메뉴 건너뛰기




Volumn 120, Issue , 2017, Pages 126-138

Engineering hepatitis B virus core particles for targeting HER2 receptors in vitro and in vivo

Author keywords

Active targeting; Affibody; Hepatitis B virus core particles; Human epidermal growth factor receptor 2; Virus like particles

Indexed keywords

AMINO ACIDS; BINS; CELLS; DISEASES; NANOPARTICLES; ONCOLOGY; PROTEINS; TUMORS;

EID: 85007545211     PISSN: 01429612     EISSN: 18785905     Source Type: Journal    
DOI: 10.1016/j.biomaterials.2016.12.012     Document Type: Article
Times cited : (25)

References (78)
  • 6
    • 84983688435 scopus 로고    scopus 로고
    • The true story and advantages of the famous Hepatitis B virus core particles: outlook 2016
    • [6] Pumpens, P., Grens, E., The true story and advantages of the famous Hepatitis B virus core particles: outlook 2016. Mol. Biol. 50:4 (2016), 489–509.
    • (2016) Mol. Biol. , vol.50 , Issue.4 , pp. 489-509
    • Pumpens, P.1    Grens, E.2
  • 7
    • 12344258790 scopus 로고    scopus 로고
    • Recombinant viral capsids as an efficient vehicle of oligonucleotide delivery into cells
    • [7] Cooper, A., Shaul, Y., Recombinant viral capsids as an efficient vehicle of oligonucleotide delivery into cells. Biochem. Biophys. Res. Commun. 327:4 (2005), 1094–1099.
    • (2005) Biochem. Biophys. Res. Commun. , vol.327 , Issue.4 , pp. 1094-1099
    • Cooper, A.1    Shaul, Y.2
  • 8
    • 78651384693 scopus 로고    scopus 로고
    • The arginine clusters of the carboxy-terminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication
    • [8] Lewellyn, E.B., Loeb, D.D., The arginine clusters of the carboxy-terminal domain of the core protein of hepatitis B virus make pleiotropic contributions to genome replication. J. Virol. 85:3 (2011), 1298–1309.
    • (2011) J. Virol. , vol.85 , Issue.3 , pp. 1298-1309
    • Lewellyn, E.B.1    Loeb, D.D.2
  • 9
    • 0033517792 scopus 로고    scopus 로고
    • A theoretical model successfully identifies features of hepatitis B virus capsid assembly
    • [9] Zlotnick, A., Johnson, J.M., Wingfield, P.W., Stahl, S.J., Endres, D., A theoretical model successfully identifies features of hepatitis B virus capsid assembly. Biochemistry 38:44 (1999), 14644–14652.
    • (1999) Biochemistry , vol.38 , Issue.44 , pp. 14644-14652
    • Zlotnick, A.1    Johnson, J.M.2    Wingfield, P.W.3    Stahl, S.J.4    Endres, D.5
  • 10
    • 33745195474 scopus 로고    scopus 로고
    • Clathrin-mediated endocytosis and lysosomal cleavage of hepatitis B virus capsid-like core particles
    • [10] Cooper, A., Shaul, Y., Clathrin-mediated endocytosis and lysosomal cleavage of hepatitis B virus capsid-like core particles. J. Biol. Chem. 281:24 (2006), 16563–16569.
    • (2006) J. Biol. Chem. , vol.281 , Issue.24 , pp. 16563-16569
    • Cooper, A.1    Shaul, Y.2
  • 13
    • 0033514992 scopus 로고    scopus 로고
    • Native display of complete foreign protein domains on the surface of hepatitis B virus capsids
    • [13] Kratz, P.A., Böttcher, B., Nassal, M., Native display of complete foreign protein domains on the surface of hepatitis B virus capsids. Proc. Natl. Acad. Sci. U. S. A. 96:5 (1999), 1915–1920.
    • (1999) Proc. Natl. Acad. Sci. U. S. A. , vol.96 , Issue.5 , pp. 1915-1920
    • Kratz, P.A.1    Böttcher, B.2    Nassal, M.3
  • 14
    • 0027932875 scopus 로고
    • Immunity to malaria elicited by hybrid hepatitis B virus core particles carrying circumsporozoite protein epitopes
    • [14] Schodel, F., Wirtz, R., Peterson, D., Hughes, J., Warren, R., Sadoff, J., Milich, D., Immunity to malaria elicited by hybrid hepatitis B virus core particles carrying circumsporozoite protein epitopes. J. Exp. Med. 180:3 (1994), 1037–1046.
    • (1994) J. Exp. Med. , vol.180 , Issue.3 , pp. 1037-1046
    • Schodel, F.1    Wirtz, R.2    Peterson, D.3    Hughes, J.4    Warren, R.5    Sadoff, J.6    Milich, D.7
  • 15
    • 43549101411 scopus 로고    scopus 로고
    • Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold
    • [15] Nygren, P.A., Alternative binding proteins: affibody binding proteins developed from a small three-helix bundle scaffold. FEBS J. 275:11 (2008), 2668–2676.
    • (2008) FEBS J. , vol.275 , Issue.11 , pp. 2668-2676
    • Nygren, P.A.1
  • 16
    • 77956176686 scopus 로고    scopus 로고
    • Structural basis for high-affinity HER2 receptor binding by an engineered protein
    • [16] Eigenbrot, C., Ultsch, M., Dubnovitsky, A., Abrahmsen, L., Hard, T., Structural basis for high-affinity HER2 receptor binding by an engineered protein. Proc. Natl. Acad. Sci. U. S. A. 107:34 (2010), 15039–15044.
    • (2010) Proc. Natl. Acad. Sci. U. S. A. , vol.107 , Issue.34 , pp. 15039-15044
    • Eigenbrot, C.1    Ultsch, M.2    Dubnovitsky, A.3    Abrahmsen, L.4    Hard, T.5
  • 18
    • 80052269043 scopus 로고    scopus 로고
    • Cryogenic transmission electron microscopy (cryo-TEM) for studying the morphology of colloidal drug delivery systems
    • [18] Kuntsche, J., Horst, J.C., Bunjes, H., Cryogenic transmission electron microscopy (cryo-TEM) for studying the morphology of colloidal drug delivery systems. Int. J. Pharm. 417:1–2 (2011), 120–137.
    • (2011) Int. J. Pharm. , vol.417 , Issue.1-2 , pp. 120-137
    • Kuntsche, J.1    Horst, J.C.2    Bunjes, H.3
  • 19
    • 34548008824 scopus 로고    scopus 로고
    • Cryoelectron microscopy of icosahedral virus particles
    • [19] Jiang, W., Chiu, W., Cryoelectron microscopy of icosahedral virus particles. Methods Mol. Biol. Clift. N.J. 369 (2007), 345–363.
    • (2007) Methods Mol. Biol. Clift. N.J. , vol.369 , pp. 345-363
    • Jiang, W.1    Chiu, W.2
  • 20
    • 84883616701 scopus 로고    scopus 로고
    • 3.5A cryoEM structure of hepatitis B virus core assembled from full-length core protein
    • [20] Yu, X., Jin, L., Jih, J., Shih, C., Zhou, Z.H., 3.5A cryoEM structure of hepatitis B virus core assembled from full-length core protein. PLoS One, 8(9), 2013, e69729.
    • (2013) PLoS One , vol.8 , Issue.9 , pp. e69729
    • Yu, X.1    Jin, L.2    Jih, J.3    Shih, C.4    Zhou, Z.H.5
  • 22
    • 84874323528 scopus 로고    scopus 로고
    • Granting specificity for breast cancer cells using a hepatitis B core particle with a HER2-targeted affibody molecule
    • [22] Nishimura, Y., Mimura, W., Mohamed Suffian, I.F., Amino, T., Ishii, J., Ogino, C., Kondo, A., Granting specificity for breast cancer cells using a hepatitis B core particle with a HER2-targeted affibody molecule. J. Biochem. 153:3 (2013), 251–256.
    • (2013) J. Biochem. , vol.153 , Issue.3 , pp. 251-256
    • Nishimura, Y.1    Mimura, W.2    Mohamed Suffian, I.F.3    Amino, T.4    Ishii, J.5    Ogino, C.6    Kondo, A.7
  • 23
    • 0028817155 scopus 로고
    • Validity of nucleic acid purities monitored by 260nm/280nm absorbance ratios
    • [23] Glasel, J.A., Validity of nucleic acid purities monitored by 260nm/280nm absorbance ratios. BioTechniques 18:1 (1995), 62–63.
    • (1995) BioTechniques , vol.18 , Issue.1 , pp. 62-63
    • Glasel, J.A.1
  • 24
    • 34547641767 scopus 로고    scopus 로고
    • Vaccination, immune and gene therapy based on virus-like particles against viral infections and cancer
    • [24] Ramqvist, T., Andreasson, K., Dalianis, T., Vaccination, immune and gene therapy based on virus-like particles against viral infections and cancer. Expert Opin. Biol. Ther. 7:7 (2007), 997–1007.
    • (2007) Expert Opin. Biol. Ther. , vol.7 , Issue.7 , pp. 997-1007
    • Ramqvist, T.1    Andreasson, K.2    Dalianis, T.3
  • 25
    • 0028832273 scopus 로고
    • Hepatitis B virus core particles as epitope carriers
    • [25] Pumpens, P., Borisova, G.P., Crowther, R.A., Grens, E., Hepatitis B virus core particles as epitope carriers. Intervirology 38:1–2 (1995), 63–74.
    • (1995) Intervirology , vol.38 , Issue.1-2 , pp. 63-74
    • Pumpens, P.1    Borisova, G.P.2    Crowther, R.A.3    Grens, E.4
  • 26
    • 77953148122 scopus 로고    scopus 로고
    • Construction and immunological evaluation of multivalent hepatitis B virus (HBV) core virus-like particles carrying HBV and HCV epitopes
    • [26] Sominskaya, I., Skrastina, D., Dislers, A., Vasiljev, D., Mihailova, M., Ose, V., Dreilina, D., Pumpens, P., Construction and immunological evaluation of multivalent hepatitis B virus (HBV) core virus-like particles carrying HBV and HCV epitopes. Clin. Vaccine Immunol. CVI 17:6 (2010), 1027–1033.
    • (2010) Clin. Vaccine Immunol. CVI , vol.17 , Issue.6 , pp. 1027-1033
    • Sominskaya, I.1    Skrastina, D.2    Dislers, A.3    Vasiljev, D.4    Mihailova, M.5    Ose, V.6    Dreilina, D.7    Pumpens, P.8
  • 27
    • 0018760172 scopus 로고
    • Expression in Escherichia coli of hepatitis B virus DNA sequences cloned in plasmid pBR322
    • [27] Burrell, C.J., Mackay, P., Greenaway, P.J., Hofschneider, P.H., Murray, K., Expression in Escherichia coli of hepatitis B virus DNA sequences cloned in plasmid pBR322. Nature 279:5708 (1979), 43–47.
    • (1979) Nature , vol.279 , Issue.5708 , pp. 43-47
    • Burrell, C.J.1    Mackay, P.2    Greenaway, P.J.3    Hofschneider, P.H.4    Murray, K.5
  • 29
    • 0019857904 scopus 로고
    • Synthesis of hepatitis B surface and core antigens in E. coli
    • [29] Edman, J.C., Hallewell, R.A., Valenzuela, P., Goodman, H.M., Rutter, W.J., Synthesis of hepatitis B surface and core antigens in E. coli. Nature 291:5815 (1981), 503–506.
    • (1981) Nature , vol.291 , Issue.5815 , pp. 503-506
    • Edman, J.C.1    Hallewell, R.A.2    Valenzuela, P.3    Goodman, H.M.4    Rutter, W.J.5
  • 30
    • 0025316017 scopus 로고
    • Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein
    • [30] Birnbaum, F., Nassal, M., Hepatitis B virus nucleocapsid assembly: primary structure requirements in the core protein. J. Virol. 64:7 (1990), 3319–3330.
    • (1990) J. Virol. , vol.64 , Issue.7 , pp. 3319-3330
    • Birnbaum, F.1    Nassal, M.2
  • 31
    • 0024500103 scopus 로고
    • Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus
    • [31] Salfeld, J., Pfaff, E., Noah, M., Schaller, H., Antigenic determinants and functional domains in core antigen and e antigen from hepatitis B virus. J. Virol. 63:2 (1989), 798–808.
    • (1989) J. Virol. , vol.63 , Issue.2 , pp. 798-808
    • Salfeld, J.1    Pfaff, E.2    Noah, M.3    Schaller, H.4
  • 32
    • 0034889864 scopus 로고    scopus 로고
    • HBV core particles as a carrier for B cell/T cell epitopes
    • [32] Pumpens, P., Grens, E., HBV core particles as a carrier for B cell/T cell epitopes. Intervirology 44:2–3 (2001), 98–114.
    • (2001) Intervirology , vol.44 , Issue.2-3 , pp. 98-114
    • Pumpens, P.1    Grens, E.2
  • 33
    • 0028307177 scopus 로고
    • Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy
    • [33] Crowther, R.A., Kiselev, N.A., Bottcher, B., Berriman, J.A., Borisova, G.P., Ose, V., Pumpens, P., Three-dimensional structure of hepatitis B virus core particles determined by electron cryomicroscopy. Cell 77:6 (1994), 943–950.
    • (1994) Cell , vol.77 , Issue.6 , pp. 943-950
    • Crowther, R.A.1    Kiselev, N.A.2    Bottcher, B.3    Berriman, J.A.4    Borisova, G.P.5    Ose, V.6    Pumpens, P.7
  • 34
    • 73149106771 scopus 로고    scopus 로고
    • Assembly and export determine the intracellular distribution of hepatitis B virus core protein subunits
    • [34] Weigand, K., Knaust, A., Schaller, H., Assembly and export determine the intracellular distribution of hepatitis B virus core protein subunits. J. Gen. Virol. 91:Pt 1 (2010), 59–67.
    • (2010) J. Gen. Virol. , vol.91 , pp. 59-67
    • Weigand, K.1    Knaust, A.2    Schaller, H.3
  • 35
    • 0032568934 scopus 로고    scopus 로고
    • The basic domain in HIV-1 Tat protein as a target for polysulfonated heparin-mimicking extracellular Tat antagonists
    • [35] Rusnati, M., Tulipano, G., Urbinati, C., Tanghetti, E., Giuliani, R., Giacca, M., Ciomei, M., Corallini, A., Presta, M., The basic domain in HIV-1 Tat protein as a target for polysulfonated heparin-mimicking extracellular Tat antagonists. J. Biol. Chem. 273:26 (1998), 16027–16037.
    • (1998) J. Biol. Chem. , vol.273 , Issue.26 , pp. 16027-16037
    • Rusnati, M.1    Tulipano, G.2    Urbinati, C.3    Tanghetti, E.4    Giuliani, R.5    Giacca, M.6    Ciomei, M.7    Corallini, A.8    Presta, M.9
  • 36
    • 0041816277 scopus 로고    scopus 로고
    • Antennapedia and HIV transactivator of transcription (TAT) “protein transduction domains” promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans
    • [36] Console, S., Marty, C., Garcia-Echeverria, C., Schwendener, R., Ballmer-Hofer, K., Antennapedia and HIV transactivator of transcription (TAT) “protein transduction domains” promote endocytosis of high molecular weight cargo upon binding to cell surface glycosaminoglycans. J. Biol. Chem. 278:37 (2003), 35109–35114.
    • (2003) J. Biol. Chem. , vol.278 , Issue.37 , pp. 35109-35114
    • Console, S.1    Marty, C.2    Garcia-Echeverria, C.3    Schwendener, R.4    Ballmer-Hofer, K.5
  • 38
    • 0026695732 scopus 로고
    • The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsulation and productive viral positive-strand DNA synthesis but not for virus assembly
    • [38] Nassal, M., The arginine-rich domain of the hepatitis B virus core protein is required for pregenome encapsulation and productive viral positive-strand DNA synthesis but not for virus assembly. J. Virol. 66:7 (1992), 4107–4116.
    • (1992) J. Virol. , vol.66 , Issue.7 , pp. 4107-4116
    • Nassal, M.1
  • 39
    • 0033152857 scopus 로고    scopus 로고
    • The crystal structure of the human hepatitis B virus capsid
    • [39] S.A. Wynne, R.A. Crowther, A.G.W. Leslie, The crystal structure of the human hepatitis B virus capsid, Mol. Cell 3(6) 771–780.
    • Mol. Cell , vol.3 , Issue.6 , pp. 771-780
    • Wynne, S.A.1    Crowther, R.A.2    Leslie, A.G.W.3
  • 40
    • 84866319710 scopus 로고    scopus 로고
    • Structures of hepatitis B virus cores presenting a model epitope and their complexes with antibodies
    • [40] Roseman, A.M., Borschukova, O., Berriman, J.A., Wynne, S.A., Pumpens, P., Crowther, R.A., Structures of hepatitis B virus cores presenting a model epitope and their complexes with antibodies. J. Mol. Biol. 423:1 (2012), 63–78.
    • (2012) J. Mol. Biol. , vol.423 , Issue.1 , pp. 63-78
    • Roseman, A.M.1    Borschukova, O.2    Berriman, J.A.3    Wynne, S.A.4    Pumpens, P.5    Crowther, R.A.6
  • 45
    • 84878011019 scopus 로고    scopus 로고
    • Development of virus-like particle technology from small highly symmetric to large complex virus-like particle structures
    • [45] Pushko, P., Pumpens, P., Grens, E., Development of virus-like particle technology from small highly symmetric to large complex virus-like particle structures. Intervirology 56:3 (2013), 141–165.
    • (2013) Intervirology , vol.56 , Issue.3 , pp. 141-165
    • Pushko, P.1    Pumpens, P.2    Grens, E.3
  • 46
    • 84978176208 scopus 로고    scopus 로고
    • Virus like particle-based vaccines against emerging infectious disease viruses
    • [46] Liu, J., Dai, S., Wang, M., Hu, Z., Wang, H., Deng, F., Virus like particle-based vaccines against emerging infectious disease viruses. Virol. Sin. 31:4 (2016), 279–287.
    • (2016) Virol. Sin. , vol.31 , Issue.4 , pp. 279-287
    • Liu, J.1    Dai, S.2    Wang, M.3    Hu, Z.4    Wang, H.5    Deng, F.6
  • 48
    • 84887165714 scopus 로고    scopus 로고
    • Factors controlling the pharmacokinetics, biodistribution and intratumoral penetration of nanoparticles
    • [48] Ernsting, M.J., Murakami, M., Roy, A., Li, S.D., Factors controlling the pharmacokinetics, biodistribution and intratumoral penetration of nanoparticles. J. Control Release 172:3 (2013), 782–794.
    • (2013) J. Control Release , vol.172 , Issue.3 , pp. 782-794
    • Ernsting, M.J.1    Murakami, M.2    Roy, A.3    Li, S.D.4
  • 49
    • 33846938312 scopus 로고    scopus 로고
    • Mouse models of breast cancer metastasis
    • [49] Fantozzi, A., Christofori, G., Mouse models of breast cancer metastasis. Breast Cancer Res. 8:4 (2006), 1–11.
    • (2006) Breast Cancer Res. , vol.8 , Issue.4 , pp. 1-11
    • Fantozzi, A.1    Christofori, G.2
  • 50
    • 16244367163 scopus 로고    scopus 로고
    • Modeling metastasis in vivo
    • [50] Khanna, C., Hunter, K., Modeling metastasis in vivo. Carcinogenesis 26:3 (2005), 513–523.
    • (2005) Carcinogenesis , vol.26 , Issue.3 , pp. 513-523
    • Khanna, C.1    Hunter, K.2
  • 51
    • 84898047818 scopus 로고    scopus 로고
    • Recent technological advances in using mouse models to study ovarian cancer
    • [51] House, C., Hernandez, L., Annunziata, C., Recent technological advances in using mouse models to study ovarian cancer. Front. Oncol., 4(26), 2014.
    • (2014) Front. Oncol. , vol.4 , Issue.26
    • House, C.1    Hernandez, L.2    Annunziata, C.3
  • 52
    • 57449102025 scopus 로고    scopus 로고
    • Efficacy assessment of sustained intraperitoneal paclitaxel therapy in a murine model of ovarian cancer using bioluminescent imaging
    • [52] Vassileva, V., Moriyama, E.H., De Souza, R., Grant, J., Allen, C.J., Wilson, B.C., Piquette-Miller, M., Efficacy assessment of sustained intraperitoneal paclitaxel therapy in a murine model of ovarian cancer using bioluminescent imaging. Br. J. Cancer 99:12 (2008), 2037–2043.
    • (2008) Br. J. Cancer , vol.99 , Issue.12 , pp. 2037-2043
    • Vassileva, V.1    Moriyama, E.H.2    De Souza, R.3    Grant, J.4    Allen, C.J.5    Wilson, B.C.6    Piquette-Miller, M.7
  • 55
    • 0032972404 scopus 로고    scopus 로고
    • Purification of E. coli-expressed HIS-tagged hepatitis B core antigen by Ni2+ -chelate affinity chromatography
    • [55] Wizemann, H., von Brunn, A., Purification of E. coli-expressed HIS-tagged hepatitis B core antigen by Ni2+ -chelate affinity chromatography. J. Virol. Methods 77:2 (1999), 189–197.
    • (1999) J. Virol. Methods , vol.77 , Issue.2 , pp. 189-197
    • Wizemann, H.1    von Brunn, A.2
  • 56
    • 0036740090 scopus 로고    scopus 로고
    • Development of annexin V mutants suitable for labeling with Tc(i)-carbonyl complex
    • [56] Tait, J.F., Smith, C., Gibson, D.F., Development of annexin V mutants suitable for labeling with Tc(i)-carbonyl complex. Bioconj. Chem. 13:5 (2002), 1119–1123.
    • (2002) Bioconj. Chem. , vol.13 , Issue.5 , pp. 1119-1123
    • Tait, J.F.1    Smith, C.2    Gibson, D.F.3
  • 57
    • 84978117035 scopus 로고    scopus 로고
    • Biodistribution and toxicity evaluation of sesbania mosaic virus nanoparticles in mice
    • [57] Vishnu Vardhan, G.P., Savithri, H.S., Murthy, M.R.N., Hema, M., Biodistribution and toxicity evaluation of sesbania mosaic virus nanoparticles in mice. Arch. Virol. 161:10 (2016), 2673–2681.
    • (2016) Arch. Virol. , vol.161 , Issue.10 , pp. 2673-2681
    • Vishnu Vardhan, G.P.1    Savithri, H.S.2    Murthy, M.R.N.3    Hema, M.4
  • 58
  • 60
    • 33747519945 scopus 로고    scopus 로고
    • Striking out at disseminated metastases: the systemic delivery of oncolytic viruses
    • [60] Fisher, K., Striking out at disseminated metastases: the systemic delivery of oncolytic viruses. Curr. Opin. Mol. Ther. 8:4 (2006), 301–313.
    • (2006) Curr. Opin. Mol. Ther. , vol.8 , Issue.4 , pp. 301-313
    • Fisher, K.1
  • 61
  • 64
    • 34250819325 scopus 로고    scopus 로고
    • Poly(ethylene glycol)-modified nanocarriers for tumor-targeted and intracellular delivery
    • [64] van Vlerken, L.E., Vyas, T.K., Amiji, M.M., Poly(ethylene glycol)-modified nanocarriers for tumor-targeted and intracellular delivery. Pharm. Res. 24:8 (2007), 1405–1414.
    • (2007) Pharm. Res. , vol.24 , Issue.8 , pp. 1405-1414
    • van Vlerken, L.E.1    Vyas, T.K.2    Amiji, M.M.3
  • 65
    • 0037503818 scopus 로고    scopus 로고
    • Hybrid virus-polymer materials. 1. Synthesis and properties of PEG-decorated cowpea mosaic virus
    • [65] Raja, K.S., Wang, Q., Gonzalez, M.J., Manchester, M., Johnson, J.E., Finn, M.G., Hybrid virus-polymer materials. 1. Synthesis and properties of PEG-decorated cowpea mosaic virus. Biomacromolecules 4:3 (2003), 472–476.
    • (2003) Biomacromolecules , vol.4 , Issue.3 , pp. 472-476
    • Raja, K.S.1    Wang, Q.2    Gonzalez, M.J.3    Manchester, M.4    Johnson, J.E.5    Finn, M.G.6
  • 67
    • 84938058760 scopus 로고    scopus 로고
    • A comparison of intravenous plus intraperitoneal chemotherapy with intravenous chemotherapy alone for the treatment of gastric cancer: a meta-analysis
    • [67] Yang, S., Feng, R., Pan, Z.-C., Jiang, T., Xu, Q., Chen, Q., A comparison of intravenous plus intraperitoneal chemotherapy with intravenous chemotherapy alone for the treatment of gastric cancer: a meta-analysis. Sci. Rep., 5, 2015, 12538.
    • (2015) Sci. Rep. , vol.5 , pp. 12538
    • Yang, S.1    Feng, R.2    Pan, Z.-C.3    Jiang, T.4    Xu, Q.5    Chen, Q.6
  • 68
    • 0017853566 scopus 로고
    • Pharmacokinetic rationale for peritoneal drug administration in the treatment of ovarian cancer
    • [68] Dedrick, R.L., Myers, C.E., Bungay, P.M., DeVita, V.T. Jr., Pharmacokinetic rationale for peritoneal drug administration in the treatment of ovarian cancer. Cancer Treat. Rep. 62:1 (1978), 1–11.
    • (1978) Cancer Treat. Rep. , vol.62 , Issue.1 , pp. 1-11
    • Dedrick, R.L.1    Myers, C.E.2    Bungay, P.M.3    DeVita, V.T.4
  • 69
    • 0031104742 scopus 로고    scopus 로고
    • Transductional efficacy and safety of an intraperitoneally delivered adenovirus encoding an Anti-erbB-2 intracellular single-chain antibody for ovarian cancer gene therapy
    • [69] Deshane, J., Siegal, G.P., Wang, M., Wright, M., Bucy, R.P., Alvarez, R.D., Curiel, D.T., Transductional efficacy and safety of an intraperitoneally delivered adenovirus encoding an Anti-erbB-2 intracellular single-chain antibody for ovarian cancer gene therapy. Gynecol. Oncol. 64:3 (1997), 378–385.
    • (1997) Gynecol. Oncol. , vol.64 , Issue.3 , pp. 378-385
    • Deshane, J.1    Siegal, G.P.2    Wang, M.3    Wright, M.4    Bucy, R.P.5    Alvarez, R.D.6    Curiel, D.T.7
  • 70
    • 0031830091 scopus 로고    scopus 로고
    • Gene therapy for primary and metastatic pancreatic cancer with intraperitoneal retroviral vector bearing the wild-type p53 gene
    • discussion 150–1
    • [70] Hwang, R.F., Gordon, E.M., Anderson, W.F., Parekh, D., Gene therapy for primary and metastatic pancreatic cancer with intraperitoneal retroviral vector bearing the wild-type p53 gene. Surgery 124:2 (1998), 143–150 discussion 150–1.
    • (1998) Surgery , vol.124 , Issue.2 , pp. 143-150
    • Hwang, R.F.1    Gordon, E.M.2    Anderson, W.F.3    Parekh, D.4
  • 72
    • 0141790758 scopus 로고    scopus 로고
    • Drug delivery and transport to solid tumors
    • [72] Jang, S.H., Wientjes, M.G., Lu, D., Au, J.L., Drug delivery and transport to solid tumors. Pharm. Res. 20:9 (2003), 1337–1350.
    • (2003) Pharm. Res. , vol.20 , Issue.9 , pp. 1337-1350
    • Jang, S.H.1    Wientjes, M.G.2    Lu, D.3    Au, J.L.4
  • 73
    • 81255143243 scopus 로고    scopus 로고
    • Improving delivery and efficacy of nanomedicines in solid tumors: role of tumor priming
    • [73] Wang, J., Lu, Z., Gao, Y., Wientjes, M.G., Au, J.L.S., Improving delivery and efficacy of nanomedicines in solid tumors: role of tumor priming. Nanomedicine 6:9 (2011), 1605–1620.
    • (2011) Nanomedicine , vol.6 , Issue.9 , pp. 1605-1620
    • Wang, J.1    Lu, Z.2    Gao, Y.3    Wientjes, M.G.4    Au, J.L.S.5
  • 75
    • 0034193258 scopus 로고    scopus 로고
    • Role of extracellular matrix assembly in interstitial transport in solid tumors
    • [75] Netti, P.A., Berk, D.A., Swartz, M.A., Grodzinsky, A.J., Jain, R.K., Role of extracellular matrix assembly in interstitial transport in solid tumors. Cancer Res. 60:9 (2000), 2497–2503.
    • (2000) Cancer Res. , vol.60 , Issue.9 , pp. 2497-2503
    • Netti, P.A.1    Berk, D.A.2    Swartz, M.A.3    Grodzinsky, A.J.4    Jain, R.K.5
  • 76
    • 33746491709 scopus 로고    scopus 로고
    • Drug penetration in solid tumours
    • [76] Minchinton, A.I., Tannock, I.F., Drug penetration in solid tumours. Nat. Rev. Cancer 6:8 (2006), 583–592.
    • (2006) Nat. Rev. Cancer , vol.6 , Issue.8 , pp. 583-592
    • Minchinton, A.I.1    Tannock, I.F.2
  • 77
    • 79961172204 scopus 로고    scopus 로고
    • Intratumoral drug delivery with nanoparticulate carriers
    • [77] Holback, H., Yeo, Y., Intratumoral drug delivery with nanoparticulate carriers. Pharm. Res. 28:8 (2011), 1819–1830.
    • (2011) Pharm. Res. , vol.28 , Issue.8 , pp. 1819-1830
    • Holback, H.1    Yeo, Y.2
  • 78
    • 84982959539 scopus 로고    scopus 로고
    • Continued use of MDA-MB-435, a melanoma cell line, as a model for human breast cancer, even in year, 2014
    • [78] Prasad, V.V.T.S., Gopalan, R.O.G., Continued use of MDA-MB-435, a melanoma cell line, as a model for human breast cancer, even in year, 2014. Npj Breast Cancer, 1, 2015, 15002.
    • (2015) Npj Breast Cancer , vol.1 , pp. 15002
    • Prasad, V.V.T.S.1    Gopalan, R.O.G.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.