메뉴 건너뛰기




Volumn 9, Issue 4, 2017, Pages

Synthetic plant virology for nanobiotechnology and nanomedicine

Author keywords

[No Author keywords available]

Indexed keywords

MEDICAL NANOTECHNOLOGY; NANOTECHNOLOGY;

EID: 85020856623     PISSN: 19395116     EISSN: 19390041     Source Type: Journal    
DOI: 10.1002/wnan.1447     Document Type: Review
Times cited : (85)

References (162)
  • 1
    • 0000256952 scopus 로고
    • Isolation of a crystalline protein possessing the properties of tobacco-mosaic virus
    • Stanley WM. Isolation of a crystalline protein possessing the properties of tobacco-mosaic virus. Science 1935, 81:644–645.
    • (1935) Science , vol.81 , pp. 644-645
    • Stanley, W.M.1
  • 2
    • 33747298984 scopus 로고
    • Liquid crystalline substances from virus-infected plants
    • Bawden FC, Pirie NW, Bernal JD, Fankuchen I. Liquid crystalline substances from virus-infected plants. Nature 1936, 138:1051–1052.
    • (1936) Nature , vol.138 , pp. 1051-1052
    • Bawden, F.C.1    Pirie, N.W.2    Bernal, J.D.3    Fankuchen, I.4
  • 3
    • 73649156890 scopus 로고
    • Physical principles in the construction of regular viruses
    • Caspar DL, Klug A. Physical principles in the construction of regular viruses. Cold Spring Harb Symp Quant Biol 1962, 27:1–24.
    • (1962) Cold Spring Harb Symp Quant Biol , vol.27 , pp. 1-24
    • Caspar, D.L.1    Klug, A.2
  • 4
    • 0017740556 scopus 로고
    • Structure of RNA and RNA binding site in tobacco mosaic virus from 4-A map calculated from X-ray fibre diagrams
    • Stubbs G, Warren S, Holmes K. Structure of RNA and RNA binding site in tobacco mosaic virus from 4-A map calculated from X-ray fibre diagrams. Nature 1977, 267:216–221.
    • (1977) Nature , vol.267 , pp. 216-221
    • Stubbs, G.1    Warren, S.2    Holmes, K.3
  • 5
    • 0018223550 scopus 로고
    • Protein disk of tobacco mosaic virus at 2.8 A resolution showing the interactions within and between subunits
    • Bloomer AC, Champness JN, Bricogne G, Staden R, Klug A. Protein disk of tobacco mosaic virus at 2.8 A resolution showing the interactions within and between subunits. Nature 1978, 276:362–368.
    • (1978) Nature , vol.276 , pp. 362-368
    • Bloomer, A.C.1    Champness, J.N.2    Bricogne, G.3    Staden, R.4    Klug, A.5
  • 8
    • 0030158570 scopus 로고    scopus 로고
    • Use of viral replicons for the expression of genes in plants
    • Porta C, Lomonossoff GP. Use of viral replicons for the expression of genes in plants. Mol Biotechnol 1996, 5:209–221.
    • (1996) Mol Biotechnol , vol.5 , pp. 209-221
    • Porta, C.1    Lomonossoff, G.P.2
  • 9
    • 0014240607 scopus 로고
    • Some observations on structure of filamentous particles of several plant viruses
    • Varma A, Gibbs AJ, Woods RD, Finch JT. Some observations on structure of filamentous particles of several plant viruses. J Gen Virol 1968, 2:107–114.
    • (1968) J Gen Virol , vol.2 , pp. 107-114
    • Varma, A.1    Gibbs, A.J.2    Woods, R.D.3    Finch, J.T.4
  • 11
    • 0025933214 scopus 로고
    • The synthesis and structure of comovirus capsids
    • Lomonossoff GP, Johnson JE. The synthesis and structure of comovirus capsids. Prog Biophys Mol Biol 1991, 55:107–137.
    • (1991) Prog Biophys Mol Biol , vol.55 , pp. 107-137
    • Lomonossoff, G.P.1    Johnson, J.E.2
  • 12
    • 0014905804 scopus 로고
    • The self-assembly of spherical plant viruses
    • Bancroft JB. The self-assembly of spherical plant viruses. Adv Virus Res 1970, 16:99–134.
    • (1970) Adv Virus Res , vol.16 , pp. 99-134
    • Bancroft, J.B.1
  • 14
    • 0033614097 scopus 로고    scopus 로고
    • The tobacco mosaic virus particle: structure and assembly
    • Klug A. The tobacco mosaic virus particle: structure and assembly. Philos Trans R Soc Lond B Biol Sci 1999, 354:531–535.
    • (1999) Philos Trans R Soc Lond B Biol Sci , vol.354 , pp. 531-535
    • Klug, A.1
  • 17
    • 33646835810 scopus 로고
    • A negative staining method for high resolution electron microscopy of viruses
    • Brenner S, Horne RW. A negative staining method for high resolution electron microscopy of viruses. Biochim Biophys Acta 1959, 34:103–110.
    • (1959) Biochim Biophys Acta , vol.34 , pp. 103-110
    • Brenner, S.1    Horne, R.W.2
  • 18
    • 0024961660 scopus 로고
    • Visualization of alpha-helices in tobacco mosaic virus by cryo-electron microscopy
    • Jeng TW, Crowther RA, Stubbs G, Chiu W. Visualization of alpha-helices in tobacco mosaic virus by cryo-electron microscopy. J Mol Biol 1989, 205:251–257.
    • (1989) J Mol Biol , vol.205 , pp. 251-257
    • Jeng, T.W.1    Crowther, R.A.2    Stubbs, G.3    Chiu, W.4
  • 19
    • 34447649588 scopus 로고    scopus 로고
    • High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus
    • Sachse C, Chen JZ, Coureux PD, Stroupe ME, Fandrich M, Grigorieff N. High-resolution electron microscopy of helical specimens: a fresh look at tobacco mosaic virus. J Mol Biol 2007, 371:812–835.
    • (2007) J Mol Biol , vol.371 , pp. 812-835
    • Sachse, C.1    Chen, J.Z.2    Coureux, P.D.3    Stroupe, M.E.4    Fandrich, M.5    Grigorieff, N.6
  • 21
    • 0029921999 scopus 로고    scopus 로고
    • Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines
    • Lomonossoff GP, Johnson JE. Use of macromolecular assemblies as expression systems for peptides and synthetic vaccines. Curr Opin Struct Biol 1996, 6:176–182.
    • (1996) Curr Opin Struct Biol , vol.6 , pp. 176-182
    • Lomonossoff, G.P.1    Johnson, J.E.2
  • 22
    • 0030334824 scopus 로고    scopus 로고
    • Structure-based design of peptide presentation on a viral surface: the crystal structure of a plant/animal virus chimera at 2.8 A resolution
    • Lin T, Porta C, Lomonossoff G, Johnson JE. Structure-based design of peptide presentation on a viral surface: the crystal structure of a plant/animal virus chimera at 2.8 A resolution. Fold Des 1996, 1:179–187.
    • (1996) Fold Des , vol.1 , pp. 179-187
    • Lin, T.1    Porta, C.2    Lomonossoff, G.3    Johnson, J.E.4
  • 23
    • 0033971483 scopus 로고    scopus 로고
    • Virus-like particles assemble in plants and bacteria expressing the coat protein gene of Indian peanut clump virus
    • Bragard C, Duncan GH, Wesley SV, Naidu RA, Mayo MA. Virus-like particles assemble in plants and bacteria expressing the coat protein gene of Indian peanut clump virus. J Gen Virol 2000, 81:267–272.
    • (2000) J Gen Virol , vol.81 , pp. 267-272
    • Bragard, C.1    Duncan, G.H.2    Wesley, S.V.3    Naidu, R.A.4    Mayo, M.A.5
  • 24
    • 0028919805 scopus 로고
    • In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA
    • Zhao X, Fox JM, Olson NH, Baker TS, Young MJ. In vitro assembly of cowpea chlorotic mottle virus from coat protein expressed in Escherichia coli and in vitro-transcribed viral cDNA. Virology 1995, 207:486–494.
    • (1995) Virology , vol.207 , pp. 486-494
    • Zhao, X.1    Fox, J.M.2    Olson, N.H.3    Baker, T.S.4    Young, M.J.5
  • 25
    • 1842843148 scopus 로고    scopus 로고
    • Heterologous expression of the modified coat protein of Cowpea chlorotic mottle bromovirus results in the assembly of protein cages with altered architectures and function
    • Brumfield S, Willits D, Tang L, Johnson JE, Douglas T, Young M. Heterologous expression of the modified coat protein of Cowpea chlorotic mottle bromovirus results in the assembly of protein cages with altered architectures and function. J Gen Virol 2004, 85:1049–1053.
    • (2004) J Gen Virol , vol.85 , pp. 1049-1053
    • Brumfield, S.1    Willits, D.2    Tang, L.3    Johnson, J.E.4    Douglas, T.5    Young, M.6
  • 26
    • 84876696128 scopus 로고    scopus 로고
    • In vivo self-assembly of TMV-like particles in yeast and bacteria for nanotechnological applications
    • Kadri A, Wege C, Jeske H. In vivo self-assembly of TMV-like particles in yeast and bacteria for nanotechnological applications. J Virol Methods 2013, 189:328–340.
    • (2013) J Virol Methods , vol.189 , pp. 328-340
    • Kadri, A.1    Wege, C.2    Jeske, H.3
  • 27
    • 77952674391 scopus 로고    scopus 로고
    • In vitro assembly of tobacco mosaic virus coat protein variants derived from fission yeast expression clones or plants
    • Mueller A, Kadri A, Jeske H, Wege C. In vitro assembly of tobacco mosaic virus coat protein variants derived from fission yeast expression clones or plants. J Virol Methods 2010, 166:77–85.
    • (2010) J Virol Methods , vol.166 , pp. 77-85
    • Mueller, A.1    Kadri, A.2    Jeske, H.3    Wege, C.4
  • 28
    • 51849165035 scopus 로고    scopus 로고
    • Plant viruses as biotemplates for materials and their use in nanotechnology
    • Young M, Willits D, Uchida M, Douglas T. Plant viruses as biotemplates for materials and their use in nanotechnology. Annu Rev Phytopathol 2008, 46:361–384.
    • (2008) Annu Rev Phytopathol , vol.46 , pp. 361-384
    • Young, M.1    Willits, D.2    Uchida, M.3    Douglas, T.4
  • 30
    • 33746266809 scopus 로고    scopus 로고
    • Generation and structural analysis of reactive empty particles derived from an icosahedral virus
    • Ochoa WF, Chatterji A, Lin T, Johnson JE. Generation and structural analysis of reactive empty particles derived from an icosahedral virus. Chem Biol 2006, 13:771–778.
    • (2006) Chem Biol , vol.13 , pp. 771-778
    • Ochoa, W.F.1    Chatterji, A.2    Lin, T.3    Johnson, J.E.4
  • 31
    • 84897097820 scopus 로고    scopus 로고
    • Transient expressions of synthetic biology in plants
    • Sainsbury F, Lomonossoff GP. Transient expressions of synthetic biology in plants. Curr Opin Plant Biol 2014, 19:1–7.
    • (2014) Curr Opin Plant Biol , vol.19 , pp. 1-7
    • Sainsbury, F.1    Lomonossoff, G.P.2
  • 32
    • 84942199859 scopus 로고    scopus 로고
    • When plant virology met Agrobacterium: the rise of the deconstructed clones
    • Peyret H, Lomonossoff GP. When plant virology met Agrobacterium: the rise of the deconstructed clones. Plant Biotechnol J 2015, 13:1121–1135.
    • (2015) Plant Biotechnol J , vol.13 , pp. 1121-1135
    • Peyret, H.1    Lomonossoff, G.P.2
  • 33
    • 70349823197 scopus 로고    scopus 로고
    • Efficient generation of cowpea mosaic virus empty virus-like particles by the proteolytic processing of precursors in insect cells and plants
    • Saunders K, Sainsbury F, Lomonossoff GP. Efficient generation of cowpea mosaic virus empty virus-like particles by the proteolytic processing of precursors in insect cells and plants. Virology 2009, 393:329–337.
    • (2009) Virology , vol.393 , pp. 329-337
    • Saunders, K.1    Sainsbury, F.2    Lomonossoff, G.P.3
  • 39
    • 84954068287 scopus 로고    scopus 로고
    • The generation of turnip crinkle virus-like particles in plants by the transient expression of wild-type and modified forms of its coat protein
    • Saunders K, Lomonossoff GP. The generation of turnip crinkle virus-like particles in plants by the transient expression of wild-type and modified forms of its coat protein. Front Plant Sci 2015, 6:1138.
    • (2015) Front Plant Sci , vol.6 , pp. 1138
    • Saunders, K.1    Lomonossoff, G.P.2
  • 40
    • 0033614130 scopus 로고    scopus 로고
    • Self-assembly of tobacco mosaic virus: the role of an intermediate aggregate in generating both specificity and speed
    • Butler PJ. Self-assembly of tobacco mosaic virus: the role of an intermediate aggregate in generating both specificity and speed. Philos Trans R Soc Lond B Biol Sci 1999, 354:537–550.
    • (1999) Philos Trans R Soc Lond B Biol Sci , vol.354 , pp. 537-550
    • Butler, P.J.1
  • 41
    • 84892992577 scopus 로고    scopus 로고
    • Tailoring the surface properties of tobacco mosaic virions by the integration of bacterially expressed mutant coat protein
    • Eiben S, Stitz N, Eber F, Wagner J, Atanasova P, Bill J, Wege C, Jeske H. Tailoring the surface properties of tobacco mosaic virions by the integration of bacterially expressed mutant coat protein. Virus Res 2014, 180:92–96.
    • (2014) Virus Res , vol.180 , pp. 92-96
    • Eiben, S.1    Stitz, N.2    Eber, F.3    Wagner, J.4    Atanasova, P.5    Bill, J.6    Wege, C.7    Jeske, H.8
  • 44
    • 38949124465 scopus 로고    scopus 로고
    • Packaging of a polymer by a viral capsid: the interplay between polymer length and capsid size
    • Hu Y, Zandi R, Anavitarte A, Knobler CM, Gelbart WM. Packaging of a polymer by a viral capsid: the interplay between polymer length and capsid size. Biophys J 2008, 94:1428–1436.
    • (2008) Biophys J , vol.94 , pp. 1428-1436
    • Hu, Y.1    Zandi, R.2    Anavitarte, A.3    Knobler, C.M.4    Gelbart, W.M.5
  • 46
    • 49749194513 scopus 로고
    • Morphological changes accompanying thermal denaturation of tobacco mosaic virus
    • Hart RG. Morphological changes accompanying thermal denaturation of tobacco mosaic virus. Biochim Biophys Acta 1956, 20:388–389.
    • (1956) Biochim Biophys Acta , vol.20 , pp. 388-389
    • Hart, R.G.1
  • 47
    • 79251474936 scopus 로고    scopus 로고
    • Thermal transition of native tobacco mosaic virus and RNA-free viral proteins into spherical nanoparticles
    • Atabekov J, Nikitin N, Arkhipenko M, Chirkov S, Karpova O. Thermal transition of native tobacco mosaic virus and RNA-free viral proteins into spherical nanoparticles. J Gen Virol 2011, 92:453–456.
    • (2011) J Gen Virol , vol.92 , pp. 453-456
    • Atabekov, J.1    Nikitin, N.2    Arkhipenko, M.3    Chirkov, S.4    Karpova, O.5
  • 48
    • 84919999019 scopus 로고    scopus 로고
    • RNA-controlled assembly of tobacco mosaic virus-derived complex structures: from nanoboomerangs to tetrapods
    • Eber FJ, Eiben S, Jeske H, Wege C. RNA-controlled assembly of tobacco mosaic virus-derived complex structures: from nanoboomerangs to tetrapods. Nanoscale 2015, 7:344–355.
    • (2015) Nanoscale , vol.7 , pp. 344-355
    • Eber, F.J.1    Eiben, S.2    Jeske, H.3    Wege, C.4
  • 49
    • 84964305210 scopus 로고    scopus 로고
    • Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized candida antarctica lipase B
    • Cuenca S, Mansilla C, Aguado M, Yuste-Calvo C, Sanchez F, Sanchez-Montero JM, Ponz F. Nanonets derived from turnip mosaic virus as scaffolds for increased enzymatic activity of immobilized candida antarctica lipase B. Front Plant Sci 2016, 7:464.
    • (2016) Front Plant Sci , vol.7 , pp. 464
    • Cuenca, S.1    Mansilla, C.2    Aguado, M.3    Yuste-Calvo, C.4    Sanchez, F.5    Sanchez-Montero, J.M.6    Ponz, F.7
  • 51
    • 84872169330 scopus 로고    scopus 로고
    • Increased tumor homing and tissue penetration of the filamentous plant viral nanoparticle Potato virus X
    • Shukla S, Ablack AL, Wen AM, Lee KL, Lewis JD, Steinmetz NF. Increased tumor homing and tissue penetration of the filamentous plant viral nanoparticle Potato virus X. Mol Pharm 2013, 10:33–42.
    • (2013) Mol Pharm , vol.10 , pp. 33-42
    • Shukla, S.1    Ablack, A.L.2    Wen, A.M.3    Lee, K.L.4    Lewis, J.D.5    Steinmetz, N.F.6
  • 52
    • 0038205586 scopus 로고    scopus 로고
    • Cowpea mosaic virus-based chimaeras. Effects of inserted peptides on the phenotype, host range, and transmissibility of the modified viruses
    • Porta C, Spall VE, Findlay KC, Gergerich RC, Farrance CE, Lomonossoff GP. Cowpea mosaic virus-based chimaeras. Effects of inserted peptides on the phenotype, host range, and transmissibility of the modified viruses. Virology 2003, 310:50–63.
    • (2003) Virology , vol.310 , pp. 50-63
    • Porta, C.1    Spall, V.E.2    Findlay, K.C.3    Gergerich, R.C.4    Farrance, C.E.5    Lomonossoff, G.P.6
  • 53
    • 33749065356 scopus 로고    scopus 로고
    • Peptide display on Potato virus X: molecular features of the coat protein-fused peptide affecting cell-to-cell and phloem movement of chimeric virus particles
    • Lico C, Capuano F, Renzone G, Donini M, Marusic C, Scaloni A, Benvenuto E, Baschieri S. Peptide display on Potato virus X: molecular features of the coat protein-fused peptide affecting cell-to-cell and phloem movement of chimeric virus particles. J Gen Virol 2006, 87:3103–3112.
    • (2006) J Gen Virol , vol.87 , pp. 3103-3112
    • Lico, C.1    Capuano, F.2    Renzone, G.3    Donini, M.4    Marusic, C.5    Scaloni, A.6    Benvenuto, E.7    Baschieri, S.8
  • 54
    • 0034099316 scopus 로고    scopus 로고
    • Influence of three-dimensional structure on the immunogenicity of a peptide expressed on the surface of a plant virus
    • Taylor KM, Lin T, Porta C, Mosser AG, Giesing HA, Lomonossoff GP, Johnson JE. Influence of three-dimensional structure on the immunogenicity of a peptide expressed on the surface of a plant virus. J Mol Recognit 2000, 13:71–82.
    • (2000) J Mol Recognit , vol.13 , pp. 71-82
    • Taylor, K.M.1    Lin, T.2    Porta, C.3    Mosser, A.G.4    Giesing, H.A.5    Lomonossoff, G.P.6    Johnson, J.E.7
  • 57
  • 58
    • 0036690067 scopus 로고    scopus 로고
    • A chemoselective biomolecular template for assembling diverse nanotubular materials
    • Demir MaS MH. A chemoselective biomolecular template for assembling diverse nanotubular materials. Nanotechnology 2002, 13:541.
    • (2002) Nanotechnology , vol.13 , pp. 541
    • Demir MaS, M.H.1
  • 61
    • 33646351280 scopus 로고    scopus 로고
    • Cowpea mosaic virus for material fabrication: addressable carboxylate groups on a programmable nanoscaffold
    • Steinmetz NF, Lomonossoff GP, Evans DJ. Cowpea mosaic virus for material fabrication: addressable carboxylate groups on a programmable nanoscaffold. Langmuir 2006, 22:3488–3490.
    • (2006) Langmuir , vol.22 , pp. 3488-3490
    • Steinmetz, N.F.1    Lomonossoff, G.P.2    Evans, D.J.3
  • 62
    • 0035989983 scopus 로고    scopus 로고
    • Natural supramolecular building blocks. Wild-type cowpea mosaic virus
    • Wang Q, Kaltgrad E, Lin T, Johnson JE, Finn MG. Natural supramolecular building blocks. Wild-type cowpea mosaic virus. Chem Biol 2002, 9:805–811.
    • (2002) Chem Biol , vol.9 , pp. 805-811
    • Wang, Q.1    Kaltgrad, E.2    Lin, T.3    Johnson, J.E.4    Finn, M.G.5
  • 64
    • 27944488746 scopus 로고    scopus 로고
    • Accelerated bioorthogonal conjugation: A practical method for the Ligation of diverse functional molecules to a polyvalent virus scaffold
    • Sen Gupta S, Kuzelka J, Singh P, Lewis WG, Manchester M, Finn MG. Accelerated bioorthogonal conjugation: A practical method for the Ligation of diverse functional molecules to a polyvalent virus scaffold. Bioconjug Chem 2005, 16:1572–1579.
    • (2005) Bioconjug Chem , vol.16 , pp. 1572-1579
    • Sen Gupta, S.1    Kuzelka, J.2    Singh, P.3    Lewis, W.G.4    Manchester, M.5    Finn, M.G.6
  • 65
    • 71049187676 scopus 로고    scopus 로고
    • Interaction of Cowpea mosaic virus (CPMV) nanoparticles with antigen presenting cells in vitro and in vivo
    • Gonzalez MJ, Plummer EM, Rae CS, Manchester M. Interaction of Cowpea mosaic virus (CPMV) nanoparticles with antigen presenting cells in vitro and in vivo. PLoS One 2009, 4:e7981.
    • (2009) PLoS One , vol.4
    • Gonzalez, M.J.1    Plummer, E.M.2    Rae, C.S.3    Manchester, M.4
  • 66
    • 0035989991 scopus 로고    scopus 로고
    • Natural supramolecular building blocks. Cysteine-added mutants of cowpea mosaic virus
    • Wang Q, Lin T, Johnson JE, Finn MG. Natural supramolecular building blocks. Cysteine-added mutants of cowpea mosaic virus. Chem Biol 2002, 9:813–819.
    • (2002) Chem Biol , vol.9 , pp. 813-819
    • Wang, Q.1    Lin, T.2    Johnson, J.E.3    Finn, M.G.4
  • 67
    • 1942529507 scopus 로고    scopus 로고
    • Crosslinking of and coupling to viral capsid proteins by tyrosine oxidation
    • Meunier S, Strable E, Finn MG. Crosslinking of and coupling to viral capsid proteins by tyrosine oxidation. Chem Biol 2004, 11:319–326.
    • (2004) Chem Biol , vol.11 , pp. 319-326
    • Meunier, S.1    Strable, E.2    Finn, M.G.3
  • 69
    • 3042688833 scopus 로고    scopus 로고
    • New addresses on an addressable virus nanoblock; uniquely reactive Lys residues on cowpea mosaic virus
    • Chatterji A, Ochoa WF, Paine M, Ratna BR, Johnson JE, Lin T. New addresses on an addressable virus nanoblock; uniquely reactive Lys residues on cowpea mosaic virus. Chem Biol 2004, 11:855–863.
    • (2004) Chem Biol
    • Chatterji, A.1    Ochoa, W.F.2    Paine, M.3    Ratna, B.R.4    Johnson, J.E.5    Lin, T.6
  • 70
    • 58349101316 scopus 로고    scopus 로고
    • Structure-based engineering of an icosahedral virus for nanomedicine and nanotechnology
    • Steinmetz NF, Lin T, Lomonossoff GP, Johnson JE. Structure-based engineering of an icosahedral virus for nanomedicine and nanotechnology. Curr Top Microbiol Immunol 2009, 327:23–58.
    • (2009) Curr Top Microbiol Immunol , vol.327 , pp. 23-58
    • Steinmetz, N.F.1    Lin, T.2    Lomonossoff, G.P.3    Johnson, J.E.4
  • 71
  • 72
    • 74249093492 scopus 로고    scopus 로고
    • Environmentally benign synthesis of virus-templated, monodisperse, iron-platinum nanoparticles
    • Shah SN, Steinmetz NF, Aljabali AA, Lomonossoff GP, Evans DJ. Environmentally benign synthesis of virus-templated, monodisperse, iron-platinum nanoparticles. Dalton Trans 2009, 40:8479–8480.
    • (2009) Dalton Trans , vol.40 , pp. 8479-8480
    • Shah, S.N.1    Steinmetz, N.F.2    Aljabali, A.A.3    Lomonossoff, G.P.4    Evans, D.J.5
  • 73
    • 0032516197 scopus 로고    scopus 로고
    • M Host–guest encapsulation of materials by assembled virus protein cages
    • Douglas TY. M Host–guest encapsulation of materials by assembled virus protein cages. Nature 1998, 393:152–155.
    • (1998) Nature , vol.393 , pp. 152-155
    • Douglas, T.Y.1
  • 75
    • 84980407604 scopus 로고    scopus 로고
    • Design of virus-based nanomaterials for medicine, biotechnology, and energy
    • Wen AM, Steinmetz NF. Design of virus-based nanomaterials for medicine, biotechnology, and energy. Chem Soc Rev 2016, 45:4074–4126.
    • (2016) Chem Soc Rev , vol.45 , pp. 4074-4126
    • Wen, A.M.1    Steinmetz, N.F.2
  • 77
    • 0037896322 scopus 로고    scopus 로고
    • Detection and characterization of an intermediate conformation during the divalent ion-dependent swelling of tomato bushy stunt virus
    • Perez J, Defrenne S, Witz J, Vachette P. Detection and characterization of an intermediate conformation during the divalent ion-dependent swelling of tomato bushy stunt virus. Cell Mol Biol (Noisy-le-Grand) 2000, 46:937–948.
    • (2000) Cell Mol Biol (Noisy-le-Grand) , vol.46 , pp. 937-948
    • Perez, J.1    Defrenne, S.2    Witz, J.3    Vachette, P.4
  • 78
    • 84877749467 scopus 로고    scopus 로고
    • A plant derived multifunctional tool for nanobiotechnology based on Tomato bushy stunt virus
    • Grasso S, Lico C, Imperatori F, Santi L. A plant derived multifunctional tool for nanobiotechnology based on Tomato bushy stunt virus. Transgenic Res 2013, 22:519–535.
    • (2013) Transgenic Res , vol.22 , pp. 519-535
    • Grasso, S.1    Lico, C.2    Imperatori, F.3    Santi, L.4
  • 79
    • 37249089864 scopus 로고    scopus 로고
    • Infusion of dye molecules into Red clover necrotic mosaic virus
    • Loo L, Guenther RH, Lommel SA, Franzen S. Infusion of dye molecules into Red clover necrotic mosaic virus. Chem Commun (Camb) 2008, 88-90. DOI: 10.1039/B714748A.
    • (2008) Chem Commun (Camb) , vol.88-90
    • Loo, L.1    Guenther, R.H.2    Lommel, S.A.3    Franzen, S.4
  • 83
    • 84887033129 scopus 로고    scopus 로고
    • Infusion of imaging and therapeutic molecules into the plant virus-based carrier cowpea mosaic virus: cargo-loading and delivery
    • Yildiz I, Lee KL, Chen K, Shukla S, Steinmetz NF. Infusion of imaging and therapeutic molecules into the plant virus-based carrier cowpea mosaic virus: cargo-loading and delivery. J Control Release 2013, 172:568–578.
    • (2013) J Control Release , vol.172 , pp. 568-578
    • Yildiz, I.1    Lee, K.L.2    Chen, K.3    Shukla, S.4    Steinmetz, N.F.5
  • 86
    • 0016697169 scopus 로고
    • The conformation of the RNA in cowpea chlorotic mottle virus: dye-binding studies
    • Adolph KW. The conformation of the RNA in cowpea chlorotic mottle virus: dye-binding studies. Eur J Biochem 1975, 53:449–455.
    • (1975) Eur J Biochem , vol.53 , pp. 449-455
    • Adolph, K.W.1
  • 87
    • 0036307741 scopus 로고    scopus 로고
    • The mechanism and pathway of pH induced swelling in cowpea chlorotic mottle virus
    • Tama F, Brooks CL 3rd. The mechanism and pathway of pH induced swelling in cowpea chlorotic mottle virus. J Mol Biol 2002, 318:733–747.
    • (2002) J Mol Biol , vol.318 , pp. 733-747
    • Tama, F.1    Brooks, C.L.2
  • 90
    • 84950151283 scopus 로고    scopus 로고
    • Sortase A-mediated N-terminal modification of cowpea chlorotic mottle virus for highly efficient cargo loading
    • Schoonen L, Pille J, Borrmann A, Nolte RJ, van Hest JC. Sortase A-mediated N-terminal modification of cowpea chlorotic mottle virus for highly efficient cargo loading. Bioconjug Chem 2015, 26:2429–2434.
    • (2015) Bioconjug Chem , vol.26 , pp. 2429-2434
    • Schoonen, L.1    Pille, J.2    Borrmann, A.3    Nolte, R.J.4    van Hest, J.C.5
  • 93
    • 84859816277 scopus 로고    scopus 로고
    • Encapsidation of DNA, a protein and a fluorophore into virus-like particles by the capsid protein of cucumber mosaic virus
    • Lu X, Thompson JR, Perry KL. Encapsidation of DNA, a protein and a fluorophore into virus-like particles by the capsid protein of cucumber mosaic virus. J Gen Virol 2012, 93:1120–1126.
    • (2012) J Gen Virol , vol.93 , pp. 1120-1126
    • Lu, X.1    Thompson, J.R.2    Perry, K.L.3
  • 95
    • 0027159063 scopus 로고
    • Differential expression of the epidermal growth factor receptor and its ligands in primary non-small cell lung cancers and adjacent benign lung
    • Rusch V, Baselga J, Cordon-Cardo C, Orazem J, Zaman M, Hoda S, McIntosh J, Kurie J, Dmitrovsky E. Differential expression of the epidermal growth factor receptor and its ligands in primary non-small cell lung cancers and adjacent benign lung. Cancer Res 1993, 53:2379–2385.
    • (1993) Cancer Res , vol.53 , pp. 2379-2385
    • Rusch, V.1    Baselga, J.2    Cordon-Cardo, C.3    Orazem, J.4    Zaman, M.5    Hoda, S.6    McIntosh, J.7    Kurie, J.8    Dmitrovsky, E.9
  • 96
    • 0028301752 scopus 로고
    • Differential regulation of folate receptor isoforms in normal and malignant tissues in vivo and in established cell lines. Physiologic and clinical implications
    • Ross JF, Chaudhuri PK, Ratnam M. Differential regulation of folate receptor isoforms in normal and malignant tissues in vivo and in established cell lines. Physiologic and clinical implications. Cancer 1994, 73:2432–2443.
    • (1994) Cancer , vol.73 , pp. 2432-2443
    • Ross, J.F.1    Chaudhuri, P.K.2    Ratnam, M.3
  • 100
    • 84889595508 scopus 로고    scopus 로고
    • Biodistribution, pharmacokinetics, and blood compatibility of native and PEGylated tobacco mosaic virus nano-rods and -spheres in mice
    • Bruckman MA, Randolph LN, VanMeter A, Hern S, Shoffstall AJ, Taurog RE, Steinmetz NF. Biodistribution, pharmacokinetics, and blood compatibility of native and PEGylated tobacco mosaic virus nano-rods and -spheres in mice. Virology 2014, 449:163–173.
    • (2014) Virology , vol.449 , pp. 163-173
    • Bruckman, M.A.1    Randolph, L.N.2    VanMeter, A.3    Hern, S.4    Shoffstall, A.J.5    Taurog, R.E.6    Steinmetz, N.F.7
  • 103
    • 65249114149 scopus 로고    scopus 로고
    • PEGylated viral nanoparticles for biomedicine: the impact of PEG chain length on VNP cell interactions in vitro and ex vivo
    • Steinmetz NF, Manchester M. PEGylated viral nanoparticles for biomedicine: the impact of PEG chain length on VNP cell interactions in vitro and ex vivo. Biomacromolecules 2009, 10:784–792.
    • (2009) Biomacromolecules , vol.10 , pp. 784-792
    • Steinmetz, N.F.1    Manchester, M.2
  • 105
    • 85001513945 scopus 로고    scopus 로고
    • High aspect ratio nanotubes formed by tobacco mosaic virus for delivery of photodynamic agents targeting melanoma
    • Lee KL, Carpenter BL, Wen AM, Ghiladi RA, Steinmetz NF. High aspect ratio nanotubes formed by tobacco mosaic virus for delivery of photodynamic agents targeting melanoma. ACS Biomat Sci Eng 2016, 2:838–844.
    • (2016) ACS Biomat Sci Eng , vol.2 , pp. 838-844
    • Lee, K.L.1    Carpenter, B.L.2    Wen, A.M.3    Ghiladi, R.A.4    Steinmetz, N.F.5
  • 108
    • 34548267667 scopus 로고    scopus 로고
    • Endocytic mechanisms for targeted drug delivery
    • Bareford LM, Swaan PW. Endocytic mechanisms for targeted drug delivery. Adv Drug Deliv Rev 2007, 59:748–758.
    • (2007) Adv Drug Deliv Rev , vol.59 , pp. 748-758
    • Bareford, L.M.1    Swaan, P.W.2
  • 109
    • 34347347264 scopus 로고    scopus 로고
    • Folic acid-conjugated protein cages of a plant virus: a novel delivery platform for doxorubicin
    • Ren Y, Wong SM, Lim LY. Folic acid-conjugated protein cages of a plant virus: a novel delivery platform for doxorubicin. Bioconjug Chem 2007, 18:836–843.
    • (2007) Bioconjug Chem , vol.18 , pp. 836-843
    • Ren, Y.1    Wong, S.M.2    Lim, L.Y.3
  • 112
    • 80355129638 scopus 로고    scopus 로고
    • Evaluation of nanoparticle uptake in tumors in real time using intravital imaging
    • Cho CF, Ablack A, Leong HS, Zijlstra A, Lewis J. Evaluation of nanoparticle uptake in tumors in real time using intravital imaging. J Vis Exp 2011, 21:2808.
    • (2011) J Vis Exp , vol.21 , pp. 2808
    • Cho, C.F.1    Ablack, A.2    Leong, H.S.3    Zijlstra, A.4    Lewis, J.5
  • 114
    • 84923259508 scopus 로고    scopus 로고
    • Detection and imaging of aggressive cancer cells using an epidermal growth factor receptor (EGFR)-targeted filamentous plant virus-based nanoparticle
    • Chariou PL, Lee KL, Wen AM, Gulati NM, Stewart PL, Steinmetz NF. Detection and imaging of aggressive cancer cells using an epidermal growth factor receptor (EGFR)-targeted filamentous plant virus-based nanoparticle. Bioconjug Chem 2015, 26:262–269.
    • (2015) Bioconjug Chem , vol.26 , pp. 262-269
    • Chariou, P.L.1    Lee, K.L.2    Wen, A.M.3    Gulati, N.M.4    Stewart, P.L.5    Steinmetz, N.F.6
  • 115
    • 84930641245 scopus 로고    scopus 로고
    • Two-photon absorbing dyes with minimal autofluorescence in tissue imaging: application to in vivo imaging of amyloid-beta plaques with a negligible background signal
    • Kim D, Moon H, Baik SH, Singha S, Jun YW, Wang T, Kim KH, Park BS, Jung J, Mook-Jung I, et al. Two-photon absorbing dyes with minimal autofluorescence in tissue imaging: application to in vivo imaging of amyloid-beta plaques with a negligible background signal. J Am Chem Soc 2015, 137:6781–6789.
    • (2015) J Am Chem Soc , vol.137 , pp. 6781-6789
    • Kim, D.1    Moon, H.2    Baik, S.H.3    Singha, S.4    Jun, Y.W.5    Wang, T.6    Kim, K.H.7    Park, B.S.8    Jung, J.9    Mook-Jung, I.10
  • 116
    • 0025342635 scopus 로고
    • Two-photon laser scanning fluorescence microscopy
    • Denk W, Strickler JH, Webb WW. Two-photon laser scanning fluorescence microscopy. Science 1990, 248:73–76.
    • (1990) Science , vol.248 , pp. 73-76
    • Denk, W.1    Strickler, J.H.2    Webb, W.W.3
  • 117
    • 0032820395 scopus 로고    scopus 로고
    • Long-term two-photon fluorescence imaging of mammalian embryos without compromising viability
    • Squirrell JM, Wokosin DL, White JG, Bavister BD. Long-term two-photon fluorescence imaging of mammalian embryos without compromising viability. Nat Biotechnol 1999, 17:763–767.
    • (1999) Nat Biotechnol , vol.17 , pp. 763-767
    • Squirrell, J.M.1    Wokosin, D.L.2    White, J.G.3    Bavister, B.D.4
  • 119
    • 84884406188 scopus 로고    scopus 로고
    • Localization of gadolinium-loaded CPMV to sites of inflammation during central nervous system autoimmunity
    • Shriver LP, Plummer EM, Thomas DM, Ho S, Manchester M. Localization of gadolinium-loaded CPMV to sites of inflammation during central nervous system autoimmunity. J Mater Chem B 2013, 1:5256–5263.
    • (2013) J Mater Chem B , vol.1 , pp. 5256-5263
    • Shriver, L.P.1    Plummer, E.M.2    Thomas, D.M.3    Ho, S.4    Manchester, M.5
  • 120
    • 84887082425 scopus 로고    scopus 로고
    • Engineering Gd-loaded nanoparticles to enhance MRI sensitivity via T(1) shortening
    • Bruckman MA, Yu X, Steinmetz NF. Engineering Gd-loaded nanoparticles to enhance MRI sensitivity via T(1) shortening. Nanotechnology 2013, 24:462001.
    • (2013) Nanotechnology , vol.24 , pp. 462001
    • Bruckman, M.A.1    Yu, X.2    Steinmetz, N.F.3
  • 121
    • 0027989588 scopus 로고
    • Microevolution of Sabin 1 strain in vitro and genetic stability of oral poliovirus vaccine
    • Rezapkin GV, Chumakov KM, Lu Z, Ran Y, Dragunsky EM, Levenbook IS. Microevolution of Sabin 1 strain in vitro and genetic stability of oral poliovirus vaccine. Virology 1994, 202:370–378.
    • (1994) Virology , vol.202 , pp. 370-378
    • Rezapkin, G.V.1    Chumakov, K.M.2    Lu, Z.3    Ran, Y.4    Dragunsky, E.M.5    Levenbook, I.S.6
  • 124
    • 79551699386 scopus 로고    scopus 로고
    • Viral nanoparticles and virus-like particles: platforms for contemporary vaccine design
    • Plummer EM, Manchester M. Viral nanoparticles and virus-like particles: platforms for contemporary vaccine design. WIREs Nanomed Nanobiotechnol 2011, 3:174–196.
    • (2011) WIREs Nanomed Nanobiotechnol , vol.3 , pp. 174-196
    • Plummer, E.M.1    Manchester, M.2
  • 126
    • 0028122633 scopus 로고
    • Development of cowpea mosaic virus as a high-yielding system for the presentation of foreign peptides
    • Porta C, Spall VE, Loveland J, Johnson JE, Barker PJ, Lomonossoff GP. Development of cowpea mosaic virus as a high-yielding system for the presentation of foreign peptides. Virology 1994, 202:949–955.
    • (1994) Virology , vol.202 , pp. 949-955
    • Porta, C.1    Spall, V.E.2    Loveland, J.3    Johnson, J.E.4    Barker, P.J.5    Lomonossoff, G.P.6
  • 127
    • 0028923242 scopus 로고
    • Human immunodeficiency virus type 1-neutralizing antibodies raised to a glycoprotein 41 peptide expressed on the surface of a plant virus
    • McLain L, Porta C, Lomonossoff GP, Durrani Z, Dimmock NJ. Human immunodeficiency virus type 1-neutralizing antibodies raised to a glycoprotein 41 peptide expressed on the surface of a plant virus. AIDS Res Hum Retroviruses 1995, 11:327–334.
    • (1995) AIDS Res Hum Retroviruses , vol.11 , pp. 327-334
    • McLain, L.1    Porta, C.2    Lomonossoff, G.P.3    Durrani, Z.4    Dimmock, N.J.5
  • 130
    • 0028800716 scopus 로고
    • Systemic production of foreign peptides on the particle surface of tobacco mosaic virus
    • Sugiyama Y, Hamamoto H, Takemoto S, Watanabe Y, Okada Y. Systemic production of foreign peptides on the particle surface of tobacco mosaic virus. FEBS Lett 1995, 359:247–250.
    • (1995) FEBS Lett , vol.359 , pp. 247-250
    • Sugiyama, Y.1    Hamamoto, H.2    Takemoto, S.3    Watanabe, Y.4    Okada, Y.5
  • 131
    • 0033529329 scopus 로고    scopus 로고
    • Protective immunity against murine hepatitis virus (MHV) induced by intranasal or subcutaneous administration of hybrids of tobacco mosaic virus that carries an MHV epitope
    • Koo M, Bendahmane M, Lettieri GA, Paoletti AD, Lane TE, Fitchen JH, Buchmeier MJ, Beachy RN. Protective immunity against murine hepatitis virus (MHV) induced by intranasal or subcutaneous administration of hybrids of tobacco mosaic virus that carries an MHV epitope. Proc Natl Acad Sci U S A 1999, 96:7774–7779.
    • (1999) Proc Natl Acad Sci U S A , vol.96 , pp. 7774-7779
    • Koo, M.1    Bendahmane, M.2    Lettieri, G.A.3    Paoletti, A.D.4    Lane, T.E.5    Fitchen, J.H.6    Buchmeier, M.J.7    Beachy, R.N.8
  • 132
    • 84930634186 scopus 로고    scopus 로고
    • Enhancing antibody response against small molecular hapten with tobacco mosaic virus as a polyvalent carrier
    • Zhao X, Chen L, Luckanagul JA, Zhang X, Lin Y, Wang Q. Enhancing antibody response against small molecular hapten with tobacco mosaic virus as a polyvalent carrier. Chembiochem 2015, 16:1279–1283.
    • (2015) Chembiochem , vol.16 , pp. 1279-1283
    • Zhao, X.1    Chen, L.2    Luckanagul, J.A.3    Zhang, X.4    Lin, Y.5    Wang, Q.6
  • 133
    • 84872610842 scopus 로고    scopus 로고
    • Virus-like particles displaying envelope domain III of dengue virus type 2 induce virus-specific antibody response in mice
    • Arora U, Tyagi P, Swaminathan S, Khanna N. Virus-like particles displaying envelope domain III of dengue virus type 2 induce virus-specific antibody response in mice. Vaccine 2013, 31:873–878.
    • (2013) Vaccine , vol.31 , pp. 873-878
    • Arora, U.1    Tyagi, P.2    Swaminathan, S.3    Khanna, N.4
  • 135
    • 84855584421 scopus 로고    scopus 로고
    • Induction of insert-specific immune response in mice by hamster polyomavirus VP1 derived virus-like particles carrying LCMV GP33 CTL epitope
    • Mazeike E, Gedvilaite A, Blohm U. Induction of insert-specific immune response in mice by hamster polyomavirus VP1 derived virus-like particles carrying LCMV GP33 CTL epitope. Virus Res 2012, 163:2–10.
    • (2012) Virus Res , vol.163 , pp. 2-10
    • Mazeike, E.1    Gedvilaite, A.2    Blohm, U.3
  • 136
    • 79955917510 scopus 로고    scopus 로고
    • Low-dose oral immunization with lyophilized tissue of herbicide-resistant lettuce expressing hepatitis B surface antigen for prototype plant-derived vaccine tablet formulation
    • Pniewski T, Kapusta J, Bociag P, Wojciechowicz J, Kostrzak A, Gdula M, Fedorowicz-Stronska O, Wojcik P, Otta H, Samardakiewicz S, et al. Low-dose oral immunization with lyophilized tissue of herbicide-resistant lettuce expressing hepatitis B surface antigen for prototype plant-derived vaccine tablet formulation. J Appl Genet 2011, 52:125–136.
    • (2011) J Appl Genet , vol.52 , pp. 125-136
    • Pniewski, T.1    Kapusta, J.2    Bociag, P.3    Wojciechowicz, J.4    Kostrzak, A.5    Gdula, M.6    Fedorowicz-Stronska, O.7    Wojcik, P.8    Otta, H.9    Samardakiewicz, S.10
  • 138
    • 34247846212 scopus 로고    scopus 로고
    • Immunogenicity of papaya mosaic virus-like particles fused to a hepatitis C virus epitope: evidence for the critical function of multimerization
    • Denis J, Majeau N, Acosta-Ramirez E, Savard C, Bedard MC, Simard S, Lecours K, Bolduc M, Pare C, Willems B, et al. Immunogenicity of papaya mosaic virus-like particles fused to a hepatitis C virus epitope: evidence for the critical function of multimerization. Virology 2007, 363:59–68.
    • (2007) Virology , vol.363 , pp. 59-68
    • Denis, J.1    Majeau, N.2    Acosta-Ramirez, E.3    Savard, C.4    Bedard, M.C.5    Simard, S.6    Lecours, K.7    Bolduc, M.8    Pare, C.9    Willems, B.10
  • 139
  • 140
    • 34248172560 scopus 로고    scopus 로고
    • Optimization of human papillomavirus type 16 (HPV-16) L1 expression in plants: comparison of the suitability of different HPV-16 L1 gene variants and different cell-compartment localization
    • Maclean J, Koekemoer M, Olivier AJ, Stewart D, Hitzeroth II, Rademacher T, Fischer R, Williamson AL, Rybicki EP. Optimization of human papillomavirus type 16 (HPV-16) L1 expression in plants: comparison of the suitability of different HPV-16 L1 gene variants and different cell-compartment localization. J Gen Virol 2007, 88:1460–1469.
    • (2007) J Gen Virol , vol.88 , pp. 1460-1469
    • Maclean, J.1    Koekemoer, M.2    Olivier, A.J.3    Stewart, D.4    Hitzeroth, I.I.5    Rademacher, T.6    Fischer, R.7    Williamson, A.L.8    Rybicki, E.P.9
  • 142
    • 84859426694 scopus 로고    scopus 로고
    • Comparative analysis of recombinant Human Papillomavirus 8 L1 production in plants by a variety of expression systems and purification methods
    • Matic S, Masenga V, Poli A, Rinaldi R, Milne RG, Vecchiati M, Noris E. Comparative analysis of recombinant Human Papillomavirus 8 L1 production in plants by a variety of expression systems and purification methods. Plant Biotechnol J 2012, 10:410–421.
    • (2012) Plant Biotechnol J , vol.10 , pp. 410-421
    • Matic, S.1    Masenga, V.2    Poli, A.3    Rinaldi, R.4    Milne, R.G.5    Vecchiati, M.6    Noris, E.7
  • 143
    • 84884413506 scopus 로고    scopus 로고
    • Immunogenic assessment of plant-produced human papillomavirus type 16 L1/L2 chimaeras
    • Pineo CB, Hitzeroth II, Rybicki EP. Immunogenic assessment of plant-produced human papillomavirus type 16 L1/L2 chimaeras. Plant Biotechnol J 2013, 11:964–975.
    • (2013) Plant Biotechnol J , vol.11 , pp. 964-975
    • Pineo, C.B.1    Hitzeroth, I.I.2    Rybicki, E.P.3
  • 144
    • 84866909567 scopus 로고    scopus 로고
    • In planta production of a candidate vaccine against bovine papillomavirus type 1
    • Love AJ, Chapman SN, Matic S, Noris E, Lomonossoff GP, Taliansky M. In planta production of a candidate vaccine against bovine papillomavirus type 1. Planta 2012, 236:1305–1313.
    • (2012) Planta , vol.236 , pp. 1305-1313
    • Love, A.J.1    Chapman, S.N.2    Matic, S.3    Noris, E.4    Lomonossoff, G.P.5    Taliansky, M.6
  • 146
    • 84901759333 scopus 로고    scopus 로고
    • Norovirus Narita 104 virus-like particles expressed in Nicotiana benthamiana induce serum and mucosal immune responses
    • Mathew LG, Herbst-Kralovetz MM, Mason HS. Norovirus Narita 104 virus-like particles expressed in Nicotiana benthamiana induce serum and mucosal immune responses. Biomed Res Int 2014, 2014:807539.
    • (2014) Biomed Res Int , vol.2014 , pp. 807539
    • Mathew, L.G.1    Herbst-Kralovetz, M.M.2    Mason, H.S.3
  • 147
    • 78751648047 scopus 로고    scopus 로고
    • Immunogenicity and virus-like particle formation of rotavirus capsid proteins produced in transgenic plants
    • Yang Y, Li X, Yang H, Qian Y, Zhang Y, Fang R, Chen X. Immunogenicity and virus-like particle formation of rotavirus capsid proteins produced in transgenic plants. Sci China Life Sci 2011, 54:82–89.
    • (2011) Sci China Life Sci , vol.54 , pp. 82-89
    • Yang, Y.1    Li, X.2    Yang, H.3    Qian, Y.4    Zhang, Y.5    Fang, R.6    Chen, X.7
  • 148
    • 84882584540 scopus 로고    scopus 로고
    • A method for rapid production of heteromultimeric protein complexes in plants: assembly of protective bluetongue virus-like particles
    • Thuenemann EC, Meyers AE, Verwey J, Rybicki EP, Lomonossoff GP. A method for rapid production of heteromultimeric protein complexes in plants: assembly of protective bluetongue virus-like particles. Plant Biotechnol J 2013, 11:839–846.
    • (2013) Plant Biotechnol J , vol.11 , pp. 839-846
    • Thuenemann, E.C.1    Meyers, A.E.2    Verwey, J.3    Rybicki, E.P.4    Lomonossoff, G.P.5
  • 150
    • 84954115169 scopus 로고    scopus 로고
    • Molecular pharming – VLPs made in plants
    • Marsian J, Lomonossoff GP. Molecular pharming – VLPs made in plants. Curr Opin Biotechnol 2016, 37:201–206.
    • (2016) Curr Opin Biotechnol , vol.37 , pp. 201-206
    • Marsian, J.1    Lomonossoff, G.P.2
  • 151
    • 0033076481 scopus 로고    scopus 로고
    • Inorganic-organic nanotube composites from template mineralization of tobacco mosaic virus
    • Shenton W, Douglas T, Young M, Stubbs G, Mann S. Inorganic-organic nanotube composites from template mineralization of tobacco mosaic virus. Adv Mater 1999, 11:253–256.
    • (1999) Adv Mater , vol.11 , pp. 253-256
    • Shenton, W.1    Douglas, T.2    Young, M.3    Stubbs, G.4    Mann, S.5
  • 152
    • 79952975902 scopus 로고    scopus 로고
    • The art of engineering viral nanoparticles
    • Pokorski JK, Steinmetz NF. The art of engineering viral nanoparticles. Mol Pharm 2011, 8:29–43.
    • (2011) Mol Pharm , vol.8 , pp. 29-43
    • Pokorski, J.K.1    Steinmetz, N.F.2
  • 153
    • 0001724794 scopus 로고    scopus 로고
    • Virus particles as templates for materials synthesis
    • Douglas T, Young M. Virus particles as templates for materials synthesis. Adv Mater 1999, 11:679–681.
    • (1999) Adv Mater , vol.11 , pp. 679-681
    • Douglas, T.1    Young, M.2
  • 154
    • 77950613476 scopus 로고    scopus 로고
    • Cowpea mosaic virus unmodified empty viruslike particles loaded with metal and metal oxide
    • Aljabali AA, Sainsbury F, Lomonossoff GP, Evans DJ. Cowpea mosaic virus unmodified empty viruslike particles loaded with metal and metal oxide. Small 2010, 6:818–821.
    • (2010) Small , vol.6 , pp. 818-821
    • Aljabali, A.A.1    Sainsbury, F.2    Lomonossoff, G.P.3    Evans, D.J.4
  • 155
    • 77949422340 scopus 로고    scopus 로고
    • Protein cages, rings and tubes: useful components of future nanodevices?
    • Heddle JG. Protein cages, rings and tubes: useful components of future nanodevices? Nanotechnol Sci Appl 2008, 1:67–78.
    • (2008) Nanotechnol Sci Appl , vol.1 , pp. 67-78
    • Heddle, J.G.1
  • 157
    • 34247495642 scopus 로고    scopus 로고
    • Digital memory device based on tobacco mosaic virus conjugated with nanoparticles
    • Tseng RJ, Tsai CL, Ma LP, Ouyang JY. Digital memory device based on tobacco mosaic virus conjugated with nanoparticles. Nat Nanotechnol 2006, 1:72–77.
    • (2006) Nat Nanotechnol , vol.1 , pp. 72-77
    • Tseng, R.J.1    Tsai, C.L.2    Ma, L.P.3    Ouyang, J.Y.4
  • 160
    • 34249748471 scopus 로고    scopus 로고
    • Synthesis of CoPt and FePt3 nanowires using the central channel of tobacco mosaic virus as a biotemplate
    • Tsukamoto R, Muraoka M, Seki M, Tabata H, Yamashita I. Synthesis of CoPt and FePt3 nanowires using the central channel of tobacco mosaic virus as a biotemplate. Chem Mater 2007, 19:2389–2391.
    • (2007) Chem Mater , vol.19 , pp. 2389-2391
    • Tsukamoto, R.1    Muraoka, M.2    Seki, M.3    Tabata, H.4    Yamashita, I.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.