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Volumn 10, Issue 5, 2015, Pages 715-727

Next generation vaccines and vectors: Designing downstream processes for recombinant protein-based virus-like particles

Author keywords

High throughput screening; Modeling; Purification; Vaccine; VLP

Indexed keywords

COST REDUCTION; DIAGNOSIS; MODELS; PURIFICATION; VACCINES; VIRUSES;

EID: 84928800935     PISSN: 18606768     EISSN: 18607314     Source Type: Journal    
DOI: 10.1002/biot.201400392     Document Type: Review
Times cited : (86)

References (170)
  • 1
    • 37549006787 scopus 로고    scopus 로고
    • Virus-like particles-universal molecular toolboxes.
    • Ludwig, C., Wagner, R., Virus-like particles-universal molecular toolboxes. Curr. Opin. Biotechnol. 2007, 18, 537-545.
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 537-545
    • Ludwig, C.1    Wagner, R.2
  • 2
    • 72049086178 scopus 로고    scopus 로고
    • Development of the RTS, S/AS malaria candidate vaccine.
    • Vekemans, J., Leach, A., Cohen, J., Development of the RTS, S/AS malaria candidate vaccine. Vaccine 2009, 27Suppl6, 67-71.
    • (2009) Vaccine , vol.27 , pp. 67-71
    • Vekemans, J.1    Leach, A.2    Cohen, J.3
  • 3
    • 84859839625 scopus 로고    scopus 로고
    • Vaccine efficacy against malaria by the combination of porcine parvovirus-like particles and vaccinia virus vectors expressing CS of Plasmodium.
    • Rodríguez, D., González-Aseguinolaza, G., Rodríguez, J. R., Vijayan, A. et al., Vaccine efficacy against malaria by the combination of porcine parvovirus-like particles and vaccinia virus vectors expressing CS of Plasmodium. PLoS One 2012, 7, doi:10.1371/journal.pone.0034445.
    • (2012) PLoS One , vol.7
    • Rodríguez, D.1    González-Aseguinolaza, G.2    Rodríguez, J.R.3    Vijayan, A.4
  • 4
    • 84899508777 scopus 로고    scopus 로고
    • Microbially synthesized modular virus-like particles and capsomeres displaying group A streptococcus hypervariable antigenic determinants.
    • Chuan, Y. P., Wibowo, N., Connors, N. K., Wu, Y. et al., Microbially synthesized modular virus-like particles and capsomeres displaying group A streptococcus hypervariable antigenic determinants. Biotechnol. Bioeng. 2014, 111, 1062-1070.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 1062-1070
    • Chuan, Y.P.1    Wibowo, N.2    Connors, N.K.3    Wu, Y.4
  • 5
    • 78649342481 scopus 로고    scopus 로고
    • Virus-like particle based vaccines for Alzheimer disease.
    • Chackerian, B., Virus-like particle based vaccines for Alzheimer disease. Hum. Vaccin. 2010, 6, 926-930.
    • (2010) Hum. Vaccin. , vol.6 , pp. 926-930
    • Chackerian, B.1
  • 6
    • 84928826676 scopus 로고    scopus 로고
    • Composition comprising vlp and amyloid beta peptide
    • Graf, A., Staufenbiel, M., Blaettler, T., Paganetti, P., Composition comprising vlp and amyloid beta peptide, US Patent 8617566, 2013.
    • (2013)
    • Graf, A.1    Staufenbiel, M.2    Blaettler, T.3    Paganetti, P.4
  • 7
    • 84904401226 scopus 로고    scopus 로고
    • Aβ-HBc virus-like particles immunization without additional adjuvant ameliorates the learning and memory and reduces Aβ deposit in PDAPP mice.
    • Jin, H., Wang, W., Zhao, S., Yang, W. et al., Aβ-HBc virus-like particles immunization without additional adjuvant ameliorates the learning and memory and reduces Aβ deposit in PDAPP mice. Vaccine 2014, 32, 4450-4456.
    • (2014) Vaccine , vol.32 , pp. 4450-4456
    • Jin, H.1    Wang, W.2    Zhao, S.3    Yang, W.4
  • 8
    • 83455217650 scopus 로고    scopus 로고
    • Fermentation process technology transfer for production of a recombinant vaccine component.
    • Sharma, S., Whalley, A., McLaughli, J., Brello, F. et al., Fermentation process technology transfer for production of a recombinant vaccine component. BioPharm International 2011, 24, 30-39.
    • (2011) BioPharm International , vol.24 , pp. 30-39
    • Sharma, S.1    Whalley, A.2    McLaughli, J.3    Brello, F.4
  • 10
    • 85015670961 scopus 로고    scopus 로고
    • Preclinical efficacy and safety of an anti-IL-1β vaccine for the treatment of type 2 diabetes.
    • Spohn, G., Schori, C., Keller, I., Sladko, K. et al., Preclinical efficacy and safety of an anti-IL-1β vaccine for the treatment of type 2 diabetes. Mol. Ther. Methods Clin. Dev. 2014, 1, doi:10.1038/mtm.2014.48.
    • (2014) Mol. Ther. Methods Clin. Dev. , vol.1
    • Spohn, G.1    Schori, C.2    Keller, I.3    Sladko, K.4
  • 11
    • 78751471791 scopus 로고    scopus 로고
    • Highly specific auto-antibodies against claudin-18 isoform 2 induced by a chimeric HBcAg virus-like particle vaccine kill tumor cells and inhibit the growth of lung metastases.
    • Klamp, T., Schumacher, J., Huber, G., Kühne, C. et al., Highly specific auto-antibodies against claudin-18 isoform 2 induced by a chimeric HBcAg virus-like particle vaccine kill tumor cells and inhibit the growth of lung metastases. Cancer Res. 2011, 71, 516-527.
    • (2011) Cancer Res. , vol.71 , pp. 516-527
    • Klamp, T.1    Schumacher, J.2    Huber, G.3    Kühne, C.4
  • 13
    • 84919614677 scopus 로고    scopus 로고
    • Virus-like particle-mediated intracellular delivery of mRNA cap analog with in vivo activity against hepatocellular carcinoma.
    • Zochowska, M., Piguet, A.-C., Jemielity, J., Kowalska, J. et al., Virus-like particle-mediated intracellular delivery of mRNA cap analog with in vivo activity against hepatocellular carcinoma. Nanomedicine 2014, 11, 67-76.
    • (2014) Nanomedicine , vol.11 , pp. 67-76
    • Zochowska, M.1    Piguet, A.-C.2    Jemielity, J.3    Kowalska, J.4
  • 14
    • 84875253322 scopus 로고    scopus 로고
    • Active immunotherapy for chronic diseases.
    • Bachmann, M. F., Whitehead, P., Active immunotherapy for chronic diseases. Vaccine 2013, 31, 1777-1784.
    • (2013) Vaccine , vol.31 , pp. 1777-1784
    • Bachmann, M.F.1    Whitehead, P.2
  • 16
    • 85012834325 scopus 로고    scopus 로고
    • 1. Viruses and virus-like particles in biotechnology: Fundamentals and applications
    • Moo-Young, M. (Ed.), Comprehensive Biotechnology, Elsevier B.V.
    • Roldão, A., Silva, A. C., Mellado, M. C. M., Tecnologia, I. D., Lisboa, U. N. D., 1. Viruses and virus-like particles in biotechnology: Fundamentals and applications, in: Moo-Young, M. (Ed.), Comprehensive Biotechnology, Elsevier B.V., 2011.
    • (2011)
    • Roldão, A.1    Silva, A.C.2    Mellado, M.C.M.3    Tecnologia, I.D.4    Lisboa, U.N.D.5
  • 17
    • 84870540478 scopus 로고    scopus 로고
    • Virus-like particles as a highly efficient vaccine platform: diversity of targets and production systems and advances in clinical development.
    • Kushnir, N., Streatfield, S. J., Yusibov, V., Virus-like particles as a highly efficient vaccine platform: diversity of targets and production systems and advances in clinical development. Vaccine 2012, 31, 58-83.
    • (2012) Vaccine , vol.31 , pp. 58-83
    • Kushnir, N.1    Streatfield, S.J.2    Yusibov, V.3
  • 18
    • 84878011019 scopus 로고    scopus 로고
    • Development of virus-like particle technology from small highly symmetric to large complex virus-like particle structures.
    • Pushko, P., Pumpens, P., Grens, E., Development of virus-like particle technology from small highly symmetric to large complex virus-like particle structures. Intervirology 2013, 56, 141-165.
    • (2013) Intervirology , vol.56 , pp. 141-165
    • Pushko, P.1    Pumpens, P.2    Grens, E.3
  • 19
    • 84871650149 scopus 로고    scopus 로고
    • Construction and characterization of virus-like particles: a review.
    • Zeltins, A., Construction and characterization of virus-like particles: a review. Mol. Biotechnol. 2013, 53, 92-107.
    • (2013) Mol. Biotechnol. , vol.53 , pp. 92-107
    • Zeltins, A.1
  • 21
    • 84873591289 scopus 로고    scopus 로고
    • Inequalities in human papillomavirus (HPV)-associated cancers: implications for the success of HPV vaccination.
    • Brisson, M., Drolet, M., Malagón, T., Inequalities in human papillomavirus (HPV)-associated cancers: implications for the success of HPV vaccination. J. Natl. Cancer Inst. 2013, 105, 158-161.
    • (2013) J. Natl. Cancer Inst. , vol.105 , pp. 158-161
    • Brisson, M.1    Drolet, M.2    Malagón, T.3
  • 22
    • 84907450493 scopus 로고    scopus 로고
    • Decreased management of genital warts in young women in australian general practice post introduction of national HPV vaccination program: Results from a nationally representative cross-sectional general practice study.
    • Harrison, C., Britt, H., Garland, S., Conway, L. et al., Decreased management of genital warts in young women in australian general practice post introduction of national HPV vaccination program: Results from a nationally representative cross-sectional general practice study. PLoS One 2014, 9, doi:10.1371/journal.pone.0105967.
    • (2014) PLoS One , vol.9
    • Harrison, C.1    Britt, H.2    Garland, S.3    Conway, L.4
  • 23
    • 0034965669 scopus 로고    scopus 로고
    • Effects in humans of intravenously administered endotoxin on soluble cell-adhesion molecule and inflammatory markers: a model of human diseases.
    • Wilson, M. F., Blum, R., Dandona, P., Mousa, S. A., Effects in humans of intravenously administered endotoxin on soluble cell-adhesion molecule and inflammatory markers: a model of human diseases. Clin. Exp. Pharmacol. Physiol. 2001, 28, 376-380.
    • (2001) Clin. Exp. Pharmacol. Physiol. , vol.28 , pp. 376-380
    • Wilson, M.F.1    Blum, R.2    Dandona, P.3    Mousa, S.A.4
  • 24
    • 84889465273 scopus 로고    scopus 로고
    • Immunogenicity of impurities in cell-derived vaccines
    • Stacey, G., Davis, J. (Eds.) Medicines from Animal Cell Culture, John Wiley & Sons, Weinheim
    • Duchene, M., Descamps, J., Pierard, I., Immunogenicity of impurities in cell-derived vaccines, in: Stacey, G., Davis, J. (Eds.) Medicines from Animal Cell Culture, John Wiley & Sons, Weinheim 2007, pp. 491-496.
    • (2007) , pp. 491-496
    • Duchene, M.1    Descamps, J.2    Pierard, I.3
  • 25
    • 80053436637 scopus 로고    scopus 로고
    • Safety and immunogenicity of a candidate parvovirus B19 vaccine.
    • Bernstein, D. I., El Sahly, H. M., Keitel, W. A., Wolff, M. et al., Safety and immunogenicity of a candidate parvovirus B19 vaccine. Vaccine 2011, 29, 7357-7363.
    • (2011) Vaccine , vol.29 , pp. 7357-7363
    • Bernstein, D.I.1    El Sahly, H.M.2    Keitel, W.A.3    Wolff, M.4
  • 26
    • 84904436379 scopus 로고    scopus 로고
    • Guidance for Industry Information and Establishment Description Information for a Vaccine
    • U.S. Food and Drug Administration, CBER, Guidance for Industry Information and Establishment Description Information for a Vaccine, 1999.
    • (1999)
  • 27
    • 34548021984 scopus 로고    scopus 로고
    • Guidelines to assure the quality, safety and efficacy of recombinant human papillomavirus virus-like particle vaccines
    • World Health Organization, Guidelines to assure the quality, safety and efficacy of recombinant human papillomavirus virus-like particle vaccines, 2006, 23-27.
    • (2006) , pp. 23-27
  • 28
    • 85018220920 scopus 로고    scopus 로고
    • safety and efficacy of recombinant malaria vaccines targeting the pre-erythrocytic and blood stages of Plasmodium falciparum
    • World Health Organization, Guidelines on the quality, safety and efficacy of recombinant malaria vaccines targeting the pre-erythrocytic and blood stages of Plasmodium falciparum, 2014.
    • (2014)
  • 29
    • 84928823599 scopus 로고    scopus 로고
    • FDA Guidance for Industry Characterization and Qualification of Cell Substrates and Other Guidance for Industry Characterization and Qualification of Cell Substrates and Other Biological Materials Used in the Production of Viral Vaccines for Infectious Disease Indications
    • U.S. Food and Drug Administration, CBER, FDA Guidance for Industry Characterization and Qualification of Cell Substrates and Other Guidance for Industry Characterization and Qualification of Cell Substrates and Other Biological Materials Used in the Production of Viral Vaccines for Infectious Disease Indications, 2007.
    • (2007)
  • 30
    • 84905389306 scopus 로고    scopus 로고
    • S. Clinical Trials Partnership, Efficacy and safety of the RTS
    • controlled trial in children and young infants at 11 African sites. PLoS Med.
    • RTS, S. Clinical Trials Partnership, Efficacy and safety of the RTS, S/AS01 malaria vaccine during 18 months after vaccination: A phase 3 randomized, controlled trial in children and young infants at 11 African sites. PLoS Med. 2014, 11, doi:10.1371/journal.pmed.1001685.
    • (2014) S/AS01 malaria vaccine during 18 months after vaccination: A phase 3 randomized , vol.11
  • 31
    • 78650071105 scopus 로고    scopus 로고
    • Acceptable levels of endotoxin in vaccine formulations during preclinical research.
    • 34-33
    • Brito, L. A., Singh, M., Acceptable levels of endotoxin in vaccine formulations during preclinical research. J. Pharm. Sci. 2011, 100, 34-3.
    • (2011) J. Pharm. Sci. , vol.100
    • Brito, L.A.1    Singh, M.2
  • 32
    • 0033486183 scopus 로고    scopus 로고
    • Purification of virus-like particles of recombinant human papillomavirus type 11 major capsid protein L1 from Saccharomyces cerevisiae
    • Cook, J. C., Joyce, J. G., George, H. A., Schultz, L. D. et al., Purification of virus-like particles of recombinant human papillomavirus type 11 major capsid protein L1 from Saccharomyces cerevisiae, Protein Expr. Purif. 1999, 17, 477-484.
    • (1999) Protein Expr. Purif. , vol.17 , pp. 477-484
    • Cook, J.C.1    Joyce, J.G.2    George, H.A.3    Schultz, L.D.4
  • 33
    • 33644744918 scopus 로고    scopus 로고
    • Assays for controlling host-cell impurities in biopharmaceuticals.
    • Wolter, T., Richter, A., Assays for controlling host-cell impurities in biopharmaceuticals. Bioprocess Int. 2005, 2, 40-46.
    • (2005) Bioprocess Int. , vol.2 , pp. 40-46
    • Wolter, T.1    Richter, A.2
  • 34
    • 33748864395 scopus 로고    scopus 로고
    • Disassembly and reassembly of yeast-derived recombinant human papillomavirus virus-like particles ( HPV VLPs )
    • Mach, H., Volkin, D. B., Troutman, R. D., Wang, B. E. I., Disassembly and reassembly of yeast-derived recombinant human papillomavirus virus-like particles ( HPV VLPs ), J. Pharm. Sci. 2006, 95, 2195-2206.
    • (2006) J. Pharm. Sci. , vol.95 , pp. 2195-2206
    • Mach, H.1    Volkin, D.B.2    Troutman, R.D.3    Wang, B.E.I.4
  • 35
    • 0031974862 scopus 로고    scopus 로고
    • Quantitative disassembly and reassembly of human papillomavirus type 11 viruslike particles in vitro.
    • McCarthy, M. P. M. C., White, W. I., Palmer-Hill, F., Koenig, S., Suzich, J. A., Quantitative disassembly and reassembly of human papillomavirus type 11 viruslike particles in vitro. J. Virol. 1998, 72, 32-41.
    • (1998) J. Virol. , vol.72 , pp. 32-41
    • McCarthy, M.P.M.C.1    White, W.I.2    Palmer-Hill, F.3    Koenig, S.4    Suzich, J.A.5
  • 36
    • 33747359853 scopus 로고    scopus 로고
    • In vitro-reassembled plant virus-like particles for loading of polyacids.
    • Ren, Y., Wong, S.-M., Lim, L.-Y., In vitro-reassembled plant virus-like particles for loading of polyacids. J. Gen. Virol. 2006, 87, 2749-2754.
    • (2006) J. Gen. Virol. , vol.87 , pp. 2749-2754
    • Ren, Y.1    Wong, S.-M.2    Lim, L.-Y.3
  • 37
    • 77958488968 scopus 로고    scopus 로고
    • Structure of hepatitis E virion-sized particle reveals an RNA-dependent viral assembly pathway.
    • Xing, L., Li, T.-C., Mayazaki, N., Simon, M. N. et al., Structure of hepatitis E virion-sized particle reveals an RNA-dependent viral assembly pathway. J. Biol. Chem. 2010, 285, 33175-33183.
    • (2010) J. Biol. Chem. , vol.285 , pp. 33175-33183
    • Xing, L.1    Li, T.-C.2    Mayazaki, N.3    Simon, M.N.4
  • 38
    • 84860335491 scopus 로고    scopus 로고
    • Innate immunity mediates follicular transport of particulate but not soluble protein antigen.
    • Link, A., Zabel, F., Schnetzler, Y., Titz, A. et al., Innate immunity mediates follicular transport of particulate but not soluble protein antigen. J. Immunol. 2012, 188, 3724-3733.
    • (2012) J. Immunol. , vol.188 , pp. 3724-3733
    • Link, A.1    Zabel, F.2    Schnetzler, Y.3    Titz, A.4
  • 39
    • 84861122841 scopus 로고    scopus 로고
    • On the effect of thermodynamic equilibrium on the assembly efficiency of complex multi-layered virus-like particles (VLP): The case of rotavirus VLP.
    • Roldão, A., Mellado, M. C. M., Lima, J. C., Carrondo, M. J. T. et al., On the effect of thermodynamic equilibrium on the assembly efficiency of complex multi-layered virus-like particles (VLP): The case of rotavirus VLP. PLoS Comput. Biol. 2012, 8, doi:10.1371/journal.pcbi.1002367.
    • (2012) PLoS Comput. Biol. , vol.8
    • Roldão, A.1    Mellado, M.C.M.2    Lima, J.C.3    Carrondo, M.J.T.4
  • 40
    • 84862796928 scopus 로고    scopus 로고
    • Disassembly and reassembly improves morphology and thermal stability of human papillomavirus type 16 virus-like particles.
    • Zhao, Q., Allen, M. J., Wang, Y., Wang, B. et al., Disassembly and reassembly improves morphology and thermal stability of human papillomavirus type 16 virus-like particles. Nanomedicine 2012, 8, 1182-1189.
    • (2012) Nanomedicine , vol.8 , pp. 1182-1189
    • Zhao, Q.1    Allen, M.J.2    Wang, Y.3    Wang, B.4
  • 41
    • 84862812041 scopus 로고    scopus 로고
    • Disassembly and reassembly of human papillomavirus virus-like particles produces more virion-like antibody reactivity.
    • Zhao, Q., Modis, Y., High, K., Towne, V. et al., Disassembly and reassembly of human papillomavirus virus-like particles produces more virion-like antibody reactivity. Virol. J. 2012, 9, doi:10.1186/1743-422X-9-5.
    • (2012) Virol. J. , vol.9
    • Zhao, Q.1    Modis, Y.2    High, K.3    Towne, V.4
  • 42
    • 84877688114 scopus 로고    scopus 로고
    • Molecular energetics in the capsomere of virus-like particle revealed by molecular dynamics simulations.
    • Zhang, L., Tang, R., Bai, S., Connors, N. K. et al., Molecular energetics in the capsomere of virus-like particle revealed by molecular dynamics simulations. J. Phys. Chem. B 2013, 117, 5411-5421.
    • (2013) J. Phys. Chem. B , vol.117 , pp. 5411-5421
    • Zhang, L.1    Tang, R.2    Bai, S.3    Connors, N.K.4
  • 43
    • 84928823286 scopus 로고    scopus 로고
    • Energetic changes caused by antigenic module insertion in a virus-like particle revealed by experiment and molecular dynamics simulations.
    • Zhang, L., Tang, R., Bai, S., Connors, N. K. et al., Energetic changes caused by antigenic module insertion in a virus-like particle revealed by experiment and molecular dynamics simulations. PLoS One 2014, 9, doi:10.1371/journal.pone.0107313.
    • (2014) PLoS One , vol.9
    • Zhang, L.1    Tang, R.2    Bai, S.3    Connors, N.K.4
  • 44
    • 23844494049 scopus 로고    scopus 로고
    • Stabilization of human papillomavirus virus-like particles by non-ionic surfactants.
    • Shi, L., Sanyal, G., Ni, A., Luo, Z. et al., Stabilization of human papillomavirus virus-like particles by non-ionic surfactants. J. Pharm. Sci. 2005, 94, 1538-1551.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1538-1551
    • Shi, L.1    Sanyal, G.2    Ni, A.3    Luo, Z.4
  • 45
    • 78651478069 scopus 로고    scopus 로고
    • Modeling the competition between aggregation and self-assembly during virus-like particle processing.
    • Ding, Y., Chuan, Y. P., He, L., Middelberg, A. P. J., Modeling the competition between aggregation and self-assembly during virus-like particle processing. Biotechnol. Bioeng. 2010, 107, 550-560.
    • (2010) Biotechnol. Bioeng. , vol.107 , pp. 550-560
    • Ding, Y.1    Chuan, Y.P.2    He, L.3    Middelberg, A.P.J.4
  • 47
    • 0034233433 scopus 로고    scopus 로고
    • Selective flocculation and precipitation for the improvement of virus-like particle recovery from yeast homogenate.
    • Tsoka, S., Ciniawskyj, O. C., Thomas, O. R., Titchener-Hooker, N. J. et al., Selective flocculation and precipitation for the improvement of virus-like particle recovery from yeast homogenate. Biotechnol. Prog. 2000, 16, 661-667.
    • (2000) Biotechnol. Prog. , vol.16 , pp. 661-667
    • Tsoka, S.1    Ciniawskyj, O.C.2    Thomas, O.R.3    Titchener-Hooker, N.J.4
  • 48
    • 80054058296 scopus 로고    scopus 로고
    • Purification and immunogenicity study of human papillomavirus 58 virus-like particles expressed in Pichia pastoris
    • Jiang, Z., Tong, G., Cai, B., Xu, Y., Lou, J., Purification and immunogenicity study of human papillomavirus 58 virus-like particles expressed in Pichia pastoris, Protein Expr. Purif. 2011, 80, 203-210.
    • (2011) Protein Expr. Purif. , vol.80 , pp. 203-210
    • Jiang, Z.1    Tong, G.2    Cai, B.3    Xu, Y.4    Lou, J.5
  • 49
    • 79959414321 scopus 로고    scopus 로고
    • Virus-like particle production with yeast: ultrastructural and immunocytochemical insights into Pichia pastoris producing high levels of the hepatitis B surface antigen.
    • Lünsdorf, H., Gurramkonda, C., Adnan, A., Khanna, N., Rinas, U., Virus-like particle production with yeast: ultrastructural and immunocytochemical insights into Pichia pastoris producing high levels of the hepatitis B surface antigen. Microb. Cell Fact. 2011, 10, doi:10.1186/1475-2859-10-48.
    • (2011) Microb. Cell Fact. , vol.10
    • Lünsdorf, H.1    Gurramkonda, C.2    Adnan, A.3    Khanna, N.4    Rinas, U.5
  • 50
    • 70349339720 scopus 로고    scopus 로고
    • Impact of cell density and viability on primary clarification of mammalian cell broth.
    • Iammarino, M., Nti-gyabaah, J., Chandler, M., Roush, D., Göklen, K., Impact of cell density and viability on primary clarification of mammalian cell broth. Bioprocess Int. 2007, 11, 38-50.
    • (2007) Bioprocess Int. , vol.11 , pp. 38-50
    • Iammarino, M.1    Nti-gyabaah, J.2    Chandler, M.3    Roush, D.4    Göklen, K.5
  • 51
    • 84887396369 scopus 로고    scopus 로고
    • Use of hollow fiber tangential flow filtration for the recovery and concentration of HIV virus-like particles produced in insect cells.
    • Negrete, A., Pai, A., Shiloach, J., Use of hollow fiber tangential flow filtration for the recovery and concentration of HIV virus-like particles produced in insect cells. J. Virol. Methods 2014, 195, 240-246.
    • (2014) J. Virol. Methods , vol.195 , pp. 240-246
    • Negrete, A.1    Pai, A.2    Shiloach, J.3
  • 52
    • 0033957760 scopus 로고    scopus 로고
    • Characterization and downstream processing of HIV-1 core and virus-like-particles produced in serum free medium.
    • Cruz, P. E., Peixoto, C. C., Devos, K., Moreira, L. et al., Characterization and downstream processing of HIV-1 core and virus-like-particles produced in serum free medium. Enzyme Microb. Technol. 2000, 26, 61-70.
    • (2000) Enzyme Microb. Technol. , vol.26 , pp. 61-70
    • Cruz, P.E.1    Peixoto, C.C.2    Devos, K.3    Moreira, L.4
  • 54
    • 32344436889 scopus 로고    scopus 로고
    • Exploitation of the adsorptive properties of depth filters for host cell protein removal during monoclonal antibody purification.
    • Yigzaw, Y., Piper, R., Tran, M., Shukla, A. A., Exploitation of the adsorptive properties of depth filters for host cell protein removal during monoclonal antibody purification. Biotechnol. Prog. 2006, 22, 288-296.
    • (2006) Biotechnol. Prog. , vol.22 , pp. 288-296
    • Yigzaw, Y.1    Piper, R.2    Tran, M.3    Shukla, A.A.4
  • 55
    • 77953415837 scopus 로고    scopus 로고
    • Primary clarification of very high-density cell culture harvests by enhanced cell settling.
    • Schirmer, E. B., Kuczewski, M., Golden, K., Lain, B. et al., Primary clarification of very high-density cell culture harvests by enhanced cell settling. Bioprocess. Int. 2010, 1, 32-39.
    • (2010) Bioprocess. Int. , vol.1 , pp. 32-39
    • Schirmer, E.B.1    Kuczewski, M.2    Golden, K.3    Lain, B.4
  • 56
    • 84863981909 scopus 로고    scopus 로고
    • Dynamic filtration with rotating disks, and rotating and vibrating membranes: an update.
    • Jaffrin, M. Y., Dynamic filtration with rotating disks, and rotating and vibrating membranes: an update. Curr. Opin. Chem. Eng. 2012, 1, 171-177.
    • (2012) Curr. Opin. Chem. Eng. , vol.1 , pp. 171-177
    • Jaffrin, M.Y.1
  • 57
    • 39149107782 scopus 로고    scopus 로고
    • Anion-exchange membrane chromatography for purification of rotavirus-like particles.
    • Vicente, T., Sousa, M. F., Peixoto, C., Mota, J. P. et al., Anion-exchange membrane chromatography for purification of rotavirus-like particles. J. Memb. Sci. 2008, 311, 270-283.
    • (2008) J. Memb. Sci. , vol.311 , pp. 270-283
    • Vicente, T.1    Sousa, M.F.2    Peixoto, C.3    Mota, J.P.4
  • 58
    • 84901193526 scopus 로고    scopus 로고
    • Fully aseptic single-use cross flow filtration system for clarification and concentration of cytomegalovirus-like particles.
    • Vicente, T., Burri, S., Wellnitz, S., Walsh, K. et al., Fully aseptic single-use cross flow filtration system for clarification and concentration of cytomegalovirus-like particles. Eng. Life Sci. 2014, 14, 318-326.
    • (2014) Eng. Life Sci. , vol.14 , pp. 318-326
    • Vicente, T.1    Burri, S.2    Wellnitz, S.3    Walsh, K.4
  • 59
    • 77957350005 scopus 로고    scopus 로고
    • Enterovirus 71 virus-like particle vaccine: improved production conditions for enhanced yield.
    • Chung, C.-Y., Chen, C.-Y., Lin, S.-Y., Chung, Y.-C. et al., Enterovirus 71 virus-like particle vaccine: improved production conditions for enhanced yield. Vaccine 2010, 28, 6951-6957.
    • (2010) Vaccine , vol.28 , pp. 6951-6957
    • Chung, C.-Y.1    Chen, C.-Y.2    Lin, S.-Y.3    Chung, Y.-C.4
  • 60
    • 42549117350 scopus 로고    scopus 로고
    • Process Scale Bioseparations for the Biopharmaceutical Industry
    • Taylor & Francis Group, Boca Raton
    • Shukla, A. A., Etzel, M. R., Gadam, S., Process Scale Bioseparations for the Biopharmaceutical Industry, Taylor & Francis Group, Boca Raton 2007.
    • (2007)
    • Shukla, A.A.1    Etzel, M.R.2    Gadam, S.3
  • 61
    • 0015237087 scopus 로고
    • Fractionation of proteins and viruses with polyethylene glycol.
    • Juckes, I. R. M., Town, C., Fractionation of proteins and viruses with polyethylene glycol. Biochim. Biophys. Acta 1971, 229, 535-546.
    • (1971) Biochim. Biophys. Acta , vol.229 , pp. 535-546
    • Juckes, I.R.M.1    Town, C.2
  • 62
    • 84862151028 scopus 로고    scopus 로고
    • Evaluation of four virus recovery methods for detecting noroviruses on fresh lettuce, sliced ham, and frozen raspberries.
    • Summa, M., von Bonsdorff, C.-H., Maunula, L., Evaluation of four virus recovery methods for detecting noroviruses on fresh lettuce, sliced ham, and frozen raspberries. J. Virol. Methods 2012, 183, 154-160.
    • (2012) J. Virol. Methods , vol.183 , pp. 154-160
    • Summa, M.1    von Bonsdorff, C.-H.2    Maunula, L.3
  • 63
    • 84901929662 scopus 로고    scopus 로고
    • Concentration and purification of enterovirus 71 using a weak anion-exchange monolithic column.
    • Kattur Venkatachalam, A. R., Szyporta, M., Kiener, T. K., Balraj, P., Kwang, J., Concentration and purification of enterovirus 71 using a weak anion-exchange monolithic column. Virol. J. 2014, 11, doi:10.1186/1743-422X-11-99.
    • (2014) Virol. J. , vol.11
    • Kattur Venkatachalam, A.R.1    Szyporta, M.2    Kiener, T.K.3    Balraj, P.4    Kwang, J.5
  • 64
    • 33947581656 scopus 로고    scopus 로고
    • Inactivation and purification of cowpea mosaic virus-like particles displaying peptide antigens from Bacillus anthracis
    • Phelps, J. P., Dang, N., Rasochova, L., Inactivation and purification of cowpea mosaic virus-like particles displaying peptide antigens from Bacillus anthracis, J. Virol. Methods 2007, 141, 146-153.
    • (2007) J. Virol. Methods , vol.141 , pp. 146-153
    • Phelps, J.P.1    Dang, N.2    Rasochova, L.3
  • 65
    • 84858150523 scopus 로고    scopus 로고
    • Purification of norovirus-like particles (VLPs) by ion exchange chromatography.
    • Koho, T., Mäntylä, T., Laurinmäki, P., Huhti, L. et al., Purification of norovirus-like particles (VLPs) by ion exchange chromatography. J. Virol. Methods 2012, 181, 6-11.
    • (2012) J. Virol. Methods , vol.181 , pp. 6-11
    • Koho, T.1    Mäntylä, T.2    Laurinmäki, P.3    Huhti, L.4
  • 66
    • 84876006230 scopus 로고    scopus 로고
    • Effective chikungunya virus-like particle vaccine produced in insect cells.
    • Metz, S. W., Gardner, J., Geertsema, C., Le, T. T. et al., Effective chikungunya virus-like particle vaccine produced in insect cells. PLoS Negl. Trop. Dis. 2013, 7, doi: 10.1371/journal.pntd.0002124.
    • (2013) PLoS Negl. Trop. Dis. , vol.7
    • Metz, S.W.1    Gardner, J.2    Geertsema, C.3    Le, T.T.4
  • 67
    • 68949170343 scopus 로고    scopus 로고
    • Liquid high concentration IgG1 antibody formulations by precipitation.
    • Matheus, S., Friess, W., Schwartz, D., Mahler, H.-C., Liquid high concentration IgG1 antibody formulations by precipitation. J. Pharm. Sci. 2009, 98, 3043-3057.
    • (2009) J. Pharm. Sci. , vol.98 , pp. 3043-3057
    • Matheus, S.1    Friess, W.2    Schwartz, D.3    Mahler, H.-C.4
  • 68
    • 77954733862 scopus 로고    scopus 로고
    • High-throughput screening techniques for rapid peg-based precipitation of igg4 mab from clarified cell culture supernatant.
    • Knevelman, C., Davies, J., Allen, L., Titchener-Hooker, N. J., High-throughput screening techniques for rapid peg-based precipitation of igg4 mab from clarified cell culture supernatant. Biotechnol. Prog. 2010, 26, 697-705.
    • (2010) Biotechnol. Prog. , vol.26 , pp. 697-705
    • Knevelman, C.1    Davies, J.2    Allen, L.3    Titchener-Hooker, N.J.4
  • 69
    • 84909957764 scopus 로고    scopus 로고
    • Schulz, H. Capture and intermediate purification of recombinant antibodies with combined precipitation methods.
    • Sommer, R., Tscheliessnig, A., Satzer, P., Schulz, H. et al. Capture and intermediate purification of recombinant antibodies with combined precipitation methods. Biochem. Eng. J. 2015, 93, 200-211.
    • (2015) Biochem. Eng. J. , vol.93 , pp. 200-211
    • Sommer, R.1    Tscheliessnig, A.2    Satzer, P.3
  • 70
    • 78651288673 scopus 로고    scopus 로고
    • A single-use purification process for the production of a monoclonal antibody produced in a PER.C6 human cell line.
    • Kuczewski, M., Schirmer, E., Lain, B., Zarbis-Papastoitsis, G., A single-use purification process for the production of a monoclonal antibody produced in a PER.C6 human cell line. Biotechnol. J. 2011, 6, 56-65.
    • (2011) Biotechnol. J. , vol.6 , pp. 56-65
    • Kuczewski, M.1    Schirmer, E.2    Lain, B.3    Zarbis-Papastoitsis, G.4
  • 71
    • 84887610049 scopus 로고    scopus 로고
    • Alternative separation steps for monoclonal antibody purification: Combination of centrifugal partitioning chromatography and precipitation.
    • Oelmeier, S., Ladd-Effio, C., Hubbuch, J., Alternative separation steps for monoclonal antibody purification: Combination of centrifugal partitioning chromatography and precipitation. J. Chromatogr. A 2013, 1319, 118-126.
    • (2013) J. Chromatogr. A , vol.1319 , pp. 118-126
    • Oelmeier, S.1    Ladd-Effio, C.2    Hubbuch, J.3
  • 72
    • 0019877808 scopus 로고
    • Mechanism of precipitation of proteins by polyethylene glycols.
    • Atha, D. H., Inghamg, K. C., Mechanism of precipitation of proteins by polyethylene glycols. J. Biol. Chem. 1981, 256, 12108-12117.
    • (1981) J. Biol. Chem. , vol.256 , pp. 12108-12117
    • Atha, D.H.1    Inghamg, K.C.2
  • 73
    • 65249121480 scopus 로고    scopus 로고
    • Depletion theory and the precipitation of protein by polymer.
    • Odijk, T., Depletion theory and the precipitation of protein by polymer. J. Phys. Chem. B 2009, 113, 3941-3946.
    • (2009) J. Phys. Chem. B , vol.113 , pp. 3941-3946
    • Odijk, T.1
  • 74
    • 84855655191 scopus 로고    scopus 로고
    • Protein precipitation by polyethylene glycol: A generalized model based on hydrodynamic radius.
    • Sim, S.-L., He, T., Tscheliessnig, A., Mueller, M. et al., Protein precipitation by polyethylene glycol: A generalized model based on hydrodynamic radius. J. Biotechnol. 2012, 157, 315-319.
    • (2012) J. Biotechnol. , vol.157 , pp. 315-319
    • Sim, S.-L.1    He, T.2    Tscheliessnig, A.3    Mueller, M.4
  • 75
    • 0016591521 scopus 로고
    • Size fractionation of double-stranded DNA by precipitation with polyethylene glycol.
    • Lis, J. T., Schleif, R., Size fractionation of double-stranded DNA by precipitation with polyethylene glycol. Nucleic Acids Res. 1975, 2, 383-389.
    • (1975) Nucleic Acids Res. , vol.2 , pp. 383-389
    • Lis, J.T.1    Schleif, R.2
  • 76
    • 39749156913 scopus 로고    scopus 로고
    • Polymethacrylate monoliths for preparative and industrial separation of biomolecular assemblies.
    • Jungbauer, A., Hahn, R., Polymethacrylate monoliths for preparative and industrial separation of biomolecular assemblies. J. Chromatogr. A 2008, 1184, 62-79.
    • (2008) J. Chromatogr. A , vol.1184 , pp. 62-79
    • Jungbauer, A.1    Hahn, R.2
  • 77
    • 68749116469 scopus 로고    scopus 로고
    • A novel stationary phase derivatized from hydrophilic gigaporous polystyrene-based microspheres for high-speed protein chromatography.
    • Qu, J.-B., Wan, X.-Z., Zhai, Y.-Q., Zhou, W.-Q. et al., A novel stationary phase derivatized from hydrophilic gigaporous polystyrene-based microspheres for high-speed protein chromatography. J. Chromatogr. A 2009, 1216, 6511-6516.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 6511-6516
    • Qu, J.-B.1    Wan, X.-Z.2    Zhai, Y.-Q.3    Zhou, W.-Q.4
  • 78
    • 84874961592 scopus 로고    scopus 로고
    • Role of tentacles and protein loading on pore accessibility and mass transfer in cation exchange materials for proteins
    • Thomas, H., Coquebert de Neuville, B., Storti, G., Morbidelli, M. et al., Role of tentacles and protein loading on pore accessibility and mass transfer in cation exchange materials for proteins. J. Chromatogr. A 2013, 1285, 48-56.
    • (2013) J. Chromatogr. A , vol.1285 , pp. 48-56
    • Thomas, H.1    Coquebert de Neuville, B.2    Storti, G.3    Morbidelli, M.4
  • 79
    • 84874955192 scopus 로고    scopus 로고
    • Recent advances in bioprocessing application of membrane chromatography.
    • Orr, V., Zhong, L., Moo-Young, M., Chou, C. P., Recent advances in bioprocessing application of membrane chromatography. Biotechnol. Adv. 2013, 31, 450-465.
    • (2013) Biotechnol. Adv. , vol.31 , pp. 450-465
    • Orr, V.1    Zhong, L.2    Moo-Young, M.3    Chou, C.P.4
  • 80
    • 47949122414 scopus 로고    scopus 로고
    • Purification and analysis of polyhistidine-tagged human parvovirus B19 VP1 and VP2 expressed in insect cells.
    • Michel, P. O., Mäkelä, A. R., Korhonen, E., Toivola, J. et al., Purification and analysis of polyhistidine-tagged human parvovirus B19 VP1 and VP2 expressed in insect cells. J. Virol. Methods 2008, 152, 1-5.
    • (2008) J. Virol. Methods , vol.152 , pp. 1-5
    • Michel, P.O.1    Mäkelä, A.R.2    Korhonen, E.3    Toivola, J.4
  • 81
    • 67649311618 scopus 로고    scopus 로고
    • Affinity purification of viral protein having heterogeneous quaternary structure: modeling the impact of soluble aggregates on chromatographic performance.
    • Lipin, D. I., Raj, A., Lua, L. H. L., Middelberg, A. P. J., Affinity purification of viral protein having heterogeneous quaternary structure: modeling the impact of soluble aggregates on chromatographic performance. J. Chromatogr. A 2009, 1216, 5696-5708.
    • (2009) J. Chromatogr. A , vol.1216 , pp. 5696-5708
    • Lipin, D.I.1    Raj, A.2    Lua, L.H.L.3    Middelberg, A.P.J.4
  • 82
    • 84876741659 scopus 로고    scopus 로고
    • An affinity chromatography method used to purify His-tag-displaying bio-nanocapsules.
    • Nishimura, Y., Takeda, K., Ishii, J., Ogino, C., Kondo, A., An affinity chromatography method used to purify His-tag-displaying bio-nanocapsules. J. Virol. Methods 2013, 189, 393-396.
    • (2013) J. Virol. Methods , vol.189 , pp. 393-396
    • Nishimura, Y.1    Takeda, K.2    Ishii, J.3    Ogino, C.4    Kondo, A.5
  • 83
    • 79955770870 scopus 로고    scopus 로고
    • Purification and concentration of non-infectious West Nile virus-like particles and infectious virions using a pseudo-affinity cellufine sulfate column.
    • Ohtaki, N., Takahashi, H., Kaneko, K., Gomi, Y. et al., Purification and concentration of non-infectious West Nile virus-like particles and infectious virions using a pseudo-affinity cellufine sulfate column. J. Virol. Methods 2011, 174, 131-135.
    • (2011) J. Virol. Methods , vol.174 , pp. 131-135
    • Ohtaki, N.1    Takahashi, H.2    Kaneko, K.3    Gomi, Y.4
  • 84
    • 84860354190 scopus 로고    scopus 로고
    • The choice of resin-bound ligand affects the structure and immunogenicity of column-purified human papillomavirus type 16 virus-like particles.
    • Kim, H. J., Lim, S. J., Kwag, H.-L., Kim, H.-J., The choice of resin-bound ligand affects the structure and immunogenicity of column-purified human papillomavirus type 16 virus-like particles. PLoS One 2012, 7, doi: 10.1371/journal.pone.0035893.
    • (2012) PLoS One , vol.7
    • Kim, H.J.1    Lim, S.J.2    Kwag, H.-L.3    Kim, H.-J.4
  • 85
    • 84876205224 scopus 로고    scopus 로고
    • Chromatographically-purified capsid proteins of red-spotted grouper nervous necrosis virus expressed in Saccharomyces cerevisiae form virus-like particles.
    • Choi, Y. R., Kim, H. J., Lee, J. Y., Kang, H. A., Kim, H.-J., Chromatographically-purified capsid proteins of red-spotted grouper nervous necrosis virus expressed in Saccharomyces cerevisiae form virus-like particles. Protein Expr. Purif. 2013, 89, 162-168.
    • (2013) Protein Expr. Purif. , vol.89 , pp. 162-168
    • Choi, Y.R.1    Kim, H.J.2    Lee, J.Y.3    Kang, H.A.4    Kim, H.-J.5
  • 86
    • 84862153648 scopus 로고    scopus 로고
    • Rapid and simplified purification of recombinant adeno-associated virus.
    • Guo, P., El-Gohary, Y., Prasadan, K., Shiota, C. et al., Rapid and simplified purification of recombinant adeno-associated virus. J. Virol. Methods 2012, 183, 139-146.
    • (2012) J. Virol. Methods , vol.183 , pp. 139-146
    • Guo, P.1    El-Gohary, Y.2    Prasadan, K.3    Shiota, C.4
  • 87
    • 27644529740 scopus 로고    scopus 로고
    • Ion-exchange chromatography of hepatitis B virus surface antigen from a recombinant Chinese hamster ovary cell line.
    • Zhou, W., Bi, J., Janson, J.-C., Dong, A. et al., Ion-exchange chromatography of hepatitis B virus surface antigen from a recombinant Chinese hamster ovary cell line. J. Chromatogr. A 2005, 1095, 119-125.
    • (2005) J. Chromatogr. A , vol.1095 , pp. 119-125
    • Zhou, W.1    Bi, J.2    Janson, J.-C.3    Dong, A.4
  • 88
    • 79953299871 scopus 로고    scopus 로고
    • Purification of recombinant adenovirus type 3 dodecahedric virus-like particles for biomedical applications using short monolithic columns.
    • Urbas, L., Jarc, B. L., Barut, M., Zochowska, M. et al., Purification of recombinant adenovirus type 3 dodecahedric virus-like particles for biomedical applications using short monolithic columns. J. Chromatogr. A 2011, 1218, 2451-2459.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 2451-2459
    • Urbas, L.1    Jarc, B.L.2    Barut, M.3    Zochowska, M.4
  • 89
    • 84908127258 scopus 로고    scopus 로고
    • Secreted production of assembled Norovirus virus-like particles from Pichia pastoris.
    • Tomé-Amat, J., Fleischer, L., Parker, S. A., Bardliving, C., Batt, C., Secreted production of assembled Norovirus virus-like particles from Pichia pastoris. Microb. Cell Fact. 2014, 13, doi: 10.1186/s12934-014-0134-z.
    • (2014) Microb. Cell Fact. , vol.13
    • Tomé-Amat, J.1    Fleischer, L.2    Parker, S.A.3    Bardliving, C.4    Batt, C.5
  • 90
    • 84881557289 scopus 로고    scopus 로고
    • Generation of a parvovirus B19 vaccine candidate.
    • Chandramouli, S., Medina-Selby, A., Coit, D., Schaefer, M. et al., Generation of a parvovirus B19 vaccine candidate. Vaccine 2013, 31, 3872-3878.
    • (2013) Vaccine , vol.31 , pp. 3872-3878
    • Chandramouli, S.1    Medina-Selby, A.2    Coit, D.3    Schaefer, M.4
  • 91
    • 34249873258 scopus 로고    scopus 로고
    • An automated microscale chromatographic purification of virus-like particles as a strategy for process development.
    • Wenger, M. D., Dephillips, P., Price, C. E., Bracewell, C. E., An automated microscale chromatographic purification of virus-like particles as a strategy for process development. Biotechnol. Appl. Biochem. 2007, 47, 131-139.
    • (2007) Biotechnol. Appl. Biochem. , vol.47 , pp. 131-139
    • Wenger, M.D.1    Dephillips, P.2    Price, C.E.3    Bracewell, C.E.4
  • 92
    • 0030606861 scopus 로고    scopus 로고
    • Method for obtaining unique selectivities in ion-exchange chromatography by addition of organic polymers to the mobile phase.
    • Gagnon, P., Godfrey, B., Ladd, D., Method for obtaining unique selectivities in ion-exchange chromatography by addition of organic polymers to the mobile phase. J. Chromatogr. A 1996, 743, 51-55.
    • (1996) J. Chromatogr. A , vol.743 , pp. 51-55
    • Gagnon, P.1    Godfrey, B.2    Ladd, D.3
  • 93
    • 76649091915 scopus 로고    scopus 로고
    • PEG enhances viral clearance on ceramic hydroxyapatite.
    • Snyder, M. A., Ng, P., Mekosh, H., Gagnon, P., PEG enhances viral clearance on ceramic hydroxyapatite. J. Sep. Sci. 2009, 32, 4048-4051.
    • (2009) J. Sep. Sci. , vol.32 , pp. 4048-4051
    • Snyder, M.A.1    Ng, P.2    Mekosh, H.3    Gagnon, P.4
  • 94
    • 84872270239 scopus 로고    scopus 로고
    • Principles and applications of steric exclusion chromatography.
    • Lee, J., Gan, H. T., Latiff, S. M. A., Chuah, C. et al., Principles and applications of steric exclusion chromatography. J. Chromatogr. A 2012, 1270, 162-170.
    • (2012) J. Chromatogr. A , vol.1270 , pp. 162-170
    • Lee, J.1    Gan, H.T.2    Latiff, S.M.A.3    Chuah, C.4
  • 95
    • 84891371507 scopus 로고    scopus 로고
    • High productivity purification of immunoglobulin G monoclonal antibodies on starch-coated magnetic nanoparticles by steric exclusion of polyethylene glycol.
    • Gagnon, P., Toh, P., Lee, J., High productivity purification of immunoglobulin G monoclonal antibodies on starch-coated magnetic nanoparticles by steric exclusion of polyethylene glycol. J. Chromatogr. A 2014, 1324, 171-80.
    • (2014) J. Chromatogr. A , vol.1324 , pp. 171-180
    • Gagnon, P.1    Toh, P.2    Lee, J.3
  • 96
    • 79958139618 scopus 로고    scopus 로고
    • Mixed-mode chromatography in downstream process development
    • Oehme, F., Peters, J., Mixed-mode chromatography in downstream process development. BioPharm. Int. 2010.
    • (2010) BioPharm. Int.
    • Oehme, F.1    Peters, J.2
  • 97
    • 84855204481 scopus 로고    scopus 로고
    • A monolith purification process for virus-like particles from yeast homogenate.
    • Burden, C. S., Jin, J., Podgornik, A., Bracewell, D. G., A monolith purification process for virus-like particles from yeast homogenate. J. Chromatogr. B 2012, 880, 82-89.
    • (2012) J. Chromatogr. B , vol.880 , pp. 82-89
    • Burden, C.S.1    Jin, J.2    Podgornik, A.3    Bracewell, D.G.4
  • 98
    • 77950101404 scopus 로고    scopus 로고
    • Aqueous two-phase systems: A viable platform in the manufacturing of biopharmaceuticals.
    • Rosa, P. A. J., Ferreira, I. F., Azevedo, A. M., Aires-Barros, M. R., Aqueous two-phase systems: A viable platform in the manufacturing of biopharmaceuticals. J. Chromatogr. A 2010, 1217), 2296-2305.
    • (2010) J. Chromatogr. A , vol.1217 , pp. 2296-2305
    • Rosa, P.A.J.1    Ferreira, I.F.2    Azevedo, A.M.3    Aires-Barros, M.R.4
  • 100
    • 84870035438 scopus 로고    scopus 로고
    • High-throughput screening-based selection and scale-up of aqueous two-phase systems for pDNA purification.
    • Wiendahl, M., Oelmeier, S. A., Dismer, F., Hubbuch, J., High-throughput screening-based selection and scale-up of aqueous two-phase systems for pDNA purification. J. Sep. Sci. 2012, 35, 3197-3207.
    • (2012) J. Sep. Sci. , vol.35 , pp. 3197-3207
    • Wiendahl, M.1    Oelmeier, S.A.2    Dismer, F.3    Hubbuch, J.4
  • 101
    • 84911915102 scopus 로고    scopus 로고
    • Fluid phase equilibria single stage aqueous two-phase extraction for monoclonal antibody purification from cell supernatant.
    • Muendges, J., Stark, I., Mohammad, S., Górak, A., Zeiner, T., Fluid phase equilibria single stage aqueous two-phase extraction for monoclonal antibody purification from cell supernatant. Fluid Phase Equilib. 2015, 385, 227-236.
    • (2015) Fluid Phase Equilib. , vol.385 , pp. 227-236
    • Muendges, J.1    Stark, I.2    Mohammad, S.3    Górak, A.4    Zeiner, T.5
  • 102
    • 84897021272 scopus 로고    scopus 로고
    • Multi-stage aqueous two-phase extraction for the purification of monoclonal antibodies.
    • Eggersgluess, J. K., Richter, M., Dieterle, M., Strube, J., Multi-stage aqueous two-phase extraction for the purification of monoclonal antibodies. Chem. Eng. Technol. 2014, 37, 675-682.
    • (2014) Chem. Eng. Technol. , vol.37 , pp. 675-682
    • Eggersgluess, J.K.1    Richter, M.2    Dieterle, M.3    Strube, J.4
  • 104
    • 79960382491 scopus 로고    scopus 로고
    • Scale-up of protein purifications using aqueous two-phase systems: Comparing multilayer toroidal coil chromatography with centrifugal partition chromatography.
    • Sutherland, I., Hewitson, P., Siebers, R., van den Heuvel, R. et al., Scale-up of protein purifications using aqueous two-phase systems: Comparing multilayer toroidal coil chromatography with centrifugal partition chromatography. J. Chromatogr. A 2011, 1218, 5527-5530.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 5527-5530
    • Sutherland, I.1    Hewitson, P.2    Siebers, R.3    van den Heuvel, R.4
  • 105
    • 84863784327 scopus 로고    scopus 로고
    • Design of a microfluidic platform for monoclonal antibody extraction using an aqueous two-phase system.
    • Silva, D. F. C., Azevedo, A. M., Fernandes, P., Chu, V. et al., Design of a microfluidic platform for monoclonal antibody extraction using an aqueous two-phase system. J. Chromatogr. A 2012, 1249, 1-7.
    • (2012) J. Chromatogr. A , vol.1249 , pp. 1-7
    • Silva, D.F.C.1    Azevedo, A.M.2    Fernandes, P.3    Chu, V.4
  • 107
    • 84887361839 scopus 로고    scopus 로고
    • Evaluation of PEG/phosphate aqueous two-phase systems for the purification of the chicken egg white protein avidin by using high-throughput techniques.
    • Diederich, P., Amrhein, S., Hämmerling, F., Hubbuch, J., Evaluation of PEG/phosphate aqueous two-phase systems for the purification of the chicken egg white protein avidin by using high-throughput techniques. Chem. Eng. Sci. 2013, 104, 945-956.
    • (2013) Chem. Eng. Sci. , vol.104 , pp. 945-956
    • Diederich, P.1    Amrhein, S.2    Hämmerling, F.3    Hubbuch, J.4
  • 109
    • 80054811510 scopus 로고    scopus 로고
    • Recovery of B19 virus-like particles by aqueous two-phase systems.
    • Luechau, F., Ling, T. C., Lyddiatt, A., Recovery of B19 virus-like particles by aqueous two-phase systems. Food Bioprod. Process. 2011, 89, 322-327.
    • (2011) Food Bioprod. Process. , vol.89 , pp. 322-327
    • Luechau, F.1    Ling, T.C.2    Lyddiatt, A.3
  • 110
    • 0036729223 scopus 로고    scopus 로고
    • Aqueous two-phase systems for the recovery of a recombinant viral coat protein from Escherichia coli.
    • Rito-Palomares, Middelberg, A. P., Aqueous two-phase systems for the recovery of a recombinant viral coat protein from Escherichia coli. J. Chem. Technol. Biotechnol. 2002, 77, 1025-1029.
    • (2002) J. Chem. Technol. Biotechnol. , vol.77 , pp. 1025-1029
    • Rito-Palomares, M.1    Middelberg, A.P.2
  • 111
    • 49849093646 scopus 로고    scopus 로고
    • Critical evaluation and comparison of fluid distribution systems for industrial scale expanded bed adsorption chromatography columns.
    • Arpanaei, A., Heebøll Nielsen, A., Hubbuch, J. J., Thomas, O. R. T., Hobley, T. J., Critical evaluation and comparison of fluid distribution systems for industrial scale expanded bed adsorption chromatography columns., J. Chromatogr. A 2008, 1198-1199, 131-139.
    • (2008) J. Chromatogr. A , vol.1198-1199 , pp. 131-139
    • Arpanaei, A.1    Heebøll Nielsen, A.2    Hubbuch, J.J.3    Thomas, O.R.T.4    Hobley, T.J.5
  • 112
    • 55049115983 scopus 로고    scopus 로고
    • Effect of different operating modes and biomass concentrations on the recovery of recombinant hepatitis B core antigen from thermal-treated unclarified Escherichia coli feedstock.
    • Ng, M. Y. T., Tan, W. S., Abdullah, N., Ling, T. C., Tey, B. T., Effect of different operating modes and biomass concentrations on the recovery of recombinant hepatitis B core antigen from thermal-treated unclarified Escherichia coli feedstock. J. Biotechnol. 2008, 138, 74-79.
    • (2008) J. Biotechnol. , vol.138 , pp. 74-79
    • Ng, M.Y.T.1    Tan, W.S.2    Abdullah, N.3    Ling, T.C.4    Tey, B.T.5
  • 113
    • 77952553509 scopus 로고    scopus 로고
    • Purification of His-tagged hepatitis B core antigen from unclarified bacterial homogenate using immobilized metal affinity-expanded bed adsorption chromatography.
    • Yap, W. B., Tey, B. T., Alitheen, N. B. M., Tan, W. S., Purification of His-tagged hepatitis B core antigen from unclarified bacterial homogenate using immobilized metal affinity-expanded bed adsorption chromatography. J. Chromatogr. A 2010, 1217, 3473-3480.
    • (2010) J. Chromatogr. A , vol.1217 , pp. 3473-3480
    • Yap, W.B.1    Tey, B.T.2    Alitheen, N.B.M.3    Tan, W.S.4
  • 114
    • 84928826761 scopus 로고    scopus 로고
    • Methods for capturing virus like particles from plants using expanded bed chromatogrpahy
    • Cabrera, R., Lihme, A., Oishi, K., Vaarst, I., Methods for capturing virus like particles from plants using expanded bed chromatogrpahy US Patent App. PCT/EP2011/068, 919, 2012.
    • (2012) , vol.919
    • Cabrera, R.1    Lihme, A.2    Oishi, K.3    Vaarst, I.4
  • 115
    • 78650482581 scopus 로고    scopus 로고
    • Release and stability testing programs for a novel virus-like particle vaccine
    • Pincus, S., Boddapati, S., Li, J., Sadowski, T., Release and stability testing programs for a novel virus-like particle vaccine. BioPharm. Int. 2010.
    • (2010) BioPharm. Int.
    • Pincus, S.1    Boddapati, S.2    Li, J.3    Sadowski, T.4
  • 116
    • 84928824039 scopus 로고    scopus 로고
    • Removal of DNA and baculovirus from influenza virus-like particles using Capto™
    • GE Healthcare, Removal of DNA and baculovirus from influenza virus-like particles using Capto™ Q. BioPharm. Int. 2011.
    • (2011) Q. BioPharm. Int.
  • 117
    • 80955180108 scopus 로고    scopus 로고
    • Reduced surface area chromatography for flow-through purification of viruses and virus like particles.
    • Iyer, G., Ramaswamy, S., Asher, D., Mehta, U. et al., Reduced surface area chromatography for flow-through purification of viruses and virus like particles. J. Chromatogr. A 2011, 1218, 3973-3981.
    • (2011) J. Chromatogr. A , vol.1218 , pp. 3973-3981
    • Iyer, G.1    Ramaswamy, S.2    Asher, D.3    Mehta, U.4
  • 118
    • 84860470797 scopus 로고    scopus 로고
    • Flow-through purification of viruses - a novel approach to vaccine purification.
    • Iyer, G., Ramaswamy, S., Cheng, K.-S., Sisowath, N. et al., Flow-through purification of viruses - a novel approach to vaccine purification. Procedia Vaccinol. 2012, 6, 106-112.
    • (2012) Procedia Vaccinol. , vol.6 , pp. 106-112
    • Iyer, G.1    Ramaswamy, S.2    Cheng, K.-S.3    Sisowath, N.4
  • 119
    • 84894116625 scopus 로고    scopus 로고
    • Coxsackievirus B3 VLPs purified by ion exchange chromatography elicit strong immune responses in mice.
    • Koho, T., Koivunen, M. R. L., Oikarinen, S., Kummola, L. et al., Coxsackievirus B3 VLPs purified by ion exchange chromatography elicit strong immune responses in mice. Antiviral Res. 2014, 104, 93-101.
    • (2014) Antiviral Res. , vol.104 , pp. 93-101
    • Koho, T.1    Koivunen, M.R.L.2    Oikarinen, S.3    Kummola, L.4
  • 120
    • 75349097689 scopus 로고    scopus 로고
    • One-step chromatographic purification of human papillomavirus type 16 L1 protein from Saccharomyces cerevisiae.
    • Kim, H. J., Kim, S. Y., Lim, S. J., Kim, J. Y. et al., One-step chromatographic purification of human papillomavirus type 16 L1 protein from Saccharomyces cerevisiae. Protein Expr. Purif. 2010, 70, 68-74.
    • (2010) Protein Expr. Purif. , vol.70 , pp. 68-74
    • Kim, H.J.1    Kim, S.Y.2    Lim, S.J.3    Kim, J.Y.4
  • 121
    • 79955788536 scopus 로고    scopus 로고
    • Process for purifying human papillomavirus virus-like particles
    • Cook III, J. C., Process for purifying human papillomavirus virus-like particles, US Patent 6602697, 2003.
    • (2003)
    • Cook, J.C.1
  • 122
    • 78349255910 scopus 로고    scopus 로고
    • Adsorption of plasmid DNA on ceramic hydroxyapatite chromatographic materials.
    • Schmoeger, E., Paril, C., Tscheliessnig, R., Jungbauer, A., Adsorption of plasmid DNA on ceramic hydroxyapatite chromatographic materials. J. Sep. Sci. 2010, 33, 3125-3136.
    • (2010) J. Sep. Sci. , vol.33 , pp. 3125-3136
    • Schmoeger, E.1    Paril, C.2    Tscheliessnig, R.3    Jungbauer, A.4
  • 123
    • 84899416287 scopus 로고    scopus 로고
    • Enhanced production of Chikungunya virus-like particles using a high-pH adapted Spodoptera frugiperda insect cell line.
    • Wagner, J. M., Pajerowski, J. D., Daniels, C. L., McHugh, P. M. et al., Enhanced production of Chikungunya virus-like particles using a high-pH adapted Spodoptera frugiperda insect cell line. PLoS One 2014, 9, doi: 10.1371/journal.pone.0094401.
    • (2014) PLoS One , vol.9
    • Wagner, J.M.1    Pajerowski, J.D.2    Daniels, C.L.3    McHugh, P.M.4
  • 124
    • 79960437296 scopus 로고    scopus 로고
    • Efficient disulfide bond formation in virus-like particles.
    • Bundy, B. C., Swartz, J. R., Efficient disulfide bond formation in virus-like particles. J. Biotechnol. 2011, 154, 230-239.
    • (2011) J. Biotechnol. , vol.154 , pp. 230-239
    • Bundy, B.C.1    Swartz, J.R.2
  • 125
    • 46649083183 scopus 로고    scopus 로고
    • A quantitative description of in vitro assembly of human papillomavirus 16 virus-like particles.
    • Mukherjee, S., Thorsteinsson, M. V., Johnston, L. B., DePhillips, P. A., Zlotnick, A., A quantitative description of in vitro assembly of human papillomavirus 16 virus-like particles. J. Mol. Biol. 2008, 381, 229-237.
    • (2008) J. Mol. Biol. , vol.381 , pp. 229-237
    • Mukherjee, S.1    Thorsteinsson, M.V.2    Johnston, L.B.3    DePhillips, P.A.4    Zlotnick, A.5
  • 126
    • 84864823463 scopus 로고    scopus 로고
    • Reactive diafiltration for assembly and formulation of virus-like particles.
    • Liew, M. W. O., Chuan, Y. P., Middelberg, A. P. J., Reactive diafiltration for assembly and formulation of virus-like particles. Biochem. Eng. J. 2012, 68, 120-128.
    • (2012) Biochem. Eng. J. , vol.68 , pp. 120-128
    • Liew, M.W.O.1    Chuan, Y.P.2    Middelberg, A.P.J.3
  • 127
    • 84944896073 scopus 로고    scopus 로고
    • Formulation and stabilization of recombinant protein based virus-like particle vaccines
    • Jain, N. K. Sahni, N., Kumru, O. S., Joshi, S. B. et al., Formulation and stabilization of recombinant protein based virus-like particle vaccines. Adv. Drug Deliv. Rev. 2014, doi: 10.1016/j.addr2014.10.023.
    • (2014) Adv. Drug Deliv. Rev.
    • Jain, N.K.1    Sahni, N.2    Kumru, O.S.3    Joshi, S.B.4
  • 128
    • 84862215230 scopus 로고    scopus 로고
    • Influenza M1 VLPs containing neuraminidase induce heterosubtypic cross-protection.
    • Quan, F.-S., Kim, M.-C., Lee, B.-J., Song, J.-M. et al., Influenza M1 VLPs containing neuraminidase induce heterosubtypic cross-protection. Virology 2012, 430, 127-135.
    • (2012) Virology , vol.430 , pp. 127-135
    • Quan, F.-S.1    Kim, M.-C.2    Lee, B.-J.3    Song, J.-M.4
  • 129
    • 60149106150 scopus 로고    scopus 로고
    • Quality by design for biopharmaceuticals.
    • Rathore, A. S., Winkle, H., Quality by design for biopharmaceuticals. Nat. Biotechnol. 2009, 27, 26-37.
    • (2009) Nat. Biotechnol. , vol.27 , pp. 26-37
    • Rathore, A.S.1    Winkle, H.2
  • 130
    • 84888200366 scopus 로고    scopus 로고
    • Utilizing dynamic light scattering as a process analytical technology for protein folding and aggregation monitoring in vaccine manufacturing.
    • Yu, Z., Reid, J. C., Yang, Y.-P., Utilizing dynamic light scattering as a process analytical technology for protein folding and aggregation monitoring in vaccine manufacturing. J. Pharm. Sci. 2013, 102, 4284-4290.
    • (2013) J. Pharm. Sci. , vol.102 , pp. 4284-4290
    • Yu, Z.1    Reid, J.C.2    Yang, Y.-P.3
  • 131
    • 0026799147 scopus 로고
    • Steric mass-action ion exchange: Displacement profiles and induced salt gradients.
    • Brooks, C. A., Cramer, S. M., Steric mass-action ion exchange: Displacement profiles and induced salt gradients. AIChE J. 1992, 38, 1969-1978.
    • (1992) AIChE J. , vol.38 , pp. 1969-1978
    • Brooks, C.A.1    Cramer, S.M.2
  • 132
    • 84893981827 scopus 로고    scopus 로고
    • Adjoint-based estimation and optimization for column liquid chromatography models.
    • Hahn, T., Sommer, A., Osberghaus, A., Heuveline, V., Hubbuch, J., Adjoint-based estimation and optimization for column liquid chromatography models. Comput. Chem. Eng. 2014, 64, 41-54.
    • (2014) Comput. Chem. Eng. , vol.64 , pp. 41-54
    • Hahn, T.1    Sommer, A.2    Osberghaus, A.3    Heuveline, V.4    Hubbuch, J.5
  • 133
    • 84907495064 scopus 로고    scopus 로고
    • Model-based integrated optimization and evaluation of a multi-step ion exchange chromatography.
    • Huuk, T. C., Hahn, T., Osberghaus, A., Hubbuch, J., Model-based integrated optimization and evaluation of a multi-step ion exchange chromatography. Sep. Purif. Technol. 2014, 136, 207-222.
    • (2014) Sep. Purif. Technol. , vol.136 , pp. 207-222
    • Huuk, T.C.1    Hahn, T.2    Osberghaus, A.3    Hubbuch, J.4
  • 134
    • 28244461283 scopus 로고    scopus 로고
    • High throughput screening of chromatographic phases for rapid process development.
    • Bensch, M., Schulze Wierling, P., von Lieres, E., Hubbuch, J., High throughput screening of chromatographic phases for rapid process development. Chem. Eng. Technol. 2005, 28, 1274-1284.
    • (2005) Chem. Eng. Technol. , vol.28 , pp. 1274-1284
    • Bensch, M.1    Schulze Wierling, P.2    von Lieres, E.3    Hubbuch, J.4
  • 135
    • 46049105929 scopus 로고    scopus 로고
    • High throughput screening for the design and optimization of chromatographic processes - miniaturization, automation and parallelization of breakthrough and elution studies.
    • Wiendahl, M., Schulze Wierling, P., Nielsen, J., Fomsgaard Christensen, D. et al., High throughput screening for the design and optimization of chromatographic processes - miniaturization, automation and parallelization of breakthrough and elution studies. Chem. Eng. Technol. 2008, 31, 893-903.
    • (2008) Chem. Eng. Technol. , vol.31 , pp. 893-903
    • Wiendahl, M.1    Schulze Wierling, P.2    Nielsen, J.3    Fomsgaard Christensen, D.4
  • 136
    • 84864550319 scopus 로고    scopus 로고
    • High throughput screening based selection of phases for aqueous two-phase system-centrifugal partitioning chromatography of monoclonal antibodies.
    • Oelmeier, S. A., Ladd Effio, C., Hubbuch, J., High throughput screening based selection of phases for aqueous two-phase system-centrifugal partitioning chromatography of monoclonal antibodies. J. Chromatogr. A 2012, 1252, 104-114.
    • (2012) J. Chromatogr. A , vol.1252 , pp. 104-114
    • Oelmeier, S.A.1    Ladd Effio, C.2    Hubbuch, J.3
  • 137
    • 84878948573 scopus 로고    scopus 로고
    • Protein and virus-like particle adsorption on perfusion chromatography media
    • Wu, Y., Simons, J., Hooson, S., Abraham, D., Carta, G., Protein and virus-like particle adsorption on perfusion chromatography media. J. Chromatogr. A 2013, 1297, 96-105.
    • (2013) J. Chromatogr. A , vol.1297 , pp. 96-105
    • Wu, Y.1    Simons, J.2    Hooson, S.3    Abraham, D.4    Carta, G.5
  • 138
    • 60349103484 scopus 로고    scopus 로고
    • Quantitative characterization of virus-like particles by asymmetrical flow field flow fractionation, electrospray differential mobility analysis, and transmission electron microscopy.
    • Pease, L. F., Lipin, D. I., Tsai, D.-H., Zachariah, M. R. et al., Quantitative characterization of virus-like particles by asymmetrical flow field flow fractionation, electrospray differential mobility analysis, and transmission electron microscopy. Biotechnol. Bioeng. 2009, 102, 845-855.
    • (2009) Biotechnol. Bioeng. , vol.102 , pp. 845-855
    • Pease, L.F.1    Lipin, D.I.2    Tsai, D.-H.3    Zachariah, M.R.4
  • 139
    • 84878864148 scopus 로고    scopus 로고
    • Virus-like particle formulation optimization by miniaturized high-throughput screening.
    • Mohr, J., Chuan, M. R., Wu, Y., Lua, L. H. L., Middelberg, A. P. J., Virus-like particle formulation optimization by miniaturized high-throughput screening. Methods 2013, 60, 248-256.
    • (2013) Methods , vol.60 , pp. 248-256
    • Mohr, J.1    Chuan, M.R.2    Wu, Y.3    Lua, L.H.L.4    Middelberg, A.P.J.5
  • 141
    • 79251613176 scopus 로고    scopus 로고
    • Interrogating viral capsid assembly with ion mobility-mass spectrometry.
    • Uetrecht, C., Barbu, I. M., Shoemaker, G. K., van Duijn, E., Heck, A. J. R., Interrogating viral capsid assembly with ion mobility-mass spectrometry. Nat. Chem. 2011, 3, 126-132.
    • (2011) Nat. Chem. , vol.3 , pp. 126-132
    • Uetrecht, C.1    Barbu, I.M.2    Shoemaker, G.K.3    van Duijn, E.4    Heck, A.J.R.5
  • 142
    • 84928825769 scopus 로고    scopus 로고
    • Virus-like particle and nano-particle vaccines 2014 - session 10 technology.
    • Ladd Effio, C., Hubbuch, J., Virus-like particle and nano-particle vaccines 2014 - session 10 technology. Hum. Vaccin. Immunother. 2014, 10, doi: 10.4161/hv.29840.
    • (2014) Hum. Vaccin. Immunother. , vol.10
    • Ladd Effio, C.1    Hubbuch, J.2
  • 143
    • 84903784731 scopus 로고    scopus 로고
    • Quantitative real-time single particle analysis of virions.
    • Heider, S., Metzner, C., Quantitative real-time single particle analysis of virions. Virology 2014, 462-463, 199-206.
    • (2014) Virology , vol.462-463 , pp. 199-206
    • Heider, S.1    Metzner, C.2
  • 144
    • 84901596042 scopus 로고    scopus 로고
    • A tool for selective inline quantification of co-eluting proteins in chromatography using spectral analysis and partial least squares regression.
    • Brestrich, N., Briskot, T., Osberghaus, A., Hubbuch, J., A tool for selective inline quantification of co-eluting proteins in chromatography using spectral analysis and partial least squares regression. Biotechnol. Bioeng. 2014, 111, 1365-1373.
    • (2014) Biotechnol. Bioeng. , vol.111 , pp. 1365-1373
    • Brestrich, N.1    Briskot, T.2    Osberghaus, A.3    Hubbuch, J.4
  • 145
    • 84890936701 scopus 로고    scopus 로고
    • Rapid manufacture and release of a GMP batch of avian influenza A(H7N9) virus-like particle vaccine made using recombinant baculovirus-Sf9 insect cell culture technology.
    • Hahn, B. T. J., Courbron, D., Hamer, M., Masoud, M. et al., Rapid manufacture and release of a GMP batch of avian influenza A(H7N9) virus-like particle vaccine made using recombinant baculovirus-Sf9 insect cell culture technology. Bioprocess. J. 2013, 12, 1-10.
    • (2013) Bioprocess. J. , vol.12 , pp. 1-10
    • Hahn, B.T.J.1    Courbron, D.2    Hamer, M.3    Masoud, M.4
  • 146
    • 84881663089 scopus 로고    scopus 로고
    • Continuous purification of influenza virus using simulated moving bed chromatography.
    • Kröber, T., Wolff, M. W., Hundt, B., Seidel-Morgenstern, A., Reichl, U., Continuous purification of influenza virus using simulated moving bed chromatography. J. Chromatogr. A 2013, 1307, 99-110.
    • (2013) J. Chromatogr. A , vol.1307 , pp. 99-110
    • Kröber, T.1    Wolff, M.W.2    Hundt, B.3    Seidel-Morgenstern, A.4    Reichl, U.5
  • 147
    • 84901014122 scopus 로고    scopus 로고
    • Adenovirus purification by two-column, size-exclusion, simulated countercurrent chromatography.
    • Nestola, P., Silva, R. J. S., Peixoto, C., Alves, P. M. et al., Adenovirus purification by two-column, size-exclusion, simulated countercurrent chromatography. J. Chromatogr. A 2014, 1347, 111-121.
    • (2014) J. Chromatogr. A , vol.1347 , pp. 111-121
    • Nestola, P.1    Silva, R.J.S.2    Peixoto, C.3    Alves, P.M.4
  • 148
    • 84888437091 scopus 로고    scopus 로고
    • Chikungunya virus-like particles are more immunogenic in a lethal AG129 mouse model compared to glycoprotein E1 or E2 subunits.
    • Metz, S. W., Martina, B. E., van den Doel, P., Geertsema, C. et al., Chikungunya virus-like particles are more immunogenic in a lethal AG129 mouse model compared to glycoprotein E1 or E2 subunits. Vaccine 2013, 31, 6092-6096.
    • (2013) Vaccine , vol.31 , pp. 6092-6096
    • Metz, S.W.1    Martina, B.E.2    van den Doel, P.3    Geertsema, C.4
  • 149
    • 80052408375 scopus 로고    scopus 로고
    • Next generation dengue vaccines: a review of candidates in preclinical development.
    • Schmitz, J., Roehrig, J., Barrett, A., Hombach, J., Next generation dengue vaccines: a review of candidates in preclinical development. Vaccine 2011, 29, 7276-7284.
    • (2011) Vaccine , vol.29 , pp. 7276-7284
    • Schmitz, J.1    Roehrig, J.2    Barrett, A.3    Hombach, J.4
  • 150
    • 84903819994 scopus 로고    scopus 로고
    • A virus-like particle based bivalent vaccine confers dual protection against enterovirus 71 and coxsackievirus A16 infections in mice.
    • Ku, Z., Liu, Q., Ye, X., Cai, Y. et al., A virus-like particle based bivalent vaccine confers dual protection against enterovirus 71 and coxsackievirus A16 infections in mice. Vaccine 2014, 32, 4296-4303.
    • (2014) Vaccine , vol.32 , pp. 4296-4303
    • Ku, Z.1    Liu, Q.2    Ye, X.3    Cai, Y.4
  • 151
    • 84861740160 scopus 로고    scopus 로고
    • Immunogenicity of HIV virus-like particles in rhesus macaques by intranasal administration.
    • Buonaguro, L., Tagliamonte, M., Visciano, M. L., Andersen, H. et al., Immunogenicity of HIV virus-like particles in rhesus macaques by intranasal administration. Clin. Vaccine Immunol. 2012, 19, 970-973.
    • (2012) Clin. Vaccine Immunol. , vol.19 , pp. 970-973
    • Buonaguro, L.1    Tagliamonte, M.2    Visciano, M.L.3    Andersen, H.4
  • 152
    • 70350075480 scopus 로고    scopus 로고
    • HPV vaccines: preclinical development.
    • Gissmann, L., HPV vaccines: preclinical development. Arch. Med. Res. 2009, 40, 466-470.
    • (2009) Arch. Med. Res. , vol.40 , pp. 466-470
    • Gissmann, L.1
  • 153
    • 84896313766 scopus 로고    scopus 로고
    • Improved characteristics and protective efficacy in an animal model of E. coli-derived recombinant double-layered rotavirus virus-like particles.
    • Li, T., Lin, H., Zhang, Y., Li, M. et al., Improved characteristics and protective efficacy in an animal model of E. coli-derived recombinant double-layered rotavirus virus-like particles. Vaccine 2014, 32, 1921-1931.
    • (2014) Vaccine , vol.32 , pp. 1921-1931
    • Li, T.1    Lin, H.2    Zhang, Y.3    Li, M.4
  • 154
    • 84928828265 scopus 로고    scopus 로고
    • Safety and tolerability of chikungunya virus-like particle vaccine in healthy adults: a phase 1 dose-escalation trial.
    • Chang, L.-J., Dowd, K. A., Mendoza, F. H., Saunders, J. G. et al., Safety and tolerability of chikungunya virus-like particle vaccine in healthy adults: a phase 1 dose-escalation trial. Lancet 2014, 6736, 25-27.
    • (2014) Lancet , vol.6736 , pp. 25-27
    • Chang, L.-J.1    Dowd, K.A.2    Mendoza, F.H.3    Saunders, J.G.4
  • 155
    • 84920878757 scopus 로고    scopus 로고
    • International community ramps up Ebola vaccine effort.
    • Mohammadi, D., International community ramps up Ebola vaccine effort. Lancet 2014, 384, 1658-1659.
    • (2014) Lancet , vol.384 , pp. 1658-1659
    • Mohammadi, D.1
  • 156
    • 84906080801 scopus 로고    scopus 로고
    • Safety and immunogenicity of a virus-like particle pandemic influenza A (H1N1) 2009 vaccine: Results from a double-blinded, randomized Phase I clinical trial in healthy Asian volunteers.
    • Low, J. G. H., Lee, L. S., Ooi, E. E., Ethirajulu, K. et al., Safety and immunogenicity of a virus-like particle pandemic influenza A (H1N1) 2009 vaccine: Results from a double-blinded, randomized Phase I clinical trial in healthy Asian volunteers. Vaccine 2014, 32, 5041-5048.
    • (2014) Vaccine , vol.32 , pp. 5041-5048
    • Low, J.G.H.1    Lee, L.S.2    Ooi, E.E.3    Ethirajulu, K.4
  • 157
    • 84908003879 scopus 로고    scopus 로고
    • Human antibody response to N-glycans present on plant-made influenza virus-like particle (VLP) vaccines.
    • Ward, B. J., Landry, N., Trépanier, S., Mercier, G. et al., Human antibody response to N-glycans present on plant-made influenza virus-like particle (VLP) vaccines. Vaccine 2014, 32, 6098-6106.
    • (2014) Vaccine , vol.32 , pp. 6098-6106
    • Ward, B.J.1    Landry, N.2    Trépanier, S.3    Mercier, G.4
  • 158
    • 84890932195 scopus 로고    scopus 로고
    • A recombinant viruslike particle influenza a (h7n9) vaccine.
    • Fries, L. F., Smith, G. E., Glenn, G. M., A recombinant viruslike particle influenza a (h7n9) vaccine. N. Engl. J. Med. 2013, 369, 2564-2566.
    • (2013) N. Engl. J. Med. , vol.369 , pp. 2564-2566
    • Fries, L.F.1    Smith, G.E.2    Glenn, G.M.3
  • 159
    • 84871661160 scopus 로고    scopus 로고
    • Safety and immunogenicity of a Sf9 insect cell-derived respiratory syncytial virus fusion protein nanoparticle vaccine.
    • Glenn, G. M., Smith, G., Fries, L., Raghunandan, R. et al., Safety and immunogenicity of a Sf9 insect cell-derived respiratory syncytial virus fusion protein nanoparticle vaccine. Vaccine 2013, 31, 524-532.
    • (2013) Vaccine , vol.31 , pp. 524-532
    • Glenn, G.M.1    Smith, G.2    Fries, L.3    Raghunandan, R.4
  • 160
    • 84928826832 scopus 로고    scopus 로고
    • Active Ab Immunotherapy Cad106 Phase Ii Dose-Adjuvant Finding Study: Immune Response.
    • Riviere, M.-E., Caputo, A., Laurent, N., Vostiar, I. et al., Active Ab Immunotherapy Cad106 Phase Ii Dose-Adjuvant Finding Study: Immune Response. Alzheimer's Dement. 2014, 10, 447-448.
    • (2014) Alzheimer's Dement. , vol.10 , pp. 447-448
    • Riviere, M.-E.1    Caputo, A.2    Laurent, N.3    Vostiar, I.4
  • 161
    • 84928826575 scopus 로고    scopus 로고
    • Active Ab Immunotherapy Cad106 Phase Ii Dose-Adjuvant Finding Study: Amyloid Pet.
    • Caputo, A., Graf, A., Riviere, M.-E., Alva, G. et al., Active Ab Immunotherapy Cad106 Phase Ii Dose-Adjuvant Finding Study: Amyloid Pet. Alzheimer's Dement. 2014, 10, 445-446.
    • (2014) Alzheimer's Dement. , vol.10 , pp. 445-446
    • Caputo, A.1    Graf, A.2    Riviere, M.-E.3    Alva, G.4
  • 162
    • 80053606312 scopus 로고    scopus 로고
    • Safety and immunogenicity of a virus-like particle pandemic influenza A (H1N1) 2009 vaccine in a blinded, randomized, placebo-controlled trial of adults in Mexico.
    • López-Macías, C., Ferat-Osorio, E., Tenorio-Calvo, T., Isibasi, A., Safety and immunogenicity of a virus-like particle pandemic influenza A (H1N1) 2009 vaccine in a blinded, randomized, placebo-controlled trial of adults in Mexico. Vaccine 2011, 29, 7826-7834.
    • (2011) Vaccine , vol.29 , pp. 7826-7834
    • López-Macías, C.1    Ferat-Osorio, E.2    Tenorio-Calvo, T.3    Isibasi, A.4
  • 163
    • 84920589100 scopus 로고    scopus 로고
    • Robust mucosal-homing antibody-secreting B cell responses induced by intramuscular administration of adjuvanted bivalent human norovirus-like particle vaccine.
    • Sundararajan, A., Sangster, M. Y., Frey, S., Atmar, R. L. et al., Robust mucosal-homing antibody-secreting B cell responses induced by intramuscular administration of adjuvanted bivalent human norovirus-like particle vaccine. Vaccine 2014, 33, 568-576.
    • (2014) Vaccine , vol.33 , pp. 568-576
    • Sundararajan, A.1    Sangster, M.Y.2    Frey, S.3    Atmar, R.L.4
  • 164
    • 84892143669 scopus 로고    scopus 로고
    • Update on vaccination clinical trials for HPV-related disease.
    • Erickson, B. K., Landers, E. E., Huh, W. K., Update on vaccination clinical trials for HPV-related disease. Clin. Ther. 2014, 36, 8-16.
    • (2014) Clin. Ther. , vol.36 , pp. 8-16
    • Erickson, B.K.1    Landers, E.E.2    Huh, W.K.3
  • 165
    • 84906100154 scopus 로고    scopus 로고
    • Efficacy of the HPV-16/18 vaccine: final according to protocol results from the blinded phase of the randomized Costa Rica HPV-16/18 vaccine trial.
    • Hildesheim, A., Wacholder, S., Catteau, G., Struyf, F. et al., Efficacy of the HPV-16/18 vaccine: final according to protocol results from the blinded phase of the randomized Costa Rica HPV-16/18 vaccine trial. Vaccine 2014, 32, 5087-5097.
    • (2014) Vaccine , vol.32 , pp. 5087-5097
    • Hildesheim, A.1    Wacholder, S.2    Catteau, G.3    Struyf, F.4
  • 166
    • 84908577108 scopus 로고    scopus 로고
    • Immunogenicity and safety of the candidate RTS, S/AS01 vaccine in young Nigerian children: A randomized, double-blind, lot-to-lot consistency trial.
    • Umeh, R., Oguche, S., Oguonu, T., Pitmang, S. et al., Immunogenicity and safety of the candidate RTS, S/AS01 vaccine in young Nigerian children: A randomized, double-blind, lot-to-lot consistency trial. Vaccine 2014, 32, 6556-6562.
    • (2014) Vaccine , vol.32 , pp. 6556-6562
    • Umeh, R.1    Oguche, S.2    Oguonu, T.3    Pitmang, S.4
  • 167
    • 84896720902 scopus 로고    scopus 로고
    • HPV vaccines to prevent cervical cancer and genital warts: An update
    • Dochez, C., Bogers, J. J., Verhelst, R., Rees, H., HPV vaccines to prevent cervical cancer and genital warts: An update Vaccine 2014, 32, 1595-1601.
    • (2014) Vaccine , vol.32 , pp. 1595-1601
    • Dochez, C.1    Bogers, J.J.2    Verhelst, R.3    Rees, H.4
  • 168
    • 27744587277 scopus 로고    scopus 로고
    • Antibody response to Engerix-B® and Recombivax-HB® hepatitis B vaccination in end-stage renal disease.
    • Lacson, E., Teng, M., Ong, J., Vienneau, L. et al., Antibody response to Engerix-B® and Recombivax-HB® hepatitis B vaccination in end-stage renal disease. Hemodial. Int. 2005, 9, 367-375.
    • (2005) Hemodial. Int. , vol.9 , pp. 367-375
    • Lacson, E.1    Teng, M.2    Ong, J.3    Vienneau, L.4
  • 169
    • 84902536500 scopus 로고    scopus 로고
    • Robust manufacturing and comprehensive characterization of recombinant hepatitis E virus-like particles in Hecolin®.
    • Zhang, X., Wei, M., Pan, H., Lin, Z. et al., Robust manufacturing and comprehensive characterization of recombinant hepatitis E virus-like particles in Hecolin®. Vaccine 2014, 32, 4039-4050.
    • (2014) Vaccine , vol.32 , pp. 4039-4050
    • Zhang, X.1    Wei, M.2    Pan, H.3    Lin, Z.4
  • 170
    • 32644455287 scopus 로고    scopus 로고
    • Purification of recombinant nucleocapsid protein of Newcastle disease virus from unclarified feedstock using expanded bed adsorption chromatography.
    • Tan, Y. P., Ling, T. C., Tan, W. S., Yusoff, K., Tey, B. T., Purification of recombinant nucleocapsid protein of Newcastle disease virus from unclarified feedstock using expanded bed adsorption chromatography. Protein Expr. Purif. 2006, 46, 114-121.
    • (2006) Protein Expr. Purif. , vol.46 , pp. 114-121
    • Tan, Y.P.1    Ling, T.C.2    Tan, W.S.3    Yusoff, K.4    Tey, B.T.5


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