메뉴 건너뛰기




Volumn 67, Issue 3, 2010, Pages 341-351

Dps-like proteins: Structural and functional insights into a versatile protein family

Author keywords

Fenton reaction; Ferroxidase; Iron binding; Metal binding; Mini ferritins; Oxidative stress; Zinc

Indexed keywords

CERULOPLASMIN; DPS PROTEIN; IRON; ZINC;

EID: 75849150278     PISSN: 1420682X     EISSN: 14209071     Source Type: Journal    
DOI: 10.1007/s00018-009-0168-2     Document Type: Review
Times cited : (117)

References (78)
  • 1
    • 0020073664 scopus 로고
    • Free manganese (II) and iron (II) cations can act as intracellular cell controls
    • Williams RJ (1982) Free manganese (II) and iron (II) cations can act as intracellular cell controls. FEBS Lett 140:3-10
    • (1982) FEBS Lett , vol.140 , pp. 3-10
    • Williams, R.J.1
  • 3
    • 50649117912 scopus 로고    scopus 로고
    • Cellular defences against superoxide and hydrogen peroxide
    • Imlay JA (2008) Cellular defences against superoxide and hydrogen peroxide. Annu Rev Biochem 77:755-776
    • (2008) Annu Rev Biochem , vol.77 , pp. 755-776
    • Imlay, J.A.1
  • 4
    • 0027083350 scopus 로고
    • A novel DNAbinding protein with regulatory and protective roles in starved Escherichia coli
    • Almirón M, Link AJ, Furlong D, Kolter R (1992) A novel DNAbinding protein with regulatory and protective roles in starved Escherichia coli. Genes Dev 6:2646-2654
    • (1992) Genes Dev , vol.6 , pp. 2646-2654
    • Almirón, M.1    Link, A.J.2    Furlong, D.3    Kolter, R.4
  • 5
    • 0031032646 scopus 로고    scopus 로고
    • A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua
    • Bozzi M, Mignogna G, Stefanini S, Barra D, Longhi C, Valenti P, Chiancone E (1997) A novel non-heme iron-binding ferritin related to the DNA-binding proteins of the Dps family in Listeria innocua. J Biol Chem 272:3259-3265
    • (1997) J Biol Chem , vol.272 , pp. 3259-3265
    • Bozzi, M.1    Mignogna, G.2    Stefanini, S.3    Barra, D.4    Longhi, C.5    Valenti, P.6    Chiancone, E.7
  • 6
    • 0028861959 scopus 로고
    • Bacillus subtilis MrgA is a Dps(PexB) homologue: Evidence for metalloregulation of an oxidative-stress gene
    • Chen L, Helmann JD (1995) Bacillus subtilis MrgA is a Dps(PexB) homologue: evidence for metalloregulation of an oxidative-stress gene. Mol Microbiol 18:295-300
    • (1995) Mol Microbiol , vol.18 , pp. 295-300
    • Chen, L.1    Helmann, J.D.2
  • 7
    • 0038813712 scopus 로고    scopus 로고
    • Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells
    • Gupta S, Chatterji D (2003) Bimodal protection of DNA by Mycobacterium smegmatis DNA-binding protein from stationary phase cells. J Biol Chem 278:5235-5241
    • (2003) J Biol Chem , vol.278 , pp. 5235-5241
    • Gupta, S.1    Chatterji, D.2
  • 8
    • 0842326209 scopus 로고    scopus 로고
    • The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence
    • Halsey TA, Vazquez-Torres A, Gravdahl DJ, Fang FC, Libby SJ (2004) The ferritin-like Dps protein is required for Salmonella enterica serovar Typhimurium oxidative stress resistance and virulence. Infect Immun 72:1155-1158
    • (2004) Infect Immun , vol.72 , pp. 1155-1158
    • Halsey, T.A.1    Vazquez-Torres, A.2    Gravdahl, D.J.3    Fang, F.C.4    Libby, S.J.5
  • 11
    • 0036091613 scopus 로고    scopus 로고
    • An ironbinding protein, Dpr, from Streptococcus mutans prevents irondependent hydroxyl radical formation in vitro
    • Yamamoto Y, Poole LB, Hantgan RR, Kamio Y (2002) An ironbinding protein, Dpr, from Streptococcus mutans prevents irondependent hydroxyl radical formation in vitro. J Bacteriol 184:2931-2939
    • (2002) J Bacteriol , vol.184 , pp. 2931-2939
    • Yamamoto, Y.1    Poole, L.B.2    Hantgan, R.R.3    Kamio, Y.4
  • 12
  • 13
    • 0033986734 scopus 로고    scopus 로고
    • The dodecameric ferritin from Listeria innocua contains a novel intersubunit iron-binding site
    • Ilari A, Stefanini S, Chiancone E, 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
  • 14
    • 0038291700 scopus 로고    scopus 로고
    • The multi-layered structure of Dps with a novel di-nuclear ferroxidase center
    • Ren B, Tibbelin G, Kajino T, Asami O, Ladenstein R (2003) The multi-layered structure of Dps with a novel di-nuclear ferroxidase center. J Mol Biol 329:467-477
    • (2003) J Mol Biol , vol.329 , pp. 467-477
    • Ren, B.1    Tibbelin, G.2    Kajino, T.3    Asami, O.4    Ladenstein, R.5
  • 15
    • 33748372577 scopus 로고    scopus 로고
    • The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus
    • Romao CV, Mitchell EP, McSweeney S (2006) The crystal structure of Deinococcus radiodurans Dps protein (DR2263) reveals the presence of a novel metal centre in the N terminus. J Biol Inorg Chem 11:891-902
    • (2006) J Biol Inorg Chem , vol.11 , pp. 891-902
    • Romao, C.V.1    Mitchell, E.P.2    McSweeney, S.3
  • 16
    • 1842686188 scopus 로고    scopus 로고
    • Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: Implications for iron incorporation
    • Kauko A, Haataja S, Pulliainen AT, Finne J, Papageorgiou AC (2004) Crystal structure of Streptococcus suis Dps-like peroxide resistance protein Dpr: implications for iron incorporation. J Mol Biol 338:547-558
    • (2004) J Mol Biol , vol.338 , pp. 547-558
    • Kauko, A.1    Haataja, S.2    Pulliainen, A.T.3    Finne, J.4    Papageorgiou, A.C.5
  • 17
    • 33750040245 scopus 로고    scopus 로고
    • Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus
    • Franceschini S, Ceci P, Alaleona F, Chiancone E, Ilari A (2006) Antioxidant Dps protein from the thermophilic cyanobacterium Thermosynechococcus elongatus. FEBS J 273:4913-4928
    • (2006) FEBS J , vol.273 , pp. 4913-4928
    • Franceschini, S.1    Ceci, P.2    Alaleona, F.3    Chiancone, E.4    Ilari, A.5
  • 19
    • 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 LO, 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 USA 101:13780-13785
    • (2004) Proc Natl Acad Sci USA , vol.101 , pp. 13780-13785
    • Zeth, K.1    Offermann, S.2    Essen, L.O.3    Oesterhelt, D.4
  • 20
    • 33748478583 scopus 로고    scopus 로고
    • Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly
    • Gauss GH, Benas P, Wiedenheft B, Young M, Douglas T, Lawrence CM (2006) Structure of the DPS-like protein from Sulfolobus solfataricus reveals a bacterioferritin-like dimetal binding site within a DPS-like dodecameric assembly. Biochemistry 45:10815-10827
    • (2006) Biochemistry , vol.45 , pp. 10815-10827
    • Gauss, G.H.1    Benas, P.2    Wiedenheft, B.3    Young, M.4    Douglas, T.5    Lawrence, C.M.6
  • 22
    • 0032728896 scopus 로고    scopus 로고
    • Expression of a new cold shock protein of 21.5 kDa and of the major cold shock protein by Streptococcus thermophilus after cold shock
    • Perrin C, Guimont C, Bracquart P, Gaillard JL (1999) Expression of a new cold shock protein of 21.5 kDa and of the major cold shock protein by Streptococcus thermophilus after cold shock. Curr Microbiol 39:342-347
    • (1999) Curr Microbiol , vol.39 , pp. 342-347
    • Perrin, C.1    Guimont, C.2    Bracquart, P.3    Gaillard, J.L.4
  • 23
    • 0034284246 scopus 로고    scopus 로고
    • The main cold shock protein of Listeria monocytogenes belongs to the family of ferritin-like proteins
    • Hébraud M, Guzzo J (2000) The main cold shock protein of Listeria monocytogenes belongs to the family of ferritin-like proteins. FEMS Microbiol Lett 190:29-34
    • (2000) FEMS Microbiol Lett , vol.190 , pp. 29-34
    • Hébraud, M.1    Guzzo, J.2
  • 24
    • 0842269876 scopus 로고    scopus 로고
    • Identification of an iron-binding protein of the Dps family expressed by Streptococcus thermophilus
    • Nicodeme M, Perrin C, Hols P, Bracquart P, Gaillard JL (2004) Identification of an iron-binding protein of the Dps family expressed by Streptococcus thermophilus. Curr Microbiol 48:51-56
    • (2004) Curr Microbiol , vol.48 , pp. 51-56
    • Nicodeme, M.1    Perrin, C.2    Hols, P.3    Bracquart, P.4    Gaillard, J.L.5
  • 25
    • 0032716841 scopus 로고    scopus 로고
    • Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid
    • Ali Azam T, Iwata A, Nishimura A, Ueda S, Ishihama A (1999) Growth phase-dependent variation in protein composition of the Escherichia coli nucleoid. J Bacteriol 181:6361-6370
    • (1999) J Bacteriol , vol.181 , pp. 6361-6370
    • Ali Azam, T.1    Iwata, A.2    Nishimura, A.3    Ueda, S.4    Ishihama, A.5
  • 26
    • 0033816764 scopus 로고    scopus 로고
    • The redox-sensitive transcriptional activator OxyR regulates the peroxide response regulon in the obligate anaerobe Bacteroides fragilis
    • Rocha ER, Owens GJ, Smith CJ (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, G.J.2    Smith, C.J.3
  • 27
    • 0037371197 scopus 로고    scopus 로고
    • Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis
    • Ueshima J, Shoji M, Ratnayake DB, Abe K, Yoshida S, Yamamoto K, Nakayama K (2003) Purification, gene cloning, gene expression, and mutants of Dps from the obligate anaerobe Porphyromonas gingivalis. Infect Immun 71:1170-1178
    • (2003) Infect Immun , vol.71 , pp. 1170-1178
    • Ueshima, J.1    Shoji, M.2    Ratnayake, D.B.3    Abe, K.4    Yoshida, S.5    Yamamoto, K.6    Nakayama, K.7
  • 28
    • 0141566368 scopus 로고    scopus 로고
    • Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli
    • Stephani K, Weichart D, Hengge R (2003) Dynamic control of Dps protein levels by ClpXP and ClpAP proteases in Escherichia coli. Mol Microbiol 49:1605-1614
    • (2003) Mol Microbiol , vol.49 , pp. 1605-1614
    • Stephani, K.1    Weichart, D.2    Hengge, R.3
  • 29
    • 39849091042 scopus 로고    scopus 로고
    • Escherichia coli Dps interacts with DnaA protein to impede initiation: A model of adaptive mutation
    • Chodavarapu S, Gomez R, Vicente M, Kaguni JM (2008) Escherichia coli Dps interacts with DnaA protein to impede initiation: a model of adaptive mutation. Mol Microbiol 67:1331-1346
    • (2008) Mol Microbiol , vol.67 , pp. 1331-1346
    • Chodavarapu, S.1    Gomez, R.2    Vicente, M.3    Kaguni, J.M.4
  • 30
    • 0031850630 scopus 로고    scopus 로고
    • Bacillus subtilis contains multiple fur homologues: Identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors
    • Bsat N, Herbig A, Casillas-Martinez L, Setlow P, Helmann JD (1998) Bacillus subtilis contains multiple Fur homologues: identification of the iron uptake (Fur) and peroxide regulon (PerR) repressors. Mol Microbiol 29:189-198
    • (1998) Mol Microbiol , vol.29 , pp. 189-198
    • Bsat, N.1    Herbig, A.2    Casillas-Martinez, L.3    Setlow, P.4    Helmann, J.D.5
  • 31
    • 0035013928 scopus 로고    scopus 로고
    • PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus
    • Horsburgh MJ, Clements MO, Crossley H, Ingham E, Foster SJ (2001) PerR controls oxidative stress resistance and iron storage proteins and is required for virulence in Staphylococcus aureus. Infect Immun 69:3744-3754
    • (2001) Infect Immun , vol.69 , pp. 3744-3754
    • Horsburgh, M.J.1    Clements, M.O.2    Crossley, H.3    Ingham, E.4    Foster, S.J.5
  • 32
    • 12344298832 scopus 로고    scopus 로고
    • The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes
    • Brenot A, King KY, Caparon MG (2005) The PerR regulon in peroxide resistance and virulence of Streptococcus pyogenes. Mol Microbiol 55:221-234
    • (2005) Mol Microbiol , vol.55 , pp. 221-234
    • Brenot, A.1    King, K.Y.2    Caparon, M.G.3
  • 33
    • 0037309086 scopus 로고    scopus 로고
    • The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni
    • Ishikawa T, Mizunoe Y, Kawabata S, Takade A, Harada M, Wai SN, Yoshida S (2003) The iron-binding protein Dps confers hydrogen peroxide stress resistance to Campylobacter jejuni. J Bacteriol 185:1010-1017
    • (2003) J Bacteriol , vol.185 , pp. 1010-1017
    • Ishikawa, T.1    Mizunoe, Y.2    Kawabata, S.3    Takade, A.4    Harada, M.5    Wai, S.N.6    Yoshida, S.7
  • 34
    • 15844374760 scopus 로고    scopus 로고
    • The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells
    • Olsen KN, Larsen MH, Gahan CG, Kallipolitis B, Wolf XA, Rea R, Hill C, Ingmer H (2005) The Dps-like protein Fri of Listeria monocytogenes promotes stress tolerance and intracellular multiplication in macrophage-like cells. Microbiology 151:925-933
    • (2005) Microbiology , vol.151 , pp. 925-933
    • Olsen, K.N.1    Larsen, M.H.2    Gahan, C.G.3    Kallipolitis, B.4    Wolf, X.A.5    Rea, R.6    Hill, C.7    Ingmer, H.8
  • 43
    • 0029082683 scopus 로고
    • The DpsA protein of Synechococcus sp. strain PCC7942 is a DNA-binding hemoprotein. Linkage of the Dps and bacterioferritin protein families
    • Peña MM, Bullerjahn GS (1995) The DpsA protein of Synechococcus sp. strain PCC7942 is a DNA-binding hemoprotein. Linkage of the Dps and bacterioferritin protein families. J Biol Chem 270:22478-22482
    • (1995) J Biol Chem , vol.270 , pp. 22478-22482
    • Peña, M.M.1    Bullerjahn, G.S.2
  • 44
    • 65649108140 scopus 로고    scopus 로고
    • The C-terminal region of HPNAP activates neutrophils and promotes their adhesion to endothelial cells
    • Kottakis F, Befani C, Asiminas A, Kontou M, Koliakos G, Choli-Papadopoulou T (2009) The C-terminal region of HPNAP activates neutrophils and promotes their adhesion to endothelial cells. Helicobacter 14:177-179
    • (2009) Helicobacter , vol.14 , pp. 177-179
    • Kottakis, F.1    Befani, C.2    Asiminas, A.3    Kontou, M.4    Koliakos, G.5    Choli-Papadopoulou, T.6
  • 46
    • 34249941286 scopus 로고    scopus 로고
    • Role of N and C-terminal tails in DNA binding and assembly in Dps: Structural studies of Mycobacterium smegmatis Dps deletion mutants
    • Roy S, Saraswathi R, Gupta S, Sekar K, Chatterji D, Vijayan M (2007) Role of N and C-terminal tails in DNA binding and assembly in Dps: structural studies of Mycobacterium smegmatis Dps deletion mutants. J Mol Biol 370:752-767
    • (2007) J Mol Biol , vol.370 , pp. 752-767
    • Roy, S.1    Saraswathi, R.2    Gupta, S.3    Sekar, K.4    Chatterji, D.5    Vijayan, M.6
  • 47
    • 0032493313 scopus 로고    scopus 로고
    • Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins
    • Yang X, Chen-Barrett Y, Arosio P, Chasteen ND (1998) Reaction paths of iron oxidation and hydrolysis in horse spleen and recombinant human ferritins. Biochemistry 37:9743-9750
    • (1998) Biochemistry , vol.37 , pp. 9743-9750
    • Yang, X.1    Chen-Barrett, Y.2    Arosio, P.3    Chasteen, N.D.4
  • 48
    • 0034254215 scopus 로고    scopus 로고
    • Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua
    • Yang X, Chiancone E, Stefanini S, Ilari A, Chasteen ND (2000) Iron oxidation and hydrolysis reactions of a novel ferritin from Listeria innocua. Biochem J 349(3):783-786 (Pubitemid 30609409)
    • (2000) Biochemical Journal , vol.349 , Issue.3 , pp. 783-786
    • Yang, X.1    Chiancone, E.2    Stefanini, S.3    Ilari, A.4    Chasteen, N.D.5
  • 49
    • 0034712683 scopus 로고    scopus 로고
    • The iron oxidation and hydrolysis chemistry of Escherichia coli bacterioferritin
    • Yang X, Le Brun NE, Thomson AJ, Moore GR, Chasteen ND (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
  • 50
    • 0037008743 scopus 로고    scopus 로고
    • Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritinlike DNA-binding protein of Escherichia coli
    • Zhao G, Ceci P, Ilari A, Giangiacomo L, Laue TM, Chiancone E, Chasteen ND (2002) Iron and hydrogen peroxide detoxification properties of DNA-binding protein from starved cells. A ferritinlike DNA-binding protein of Escherichia coli. J Biol Chem 277:27689-27696
    • (2002) J Biol Chem , vol.277 , pp. 27689-27696
    • Zhao, G.1    Ceci, P.2    Ilari, A.3    Giangiacomo, L.4    Laue, T.M.5    Chiancone, E.6    Chasteen, N.D.7
  • 51
    • 17144402211 scopus 로고    scopus 로고
    • The so-called Listeria innocua ferritin is a Dps protein. Iron incorporation, detoxification, and DNA protection properties
    • Su M, Cavallo S, Stefanini S, Chiancone E, Chasteen ND (2005) The so-called Listeria innocua ferritin is a Dps protein. Iron incorporation, detoxification, and DNA protection properties. Biochemistry 44:5572-5578
    • (2005) Biochemistry , vol.44 , pp. 5572-5578
    • Su, M.1    Cavallo, S.2    Stefanini, S.3    Chiancone, E.4    Chasteen, N.D.5
  • 52
    • 67650567341 scopus 로고    scopus 로고
    • Iron translocation into and out of Listeria innocua Dps and size distribution of the protein-enclosed nanomineral are modulated by the electrostatic gradient at the 3-fold "ferritinlike" pores
    • Bellapadrona G, Stefanini S, Zamparelli C, Theil EC, Chiancone E (2009) Iron translocation into and out of Listeria innocua Dps and size distribution of the protein-enclosed nanomineral are modulated by the electrostatic gradient at the 3-fold "ferritinlike" pores. J Biol Chem 284:19101-19109
    • (2009) J Biol Chem , vol.284 , pp. 19101-19109
    • Bellapadrona, G.1    Stefanini, S.2    Zamparelli, C.3    Theil, E.C.4    Chiancone, E.5
  • 53
    • 33751057232 scopus 로고    scopus 로고
    • Iron incorporation in Streptococcus suis Dps-like peroxide resistance protein Dpr requires mobility in the ferroxidase center and leads to the formation of a ferrihydrite-like core
    • Kauko A, Pulliainen AT, Haataja S, Meyer-Klaucke W, Finne J, Papageorgiou AC (2006) Iron incorporation in Streptococcus suis Dps-like peroxide resistance protein Dpr requires mobility in the ferroxidase center and leads to the formation of a ferrihydrite-like core. J Mol Biol 364:97-109
    • (2006) J Mol Biol , vol.364 , pp. 97-109
    • Kauko, A.1    Pulliainen, A.T.2    Haataja, S.3    Meyer-Klaucke, W.4    Finne, J.5    Papageorgiou, A.C.6
  • 54
    • 0037020069 scopus 로고    scopus 로고
    • Iron incorporation into Escherichia coli Dps gives rise to a ferritinlike microcrystalline core
    • Ilari A, Ceci P, Ferrari D, Rossi GL, Chiancone E (2002) Iron incorporation into Escherichia coli Dps gives rise to a ferritinlike microcrystalline core. J Biol Chem 277:37619-37623
    • (2002) J Biol Chem , vol.277 , pp. 37619-37623
    • Ilari, A.1    Ceci, P.2    Ferrari, D.3    Rossi, G.L.4    Chiancone, E.5
  • 56
    • 0023998117 scopus 로고
    • New data and a revised structural model for ferrihydrite
    • Eggleton RA, Fitzpatrick RW (1988) New data and a revised structural model for ferrihydrite. Clays Clay Miner 36:111-124
    • (1988) Clays Clay Miner , vol.36 , pp. 111-124
    • Eggleton, R.A.1    Fitzpatrick, R.W.2
  • 57
    • 35348831736 scopus 로고    scopus 로고
    • Comparison of the kinetics of iron release from a marine (Trichodesmium erythraeum) Dps protein and mammalian ferritin in the presence and absence of ligands
    • Castruita M, Elmegreen LA, Shaked Y, Stiefel EI, Morel FM (2007) Comparison of the kinetics of iron release from a marine (Trichodesmium erythraeum) Dps protein and mammalian ferritin in the presence and absence of ligands. J Inorg Biochem 101:1686-1691
    • (2007) J Inorg Biochem , vol.101 , pp. 1686-1691
    • Castruita, M.1    Elmegreen, L.A.2    Shaked, Y.3    Stiefel, E.I.4    Morel, F.M.5
  • 58
    • 0033580643 scopus 로고    scopus 로고
    • Forming the phosphate layer in reconstituted horse spleen ferritin and the role of phosphate in promoting core surface redox reactions
    • Johnson JL, Cannon M, Watt RK, Frankel RB, Watt GD (1999) Forming the phosphate layer in reconstituted horse spleen ferritin and the role of phosphate in promoting core surface redox reactions. Biochemistry 38:6706-6713
    • (1999) Biochemistry , vol.38 , pp. 6706-6713
    • Johnson, J.L.1    Cannon, M.2    Watt, R.K.3    Frankel, R.B.4    Watt, G.D.5
  • 60
    • 3042582299 scopus 로고    scopus 로고
    • X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules
    • Roy S, Gupta S, Das S, Sekar K, Chatterji D, Vijayan M (2004) X-ray analysis of Mycobacterium smegmatis Dps and a comparative study involving other Dps and Dps-like molecules. J Mol Biol 339:1103-1113
    • (2004) J Mol Biol , vol.339 , pp. 1103-1113
    • Roy, S.1    Gupta, S.2    Das, S.3    Sekar, K.4    Chatterji, D.5    Vijayan, M.6
  • 64
    • 51949087233 scopus 로고    scopus 로고
    • An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses
    • Tsou CC, Chiang-Ni C, Lin YS, Chuang WJ, Lin MT, Liu CC, Wu JJ (2008) An iron-binding protein, Dpr, decreases hydrogen peroxide stress and protects Streptococcus pyogenes against multiple stresses. Infect Immun 76:4038-4045
    • (2008) Infect Immun , vol.76 , pp. 4038-4045
    • Tsou, C.C.1    Chiang-Ni, C.2    Lin, Y.S.3    Chuang, W.J.4    Lin, M.T.5    Liu, C.C.6    Wu, J.J.7
  • 65
    • 33746312043 scopus 로고    scopus 로고
    • Ferritin nanoparticle technology. A new platform for antigen presentation and vaccine development
    • Li CQ, Soistman E, Carter DC (2006) Ferritin nanoparticle technology. A new platform for antigen presentation and vaccine development. Ind Biotechnol 2:143
    • (2006) Ind Biotechnol , vol.2 , pp. 143
    • Li, C.Q.1    Soistman, E.2    Carter, D.C.3
  • 66
    • 45849103882 scopus 로고    scopus 로고
    • Apoferritin- templated yttrium phosphate nanoparticle conjugates for radioimmunotherapy of cancers
    • Wu H, Wang J, Wang ZM, Fisher DR, Lin YH (2008) Apoferritin- templated yttrium phosphate nanoparticle conjugates for radioimmunotherapy of cancers. J Nanosci Nanotechnol 8:2316-2322
    • (2008) J Nanosci Nanotechnol , vol.8 , pp. 2316-2322
    • Wu, H.1    Wang, J.2    Wang, Z.M.3    Fisher, D.R.4    Lin, Y.H.5
  • 68
    • 23644436163 scopus 로고    scopus 로고
    • Preparation of Cu and CuFe Prussian Blue derivative nanoparticles using the apoferritin cavity as nanoreactor
    • Galvez N, Sanchez P, Dominguez-Vera JM (2005) Preparation of Cu and CuFe Prussian Blue derivative nanoparticles using the apoferritin cavity as nanoreactor. Dalton Trans7(15):2492-2494
    • (2005) Dalton Trans7 , vol.15 , pp. 2492-2494
    • Galvez, N.1    Sanchez, P.2    Dominguez-Vera, J.M.3
  • 69
    • 24944519249 scopus 로고    scopus 로고
    • Constrained iron catalysts for single-walled carbon nanotube growth
    • Kramer RM, Sowards LA, Pender MJ, Stone MO, Naik RR (2005) Constrained iron catalysts for single-walled carbon nanotube growth. Langmuir 21:8466-8470
    • (2005) Langmuir , vol.21 , pp. 8466-8470
    • Kramer, R.M.1    Sowards, L.A.2    Pender, M.J.3    Stone, M.O.4    Naik, R.R.5
  • 70
    • 74149091227 scopus 로고    scopus 로고
    • The Dps protein of Escherichia coli is involved in copper homeostasis
    • doi:10.1016/j.micres.2008.12.003
    • Thieme D, Grass G (2009) The Dps protein of Escherichia coli is involved in copper homeostasis. Microbiol Res. doi:10.1016/j.micres.2008.12.003
    • (2009) Microbiol Res.
    • Thieme, D.1    Grass, G.2
  • 71
    • 57049124285 scopus 로고    scopus 로고
    • Acid stress damage of DNA is prevented by Dps binding in Escherichia coli O157:H7
    • Jeong K, Hung K, Baumler D, Byrd J, Kaspar C (2008) Acid stress damage of DNA is prevented by Dps binding in Escherichia coli O157:H7. BMC Microbiol 8:181
    • (2008) BMC Microbiol , vol.8 , pp. 181
    • Jeong, K.1    Hung, K.2    Baumler, D.3    Byrd, J.4    Kaspar, C.5
  • 73
    • 34249846924 scopus 로고    scopus 로고
    • The neutrophil- activating Dps protein of Helicobacter pylori, HP-NAP, adopts a mechanism different from Escherichia coli Dps to bind and condense DNA
    • Ceci P, Mangiarotti L, Rivetti C, Chiancone E (2007) The neutrophil- activating Dps protein of Helicobacter pylori, HP-NAP, adopts a mechanism different from Escherichia coli Dps to bind and condense DNA. Nucleic Acids Res 35:2247-2256
    • (2007) Nucleic Acids Res , vol.35 , pp. 2247-2256
    • Ceci, P.1    Mangiarotti, L.2    Rivetti, C.3    Chiancone, E.4
  • 74
    • 14744297017 scopus 로고    scopus 로고
    • Differential DNA binding and protection by dimeric and dodecameric forms of the ferritin homolog Dps from Deinococcus radiodurans
    • Grove A, Wilkinson S (2005) Differential DNA binding and protection by dimeric and dodecameric forms of the ferritin homolog Dps from Deinococcus radiodurans. J Mol Biol 347:495-508
    • (2005) J Mol Biol , vol.347 , pp. 495-508
    • Grove, A.1    Wilkinson, S.2
  • 76
    • 0037805747 scopus 로고    scopus 로고
    • The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: X-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties
    • Ceci P, Ilari A, Falvo E, Chiancone E (2003) The Dps protein of Agrobacterium tumefaciens does not bind to DNA but protects it toward oxidative cleavage: X-ray crystal structure, iron binding, and hydroxyl-radical scavenging properties. J Biol Chem 278:20319-20326
    • (2003) J Biol Chem , vol.278 , pp. 20319-20326
    • Ceci, P.1    Ilari, A.2    Falvo, E.3    Chiancone, E.4
  • 77
    • 0037424379 scopus 로고    scopus 로고
    • 2 resistance mediated by Streptococcal Dpr. Demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis
    • 2 resistance mediated by Streptococcal Dpr. Demonstration of the functional involvement of the putative ferroxidase center by site-directed mutagenesis in Streptococcus suis. J Biol Chem 278:7996-8005
    • (2003) J Biol Chem , vol.278 , pp. 7996-8005
    • Pulliainen, A.T.1    Haataja, S.2    Kahkonen, S.3    Finne, J.4
  • 78
    • 54049083387 scopus 로고    scopus 로고
    • Visualizing phylogenetic trees using TreeView
    • chap 6 unit 6 2
    • Page RD (2002) Visualizing phylogenetic trees using TreeView. Curr Protoc Bioinformatics, chap 6, unit 6 2
    • (2002) Curr Protoc Bioinformatics
    • Page, R.D.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.