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Volumn 45, Issue 36, 2006, Pages 10815-10827

Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly

Author keywords

[No Author keywords available]

Indexed keywords

DNA; GENETIC ENGINEERING; MOLECULAR STRUCTURE; OLIGOMERS; PROTEINS;

EID: 33748478583     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi060782u     Document Type: Article
Times cited : (55)

References (63)
  • 2
    • 0344412956 scopus 로고    scopus 로고
    • Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center
    • Baaghil, S., Lewin, A., Moore, G. R., and Le Brun, N. E. (2003) Core formation in Escherichia coli bacterioferritin requires a functional ferroxidase center, Biochemistry 42, 14047-14056.
    • (2003) Biochemistry , vol.42 , pp. 14047-14056
    • Baaghil, S.1    Lewin, A.2    Moore, G.R.3    Le Brun, N.E.4
  • 3
    • 10244243805 scopus 로고    scopus 로고
    • DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus
    • Ceci, P., Cellai, S., Falvo, E., Rivetti, C., Rossi, G. L., and Chiancone, E. (2004) DNA condensation and self-aggregation of Escherichia coli Dps are coupled phenomena related to the properties of the N-terminus, Nucleic Acids Res. 32, 5935-5944.
    • (2004) Nucleic Acids Res. , vol.32 , pp. 5935-5944
    • Ceci, P.1    Cellai, S.2    Falvo, E.3    Rivetti, C.4    Rossi, G.L.5    Chiancone, E.6
  • 4
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells: A ferritin-like DNA-binding protein of Escherichia coli
    • Zhao, G. H., Ceci, P., Ilari, A., Giangiacomo, L., Laue, T. M., Chiancone, E., and Chasteen, N. D. (2002) Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells: A ferritin-like DNA-binding protein of Escherichia coli, J. Biol. Chem. 277, 27689-27696.
    • (2002) J. Biol. Chem. , vol.277 , pp. 27689-27696
    • Zhao, G.H.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7
  • 5
    • 17144367329 scopus 로고    scopus 로고
    • The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification but not for iron uptake. A study with site-specific mutants
    • Ilari, A., Latella, M. C., Ceci, P., Ribacchi, F., Su, M., Giangiacomo, L., Stefanini, S., Chasteen, N. D., and Chiancone, E. (2005) The unusual intersubunit ferroxidase center of Listeria innocua Dps is required for hydrogen peroxide detoxification but not for iron uptake. A study with site-specific mutants, Biochemistry 44, 5579-5587.
    • (2005) Biochemistry , vol.44 , pp. 5579-5587
    • Ilari, A.1    Latella, M.C.2    Ceci, P.3    Ribacchi, F.4    Su, M.5    Giangiacomo, L.6    Stefanini, S.7    Chasteen, N.D.8    Chiancone, E.9
  • 6
    • 0037020091 scopus 로고    scopus 로고
    • Iron detoxification properties of Escherichia coli bacterioferritin. Attenuation of oxyradical chemistry
    • Bou-Abdallah, F., Lewin, A. C., Le Brun, N. E., Moore, G. R., and Chasteen, N. D. (2002) Iron detoxification properties of Escherichia coli bacterioferritin. Attenuation of oxyradical chemistry, J. Biol. Chem. 277, 37064-37069.
    • (2002) J. Biol. Chem. , vol.277 , pp. 37064-37069
    • Bou-Abdallah, F.1    Lewin, A.C.2    Le Brun, N.E.3    Moore, G.R.4    Chasteen, N.D.5
  • 7
    • 0031959912 scopus 로고    scopus 로고
    • The crystal structure of Dps, a ferritin homolog that binds and protects DNA
    • Grant, R. A., Filman, D. J., Finkel, S. E., Kolter, R., and Hogle, J. M. (1998) The crystal structure of Dps, a ferritin homolog that binds and protects DNA, Nat. Struct. Biol. 5, 294-303.
    • (1998) Nat. Struct. Biol. , vol.5 , pp. 294-303
    • Grant, R.A.1    Filman, D.J.2    Finkel, S.E.3    Kolter, R.4    Hogle, J.M.5
  • 10
    • 4644286770 scopus 로고    scopus 로고
    • Iron-oxo clusters biomineralizing on protein surfaces: Structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states
    • Zeth, K., Offermann, S., Essen, L. O., and Oesterhelt, D. (2004) Iron-oxo clusters biomineralizing on protein surfaces: Structural analysis of Halobacterium salinarum DpsA in its low- and high-iron states, Proc. Natl Acad. Sci. U.S.A. 101, 13780-13785.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13780-13785
    • Zeth, K.1    Offermann, S.2    Essen, L.O.3    Oesterhelt, D.4
  • 11
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • Ilari, A., Stefanini, S., Chiancone, E., and Tsernoglou, D. (2000) The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site, Nat. Struct. Biol. 7, 38-43.
    • (2000) Nat. Struct. Biol. , vol.7 , pp. 38-43
    • Ilari, A.1    Stefanini, S.2    Chiancone, E.3    Tsernoglou, D.4
  • 16
    • 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
  • 17
    • 3042934967 scopus 로고
    • Tissue sulfhydryl groups
    • Ellman, G. L. (1959) Tissue sulfhydryl groups, Arch. Biochem. Biophys. 82, 70-77.
    • (1959) Arch. Biochem. Biophys. , vol.82 , pp. 70-77
    • Ellman, G.L.1
  • 18
    • 0031059866 scopus 로고    scopus 로고
    • Processing of X-ray diffraction data collected in oscillation mode
    • (Carter, C., and Sweet, R., Eds.), Academic Press, New York
    • Otwinowski, Z., and Minor, W. (1997) Processing of X-ray diffraction data collected in oscillation mode, in Macromolecular Crystallography, Part A (Carter, C., and Sweet, R., Eds.) pp 307-326, Academic Press, New York.
    • (1997) Macromolecular Crystallography, Part A , pp. 307-326
    • Otwinowski, Z.1    Minor, W.2
  • 20
    • 0037237545 scopus 로고    scopus 로고
    • Automated main-chain model building by template matching and iterative fragment extension
    • Terwilliger, T. C. (2003) Automated main-chain model building by template matching and iterative fragment extension, Acta Crystallogr, Sect D 59, 38-44.
    • (2003) Acta Crystallogr., Sect D , vol.59 , pp. 38-44
    • Terwilliger, T.C.1
  • 21
    • 0028103275 scopus 로고
    • The CCP4 suite: Programs for protein crystallography
    • CCP4. (1994) The CCP4 suite: programs for protein crystallography, Acta Crystallogr., Sect D 50, 760-763.
    • (1994) Acta Crystallogr., Sect D , vol.50 , pp. 760-763
  • 22
    • 84889120137 scopus 로고
    • Improved methods for building protein models in electron density maps and the location of errors in these models
    • Jones, T. A., Zou, J. Y., Cowan, S. W., and Kjeldgaard, M. (1991) Improved methods for building protein models in electron density maps and the location of errors in these models, Acta Crystallogr., Sect A 47, 110-119.
    • (1991) Acta Crystallogr., Sect A , vol.47 , pp. 110-119
    • Jones, T.A.1    Zou, J.Y.2    Cowan, S.W.3    Kjeldgaard, M.4
  • 23
    • 0030924992 scopus 로고    scopus 로고
    • Refinement of macromolecular structures by the maximum-likelihood method
    • Murshudov, G. N., Vagin, A. A., and Dodson, E. J. (1997) Refinement of macromolecular structures by the maximum-likelihood method, Acta Crystallogr., Sect D 53, 240-255.
    • (1997) Acta Crystallogr., Sect D , vol.53 , pp. 240-255
    • Murshudov, G.N.1    Vagin, A.A.2    Dodson, E.J.3
  • 24
    • 0035182073 scopus 로고    scopus 로고
    • Use of TLS parameters to model anisotropic displacements in macromolecular refinement
    • Winn, M. D., Isupov, M. N., and Murshudov, G. N. (2001) Use of TLS parameters to model anisotropic displacements in macromolecular refinement, Acta Crystallogr., Sect D 57, 122-33.
    • (2001) Acta Crystallogr., Sect D , vol.57 , pp. 122-133
    • Winn, M.D.1    Isupov, M.N.2    Murshudov, G.N.3
  • 25
    • 0000243829 scopus 로고
    • PROCHECK: A program to check the stereochemical quality of protein structures
    • Laskowski, R. A., MacArthur, M. W., Moss, D. S., and Thornton, J. M. (1993) PROCHECK: a program to check the stereochemical quality of protein structures, J. Appl. Crystallogr. 26, 283-291.
    • (1993) J. Appl. Crystallogr. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.S.3    Thornton, J.M.4
  • 26
    • 0027440362 scopus 로고
    • Protein structure comparison by alignment of distance matrices
    • Holm, L., and Sander, C. (1993) Protein structure comparison by alignment of distance matrices, J. Mol. Biol. 233, 123-138.
    • (1993) J. Mol. Biol. , vol.233 , pp. 123-138
    • Holm, L.1    Sander, C.2
  • 27
    • 33748491129 scopus 로고    scopus 로고
    • DeLano, W. L. (2002), DeLano Scientific
    • DeLano, W. L. (2002), DeLano Scientific.
  • 28
    • 33748506735 scopus 로고    scopus 로고
    • Christopher, J. A. (1998)
    • Christopher, J. A. (1998).
  • 31
    • 0031029483 scopus 로고    scopus 로고
    • Dinuclear center of ferritin: Studies of iron binding and oxidation show differences in the two iron sites
    • Treffry, A., Zhao, Z. W., Quail, M. A., Guest, J. R., and Harrison, P. M. (1997) Dinuclear center of ferritin: Studies of iron binding and oxidation show differences in the two iron sites, Biochemistry 36, 432-441.
    • (1997) Biochemistry , vol.36 , pp. 432-441
    • Treffry, A.1    Zhao, Z.W.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5
  • 33
    • 0028467772 scopus 로고
    • Structure of a unique 2-fold symmetric haem-binding site
    • Frolow, F., Kalb, A. J., and Yariv, J. (1994) Structure of a unique 2-fold symmetric haem-binding site, Nat. Struct. Biol. 1, 453-460.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 453-460
    • Frolow, F.1    Kalb, A.J.2    Yariv, J.3
  • 34
    • 33645690696 scopus 로고    scopus 로고
    • Redox-dependent structural changes in the Azotobacter vinelandii bacterioferritin: New insights into the ferroxidase and iron transport mechanism
    • Swartz, L., Kuchinskas, M., Li, H., Poulos, T. L., and Lanzilotta, W. N. (2006) Redox-dependent structural changes in the Azotobacter vinelandii bacterioferritin: new insights into the ferroxidase and iron transport mechanism, Biochemistry 45, 4421-4428.
    • (2006) Biochemistry , vol.45 , pp. 4421-4428
    • Swartz, L.1    Kuchinskas, M.2    Li, H.3    Poulos, T.L.4    Lanzilotta, W.N.5
  • 36
    • 0038219647 scopus 로고    scopus 로고
    • Ferritins, iron uptake and storage from the bacterioferritin viewpoint
    • Carrondo, M. A. (2003) Ferritins, iron uptake and storage from the bacterioferritin viewpoint, EMBO J. 22, 1959-1968.
    • (2003) EMBO J. , vol.22 , pp. 1959-1968
    • Carrondo, M.A.1
  • 37
    • 24344492710 scopus 로고    scopus 로고
    • Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF
    • Roberts, B. R., Wood, Z. A., Jonsson, T. J., Poole, L. B., and Karplus, P. A. (2005) Oxidized and synchrotron cleaved structures of the disulfide redox center in the N-terminal domain of Salmonella typhimurium AhpF, Protein Sci. 14, 2414-2420.
    • (2005) Protein Sci. , vol.14 , pp. 2414-2420
    • Roberts, B.R.1    Wood, Z.A.2    Jonsson, T.J.3    Poole, L.B.4    Karplus, P.A.5
  • 39
    • 0037162464 scopus 로고    scopus 로고
    • Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds
    • Mallick, P., Boutz, D. R., Eisenberg, D., and Yeates, T. O. (2002) Genomic evidence that the intracellular proteins of archaeal microbes contain disulfide bonds, Proc. Natl. Acad. Sci. U.S.A. 99, 9679-9684.
    • (2002) Proc. Natl. Acad. Sci. U.S.A. , vol.99 , pp. 9679-9684
    • Mallick, P.1    Boutz, D.R.2    Eisenberg, D.3    Yeates, T.O.4
  • 40
    • 3242886780 scopus 로고    scopus 로고
    • GDAP: A web tool for genome-wide protein disulfide bond prediction
    • O'Connor, B. D., and Yeates, T. O. (2004) GDAP: a web tool for genome-wide protein disulfide bond prediction, Nucleic Acids Res. 32, W360-W364.
    • (2004) Nucleic Acids Res. , vol.32
    • O'Connor, B.D.1    Yeates, T.O.2
  • 41
    • 0031808808 scopus 로고    scopus 로고
    • Calculated electrostatic gradients in recombinant human H-chain ferritin
    • Douglas, T., and Ripoll, D. R. (1998) Calculated electrostatic gradients in recombinant human H-chain ferritin. Protein Sci. 7, 1083-1091.
    • (1998) Protein Sci. , vol.7 , pp. 1083-1091
    • Douglas, T.1    Ripoll, D.R.2
  • 42
    • 0035954391 scopus 로고    scopus 로고
    • "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites
    • Jin, W., Takagi, H., Pancorbo, B., and Theil, E. C. (2001) "Opening" the ferritin pore for iron release by mutation of conserved amino acids at interhelix and loop sites, Biochemistry 40, 7525-7532.
    • (2001) Biochemistry , vol.40 , pp. 7525-7532
    • Jin, W.1    Takagi, H.2    Pancorbo, B.3    Theil, E.C.4
  • 43
    • 0020541188 scopus 로고
    • Ribonucleotide reductase- A radical enzyme
    • Reichard, P., and Ehrenberg, A. (1983) Ribonucleotide reductase- a radical enzyme, Science 221, 514-319.
    • (1983) Science , vol.221 , pp. 514-1319
    • Reichard, P.1    Ehrenberg, A.2
  • 44
    • 0027732697 scopus 로고
    • Defining the roles of the threefold channels in iron uptake, iron oxidation and iron-core formation in ferritin: A study aided by site-directed mutagenesis
    • Treffry, A., Bauminger, E. R., Hechel, D., Hodson, N. W., Nowik, I., Yewdall, S. J., and Harrison, P. M. (1993) Defining the roles of the threefold channels in iron uptake, iron oxidation and iron-core formation in ferritin: a study aided by site-directed mutagenesis, Biochem. J. 296, 721-728.
    • (1993) Biochem. J. , vol.296 , pp. 721-728
    • Treffry, A.1    Bauminger, E.R.2    Hechel, D.3    Hodson, N.W.4    Nowik, I.5    Yewdall, S.J.6    Harrison, P.M.7
  • 45
    • 0028825383 scopus 로고
    • Iron(II) oxidation by H chain ferritin: Evidence from site-directed mutagenesis that a transient blue species is formed at the dinuclear iron center
    • Treffry, A., Zhao, Z., Quail, M. A., Guest, J. R., and Harrison, P. M. (1995) Iron(II) oxidation by H chain ferritin: evidence from site-directed mutagenesis that a transient blue species is formed at the dinuclear iron center, Biochemistry 34, 15204-15213.
    • (1995) Biochemistry , vol.34 , pp. 15204-15213
    • Treffry, A.1    Zhao, Z.2    Quail, M.A.3    Guest, J.R.4    Harrison, P.M.5
  • 46
    • 0030781957 scopus 로고    scopus 로고
    • The influence of conserved tyrosine 30 and tissue-dependent differences in sequence of ferritin function: Use of blue and purple F(III) species as reporters of ferroxidation
    • Fetter, J., Cohen, J., Danger, D., Sanders-Loehr, J., and Theil, E. C. (1997) The influence of conserved tyrosine 30 and tissue-dependent differences in sequence of ferritin function: use of blue and purple F(III) species as reporters of ferroxidation, J. Biol. Inorg. Chem. 2, 652-661.
    • (1997) J. Biol. Inorg. Chem. , vol.2 , pp. 652-661
    • Fetter, J.1    Cohen, J.2    Danger, D.3    Sanders-Loehr, J.4    Theil, E.C.5
  • 47
    • 0034712683 scopus 로고    scopus 로고
    • The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin
    • Yang, X., Le Brun, N. E., Thomson, A. J., Moore, G. R., and Chasteen, N. D. (2000) The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin, Biochemistry 39, 4915-4923.
    • (2000) Biochemistry , vol.39 , pp. 4915-4923
    • Yang, X.1    Le Brun, N.E.2    Thomson, A.J.3    Moore, G.R.4    Chasteen, N.D.5
  • 48
    • 9744232974 scopus 로고    scopus 로고
    • Bacterial defenses against oxidants: Mechanistic features of cysteine-based peroxidases and their flavoprotein reductases
    • Poole, L. B. (2005) Bacterial defenses against oxidants: mechanistic features of cysteine-based peroxidases and their flavoprotein reductases, Arch. Biochem. Biophys. 433, 240-254.
    • (2005) Arch. Biochem. Biophys. , vol.433 , pp. 240-254
    • Poole, L.B.1
  • 50
    • 0031582202 scopus 로고    scopus 로고
    • Scavengase p20: A novel family of bacterial antioxidant enzymes
    • Wan, X. Y., Zhou, Y., Yan, Z. Y., Wang, H. L., Hou, Y. D., and Jin, D. Y. (1997) Scavengase p20: a novel family of bacterial antioxidant enzymes, FEBS Lett. 407, 32-36.
    • (1997) FEBS Lett. , vol.407 , pp. 32-36
    • Wan, X.Y.1    Zhou, Y.2    Yan, Z.Y.3    Wang, H.L.4    Hou, Y.D.5    Jin, D.Y.6
  • 51
    • 0031589201 scopus 로고    scopus 로고
    • Bacterial scavengase p20 is structurally and functionally related to peroxiredoxins
    • Zhou, Y., Wan, X. Y., Wang, H. L., Yan, Z. Y., Hou, Y. D., and Jin, D. Y. (1997) Bacterial scavengase p20 is structurally and functionally related to peroxiredoxins, Biochem. Biophys. Res. Commun. 233, 848-852.
    • (1997) Biochem. Biophys. Res. Commun. , vol.233 , pp. 848-852
    • Zhou, Y.1    Wan, X.Y.2    Wang, H.L.3    Yan, Z.Y.4    Hou, Y.D.5    Jin, D.Y.6
  • 52
    • 0034723165 scopus 로고    scopus 로고
    • Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family
    • Jeong, W., Cha, M. K., and Kim, I. H. (2000) Thioredoxin-dependent hydroperoxide peroxidase activity of bacterioferritin comigratory protein (BCP) as a new member of the thiol-specific antioxidant protein (TSA)/Alkyl hydroperoxide peroxidase C (AhpC) family, J. Biol. Chem. 275, 2924-2930.
    • (2000) J. Biol. Chem. , vol.275 , pp. 2924-2930
    • Jeong, W.1    Cha, M.K.2    Kim, I.H.3
  • 53
    • 0016045364 scopus 로고
    • Differentiation and medical importance of saccharolytic intestinal anaerobes
    • Werner, H. (1974) Differentiation and medical importance of saccharolytic intestinal anaerobes, Arzneim.-Forsch. 24, 340-343.
    • (1974) Arzneim.-Forsch. , vol.24 , pp. 340-343
    • Werner, H.1
  • 55
    • 0002463721 scopus 로고    scopus 로고
    • Oxidative Stress
    • (Storz, G., and Hengge-Aronis, R., Eds.), ASM Press, Washington, D.C.
    • Storz, G., and Zheng, M. (2000) Oxidative Stress, in Bacterial Stress Responses (Storz, G., and Hengge-Aronis, R., Eds.) pp 47-60, ASM Press, Washington, D.C.
    • (2000) Bacterial Stress Responses , pp. 47-60
    • Storz, G.1    Zheng, M.2
  • 56
    • 0030613766 scopus 로고    scopus 로고
    • Regulation of Bacteriodes fragilis katB mRNA by oxidative stress and carbon limitation
    • Rocha, E. R., and Smith, C. J. (1997) Regulation of Bacteriodes fragilis katB mRNA by oxidative stress and carbon limitation, J. Bacteriol. 179, 7033-7039.
    • (1997) J. Bacteriol. , vol.179 , pp. 7033-7039
    • Rocha, E.R.1    Smith, C.J.2
  • 57
    • 0029019571 scopus 로고
    • Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis
    • Rocha, E. R., and Smith, C. J. (1995) Biochemical and genetic analyses of a catalase from the anaerobic bacterium Bacteroides fragilis, J. Bacteriol. 177, 3111-3119.
    • (1995) J. Bacteriol. , vol.177 , pp. 3111-3119
    • Rocha, E.R.1    Smith, C.J.2
  • 58
    • 0029848194 scopus 로고    scopus 로고
    • Oxidative stress response in an anaerobe, Bacteroides fragilis: A role for catalase in protection against hydrogen peroxide
    • Rocha, E. R., Selby, T., Coleman, J. P., and Smith, C. J. (1996) Oxidative stress response in an anaerobe, Bacteroides fragilis: a role for catalase in protection against hydrogen peroxide, J. Bacteriol. 178, 6895-6903.
    • (1996) J. Bacteriol. , vol.178 , pp. 6895-6903
    • Rocha, E.R.1    Selby, T.2    Coleman, J.P.3    Smith, C.J.4
  • 59
    • 0033816764 scopus 로고    scopus 로고
    • The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe Bacteroides fragilis
    • Rocha, E. R., Owens, G., Jr., and Smith, C. J. (2000) The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe Bacteroides fragilis, J. Bacteriol. 182, 5059-5069.
    • (2000) J. Bacteriol. , vol.182 , pp. 5059-5069
    • Rocha, E.R.1    Owens Jr., G.2    Smith, C.J.3
  • 60
    • 0141887670 scopus 로고    scopus 로고
    • Genetic analysis of an important oxidative stress locus in the anaerobe Bacteroides fragilis
    • Herren, C. D., Rocha, E. R., and Smith, C. J. (2003) Genetic analysis of an important oxidative stress locus in the anaerobe Bacteroides fragilis, Gene 316, 167-175.
    • (2003) Gene , vol.316 , pp. 167-175
    • Herren, C.D.1    Rocha, E.R.2    Smith, C.J.3
  • 61
    • 4344664059 scopus 로고    scopus 로고
    • Transcriptional regulation of the Bacteroides fragilis ferritin gene (ftnA) by redox stress
    • Rocha, E. R., and Smith, C. J. (2004) Transcriptional regulation of the Bacteroides fragilis ferritin gene (ftnA) by redox stress, Microbiology 150, 2125-2134.
    • (2004) Microbiology , vol.150 , pp. 2125-2134
    • Rocha, E.R.1    Smith, C.J.2


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