 749
    • (1991) Infect. Immun. , vol.59 , pp. 745-749
    • Dorman, C.J.1
  • 226
    • 0029036349 scopus 로고
    • DNA topology and the global control of bacterial gene expression: Implications for the regulation of virulence gene expression
    • C.J. Dorman DNA topology and the global control of bacterial gene expression: implications for the regulation of virulence gene expression Microbiology 141 1995 1271 1280
    • (1995) Microbiology , vol.141 , pp. 1271-1280
    • Dorman, C.J.1
  • 227
    • 0030161428 scopus 로고    scopus 로고
    • Flexible response: DNA supercoiling, transcription and bacterial adaptation to environmental stress
    • C.J. Dorman Flexible response: DNA supercoiling, transcription and bacterial adaptation to environmental stress Trends Microbiol. 4 1996 214 216
    • (1996) Trends Microbiol. , vol.4 , pp. 214-216
    • Dorman, C.J.1
  • 228
    • 0026555506 scopus 로고
    • Control of bacterial DNA supercoiling
    • K. Drilca Control of bacterial DNA supercoiling Mol. Microbiol. 6 1992 425 433
    • (1992) Mol. Microbiol. , vol.6 , pp. 425-433
    • Drilca, K.1
  • 229
    • 0034729202 scopus 로고    scopus 로고
    • DNA topology and adaptation of Salmonella typhimurium to an intracellular environment
    • D.G. Marshall, F. Bowe, C. Hale, G. Dougan, and C.J. Dorman DNA topology and adaptation of Salmonella typhimurium to an intracellular environment Phil. Trans. R. Soc. London B 355 2000 565 574
    • (2000) Phil. Trans. R. Soc. London B , vol.355 , pp. 565-574
    • Marshall, D.G.1    Bowe, F.2    Hale, C.3    Dougan, G.4    Dorman, C.J.5
  • 230
    • 0031786750 scopus 로고    scopus 로고
    • Does the membrane's physical state control the expression of heat shock and other genes?
    • L. Vigh, B. Maresca, and J.L. Harwood Does the membrane's physical state control the expression of heat shock and other genes? Trends Biochem. Sci. 23 1998 369 374
    • (1998) Trends Biochem. Sci. , vol.23 , pp. 369-374
    • Vigh, L.1    Maresca, B.2    Harwood, J.L.3
  • 231
    • 0343167931 scopus 로고    scopus 로고
    • DNA topology and the thermal stress response, a tale from mesophiles and hyperthermophiles
    • P. Lopez-Garcia, and P. Forterre DNA topology and the thermal stress response, a tale from mesophiles and hyperthermophiles BioEssays 22 2000 738 746
    • (2000) BioEssays , vol.22 , pp. 738-746
    • Lopez-Garcia, P.1    Forterre, P.2
  • 234
    • 0035490872 scopus 로고    scopus 로고
    • b in heat, ethanol, acid, and oxidative stress resistance and during carbon starvation in Listeria monocytogenes
    • B in heat, ethanol, acid, and oxidative stress resistance and during carbon starvation in Listeria monocytogenes Appl. Environ. Microbiol. 67 2001 4454 4457
    • (2001) Appl. Environ. Microbiol. , vol.67 , pp. 4454-4457
    • Ferreira, A.1    Byrne, C.P.O.'.2    Boor, K.J.3
  • 235
    • 0028019587 scopus 로고
    • The role of sigma factor sigma S (KatF) in bacterial global regulation
    • P.C. Loewen, and R. Hengge-Aronis The role of sigma factor sigma S (KatF) in bacterial global regulation Annu. Rev. Microbiol. 48 1994 53 80
    • (1994) Annu. Rev. Microbiol. , vol.48 , pp. 53-80
    • Loewen, P.C.1    Hengge-Aronis, R.2
  • 236
    • 0032586856 scopus 로고    scopus 로고
    • b-dependent general stress response confers multiple stress resistance in Bacillus subtilis
    • B-dependent general stress response confers multiple stress resistance in Bacillus subtilis J. Bacteriol. 181 1999 3942 3948
    • (1999) J. Bacteriol. , vol.181 , pp. 3942-3948
    • Völker, U.1    Maul, B.2    Hecker, M.3
  • 238
    • 0345306166 scopus 로고    scopus 로고
    • b-dependent expression patterns of compatible solute transporter genes opuCA and lmo1421 and the conjugated bile salt hydrolase gene bsh in Listeria monocytogenes
    • B-dependent expression patterns of compatible solute transporter genes opuCA and lmo1421 and the conjugated bile salt hydrolase gene bsh in Listeria monocytogenes Microbiology 149 2003 3247 3256
    • (2003) Microbiology , vol.149 , pp. 3247-3256
    • Sue, D.1    Boor, K.J.2    Wiedmann, M.3
  • 239
    • 0026511987 scopus 로고
    • Environmental signals controlling expression of virulence determinants in bacteria
    • J.J. Mekalanos Environmental signals controlling expression of virulence determinants in bacteria J. Bacteriol. 174 1992 1 7
    • (1992) J. Bacteriol. , vol.174 , pp. 1-7
    • Mekalanos, J.J.1
  • 240
    • 0003582512 scopus 로고
    • A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence
    • S.I. Miller, A.M. Kukral, and J.J. Mekalanos A two-component regulatory system (phoP phoQ) controls Salmonella typhimurium virulence Proc. Natl. Acad. Sci. USA 86 1989 5054 5058
    • (1989) Proc. Natl. Acad. Sci. USA , vol.86 , pp. 5054-5058
    • Miller, S.I.1    Kukral, A.M.2    Mekalanos, J.J.3
  • 242
    • 0034443263 scopus 로고    scopus 로고
    • Salmonella enterica Serovar Typhimurium invasion is repressed in the presence of bile
    • A.M. Prouty, and J.S. Gunn Salmonella enterica Serovar Typhimurium invasion is repressed in the presence of bile Infect. Immun. 68 2000 6763 6769
    • (2000) Infect. Immun. , vol.68 , pp. 6763-6769
    • Prouty, A.M.1    Gunn, J.S.2
  • 243
    • 0028801454 scopus 로고
    • Inhibitory effect of bile on bacterial invasion of enterocytes
    • C.L. Wells, R.P. Jechorek, and S.L. Erlandsen Inhibitory effect of bile on bacterial invasion of enterocytes Crit. Care Med. 23 1995 301 307
    • (1995) Crit. Care Med. , vol.23 , pp. 301-307
    • Wells, C.L.1    Jechorek, R.P.2    Erlandsen, S.L.3
  • 244
    • 0029147485 scopus 로고
    • Increased protein secretion and adherence to HeLa cells by Shigella spp. following growth in the presence of bile salts
    • L.M. Pope, K.E. Reed, and S.M. Payne Increased protein secretion and adherence to HeLa cells by Shigella spp. following growth in the presence of bile salts Infect. Immun. 63 1995 3642 3648
    • (1995) Infect. Immun. , vol.63 , pp. 3642-3648
    • Pope, L.M.1    Reed, K.E.2    Payne, S.M.3
  • 245
    • 0029779236 scopus 로고    scopus 로고
    • Production of thermostable direct hemolysin by Vibrio parahaemolyticus enhanced by conjugated bile acids
    • R. Osawa, and S. Yamai Production of thermostable direct hemolysin by Vibrio parahaemolyticus enhanced by conjugated bile acids Appl. Environ. Microbiol. 62 1996 3023 3025
    • (1996) Appl. Environ. Microbiol. , vol.62 , pp. 3023-3025
    • Osawa, R.1    Yamai, S.2
  • 246
    • 0036548620 scopus 로고    scopus 로고
    • Levels of thermostable direct hemolysin produced by Vibrio parahaemolyticus 03:K6 and other serovars grown anaerobically with the presence of a bile acid
    • R. Osawa, E. Arakawa, T. Okitsu, S. Yamai, and H. Watanabe Levels of thermostable direct hemolysin produced by Vibrio parahaemolyticus 03:K6 and other serovars grown anaerobically with the presence of a bile acid Curr. Microbiol. 44 2002 302 305
    • (2002) Curr. Microbiol. , vol.44 , pp. 302-305
    • Osawa, R.1    Arakawa, E.2    Okitsu, T.3    Yamai, S.4    Watanabe, H.5
  • 248
    • 0027812251 scopus 로고
    • In vivo expression of virulence genes of Y. pseudotuberculosis
    • A. Forsberg, and R. Rosqvist In vivo expression of virulence genes of Y. pseudotuberculosis Infect. Agents Dis. 2 1994 275 278
    • (1994) Infect. Agents Dis. , vol.2 , pp. 275-278
    • Forsberg, A.1    Rosqvist, R.2
  • 250
    • 0031029971 scopus 로고    scopus 로고
    • Bile affects production of virulence factors and motility of Vibrio cholerae
    • S. Gupta, and R. Chowdhury Bile affects production of virulence factors and motility of Vibrio cholerae Infect. Immun. 65 1997 1131 1134
    • (1997) Infect. Immun. , vol.65 , pp. 1131-1134
    • Gupta, S.1    Chowdhury, R.2
  • 251
    • 0032987096 scopus 로고    scopus 로고
    • Environmental signals modulate ToxT-dependent virulence factor expression in Vibrio cholerae
    • D.A. Schuhmacher, and K.E. Klose Environmental signals modulate ToxT-dependent virulence factor expression in Vibrio cholerae J. Bacteriol. 181 1999 1508 1514
    • (1999) J. Bacteriol. , vol.181 , pp. 1508-1514
    • Schuhmacher, D.A.1    Klose, K.E.2
  • 252
    • 0038013943 scopus 로고    scopus 로고
    • From motility to virulence: Sensing and responding to environmental signals in Vibrio cholerae
    • E.S. Krukonis, and V.J. DiRita From motility to virulence: sensing and responding to environmental signals in Vibrio cholerae Curr. Opin. Microbiol. 6 2003 186 190
    • (2003) Curr. Opin. Microbiol. , vol.6 , pp. 186-190
    • Krukonis, E.S.1    Dirita, V.J.2
  • 253
    • 0035370231 scopus 로고    scopus 로고
    • Secretion of the virulence-associated Campylobacter invasion antigens from Campylobacter jejuni requires a stimulatory signal
    • V. Rivera-Amill, B.J. Kim, J. Seshu, and M.E. Konkel Secretion of the virulence-associated Campylobacter invasion antigens from Campylobacter jejuni requires a stimulatory signal J. Infect. Dis. 183 2001 1607 1616
    • (2001) J. Infect. Dis. , vol.183 , pp. 1607-1616
    • Rivera-Amill, V.1    Kim, B.J.2    Seshu, J.3    Konkel, M.E.4
  • 255
    • 0030009060 scopus 로고    scopus 로고
    • An environmentally regulated pilus-like appendage involved in Campylobacter pathogenesis
    • P. Doig, R. Yao, D.H. Burr, P. Guerry, and T.J. Trust An environmentally regulated pilus-like appendage involved in Campylobacter pathogenesis Mol. Microbiol. 20 1996 885 894
    • (1996) Mol. Microbiol. , vol.20 , pp. 885-894
    • Doig, P.1    Yao, R.2    Burr, D.H.3    Guerry, P.4    Trust, T.J.5
  • 256
    • 0034744732 scopus 로고    scopus 로고
    • Bile-induced "pili in Campylobacter jejuni are bacteria-independent artefacts of the culture medium
    • E.C. Gaynor, N. Ghori, and S. Falkow Bile-induced "pili in Campylobacter jejuni are bacteria-independent artefacts of the culture medium Mol. Microbiol. 39 2001 1546 1549
    • (2001) Mol. Microbiol. , vol.39 , pp. 1546-1549
    • Gaynor, E.C.1    Ghori, N.2    Falkow, S.3
  • 258
    • 33645209092 scopus 로고
    • Biliary tract disease
    • I.A.D. Bouchier Third ed. Baillière Tindall London
    • I.A.D. Bouchier Biliary tract disease I.A.D. Bouchier Gastroenterology Third ed. 1982 Baillière Tindall London 302 327
    • (1982) Gastroenterology , pp. 302-327
    • Bouchier, I.A.D.1
  • 259
    • 0030990103 scopus 로고    scopus 로고
    • Alterations of the outer membrane composition in Escherichia coli lacking the histone-like protein HU
    • E. Painbeni, M. Caroff, and J. Rouviere-Yaniv Alterations of the outer membrane composition in Escherichia coli lacking the histone-like protein HU Proc. Natl. Acad. Sci. 94 1997 6712 6717
    • (1997) Proc. Natl. Acad. Sci. , vol.94 , pp. 6712-6717
    • Painbeni, E.1    Caroff, M.2    Rouviere-Yaniv, J.3


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