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Volumn 41, Issue 2, 2016, Pages 190-203

Ferroxidase-Mediated Iron Oxide Biomineralization: Novel Pathways to Multifunctional Nanoparticles

Author keywords

Biomineralization; Dps; Encapsulin; Ferritin; Nanobiotechnology

Indexed keywords

BACTERIAL ENZYME; CERULOPLASMIN; FERRITIN; IRON OXIDE; NANOPARTICLE; FERRIC ION; FERRIC OXIDE; MINERAL;

EID: 84959111632     PISSN: 09680004     EISSN: 13624326     Source Type: Journal    
DOI: 10.1016/j.tibs.2015.11.011     Document Type: Review
Times cited : (48)

References (94)
  • 1
    • 84905584401 scopus 로고    scopus 로고
    • Bone hierarchical structure in three dimensions
    • Reznikov N., et al. Bone hierarchical structure in three dimensions. Acta Biomater. 2014, 10:3815-3826.
    • (2014) Acta Biomater. , vol.10 , pp. 3815-3826
    • Reznikov, N.1
  • 2
    • 84886025490 scopus 로고    scopus 로고
    • A Review of phosphate mineral nucleation in biology and geobiology
    • Omelon S., et al. A Review of phosphate mineral nucleation in biology and geobiology. Calcif. Tissue Int. 2013, 93:382-396.
    • (2013) Calcif. Tissue Int. , vol.93 , pp. 382-396
    • Omelon, S.1
  • 3
    • 84868567752 scopus 로고    scopus 로고
    • Silica biomorphs: complex biomimetic hybrid materials from 'sand and chalk'
    • Kellermeier M., et al. Silica biomorphs: complex biomimetic hybrid materials from 'sand and chalk'. Eur. J. Inorg. Chem. 2012, 5123-5144.
    • (2012) Eur. J. Inorg. Chem. , pp. 5123-5144
    • Kellermeier, M.1
  • 4
    • 84906309810 scopus 로고    scopus 로고
    • Enzyme-based biosilica and biocalcite: biomaterials for the future in regenerative medicine
    • Wang X., et al. Enzyme-based biosilica and biocalcite: biomaterials for the future in regenerative medicine. Trends Biotechnol. 2014, 32:441-447.
    • (2014) Trends Biotechnol. , vol.32 , pp. 441-447
    • Wang, X.1
  • 5
    • 84883745459 scopus 로고    scopus 로고
    • Magnetotactic bacteria form magnetite from a phosphate-rich ferric hydroxide via nanometric ferric (oxyhydr) oxide intermediates
    • Baumgartner J., et al. Magnetotactic bacteria form magnetite from a phosphate-rich ferric hydroxide via nanometric ferric (oxyhydr) oxide intermediates. Proc. Natl. Acad. Sci. U.S.A. 2013, 110:14883-14888.
    • (2013) Proc. Natl. Acad. Sci. U.S.A. , vol.110 , pp. 14883-14888
    • Baumgartner, J.1
  • 6
    • 84926434215 scopus 로고    scopus 로고
    • From bacteria to mollusks: the principles underlying the biomineralization of iron oxide materials
    • Faivre D., Godec T.U. From bacteria to mollusks: the principles underlying the biomineralization of iron oxide materials. Angew. Chem. Int. Ed. 2015, 54:4728-4747.
    • (2015) Angew. Chem. Int. Ed. , vol.54 , pp. 4728-4747
    • Faivre, D.1    Godec, T.U.2
  • 7
    • 84906944516 scopus 로고    scopus 로고
    • Life with compass: diversity and biogeography of magnetotactic bacteria
    • Lin W., et al. Life with compass: diversity and biogeography of magnetotactic bacteria. Environ. Microbiol. 2014, 16:2646-2658.
    • (2014) Environ. Microbiol. , vol.16 , pp. 2646-2658
    • Lin, W.1
  • 8
    • 84897635270 scopus 로고    scopus 로고
    • The effect and role of environmental conditions on magnetosome synthesis
    • Moisescu C., et al. The effect and role of environmental conditions on magnetosome synthesis. Front. Microbiol. 2014, 5:1-12.
    • (2014) Front. Microbiol. , vol.5 , pp. 1-12
    • Moisescu, C.1
  • 9
    • 84890259010 scopus 로고    scopus 로고
    • The magnetosome model: insights into the mechanisms of bacterial biomineralization
    • Rahn-Lee L., Komeili A. The magnetosome model: insights into the mechanisms of bacterial biomineralization. Front. Microbiol. 2013, 4:1-8.
    • (2013) Front. Microbiol. , vol.4 , pp. 1-8
    • Rahn-Lee, L.1    Komeili, A.2
  • 10
    • 84906825913 scopus 로고    scopus 로고
    • A virus-like nanocompartment that stores iron and protects bacteria from oxidative stress
    • McHugh C.A., et al. A virus-like nanocompartment that stores iron and protects bacteria from oxidative stress. EMBO J. 2014, 33:1896-1911.
    • (2014) EMBO J. , vol.33 , pp. 1896-1911
    • McHugh, C.A.1
  • 11
    • 79953309867 scopus 로고    scopus 로고
    • Ferritin protein nanocages use ion channels, catalytic sites, and nucleation channels to manage iron/oxygen chemistry
    • Theil E.C. Ferritin protein nanocages use ion channels, catalytic sites, and nucleation channels to manage iron/oxygen chemistry. Curr. Opin. Chem. Biol. 2011, 15:304-311.
    • (2011) Curr. Opin. Chem. Biol. , vol.15 , pp. 304-311
    • Theil, E.C.1
  • 12
    • 84864375724 scopus 로고    scopus 로고
    • Dps biomineralizing proteins: multifunctional architects of nature
    • Zeth K. Dps biomineralizing proteins: multifunctional architects of nature. Biochem. J. 2012, 445:297-311.
    • (2012) Biochem. J. , vol.445 , pp. 297-311
    • Zeth, K.1
  • 13
    • 84870811653 scopus 로고    scopus 로고
    • Iron utilization in marine cyanobacteria and eukaryotic algae
    • Morrissey J., Bowler C. Iron utilization in marine cyanobacteria and eukaryotic algae. Front. Microbiol. 2012, 3:1-13.
    • (2012) Front. Microbiol. , vol.3 , pp. 1-13
    • Morrissey, J.1    Bowler, C.2
  • 14
    • 77953809155 scopus 로고    scopus 로고
    • The multifaceted capacity of Dps proteins to combat bacterial stress conditions: detoxification of iron and hydrogen peroxide and DNA binding
    • Chiancone E., Ceci P. The multifaceted capacity of Dps proteins to combat bacterial stress conditions: detoxification of iron and hydrogen peroxide and DNA binding. Biochim. Biophys. Acta 2010, 1800:798-805.
    • (2010) Biochim. Biophys. Acta , vol.1800 , pp. 798-805
    • Chiancone, E.1    Ceci, P.2
  • 15
    • 21544465580 scopus 로고    scopus 로고
    • Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx-mutants of Escherichia coli
    • Park S., et al. Substantial DNA damage from submicromolar intracellular hydrogen peroxide detected in Hpx-mutants of Escherichia coli. Proc. Natl. Acad. Sci. U.S.A. 2005, 102:14833-14888.
    • (2005) Proc. Natl. Acad. Sci. U.S.A. , vol.102 , pp. 14833-14888
    • Park, S.1
  • 16
    • 67349100157 scopus 로고    scopus 로고
    • Ferritins: a family of molecules for iron storage, antioxidation and more
    • Arosio P., et al. Ferritins: a family of molecules for iron storage, antioxidation and more. Biochim. Biophys. Acta 2009, 1790:589-599.
    • (2009) Biochim. Biophys. Acta , vol.1790 , pp. 589-599
    • Arosio, P.1
  • 18
    • 77950591971 scopus 로고    scopus 로고
    • Cre-lox-based method for generation of large deletions within the genomic magnetosome island of Magnetospirillum gryphiswaldense
    • Ullrich S., Schuler D. Cre-lox-based method for generation of large deletions within the genomic magnetosome island of Magnetospirillum gryphiswaldense. Appl. Environ. Microbiol. 2010, 76:2439-2444.
    • (2010) Appl. Environ. Microbiol. , vol.76 , pp. 2439-2444
    • Ullrich, S.1    Schuler, D.2
  • 19
  • 20
    • 79956112556 scopus 로고
    • Magnetite and magnetotaxis in algae
    • Torres F.F., et al. Magnetite and magnetotaxis in algae. Biophys. J. 1986, 50:375-378.
    • (1986) Biophys. J. , vol.50 , pp. 375-378
    • Torres, F.F.1
  • 21
    • 84935835822 scopus 로고    scopus 로고
    • Bioinspired nanoreactors for the biomineralisation of metallic-based nanoparticles for nanomedicine
    • Bain J., Staniland S.S. Bioinspired nanoreactors for the biomineralisation of metallic-based nanoparticles for nanomedicine. Phys. Chem. Chem. Phys. 2015, 17:15508-15521.
    • (2015) Phys. Chem. Chem. Phys. , vol.17 , pp. 15508-15521
    • Bain, J.1    Staniland, S.S.2
  • 22
    • 84892535469 scopus 로고    scopus 로고
    • Compartmentalization and organelle formation in bacteria
    • Cornejo E., et al. Compartmentalization and organelle formation in bacteria. Curr. Opin. Cell Biol. 2014, 26:132-138.
    • (2014) Curr. Opin. Cell Biol. , vol.26 , pp. 132-138
    • Cornejo, E.1
  • 24
    • 80053390425 scopus 로고    scopus 로고
    • Structure and mechanism of iron translocation by a Dps protein from Microbacterium arborescens
    • Pesek J., et al. Structure and mechanism of iron translocation by a Dps protein from Microbacterium arborescens. J. Biol. Chem. 2011, 286:34872-34882.
    • (2011) J. Biol. Chem. , vol.286 , pp. 34872-34882
    • Pesek, J.1
  • 25
    • 84899005526 scopus 로고    scopus 로고
    • A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis
    • Williams S.M., et al. A histidine aspartate ionic lock gates the iron passage in miniferritins from Mycobacterium smegmatis. J. Biol. Chem. 2014, 286:11042-11058.
    • (2014) J. Biol. Chem. , vol.286 , pp. 11042-11058
    • Williams, S.M.1
  • 26
    • 84922480881 scopus 로고    scopus 로고
    • A tale of tails: deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolor
    • Hitchings M.D., et al. A tale of tails: deciphering the contribution of terminal tails to the biochemical properties of two Dps proteins from Streptomyces coelicolor. Cell. Mol. Life Sci. 2014, 71:4911-4926.
    • (2014) Cell. Mol. Life Sci. , vol.71 , pp. 4911-4926
    • Hitchings, M.D.1
  • 27
    • 84931274502 scopus 로고    scopus 로고
    • Halophiles and their enzymes: negativity put to good use
    • DasSarma S., DasSarma P. Halophiles and their enzymes: negativity put to good use. Curr. Opin. Microbiol. 2015, 25:120-126.
    • (2015) Curr. Opin. Microbiol. , vol.25 , pp. 120-126
    • DasSarma, S.1    DasSarma, P.2
  • 28
    • 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., et al. 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. 2004, 101:13780-13785.
    • (2004) Proc. Natl. Acad. Sci. U.S.A. , vol.101 , pp. 13780-13785
    • Zeth, K.1
  • 29
    • 0030608152 scopus 로고    scopus 로고
    • The ferritins: molecular properties, iron storage function and cellular regulation
    • Harrison P.M., Arosio P. The ferritins: molecular properties, iron storage function and cellular regulation. Biochem. Biophys. Acta 1996, 1275:161-203.
    • (1996) Biochem. Biophys. Acta , vol.1275 , pp. 161-203
    • Harrison, P.M.1    Arosio, P.2
  • 30
    • 84887112912 scopus 로고    scopus 로고
    • Ferritin: the protein nanocage and iron biomineral in health and in disease
    • Theil E.C. Ferritin: the protein nanocage and iron biomineral in health and in disease. Inorg. Chem. 2013, 52:12223-12233.
    • (2013) Inorg. Chem. , vol.52 , pp. 12223-12233
    • Theil, E.C.1
  • 31
    • 84914175069 scopus 로고    scopus 로고
    • Loop electrostatics modulates the intersubunit interactions in ferritin
    • Bernacchioni C., et al. Loop electrostatics modulates the intersubunit interactions in ferritin. ACS Chem. Biol. 2014, 9:2517-2525.
    • (2014) ACS Chem. Biol. , vol.9 , pp. 2517-2525
    • Bernacchioni, C.1
  • 32
    • 84927661468 scopus 로고    scopus 로고
    • 2+ substrate ions move through ferritin protein nanocages to oxidoreductase sites
    • 2+ substrate ions move through ferritin protein nanocages to oxidoreductase sites. Acta Crystallogr. Sect. D Biol. Crystallogr. 2015, 71:941-953.
    • (2015) Acta Crystallogr. Sect. D Biol. Crystallogr. , vol.71 , pp. 941-953
    • Pozzi, C.1
  • 33
    • 51349084876 scopus 로고    scopus 로고
    • Structural basis of enzyme encapsulation into a bacterial nanocompartment
    • Sutter M., et al. Structural basis of enzyme encapsulation into a bacterial nanocompartment. Nat. Struct. Mol. Biol. 2008, 15:939-947.
    • (2008) Nat. Struct. Mol. Biol. , vol.15 , pp. 939-947
    • Sutter, M.1
  • 34
    • 34247209698 scopus 로고    scopus 로고
    • The crystal structure of a virus-like particle from the hyperthermophilic archaeon Pyrococcus furiosus provides insight into the evolution of viruses
    • Akita F., et al. The crystal structure of a virus-like particle from the hyperthermophilic archaeon Pyrococcus furiosus provides insight into the evolution of viruses. J. Mol. Biol. 2007, 368:1469-1483.
    • (2007) J. Mol. Biol. , vol.368 , pp. 1469-1483
    • Akita, F.1
  • 35
    • 84860821329 scopus 로고    scopus 로고
    • Structure unifies the viral universe
    • Abrescia N.G.A., et al. Structure unifies the viral universe. Annu. Rev. Biochem. 2012, 81:795-822.
    • (2012) Annu. Rev. Biochem. , vol.81 , pp. 795-822
    • Abrescia, N.G.A.1
  • 36
    • 84876887523 scopus 로고    scopus 로고
    • Assembly in vitro of Rhodococcus jostii RHA1 encapsulin and peroxidase DypB to form a nanocompartment
    • Rahmanpour R., Bugg T.D.H. Assembly in vitro of Rhodococcus jostii RHA1 encapsulin and peroxidase DypB to form a nanocompartment. FEBS J. 2013, 280:2097-2104.
    • (2013) FEBS J. , vol.280 , pp. 2097-2104
    • Rahmanpour, R.1    Bugg, T.D.H.2
  • 37
    • 84928380985 scopus 로고    scopus 로고
    • Characterisation of Dyp-type peroxidases from Pseudomonas fluorescens Pf-5: oxidation of Mn (II) and polymeric lignin by Dyp1B
    • Rahmanpour R., Bugg T.D.H. Characterisation of Dyp-type peroxidases from Pseudomonas fluorescens Pf-5: oxidation of Mn (II) and polymeric lignin by Dyp1B. Arch. Biochem. Biophys. 2015, 574:93-98.
    • (2015) Arch. Biochem. Biophys. , vol.574 , pp. 93-98
    • Rahmanpour, R.1    Bugg, T.D.H.2
  • 38
    • 2942549658 scopus 로고    scopus 로고
    • Electron nanodiffraction and high-resolution electron microscopy studies of the structure and composition of physiological and pathological ferritin
    • Quintana C., et al. Electron nanodiffraction and high-resolution electron microscopy studies of the structure and composition of physiological and pathological ferritin. J. Struct. Biol. 2004, 147:166-178.
    • (2004) J. Struct. Biol. , vol.147 , pp. 166-178
    • Quintana, C.1
  • 39
    • 84923666786 scopus 로고    scopus 로고
    • Ferritin: a versatile building block for bionanotechnology
    • Jutz G., et al. Ferritin: a versatile building block for bionanotechnology. Chem. Rev. 2015, 115:1653-1701.
    • (2015) Chem. Rev. , vol.115 , pp. 1653-1701
    • Jutz, G.1
  • 40
    • 34250721667 scopus 로고    scopus 로고
    • Biological containers: protein cages as multifunctional nanoplatforms
    • Uchida M., et al. Biological containers: protein cages as multifunctional nanoplatforms. Adv. Mater. 2007, 19:1025-1042.
    • (2007) Adv. Mater. , vol.19 , pp. 1025-1042
    • Uchida, M.1
  • 41
    • 0028887435 scopus 로고
    • Synthesis and structure of an iron(III) sulfide-ferritin bioinorganic nanocomposite
    • Douglas T., et al. Synthesis and structure of an iron(III) sulfide-ferritin bioinorganic nanocomposite. Science 1995, 269:54-57.
    • (1995) Science , vol.269 , pp. 54-57
    • Douglas, T.1
  • 42
    • 84882345880 scopus 로고    scopus 로고
    • Ferritin protein encapsulated photoluminescent rare earth nanoparticle
    • Harada T., Yoshimura H. Ferritin protein encapsulated photoluminescent rare earth nanoparticle. J. Appl. Phys. 2013, 114:044309.
    • (2013) J. Appl. Phys. , vol.114 , pp. 044309
    • Harada, T.1    Yoshimura, H.2
  • 43
    • 77956896922 scopus 로고    scopus 로고
    • Circularly polarized luminescent CDs quantum dots prepared in a protein nanocage
    • Naito M., et al. Circularly polarized luminescent CDs quantum dots prepared in a protein nanocage. Angew. Chem. Int. Ed. 2010, 49:7006-7009.
    • (2010) Angew. Chem. Int. Ed. , vol.49 , pp. 7006-7009
    • Naito, M.1
  • 44
    • 79958019779 scopus 로고    scopus 로고
    • Bioinspired synthesis of homogenous cerium oxide nanoparticles and two- or three-dimensional nanoparticle arrays using protein supramolecules
    • Okuda, et al. Bioinspired synthesis of homogenous cerium oxide nanoparticles and two- or three-dimensional nanoparticle arrays using protein supramolecules. Cryst. Growth Des. 2011, 11:2540-2545.
    • (2011) Cryst. Growth Des. , vol.11 , pp. 2540-2545
    • Okuda1
  • 45
    • 41149103849 scopus 로고    scopus 로고
    • Viral capsids as templates for the production of monodisperse Prussian blue nanoparticles
    • De la Escosura A., et al. Viral capsids as templates for the production of monodisperse Prussian blue nanoparticles. Chem. Commun. 2008, 1542-1544.
    • (2008) Chem. Commun. , pp. 1542-1544
    • De la Escosura, A.1
  • 46
    • 49149088384 scopus 로고    scopus 로고
    • 2 inside a viral capsid
    • 2 inside a viral capsid. J. Mater. Chem. 2008, 18:3821-3823.
    • (2008) J. Mater. Chem. , vol.18 , pp. 3821-3823
    • Klem, M.T.1
  • 47
    • 77953812742 scopus 로고    scopus 로고
    • Ferritin in the field of nanodevices
    • Yamashita I., et al. Ferritin in the field of nanodevices. Biochim. Biophys. Acta. 2010, 1800:846-857.
    • (2010) Biochim. Biophys. Acta. , vol.1800 , pp. 846-857
    • Yamashita, I.1
  • 48
    • 78549239529 scopus 로고    scopus 로고
    • Bio-templated CdSe nanoparticle synthesis in a cage shaped protein Listeria-Dps, and their two dimensional ordered array self-assembly
    • Okuda M., et al. Bio-templated CdSe nanoparticle synthesis in a cage shaped protein Listeria-Dps, and their two dimensional ordered array self-assembly. Chem. Commun. 2010, 46:8797-8799.
    • (2010) Chem. Commun. , vol.46 , pp. 8797-8799
    • Okuda, M.1
  • 49
    • 19944416556 scopus 로고    scopus 로고
    • Self-organized inorganic nanoparticle arrays on protein lattices
    • Okuda M., et al. Self-organized inorganic nanoparticle arrays on protein lattices. Nano Lett. 2005, 5:991-993.
    • (2005) Nano Lett. , vol.5 , pp. 991-993
    • Okuda, M.1
  • 50
    • 84867021053 scopus 로고    scopus 로고
    • Nanoparticles: protein-mediated crystalline magnetic superstructures
    • Okuda M., et al. Nanoparticles: protein-mediated crystalline magnetic superstructures. Nanotechnology 2012, 23:415601.
    • (2012) Nanotechnology , vol.23 , pp. 415601
    • Okuda, M.1
  • 51
    • 0028276960 scopus 로고
    • The role of L-chain in ferritin iron incorporation Studies of homo and heteropolymers
    • Levi S., et al. The role of L-chain in ferritin iron incorporation Studies of homo and heteropolymers. J. Mol. Biol. 1994, 238:649-654.
    • (1994) J. Mol. Biol. , vol.238 , pp. 649-654
    • Levi, S.1
  • 52
    • 77955673728 scopus 로고    scopus 로고
    • Size and crystallinity in protein-templated inorganic nanoparticles
    • Jolley C.C., et al. Size and crystallinity in protein-templated inorganic nanoparticles. Chem. Mater. 2010, 22:4612-4618.
    • (2010) Chem. Mater. , vol.22 , pp. 4612-4618
    • Jolley, C.C.1
  • 53
    • 0027126202 scopus 로고
    • Magnetoferritin: in vitro synthesis of a novel magnetic protein
    • Meldrum F.C., et al. Magnetoferritin: in vitro synthesis of a novel magnetic protein. Science 1992, 257:522-523.
    • (1992) Science , vol.257 , pp. 522-523
    • Meldrum, F.C.1
  • 54
    • 75649117396 scopus 로고    scopus 로고
    • Synthesis of iron oxide nanoparticles in Listeria innocua Dps (DNA-binding protein from starved cells): a study with the wild-type protein and a catalytic centre mutant
    • Ceci P., et al. Synthesis of iron oxide nanoparticles in Listeria innocua Dps (DNA-binding protein from starved cells): a study with the wild-type protein and a catalytic centre mutant. Chem. Eur. J. 2010, 16:709-717.
    • (2010) Chem. Eur. J. , vol.16 , pp. 709-717
    • Ceci, P.1
  • 55
    • 84882337392 scopus 로고    scopus 로고
    • Magnonic metamaterials
    • Tech, X.Y. Jiang (Ed.)
    • Kruglyak V.V., et al. Magnonic metamaterials. Metamaterials 2012, 341-370. Tech. X.Y. Jiang (Ed.).
    • (2012) Metamaterials , pp. 341-370
    • Kruglyak, V.V.1
  • 56
    • 84861740604 scopus 로고    scopus 로고
    • Energy barrier distribution for dispersed mixed oxide magnetic nanoparticles
    • Okuda M., et al. Energy barrier distribution for dispersed mixed oxide magnetic nanoparticles. J. Appl. Phys. 2012, 111:10-13.
    • (2012) J. Appl. Phys. , vol.111 , pp. 10-13
    • Okuda, M.1
  • 57
    • 32044436332 scopus 로고    scopus 로고
    • Floating nanodot gate memory devices based on biomineralized inorganic nanodot array as a storage node
    • Miura A., et al. Floating nanodot gate memory devices based on biomineralized inorganic nanodot array as a storage node. Jpn. J. Appl. Phys. 2006, 45:1-3.
    • (2006) Jpn. J. Appl. Phys. , vol.45 , pp. 1-3
    • Miura, A.1
  • 58
    • 34547849962 scopus 로고    scopus 로고
    • Floating gate metal-oxide-semiconductor capacitor employing array of high-density nanodots produced by protein supramolecule
    • Yamada K., et al. Floating gate metal-oxide-semiconductor capacitor employing array of high-density nanodots produced by protein supramolecule. Jpn. J. Appl. Phys. 2006, 45:8946-8951.
    • (2006) Jpn. J. Appl. Phys. , vol.45 , pp. 8946-8951
    • Yamada, K.1
  • 59
    • 30744450719 scopus 로고    scopus 로고
    • Electron confinement in a metal nanodot monolayer embedded in silicon dioxide produced using ferritin protein
    • Hikono T., et al. Electron confinement in a metal nanodot monolayer embedded in silicon dioxide produced using ferritin protein. Appl. Phys. Lett. 2006, 88:023108.
    • (2006) Appl. Phys. Lett. , vol.88 , pp. 023108
    • Hikono, T.1
  • 60
    • 84928578628 scopus 로고    scopus 로고
    • Floating gate memory with charge storage dots array formed by Dps protein modified with site-specific binding peptides
    • Kamitake H., et al. Floating gate memory with charge storage dots array formed by Dps protein modified with site-specific binding peptides. Nanotechnology 2015, 26:195201.
    • (2015) Nanotechnology , vol.26 , pp. 195201
    • Kamitake, H.1
  • 61
    • 0344012217 scopus 로고    scopus 로고
    • A hexapeptide motif that electrostatically binds to the surface of titanium
    • Sano K.I., Shiba K. A hexapeptide motif that electrostatically binds to the surface of titanium. J. Am. Chem. Soc. 2003, 125:14234-14235.
    • (2003) J. Am. Chem. Soc. , vol.125 , pp. 14234-14235
    • Sano, K.I.1    Shiba, K.2
  • 62
    • 33748565001 scopus 로고    scopus 로고
    • Selective nanoscale positioning of ferritin and nanoparticles by means of target-specific peptides
    • Yamashita I., et al. Selective nanoscale positioning of ferritin and nanoparticles by means of target-specific peptides. Small 2006, 2:1148-1152.
    • (2006) Small , vol.2 , pp. 1148-1152
    • Yamashita, I.1
  • 63
    • 65249172145 scopus 로고    scopus 로고
    • Hexagonal close-packed array formed by selective adsorption onto hexagonal patterns
    • Matsukawa N., et al. Hexagonal close-packed array formed by selective adsorption onto hexagonal patterns. Langmuir 2009, 25:3327-3330.
    • (2009) Langmuir , vol.25 , pp. 3327-3330
    • Matsukawa, N.1
  • 64
    • 84885394400 scopus 로고    scopus 로고
    • Nonvolatile flash memory based on biologically integrated hierarchical nanostructures
    • Sano K.I., et al. Nonvolatile flash memory based on biologically integrated hierarchical nanostructures. Langmuir 2013, 29:12483-12489.
    • (2013) Langmuir , vol.29 , pp. 12483-12489
    • Sano, K.I.1
  • 65
    • 33845933127 scopus 로고    scopus 로고
    • Targeting of cancer cells with ferromagnetic ferritin cage nanoparticles
    • Uchida M., et al. Targeting of cancer cells with ferromagnetic ferritin cage nanoparticles. J. Am. Chem. Soc. 2006, 128:16626-16633.
    • (2006) J. Am. Chem. Soc. , vol.128 , pp. 16626-16633
    • Uchida, M.1
  • 66
    • 84901650228 scopus 로고    scopus 로고
    • A smart platform for hyperthermia application in cancer treatment: cobalt-doped ferrite nanoparticles mineralized in human ferritin cages
    • Fantechi E., et al. A smart platform for hyperthermia application in cancer treatment: cobalt-doped ferrite nanoparticles mineralized in human ferritin cages. ACS Nano 2014, 8:4705-4719.
    • (2014) ACS Nano , vol.8 , pp. 4705-4719
    • Fantechi, E.1
  • 67
    • 84861481588 scopus 로고    scopus 로고
    • RGD-conjugated human ferritin nanoparticles for imaging vascular inflammation and angiogenesis in experimental carotid and aortic disease
    • Kitagawa T., et al. RGD-conjugated human ferritin nanoparticles for imaging vascular inflammation and angiogenesis in experimental carotid and aortic disease. Mol. Imaging Biol. 2014, 14:315-324.
    • (2014) Mol. Imaging Biol. , vol.14 , pp. 315-324
    • Kitagawa, T.1
  • 68
    • 84863716553 scopus 로고    scopus 로고
    • Magnetoferritin nanoparticles for targeting and visualizing tumour tissues
    • Fan K., et al. Magnetoferritin nanoparticles for targeting and visualizing tumour tissues. Nat. Nanotechnol. 2012, 7:459-464.
    • (2012) Nat. Nanotechnol. , vol.7 , pp. 459-464
    • Fan, K.1
  • 69
    • 0031638368 scopus 로고    scopus 로고
    • The material bone: structure-mechanical function relations
    • Weiner S., Wagner H.D. The material bone: structure-mechanical function relations. Annu. Rev. Mater. Sci. 1998, 28:271-298.
    • (1998) Annu. Rev. Mater. Sci. , vol.28 , pp. 271-298
    • Weiner, S.1    Wagner, H.D.2
  • 70
    • 0033617958 scopus 로고    scopus 로고
    • Mineralization in ferritin: an efficient means of iron storage
    • Chasteen N.D., Harrison P.M. Mineralization in ferritin: an efficient means of iron storage. J. Struct. Biol. 1999, 126:182-194.
    • (1999) J. Struct. Biol. , vol.126 , pp. 182-194
    • Chasteen, N.D.1    Harrison, P.M.2
  • 71
    • 84864332804 scopus 로고    scopus 로고
    • The predominant role of collagen in the nucleation, growth, structure and orientation of bone apatite
    • Wang Y., et al. The predominant role of collagen in the nucleation, growth, structure and orientation of bone apatite. Nat. Mater. 2012, 11:724-733.
    • (2012) Nat. Mater. , vol.11 , pp. 724-733
    • Wang, Y.1
  • 72
    • 17644402318 scopus 로고    scopus 로고
    • Biologically induced mineralization by bacteria
    • Frankel R.B., Bazylinski D.A. Biologically induced mineralization by bacteria. Rev. Mineral. Geochem. 2003, 54:95-114.
    • (2003) Rev. Mineral. Geochem. , vol.54 , pp. 95-114
    • Frankel, R.B.1    Bazylinski, D.A.2
  • 73
    • 79960148742 scopus 로고    scopus 로고
    • Crystallization pathways in biomineralization
    • Weiner S., Addadi L. Crystallization pathways in biomineralization. Annu. Rev. Mater. Res. 2011, 41:21-40.
    • (2011) Annu. Rev. Mater. Res. , vol.41 , pp. 21-40
    • Weiner, S.1    Addadi, L.2
  • 74
    • 84940957133 scopus 로고    scopus 로고
    • Ferritin family proteins and their use in bionanotechnology
    • He D., Marles-Wright J. Ferritin family proteins and their use in bionanotechnology. Nat. Biotechnol. 2015, 32:651-657.
    • (2015) Nat. Biotechnol. , vol.32 , pp. 651-657
    • He, D.1    Marles-Wright, J.2
  • 75
    • 84876811958 scopus 로고    scopus 로고
    • The bacterial magnetosome: a unique prokaryotic organelle
    • Lower B.H., Bazylinski D.A. The bacterial magnetosome: a unique prokaryotic organelle. J. Mol. Microbiol. Biotechnol. 2013, 23:63-80.
    • (2013) J. Mol. Microbiol. Biotechnol. , vol.23 , pp. 63-80
    • Lower, B.H.1    Bazylinski, D.A.2
  • 76
    • 84931323655 scopus 로고    scopus 로고
    • Toward 10 nm half-pitch in EUV lithography: results on resist screening and pattern collapse mitigation techniques
    • Kulmala T.S., et al. Toward 10 nm half-pitch in EUV lithography: results on resist screening and pattern collapse mitigation techniques. Proc. SPIE 2015, 9422:942204.
    • (2015) Proc. SPIE , vol.9422 , pp. 942204
    • Kulmala, T.S.1
  • 77
    • 84931362294 scopus 로고    scopus 로고
    • Novel EUV resist development for sub-14 nm half pitch
    • Hori M., et al. Novel EUV resist development for sub-14 nm half pitch. Proc. SPIE 2015, 9422:942224.
    • (2015) Proc. SPIE , vol.9422 , pp. 942224
    • Hori, M.1
  • 78
    • 84923309112 scopus 로고    scopus 로고
    • Programmable materials and the nature of the DNA bond
    • Jones M.R., et al. Programmable materials and the nature of the DNA bond. Science 2015, 347:1260901.
    • (2015) Science , vol.347 , pp. 1260901
    • Jones, M.R.1
  • 79
    • 84862490523 scopus 로고    scopus 로고
    • Structural DNA nanotechnology: from design to applications
    • Zadegan R.M., Norton M.L. Structural DNA nanotechnology: from design to applications. Int. J. Mol. Sci. 2012, 13:7149-7162.
    • (2012) Int. J. Mol. Sci. , vol.13 , pp. 7149-7162
    • Zadegan, R.M.1    Norton, M.L.2
  • 80
    • 84961290301 scopus 로고    scopus 로고
    • Mechanical design of DNA nanostructures
    • Castro C.E., et al. Mechanical design of DNA nanostructures. Nanoscale 2015, 7:5913-5921.
    • (2015) Nanoscale , vol.7 , pp. 5913-5921
    • Castro, C.E.1
  • 81
    • 33645028600 scopus 로고    scopus 로고
    • Folding DNA to create nanoscale shapes and patterns
    • Rothemund P.W.K. Folding DNA to create nanoscale shapes and patterns. Nature 2006, 440:297-302.
    • (2006) Nature , vol.440 , pp. 297-302
    • Rothemund, P.W.K.1
  • 82
    • 65549170920 scopus 로고    scopus 로고
    • Self-assembly of a nanoscale DNA box with a controllable lid
    • Andersen E.S., et al. Self-assembly of a nanoscale DNA box with a controllable lid. Nature 2009, 459:73-76.
    • (2009) Nature , vol.459 , pp. 73-76
    • Andersen, E.S.1
  • 83
    • 84870471028 scopus 로고    scopus 로고
    • Construction of a 4 zeptoliters switchable 3D DNA box origami
    • Zadegan R.M., et al. Construction of a 4 zeptoliters switchable 3D DNA box origami. ACS Nano 2012, 6:10050-10053.
    • (2012) ACS Nano , vol.6 , pp. 10050-10053
    • Zadegan, R.M.1
  • 84
    • 84902584254 scopus 로고    scopus 로고
    • Nanomechanical molecular devices made of DNA origami
    • Kuzuya A., Ohya Y. Nanomechanical molecular devices made of DNA origami. Acc. Chem. Res. 2014, 47:1742-1749.
    • (2014) Acc. Chem. Res. , vol.47 , pp. 1742-1749
    • Kuzuya, A.1    Ohya, Y.2
  • 85
    • 84896725070 scopus 로고    scopus 로고
    • Stable RNA nanoparticles as potential new generation drugs for cancer therapy
    • Shu Y., et al. Stable RNA nanoparticles as potential new generation drugs for cancer therapy. Adv. Drug Delivery Rev. 2014, 66:74-89.
    • (2014) Adv. Drug Delivery Rev. , vol.66 , pp. 74-89
    • Shu, Y.1
  • 86
    • 84922279304 scopus 로고    scopus 로고
    • Encapsulation of a gold nanoparticle in a DNA origami container
    • Kuzuya A., et al. Encapsulation of a gold nanoparticle in a DNA origami container. Polymer J. 2015, 47:177-182.
    • (2015) Polymer J. , vol.47 , pp. 177-182
    • Kuzuya, A.1
  • 87
    • 84929352877 scopus 로고    scopus 로고
    • Surface plasmon resonance: a versatile technique for biosensors applications
    • Nguyen H.H., et al. Surface plasmon resonance: a versatile technique for biosensors applications. Sensors 2015, 15:10481-10510.
    • (2015) Sensors , vol.15 , pp. 10481-10510
    • Nguyen, H.H.1
  • 88
    • 77956651527 scopus 로고    scopus 로고
    • Virus hybrids as nanomaterials for biotechnology
    • Soto C.M., Ratna B.R. Virus hybrids as nanomaterials for biotechnology. Curr. Opin. Biotechnol. 2010, 21:426-438.
    • (2010) Curr. Opin. Biotechnol. , vol.21 , pp. 426-438
    • Soto, C.M.1    Ratna, B.R.2
  • 89
    • 84889571890 scopus 로고    scopus 로고
    • Pathogen-like particles: biomimetic vaccine carriers engineered at the nanoscale
    • Rosenthal J.A., et al. Pathogen-like particles: biomimetic vaccine carriers engineered at the nanoscale. Curr. Opin. Biotechnol. 2014, 28:51-58.
    • (2014) Curr. Opin. Biotechnol. , vol.28 , pp. 51-58
    • Rosenthal, J.A.1
  • 90
    • 84888330587 scopus 로고    scopus 로고
    • Self-assembled two-dimensional protein arrays in bionanotechnology: from S-layers to designated lattices
    • Baneyx F., Matthaei J.F. Self-assembled two-dimensional protein arrays in bionanotechnology: from S-layers to designated lattices. Curr. Opin. Biotechnol. 2014, 28:39-45.
    • (2014) Curr. Opin. Biotechnol. , vol.28 , pp. 39-45
    • Baneyx, F.1    Matthaei, J.F.2
  • 91
    • 84855250778 scopus 로고    scopus 로고
    • Developments in nanocrystal memory
    • Chang T.C., et al. Developments in nanocrystal memory. Mater. Today 2011, 14:608-615.
    • (2011) Mater. Today , vol.14 , pp. 608-615
    • Chang, T.C.1
  • 92
    • 84885871904 scopus 로고    scopus 로고
    • Towards the development of flexible non-volatile memories
    • Han S-T., et al. Towards the development of flexible non-volatile memories. Adv. Mater. 2013, 25:5425-5449.
    • (2013) Adv. Mater. , vol.25 , pp. 5425-5449
    • Han, S.-T.1
  • 93
    • 0031212918 scopus 로고    scopus 로고
    • Flash memory cells - an overview
    • Pavan P., et al. Flash memory cells - an overview. Proc. IEEE 1997, 85:1248-1271.
    • (1997) Proc. IEEE , vol.85 , pp. 1248-1271
    • Pavan, P.1
  • 94
    • 3142773890 scopus 로고    scopus 로고
    • Introduction to flash memory
    • Bez R., et al. Introduction to flash memory. Proc. IEEE 2003, 91:489-501.
    • (2003) Proc. IEEE , vol.91 , pp. 489-501
    • Bez, R.1


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