메뉴 건너뛰기




Volumn 193, Issue 7, 2011, Pages 1643-1652

A selenium-dependent xanthine dehydrogenase triggers biofilm proliferation in Enterococcus faecalis through oxidant production

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL DNA; GLUCOSE; HYDROGEN PEROXIDE; MESSENGER RNA; METALLOPROTEIN; MOLYBDENUM; SELENITE; SELENIUM; SELENIUM 75; SUPEROXIDE; URIC ACID; XANTHINE DEHYDROGENASE;

EID: 79952785357     PISSN: 00219193     EISSN: 10985530     Source Type: Journal    
DOI: 10.1128/JB.01063-10     Document Type: Article
Times cited : (40)

References (64)
  • 2
    • 77952563903 scopus 로고    scopus 로고
    • Selenoproteins-what unique properties can arise with selenocysteine in place of cysteine?
    • Arner, E. S. 2010. Selenoproteins-what unique properties can arise with selenocysteine in place of cysteine? Exp. Cell Res. 316:1296-1303.
    • (2010) Exp. Cell Res. , vol.316 , pp. 1296-1303
    • Arner, E.S.1
  • 3
    • 0025996978 scopus 로고
    • Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium
    • Axley, M. J., A. Bock, and T. C. Stadtman. 1991. Catalytic properties of an Escherichia coli formate dehydrogenase mutant in which sulfur replaces selenium. Proc. Natl. Acad. Sci. U. S. A. 88:8450-8454.
    • (1991) Proc. Natl. Acad. Sci. U. S. A. , vol.88 , pp. 8450-8454
    • Axley, M.J.1    Bock, A.2    Stadtman, T.C.3
  • 4
    • 0024384581 scopus 로고
    • Selenium metabolism and selenium-dependent enzymes in microorganisms
    • Axley, M. J., and T. C. Stadtman. 1989. Selenium metabolism and selenium-dependent enzymes in microorganisms. Annu. Rev. Nutr. 9:127-137.
    • (1989) Annu. Rev. Nutr. , vol.9 , pp. 127-137
    • Axley, M.J.1    Stadtman, T.C.2
  • 5
    • 34548846129 scopus 로고    scopus 로고
    • Nitrite confers protection against myocardial infarction: Role of xanthine oxidoreductase, NADPH oxidase and K(ATP) channels
    • Baker, J. E., et al. 2007. Nitrite confers protection against myocardial infarction: role of xanthine oxidoreductase, NADPH oxidase and K(ATP) channels. J. Mol. Cell. Cardiol. 43:437-444.
    • (2007) J. Mol. Cell. Cardiol. , vol.43 , pp. 437-444
    • Baker, J.E.1
  • 6
    • 13944278132 scopus 로고    scopus 로고
    • Mitochondria, oxidants, and aging
    • DOI 10.1016/j.cell.2005.02.001
    • Balaban, R. S., S. Nemoto, and T. Finkel. 2005. Mitochondria, oxidants, and aging. Cell 120:483-495. (Pubitemid 40269763)
    • (2005) Cell , vol.120 , Issue.4 , pp. 483-495
    • Balaban, R.S.1    Nemoto, S.2    Finkel, T.3
  • 7
    • 65249083873 scopus 로고    scopus 로고
    • Functional genomics of Enterococcus faecalis: Multiple novel genetic determinants for biofilm formation in the core genome
    • Ballering, K. S., et al. 2009. Functional genomics of Enterococcus faecalis: multiple novel genetic determinants for biofilm formation in the core genome. J. Bacteriol. 191:2806-2814.
    • (2009) J. Bacteriol. , vol.191 , pp. 2806-2814
    • Ballering, K.S.1
  • 8
    • 79952810030 scopus 로고
    • Clostridium acidi-uridi and Clostridium cylindrosporum, organisms fermenting uric acid and some other purines
    • Barker, H. A., and J. V. Beck. 1942. Clostridium acidi-uridi and Clostridium cylindrosporum, organisms fermenting uric acid and some other purines. J. Bacteriol. 43:291-304.
    • (1942) J. Bacteriol. , vol.43 , pp. 291-304
    • Barker, H.A.1    Beck, J.V.2
  • 9
    • 1642484244 scopus 로고    scopus 로고
    • Xanthine oxidoreductase and cardiovascular disease: Molecular mechanisms and pathophysiological implications
    • Berry, C. E., and J. M. Hare. 2004. Xanthine oxidoreductase and cardiovascular disease: molecular mechanisms and pathophysiological implications. J. Physiol. 555:589-606.
    • (2004) J. Physiol. , vol.555 , pp. 589-606
    • Berry, C.E.1    Hare, J.M.2
  • 10
    • 76249086967 scopus 로고    scopus 로고
    • The Enterococcus faecalis superoxide dismutase is essential for its tolerance to vancomycin and penicillin
    • Bizzini, A., C. Zhao, Y. Auffray, and A. Hartke. 2009. The Enterococcus faecalis superoxide dismutase is essential for its tolerance to vancomycin and penicillin. J. Antimicrob. Chemother. 64:1196-1202.
    • (2009) J. Antimicrob. Chemother. , vol.64 , pp. 1196-1202
    • Bizzini, A.1    Zhao, C.2    Auffray, Y.3    Hartke, A.4
  • 11
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford, M. M. 1976. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72:248-254.
    • (1976) Anal. Biochem. , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 12
    • 12944263727 scopus 로고
    • Purification and characterization of xanthine dehydrogenase from Clostridium acidiurici and Clostridium cylindrosporum
    • Bradshaw, W. H., and H. A. Barker. 1960. Purification and characterization of xanthine dehydrogenase from Clostridium acidiurici and Clostridium cylindrosporum. J. Biol. Chem. 235:3620-3629.
    • (1960) J. Biol. Chem. , vol.235 , pp. 3620-3629
    • Bradshaw, W.H.1    Barker, H.A.2
  • 13
    • 0020630570 scopus 로고
    • Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri
    • Dilworth, G. L. 1983. Occurrence of molybdenum in the nicotinic acid hydroxylase from Clostridium barkeri. Arch. Biochem. Biophys. 221:565-569.
    • (1983) Arch. Biochem. Biophys. , vol.221 , pp. 565-569
    • Dilworth, G.L.1
  • 14
    • 0020393233 scopus 로고
    • Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeri
    • Dilworth, G. L. 1982. Properties of the selenium-containing moiety of nicotinic acid hydroxylase from Clostridium barkeri. Arch. Biochem. Biophys. 219:30-38.
    • (1982) Arch. Biochem. Biophys. , vol.219 , pp. 30-38
    • Dilworth, G.L.1
  • 15
    • 0020641332 scopus 로고
    • Purine and glycine metabolism by purinolytic clostridia
    • Durre, P., and J. R. Andreesen. 1983. Purine and glycine metabolism by purinolytic clostridia. J. Bacteriol. 154:192-199.
    • (1983) J. Bacteriol. , vol.154 , pp. 192-199
    • Durre, P.1    Andreesen, J.R.2
  • 16
    • 0019905990 scopus 로고
    • Selenium-dependent growth and glycine fermentation by Clostridium purinolyticum
    • Durre, P., and J. R. Andreesen. 1982. Selenium-dependent growth and glycine fermentation by Clostridium purinolyticum. J. Gen. Microbiol. 128: 1457-1466.
    • (1982) J. Gen. Microbiol. , vol.128 , pp. 1457-1466
    • Durre, P.1    Andreesen, J.R.2
  • 17
    • 0027957511 scopus 로고
    • Nicotinic acid hydroxylase from Clostridium barkeri: Electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme
    • Gladyshev, V. N., S. V. Khangulov, and T. C. Stadtman. 1994. Nicotinic acid hydroxylase from Clostridium barkeri: electron paramagnetic resonance studies show that selenium is coordinated with molybdenum in the catalytically active selenium-dependent enzyme. Proc. Natl. Acad. Sci. U. S. A. 91:232-236.
    • (1994) Proc. Natl. Acad. Sci. U. S. A. , vol.91 , pp. 232-236
    • Gladyshev, V.N.1    Khangulov, S.V.2    Stadtman, T.C.3
  • 18
    • 0030068830 scopus 로고    scopus 로고
    • Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri
    • Gladyshev, V. N., S. V. Khangulov, and T. C. Stadtman. 1996. Properties of the selenium- and molybdenum-containing nicotinic acid hydroxylase from Clostridium barkeri. Biochemistry 35:212-223.
    • (1996) Biochemistry , vol.35 , pp. 212-223
    • Gladyshev, V.N.1    Khangulov, S.V.2    Stadtman, T.C.3
  • 19
    • 0033588028 scopus 로고    scopus 로고
    • An analysis of the binding of repressor protein ModE to modABCD (molybdate transport) operator/promoter DNA of Escherichia coli
    • Grunden, A. M., W. T. Self, M. Villain, J. E. Blalock, and K. T. Shanmugam. 1999. An analysis of the binding of repressor protein ModE to modABCD (molybdate transport) operator/promoter DNA of Escherichia coli. J. Biol. Chem. 274:24308-24315.
    • (1999) J. Biol. Chem. , vol.274 , pp. 24308-24315
    • Grunden, A.M.1    Self, W.T.2    Villain, M.3    Blalock, J.E.4    Shanmugam, K.T.5
  • 20
    • 41549149124 scopus 로고    scopus 로고
    • Orphan SelD proteins and seleniumdependent molybdenum hydroxylases
    • Haft, D. H., and W. T. Self. 2008. Orphan SelD proteins and seleniumdependent molybdenum hydroxylases. Biol. Direct 3:4.
    • (2008) Biol. Direct , vol.3 , pp. 4
    • Haft, D.H.1    Self, W.T.2
  • 21
    • 0030928460 scopus 로고    scopus 로고
    • The reaction of reduced xanthine dehydrogenase with molecular oxygen. Reaction kinetics and measurement of superoxide radical
    • Harris, C. M., and V. Massey. 1997. The reaction of reduced xanthine dehydrogenase with molecular oxygen. Reaction kinetics and measurement of superoxide radical. J. Biol. Chem. 272:8370-8379.
    • (1997) J. Biol. Chem. , vol.272 , pp. 8370-8379
    • Harris, C.M.1    Massey, V.2
  • 22
    • 0031792568 scopus 로고    scopus 로고
    • Molybdate-dependent transcription of hyc and nar operons of Escherichia coli requires MoeA protein and ModE-molybdate
    • Hasona, A., W. T. Self, R. M. Ray, and K. T. Shanmugam. 1998. Molybdate-dependent transcription of hyc and nar operons of Escherichia coli requires MoeA protein and ModE-molybdate. FEMS Microbiol. Lett. 169:111-116.
    • (1998) FEMS Microbiol. Lett. , vol.169 , pp. 111-116
    • Hasona, A.1    Self, W.T.2    Ray, R.M.3    Shanmugam, K.T.4
  • 23
    • 9944248111 scopus 로고    scopus 로고
    • Molybdenum-containing hydroxylases
    • Hille, R. 2005. Molybdenum-containing hydroxylases. Arch. Biochem. Biophys. 433:107-116.
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 107-116
    • Hille, R.1
  • 24
    • 0036629252 scopus 로고    scopus 로고
    • Molybdenum and tungsten in biology
    • Hille, R. 2002. Molybdenum and tungsten in biology. Trends Biochem. Sci. 27:360-367.
    • (2002) Trends Biochem. Sci. , vol.27 , pp. 360-367
    • Hille, R.1
  • 25
    • 0014669638 scopus 로고
    • Nicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase
    • Holcenberg, J. S., and E. R. Stadtman. 1969. Nicotinic acid metabolism. 3. Purification and properties of a nicotinic acid hydroxylase. J. Biol. Chem. 244:1194-1203.
    • (1969) J. Biol. Chem. , vol.244 , pp. 1194-1203
    • Holcenberg, J.S.1    Stadtman, E.R.2
  • 26
    • 0026806101 scopus 로고
    • Purification and properties of milk xanthine dehydrogenase
    • Hunt, J., and V. Massey. 1992. Purification and properties of milk xanthine dehydrogenase. J. Biol. Chem. 267:21479-21485.
    • (1992) J. Biol. Chem. , vol.267 , pp. 21479-21485
    • Hunt, J.1    Massey, V.2
  • 27
    • 0036209728 scopus 로고    scopus 로고
    • Enterococcus faecalis produces extracellular superoxide and hydrogen peroxide that damages colonic epithelial cell DNA
    • Huycke, M. M., V. Abrams, and D. R. Moore. 2002. Enterococcus faecalis produces extracellular superoxide and hydrogen peroxide that damages colonic epithelial cell DNA. Carcinogenesis 23:529-536.
    • (2002) Carcinogenesis , vol.23 , pp. 529-536
    • Huycke, M.M.1    Abrams, V.2    Moore, D.R.3
  • 28
    • 0030803631 scopus 로고    scopus 로고
    • In vivo survival of Enterococcus faecalis is enhanced by extracellular superoxide production
    • Huycke, M. M., and M. S. Gilmore. 1997. In vivo survival of Enterococcus faecalis is enhanced by extracellular superoxide production. Adv. Exp. Med. Biol. 418:781-784.
    • (1997) Adv. Exp. Med. Biol. , vol.418 , pp. 781-784
    • Huycke, M.M.1    Gilmore, M.S.2
  • 29
    • 0030020722 scopus 로고    scopus 로고
    • Augmented production of extracellular superoxide by blood isolates of Enterococcus faecalis
    • Huycke, M. M., W. Joyce, and M. F. Wack. 1996. Augmented production of extracellular superoxide by blood isolates of Enterococcus faecalis. J. Infect. Dis. 173:743-746.
    • (1996) J. Infect. Dis. , vol.173 , pp. 743-746
    • Huycke, M.M.1    Joyce, W.2    Wack, M.F.3
  • 30
    • 0037105297 scopus 로고    scopus 로고
    • In vivo production of hydroxyl radical by Enterococcus faecalis colonizing the intestinal tract using aromatic hydroxylation
    • Huycke, M. M., and D. R. Moore. 2002. In vivo production of hydroxyl radical by Enterococcus faecalis colonizing the intestinal tract using aromatic hydroxylation. Free Radic. Biol. Med. 33:818-826.
    • (2002) Free Radic. Biol. Med. , vol.33 , pp. 818-826
    • Huycke, M.M.1    Moore, D.R.2
  • 31
    • 65349126977 scopus 로고    scopus 로고
    • Auranofin disrupts selenium metabolism in Clostridium difficile by forming a stable Au-Se adduct
    • Jackson-Rosario, S., et al. 2009. Auranofin disrupts selenium metabolism in Clostridium difficile by forming a stable Au-Se adduct. J. Biol. Inorg. Chem. 14:507-519.
    • (2009) J. Biol. Inorg. Chem. , vol.14 , pp. 507-519
    • Jackson-Rosario, S.1
  • 32
    • 67549096978 scopus 로고    scopus 로고
    • Inhibition of selenium metabolism in the oral pathogen Treponema denticola
    • Jackson-Rosario, S., and W. T. Self. 2009. Inhibition of selenium metabolism in the oral pathogen Treponema denticola. J. Bacteriol. 191:4035-4040.
    • (2009) J. Bacteriol. , vol.191 , pp. 4035-4040
    • Jackson-Rosario, S.1    Self, W.T.2
  • 34
    • 0346435112 scopus 로고    scopus 로고
    • Esp-independent biofilm formation by Enterococcus faecalis
    • Kristich, C. J., Y. H. Li, D. G. Cvitkovitch, and G. M. Dunny. 2004. Esp-independent biofilm formation by Enterococcus faecalis. J. Bacteriol. 186: 154-163.
    • (2004) J. Bacteriol. , vol.186 , pp. 154-163
    • Kristich, C.J.1    Li, Y.H.2    Cvitkovitch, D.G.3    Dunny, G.M.4
  • 35
    • 0023958637 scopus 로고
    • Escherichia coli genes whose products are involved in selenium metabolism
    • Leinfelder, W., et al. 1988. Escherichia coli genes whose products are involved in selenium metabolism. J. Bacteriol. 170:540-546.
    • (1988) J. Bacteriol. , vol.170 , pp. 540-546
    • Leinfelder, W.1
  • 36
    • 0030824355 scopus 로고    scopus 로고
    • Milk xanthine oxidoreductase: The first one hundred years
    • Massey, V., and C. M. Harris. 1997. Milk xanthine oxidoreductase: the first one hundred years. Biochem. Soc. Trans. 25:750-755.
    • (1997) Biochem. Soc. Trans. , vol.25 , pp. 750-755
    • Massey, V.1    Harris, C.M.2
  • 37
    • 77951215521 scopus 로고    scopus 로고
    • Reaction mechanism and molecular basis for selenium/ sulfur discrimination of selenocysteine lyase
    • Omi, R., et al. 2010. Reaction mechanism and molecular basis for selenium/ sulfur discrimination of selenocysteine lyase. J. Biol. Chem. 285:12133-12139.
    • (2010) J. Biol. Chem. , vol.285 , pp. 12133-12139
    • Omi, R.1
  • 38
    • 0001033907 scopus 로고
    • Nicotinic acid metabolism. I. Distribution of isotope in fermentation products of labelled nicotinic acid
    • Pastan, I., L. Tsai, and E. R. Stadtman. 1964. Nicotinic acid metabolism. I. Distribution of isotope in fermentation products of labelled nicotinic acid. J. Biol. Chem. 239:902-906.
    • (1964) J. Biol. Chem. , vol.239 , pp. 902-906
    • Pastan, I.1    Tsai, L.2    Stadtman, E.R.3
  • 39
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • Pfaffl, M. W. 2001. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29:e45.
    • (2001) Nucleic Acids Res. , vol.29
    • Pfaffl, M.W.1
  • 40
    • 4344677013 scopus 로고    scopus 로고
    • Effects of glucose on fsr-mediated biofilm formation in Enterococcus faecalis
    • Pillai, S. K., et al. 2004. Effects of glucose on fsr-mediated biofilm formation in Enterococcus faecalis. J. Infect. Dis. 190:967-970.
    • (2004) J. Infect. Dis. , vol.190 , pp. 967-970
    • Pillai, S.K.1
  • 41
    • 0141705801 scopus 로고
    • Purine fermentation by Clostridium cylindrosporum. II. Purine transformations
    • Rabinowitz, J. C., and H. A. Barker. 1956. Purine fermentation by Clostridium cylindrosporum. II. Purine transformations. J. Biol. Chem. 218:161-173.
    • (1956) J. Biol. Chem. , vol.218 , pp. 161-173
    • Rabinowitz, J.C.1    Barker, H.A.2
  • 42
    • 0026356524 scopus 로고
    • Expression and operon structure of the sel genes of Escherichia coli and identification of a third selenium-containing formate dehydrogenase isoenzyme
    • Sawers, G., J. Heider, E. Zehelein, and A. Bock. 1991. Expression and operon structure of the sel genes of Escherichia coli and identification of a third selenium-containing formate dehydrogenase isoenzyme. J. Bacteriol. 173:4983-4993.
    • (1991) J. Bacteriol. , vol.173 , pp. 4983-4993
    • Sawers, G.1    Heider, J.2    Zehelein, E.3    Bock, A.4
  • 43
    • 0033568431 scopus 로고    scopus 로고
    • Selenium-containing xanthine dehydrogenase from Eubacterium barkeri
    • Schrader, T., A. Rienhofer, and J. R. Andreesen. 1999. Selenium-containing xanthine dehydrogenase from Eubacterium barkeri. Eur. J. Biochem. 264:862-871.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 862-871
    • Schrader, T.1    Rienhofer, A.2    Andreesen, J.R.3
  • 44
    • 0036228518 scopus 로고    scopus 로고
    • A molybdenum-containing dehydrogenase catalyzing an unusual 2-hydroxylation of nicotinic acid
    • Schrader, T., B. Thiemer, and J. R. Andreesen. 2002. A molybdenum-containing dehydrogenase catalyzing an unusual 2-hydroxylation of nicotinic acid. Appl. Microbiol. Biotechnol. 58:612-617.
    • (2002) Appl. Microbiol. Biotechnol. , vol.58 , pp. 612-617
    • Schrader, T.1    Thiemer, B.2    Andreesen, J.R.3
  • 45
    • 0036209596 scopus 로고    scopus 로고
    • Regulation of purine hydroxylase and xanthine dehydrogenase from Clostridium purinolyticum in response to purines, selenium, and molybdenum
    • DOI 10.1128/JB.184.7.2039-2044.2002
    • Self, W. T. 2002. Regulation of purine hydroxylase and xanthine dehydrogenase from Clostridium purinolyticum in response to purines, selenium, and molybdenum. J. Bacteriol. 184:2039-2044. (Pubitemid 34275549)
    • (2002) Journal of Bacteriology , vol.184 , Issue.7 , pp. 2039-2044
    • Self, W.T.1
  • 46
    • 0032949461 scopus 로고    scopus 로고
    • Transcriptional regulation of molybdoenzyme synthesis in Escherichia coli in response to molybdenum: ModE-molybdate, a repressor of the modABCD (molybdate transport) operon is a secondary transcriptional activator for the hyc and nar operons
    • Self, W. T., A. M. Grunden, A. Hasona, and K. T. Shanmugam. 1999. Transcriptional regulation of molybdoenzyme synthesis in Escherichia coli in response to molybdenum: ModE-molybdate, a repressor of the modABCD (molybdate transport) operon is a secondary transcriptional activator for the hyc and nar operons. Microbiology 145:41-55.
    • (1999) Microbiology , vol.145 , pp. 41-55
    • Self, W.T.1    Grunden, A.M.2    Hasona, A.3    Shanmugam, K.T.4
  • 47
    • 0035168344 scopus 로고    scopus 로고
    • N-terminal truncations in the FhlA protein result in formate- and MoeA-independent expression of the hyc (formate hydrogenlyase) operon of Escherichia coli
    • Self, W. T., A. Hasona, and K. T. Shanmugam. 2001. N-terminal truncations in the FhlA protein result in formate- and MoeA-independent expression of the hyc (formate hydrogenlyase) operon of Escherichia coli. Microbiology 147:3093-3104.
    • (2001) Microbiology , vol.147 , pp. 3093-3104
    • Self, W.T.1    Hasona, A.2    Shanmugam, K.T.3
  • 48
    • 0033969363 scopus 로고    scopus 로고
    • Isolation and characterization of mutated FhlA proteins which activate transcription of the hyc operon (formate hydrogenlyase) of Escherichia coli in the absence of molybdate(1)
    • Self, W. T., and K. T. Shanmugam. 2000. Isolation and characterization of mutated FhlA proteins which activate transcription of the hyc operon (formate hydrogenlyase) of Escherichia coli in the absence of molybdate(1). FEMS Microbiol. Lett. 184:47-52.
    • (2000) FEMS Microbiol. Lett. , vol.184 , pp. 47-52
    • Self, W.T.1    Shanmugam, K.T.2
  • 49
    • 0034691160 scopus 로고    scopus 로고
    • Selenium-dependent metabolism of purines: A selenium-dependent purine hydroxylase and xanthine dehydrogenase were purified from Clostridium purinolyticum and characterized
    • Self, W. T., and T. C. Stadtman. 2000. Selenium-dependent metabolism of purines: a selenium-dependent purine hydroxylase and xanthine dehydrogenase were purified from Clostridium purinolyticum and characterized. Proc. Natl. Acad. Sci. U. S. A. 97:7208-7213.
    • (2000) Proc. Natl. Acad. Sci. U. S. A. , vol.97 , pp. 7208-7213
    • Self, W.T.1    Stadtman, T.C.2
  • 50
    • 0141567102 scopus 로고    scopus 로고
    • Cofactor determination and spectroscopic characterization of the selenium-dependent purine hydroxylase from Clostridium purinolyticum
    • Self, W. T., M. D. Wolfe, and T. C. Stadtman. 2003. Cofactor determination and spectroscopic characterization of the selenium-dependent purine hydroxylase from Clostridium purinolyticum. Biochemistry 42: 11382-11390.
    • (2003) Biochemistry , vol.42 , pp. 11382-11390
    • Self, W.T.1    Wolfe, M.D.2    Stadtman, T.C.3
  • 51
    • 0018848050 scopus 로고
    • Selenium-dependent enzymes
    • Stadtman, T. C. 1980. Selenium-dependent enzymes. Annu. Rev. Biochem. 49:93-110.
    • (1980) Annu. Rev. Biochem. , vol.49 , pp. 93-110
    • Stadtman, T.C.1
  • 52
    • 0034046615 scopus 로고    scopus 로고
    • Selenium biochemistry. Mammalian selenoenzymes
    • Stadtman, T. C. 2000. Selenium biochemistry. Mammalian selenoenzymes. Ann. N. Y. Acad. Sci. 899:399-402.
    • (2000) Ann. N. Y. Acad. Sci. , vol.899 , pp. 399-402
    • Stadtman, T.C.1
  • 54
    • 4644372071 scopus 로고    scopus 로고
    • Enterococcal surface protein, Esp, enhances biofilm formation by Enterococcus faecalis
    • Tendolkar, P. M., A. S. Baghdayan, M. S. Gilmore, and N. Shankar. 2004. Enterococcal surface protein, Esp, enhances biofilm formation by Enterococcus faecalis. Infect. Immun. 72:6032-6039.
    • (2004) Infect. Immun. , vol.72 , pp. 6032-6039
    • Tendolkar, P.M.1    Baghdayan, A.S.2    Gilmore, M.S.3    Shankar, N.4
  • 55
    • 65549148589 scopus 로고    scopus 로고
    • A fratricidal mechanism is responsible for eDNA release and contributes to biofilm development of Enterococcus faecalis
    • Thomas, V. C., et al. 2009. A fratricidal mechanism is responsible for eDNA release and contributes to biofilm development of Enterococcus faecalis. Mol. Microbiol. 72:1022-1036.
    • (2009) Mol. Microbiol. , vol.72 , pp. 1022-1036
    • Thomas, V.C.1
  • 56
    • 70350434311 scopus 로고    scopus 로고
    • Capsular polysaccharide production in Enterococcus faecalis and contribution of CpsF to capsule serospecificity
    • Thurlow, L. R., V. C. Thomas, and L. E. Hancock. 2009. Capsular polysaccharide production in Enterococcus faecalis and contribution of CpsF to capsule serospecificity. J. Bacteriol. 191:6203-6210.
    • (2009) J. Bacteriol. , vol.191 , pp. 6203-6210
    • Thurlow, L.R.1    Thomas, V.C.2    Hancock, L.E.3
  • 57
    • 0014027343 scopus 로고
    • Nicotinic acid metabolism. II. The isolation and characterization of intermediates in the fermentation of nicotinic acid
    • Tsai, L., I. Pastan, and E. R. Stadtman. 1966. Nicotinic acid metabolism. II. The isolation and characterization of intermediates in the fermentation of nicotinic acid. J. Biol. Chem. 241:1807-1813.
    • (1966) J. Biol. Chem. , vol.241 , pp. 1807-1813
    • Tsai, L.1    Pastan, I.2    Stadtman, E.R.3
  • 58
    • 0028932348 scopus 로고
    • Purification and characterization of threonine dehydrogenase from Clostridium sticklandii
    • Wagner, M., and J. R. Andreesen. 1995. Purification and characterization of threonine dehydrogenase from Clostridium sticklandii. Arch. Microbiol. 163:286-290.
    • (1995) Arch. Microbiol. , vol.163 , pp. 286-290
    • Wagner, M.1    Andreesen, J.R.2
  • 59
    • 0018366881 scopus 로고
    • Selenium requirement for active xanthine dehydrogenase from Clostridium acidiurici and Clostridium cylindrosporum
    • Wagner, R., and J. R. Andreesen. 1979. Selenium requirement for active xanthine dehydrogenase from Clostridium acidiurici and Clostridium cylindrosporum. Arch. Microbiol. 121:255-260.
    • (1979) Arch. Microbiol. , vol.121 , pp. 255-260
    • Wagner, R.1    Andreesen, J.R.2
  • 60
    • 57149115147 scopus 로고    scopus 로고
    • Enterococcus faecalis induces aneuploidy and tetraploidy in colonic epithelial cells through a bystander effect
    • Wang, X., et al. 2008. Enterococcus faecalis induces aneuploidy and tetraploidy in colonic epithelial cells through a bystander effect. Cancer Res. 68:9909-9917.
    • (2008) Cancer Res. , vol.68 , pp. 9909-9917
    • Wang, X.1
  • 61
    • 33847037554 scopus 로고    scopus 로고
    • Extracellular superoxide production by Enterococcus faecalis promotes chromosomal instability in mammalian cells
    • Wang, X., and M. M. Huycke. 2007. Extracellular superoxide production by Enterococcus faecalis promotes chromosomal instability in mammalian cells. Gastroenterology 132:551-561.
    • (2007) Gastroenterology , vol.132 , pp. 551-561
    • Wang, X.1    Huycke, M.M.2
  • 62
    • 57149137473 scopus 로고    scopus 로고
    • Antimicrobial susceptibility of monoculture biofilms of a clinical isolate of Enterococcus faecalis
    • Williamson, A. E., J. W. Cardon, and D. R. Drake. 2009. Antimicrobial susceptibility of monoculture biofilms of a clinical isolate of Enterococcus faecalis. J. Endod. 35:95-97.
    • (2009) J. Endod. , vol.35 , pp. 95-97
    • Williamson, A.E.1    Cardon, J.W.2    Drake, D.R.3
  • 63
    • 0345826117 scopus 로고    scopus 로고
    • Functional diversity of the rhodanese homology domain: The Escherichia coli ybbB gene encodes a selenophosphate-dependent tRNA 2-selenouridine synthase
    • Wolfe, M. D., et al. 2004. Functional diversity of the rhodanese homology domain: the Escherichia coli ybbB gene encodes a selenophosphate-dependent tRNA 2-selenouridine synthase. J. Biol. Chem. 279:1801-1809.
    • (2004) J. Biol. Chem. , vol.279 , pp. 1801-1809
    • Wolfe, M.D.1
  • 64
    • 46049083961 scopus 로고    scopus 로고
    • In silico identification of genes involved in selenium metabolism: Evidence for a third selenium utilization trait
    • Zhang, Y., A. A. Turanov, D. L. Hatfield, and V. N. Gladyshev. 2008. In silico identification of genes involved in selenium metabolism: evidence for a third selenium utilization trait. BMC Genomics 9:251.
    • (2008) BMC Genomics , vol.9 , pp. 251
    • Zhang, Y.1    Turanov, A.A.2    Hatfield, D.L.3    Gladyshev, V.N.4


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.