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Volumn 29, Issue 6, 2011, Pages 869-878

Rational design and optimization of downstream processes of virus particles for biopharmaceutical applications: Current advances

Author keywords

Analytical technologies; Ion exchange chromatography; Mathematical model; Membrane processes; Viral vector; Virus like particle

Indexed keywords

ANALYTICAL TECHNOLOGY; ION-EXCHANGE CHROMATOGRAPHY; MEMBRANE PROCESSES; VIRAL VECTORS; VIRUS-LIKE PARTICLES;

EID: 80053444587     PISSN: 07349750     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.biotechadv.2011.07.004     Document Type: Review
Times cited : (56)

References (117)
  • 1
    • 0019940499 scopus 로고
    • Rapid purification of extracellular and intracellular moloney murine leukemia virus
    • Aboud M., Wolfson M., Hassan Y., Huleihel M. Rapid purification of extracellular and intracellular moloney murine leukemia virus. Arch Virol 1982, 71:185-195.
    • (1982) Arch Virol , vol.71 , pp. 185-195
    • Aboud, M.1    Wolfson, M.2    Hassan, Y.3    Huleihel, M.4
  • 2
    • 77950858020 scopus 로고    scopus 로고
    • High aav vector purity results in serotype- and tissue-independent enhancement of transduction efficiency
    • Ayuso E., Mingozzi F., Montane J., Leon X., Anguela X.M., Haurigot V., et al. High aav vector purity results in serotype- and tissue-independent enhancement of transduction efficiency. Gene Ther 2010, 17:503-510.
    • (2010) Gene Ther , vol.17 , pp. 503-510
    • Ayuso, E.1    Mingozzi, F.2    Montane, J.3    Leon, X.4    Anguela, X.M.5    Haurigot, V.6
  • 3
    • 0032936272 scopus 로고    scopus 로고
    • Concentration of recombinant baculovirus by cation-exchange chromatography
    • Barsoum J. Concentration of recombinant baculovirus by cation-exchange chromatography. Biotechniques 1999, 26:834-836.
    • (1999) Biotechniques , vol.26 , pp. 834-836
    • Barsoum, J.1
  • 5
    • 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
  • 6
    • 17644424942 scopus 로고    scopus 로고
    • The process development challenge for a new vaccine
    • Buckland B.C. The process development challenge for a new vaccine. Nat Med 2005, 11:S16-S19.
    • (2005) Nat Med , vol.11
    • Buckland, B.C.1
  • 7
    • 75349098046 scopus 로고    scopus 로고
    • Thermosensitivity of the reverse transcription process as an inactivation mechanism of lentiviral vectors
    • Carmo M., Dias J.D., Panet A., Coroadinha A.S., Carrondo M.J.T., Alves P.M., et al. Thermosensitivity of the reverse transcription process as an inactivation mechanism of lentiviral vectors. Hum Gene Ther 2009, 20:1168-1176.
    • (2009) Hum Gene Ther , vol.20 , pp. 1168-1176
    • Carmo, M.1    Dias, J.D.2    Panet, A.3    Coroadinha, A.S.4    Carrondo, M.J.T.5    Alves, P.M.6
  • 8
    • 33845223389 scopus 로고    scopus 로고
    • Primary recovery and chromatographic purification of adeno-associated virus type 2 produced by baculovirus/insect cell system
    • Chahal P.S., Aucoin M.G., Kamen A. Primary recovery and chromatographic purification of adeno-associated virus type 2 produced by baculovirus/insect cell system. J Virol Methods 2007, 139:61-70.
    • (2007) J Virol Methods , vol.139 , pp. 61-70
    • Chahal, P.S.1    Aucoin, M.G.2    Kamen, A.3
  • 9
    • 33746216141 scopus 로고    scopus 로고
    • Membrane processes in biotechnology: an overview
    • Charcosset C. Membrane processes in biotechnology: an overview. Biotechnol Adv 2006, 24:482-492.
    • (2006) Biotechnol Adv , vol.24 , pp. 482-492
    • Charcosset, C.1
  • 10
    • 73249139796 scopus 로고    scopus 로고
    • Concanavalin a affinity chromatography for efficient baculovirus purification
    • Chen G.Y., Chen C.Y., Chang M.D.T., Matsuura Y., Hu Y.C. Concanavalin a affinity chromatography for efficient baculovirus purification. Biotechnol Prog 2009, 25:1669-1677.
    • (2009) Biotechnol Prog , vol.25 , pp. 1669-1677
    • Chen, G.Y.1    Chen, C.Y.2    Chang, M.D.T.3    Matsuura, Y.4    Hu, Y.C.5
  • 11
    • 46249092863 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: I. method development and column modeling
    • Coffman J.L., Kramarczyk J.F., Kelley B.D. High-throughput screening of chromatographic separations: I. method development and column modeling. Biotechnol Bioeng 2008, 100:605-618.
    • (2008) Biotechnol Bioeng , vol.100 , pp. 605-618
    • Coffman, J.L.1    Kramarczyk, J.F.2    Kelley, B.D.3
  • 12
    • 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., Hurni W.M., Jansen K.U., 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    Hurni, W.M.5    Jansen, K.U.6
  • 13
    • 14244249300 scopus 로고    scopus 로고
    • Cell-based protein vaccines for influenza
    • Cox M.M.J. Cell-based protein vaccines for influenza. Curr Opin Mol Ther 2005, 7:24-29.
    • (2005) Curr Opin Mol Ther , vol.7 , pp. 24-29
    • Cox, M.M.J.1
  • 14
    • 0141922918 scopus 로고    scopus 로고
    • Shifting paradigms: biopharmaceuticals versus low molecular weight drugs
    • A Special Issue for Professor Hans E. Junginger on the occasion of his 60th birthday
    • Crommelin D.J.A., Storm G., Verrijk R., de Leede L., Jiskoot W., Hennink W.E. Shifting paradigms: biopharmaceuticals versus low molecular weight drugs. Int J Pharm 2003, 266:3-16. A Special Issue for Professor Hans E. Junginger on the occasion of his 60th birthday.
    • (2003) Int J Pharm , vol.266 , pp. 3-16
    • Crommelin, D.J.A.1    Storm, G.2    Verrijk, R.3    de Leede, L.4    Jiskoot, W.5    Hennink, W.E.6
  • 15
    • 0037073184 scopus 로고    scopus 로고
    • Integrated process optimization: lessons from retrovirus and virus-like particle production
    • Cruz P.E., Maranga L., Carrondo M.J.T. Integrated process optimization: lessons from retrovirus and virus-like particle production. J Biotechnol 2002, 99:199-214.
    • (2002) J Biotechnol , vol.99 , pp. 199-214
    • Cruz, P.E.1    Maranga, L.2    Carrondo, M.J.T.3
  • 16
    • 4644321610 scopus 로고    scopus 로고
    • Purification of recombinant adeno-associated virus type 8 vectors by ion exchange chromatography generates clinical grade vector stock
    • Davidoff A.M., Ng C.Y., Sleep S., Gray J., Azam S., Zhao Y., et al. Purification of recombinant adeno-associated virus type 8 vectors by ion exchange chromatography generates clinical grade vector stock. J Virol Methods 2004, 121:209-215.
    • (2004) J Virol Methods , vol.121 , pp. 209-215
    • Davidoff, A.M.1    Ng, C.Y.2    Sleep, S.3    Gray, J.4    Azam, S.5    Zhao, Y.6
  • 18
    • 34247199425 scopus 로고    scopus 로고
    • A novel approach to characterize the binding orientation of lysozyme on ion-exchange resins
    • Dismer F., Hubbuch J. A novel approach to characterize the binding orientation of lysozyme on ion-exchange resins. J Chromatogr A 2007, 1149:312-320.
    • (2007) J Chromatogr A , vol.1149 , pp. 312-320
    • Dismer, F.1    Hubbuch, J.2
  • 19
    • 74949107000 scopus 로고    scopus 로고
    • 3d structure-based protein retention prediction for ion-exchange chromatography
    • Dismer F., Hubbuch J. 3d structure-based protein retention prediction for ion-exchange chromatography. J Chromatogr A 2010, 1217:1343-1353.
    • (2010) J Chromatogr A , vol.1217 , pp. 1343-1353
    • Dismer, F.1    Hubbuch, J.2
  • 20
    • 44349133384 scopus 로고    scopus 로고
    • Effects of ionic strength and mobile phase ph on the binding orientation of lysozyme on different ion-exchange adsorbents
    • Dismer F., Petzold M., Hubbuch J. Effects of ionic strength and mobile phase ph on the binding orientation of lysozyme on different ion-exchange adsorbents. J Chromatogr A 2008, 1194:11-21.
    • (2008) J Chromatogr A , vol.1194 , pp. 11-21
    • Dismer, F.1    Petzold, M.2    Hubbuch, J.3
  • 21
    • 77649338932 scopus 로고    scopus 로고
    • An efficient process for the purification of helper-dependent adenoviral vector and removal of helper virus by iodixanol ultracentrifugation
    • Dormond E., Chahal P., Bernier A., Tran R., Perrier M., Kamen A. An efficient process for the purification of helper-dependent adenoviral vector and removal of helper virus by iodixanol ultracentrifugation. J Virol Methods 2010, 165:83-89.
    • (2010) J Virol Methods , vol.165 , pp. 83-89
    • Dormond, E.1    Chahal, P.2    Bernier, A.3    Tran, R.4    Perrier, M.5    Kamen, A.6
  • 24
    • 61449212077 scopus 로고    scopus 로고
    • Viral clearance using monoliths
    • Etzel M.R., Riordan W.T. Viral clearance using monoliths. J Chromatogr A 2009, 1216:2621-2624.
    • (2009) J Chromatogr A , vol.1216 , pp. 2621-2624
    • Etzel, M.R.1    Riordan, W.T.2
  • 28
    • 84890642098 scopus 로고    scopus 로고
    • Advances in technology and process development for industrial-scale monoclonal antibody purification
    • John Wiley & Sons, U. Gottschalk (Ed.)
    • Fontes N., van Reis R. Advances in technology and process development for industrial-scale monoclonal antibody purification. Process scale purification of antibodies 2009, 203-221. John Wiley & Sons. U. Gottschalk (Ed.).
    • (2009) Process scale purification of antibodies , pp. 203-221
    • Fontes, N.1    van Reis, R.2
  • 29
    • 0034771028 scopus 로고    scopus 로고
    • Proteolytic activity and recombinant protein production in virus-infected sf-9 insect cell cultures supplemented with carboxyl and cysteine protease inhibitors
    • Gotoh T., Miyazaki Y., Sato W., Kikuchi K., Bentley W.E. Proteolytic activity and recombinant protein production in virus-infected sf-9 insect cell cultures supplemented with carboxyl and cysteine protease inhibitors. J Biosci Bioeng 2001, 92:248-255.
    • (2001) J Biosci Bioeng , vol.92 , pp. 248-255
    • Gotoh, T.1    Miyazaki, Y.2    Sato, W.3    Kikuchi, K.4    Bentley, W.E.5
  • 30
    • 45149110469 scopus 로고    scopus 로고
    • Bioseparation in antibody manufacturing: the good, the bad and the ugly
    • Gottschalk U. Bioseparation in antibody manufacturing: the good, the bad and the ugly. Biotechnol Prog 2008, 24:496-503.
    • (2008) Biotechnol Prog , vol.24 , pp. 496-503
    • Gottschalk, U.1
  • 34
    • 33646065318 scopus 로고    scopus 로고
    • Assembly of human papillomavirus type-16 virus-like particles: multifactorial study of assembly and competing aggregation
    • Hanslip S., Zaccai N., Middelberg A., Falconer R. Assembly of human papillomavirus type-16 virus-like particles: multifactorial study of assembly and competing aggregation. Biotechnol Prog 2006, 22:554-560.
    • (2006) Biotechnol Prog , vol.22 , pp. 554-560
    • Hanslip, S.1    Zaccai, N.2    Middelberg, A.3    Falconer, R.4
  • 35
    • 0031172715 scopus 로고    scopus 로고
    • Expanded-bed adsorption in industrial bioprocessing: recent developments
    • Hjorth R. Expanded-bed adsorption in industrial bioprocessing: recent developments. Trends Biotechnol 1997, 15:230-235.
    • (1997) Trends Biotechnol , vol.15 , pp. 230-235
    • Hjorth, R.1
  • 36
    • 4143091531 scopus 로고    scopus 로고
    • Immobilized cobalt affinity chromatography provides a novel, efficient method for herpes simplex virus type 1 gene vector purification
    • Jiang C., Wechuck J.B., Goins W.F., Krisky D.M., Wolfe D., Ataai M.M., et al. Immobilized cobalt affinity chromatography provides a novel, efficient method for herpes simplex virus type 1 gene vector purification. J Virol 2004, 78:8994-9006.
    • (2004) J Virol , vol.78 , pp. 8994-9006
    • Jiang, C.1    Wechuck, J.B.2    Goins, W.F.3    Krisky, D.M.4    Wolfe, D.5    Ataai, M.M.6
  • 37
    • 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
  • 38
    • 34250752657 scopus 로고    scopus 로고
    • Direct capture of influenza a virus from cell culture supernatant with sartobind anion-exchange membrane adsorbers
    • Kalbfuss B., Wolff M., Geisler L., Tappe A., Wickramasinghe R., Thom V., et al. Direct capture of influenza a virus from cell culture supernatant with sartobind anion-exchange membrane adsorbers. J Membr Sci 2007, 299:251-260.
    • (2007) J Membr Sci , vol.299 , pp. 251-260
    • Kalbfuss, B.1    Wolff, M.2    Geisler, L.3    Tappe, A.4    Wickramasinghe, R.5    Thom, V.6
  • 39
    • 0036019204 scopus 로고    scopus 로고
    • Scalable purification of adeno-associated virus type 2, 4, or 5 using ion-exchange chromatography
    • Kaludov N., Handelman B., Chiorini J.A. Scalable purification of adeno-associated virus type 2, 4, or 5 using ion-exchange chromatography. Hum Gene Ther 2002, 13:1235-1243.
    • (2002) Hum Gene Ther , vol.13 , pp. 1235-1243
    • Kaludov, N.1    Handelman, B.2    Chiorini, J.A.3
  • 41
    • 84890727968 scopus 로고    scopus 로고
    • Downstream processing of monoclonal antibodies: current practices and future opportunities
    • John Wiley & Sons, U. Gottschalk (Ed.)
    • Kelley B., Blank G., Lee A. Downstream processing of monoclonal antibodies: current practices and future opportunities. Process scale purification of antibodies 2009, 1-23. John Wiley & Sons. U. Gottschalk (Ed.).
    • (2009) Process scale purification of antibodies , pp. 1-23
    • Kelley, B.1    Blank, G.2    Lee, A.3
  • 42
    • 45149128337 scopus 로고    scopus 로고
    • Analytical strategy for biopharmaceutical development
    • Taylor and Francis, A. Shukla, M.R. Etzel, S. Gadam (Eds.)
    • Kelner D., Bhalgat M. Analytical strategy for biopharmaceutical development. Process scale bioseparations for the biopharmaceutical industry 2007, Taylor and Francis. A. Shukla, M.R. Etzel, S. Gadam (Eds.).
    • (2007) Process scale bioseparations for the biopharmaceutical industry
    • Kelner, D.1    Bhalgat, M.2
  • 43
    • 33747204330 scopus 로고    scopus 로고
    • Innovative modular membrane adsorber system for high-throughput downstream screening for protein purification
    • Kokpinar O., Harkensee D., Kasper C., Scheper T., Zeidler R., Reif O.W., et al. Innovative modular membrane adsorber system for high-throughput downstream screening for protein purification. Biotechnol Prog 2006, 22:1215-1219.
    • (2006) Biotechnol Prog , vol.22 , pp. 1215-1219
    • Kokpinar, O.1    Harkensee, D.2    Kasper, C.3    Scheper, T.4    Zeidler, R.5    Reif, O.W.6
  • 44
    • 16344374932 scopus 로고    scopus 로고
    • Development of a purification process for adenovirus: controlling virus aggregation to improve the clearance of host cell dna
    • Konz J.O., Lee A.L., Lewis J.A., Sagar S.L. Development of a purification process for adenovirus: controlling virus aggregation to improve the clearance of host cell dna. Biotechnol Prog 2005, 21:466-472.
    • (2005) Biotechnol Prog , vol.21 , pp. 466-472
    • Konz, J.O.1    Lee, A.L.2    Lewis, J.A.3    Sagar, S.L.4
  • 45
    • 84934443352 scopus 로고    scopus 로고
    • Scaleable purification of adenovirus vectors
    • Konz J.O., Pitts L.R., Sagar S.L. Scaleable purification of adenovirus vectors. Methods Mol Biol 2008, 434:13-23.
    • (2008) Methods Mol Biol , vol.434 , pp. 13-23
    • Konz, J.O.1    Pitts, L.R.2    Sagar, S.L.3
  • 46
    • 3242753394 scopus 로고    scopus 로고
    • Concentration of plant viruses using monolithic chromatographic supports
    • Kramberger P., Petrovic N., Strancar A., Ravnikar M. Concentration of plant viruses using monolithic chromatographic supports. J Virol Methods 2004, 120:51-57.
    • (2004) J Virol Methods , vol.120 , pp. 51-57
    • Kramberger, P.1    Petrovic, N.2    Strancar, A.3    Ravnikar, M.4
  • 47
    • 77953501407 scopus 로고    scopus 로고
    • Dna depletion by precipitation in the purification of cell culture-derived influenza vaccines
    • Kroeber T., Knoechlein A., Eisold K., Kalbfuss-Zimmermann B., Reichl U. Dna depletion by precipitation in the purification of cell culture-derived influenza vaccines. Chem Eng Technol 2010, 33:941-959.
    • (2010) Chem Eng Technol , vol.33 , pp. 941-959
    • Kroeber, T.1    Knoechlein, A.2    Eisold, K.3    Kalbfuss-Zimmermann, B.4    Reichl, U.5
  • 48
    • 0037145630 scopus 로고    scopus 로고
    • Purification of a functional gene therapy vector derived from moloney murine leukaemia virus using membrane filtration and ceramic hydroxyapatite chromatography
    • Kuiper M., Sanches R.M., Walford J.A., Slater N.K. Purification of a functional gene therapy vector derived from moloney murine leukaemia virus using membrane filtration and ceramic hydroxyapatite chromatography. Biotechnol Bioeng 2002, 80:445-453.
    • (2002) Biotechnol Bioeng , vol.80 , pp. 445-453
    • Kuiper, M.1    Sanches, R.M.2    Walford, J.A.3    Slater, N.K.4
  • 49
    • 64749107970 scopus 로고    scopus 로고
    • Production, concentration and titration of pseudotyped hiv-1-based lentiviral vectors
    • Kutner R.H., Zhang X.Y., Reiser J. Production, concentration and titration of pseudotyped hiv-1-based lentiviral vectors. Nat Protoc 2009, 4:495-505.
    • (2009) Nat Protoc , vol.4 , pp. 495-505
    • Kutner, R.H.1    Zhang, X.Y.2    Reiser, J.3
  • 50
    • 23844493072 scopus 로고    scopus 로고
    • A priori prediction of adsorption isotherm parameters and chromatographic behavior in ion-exchange systems
    • Ladiwala A., Rege K., Breneman C.M., Cramer S.M. A priori prediction of adsorption isotherm parameters and chromatographic behavior in ion-exchange systems. Proc Natl Acad Sci USA 2005, 102:11710-11715.
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 11710-11715
    • Ladiwala, A.1    Rege, K.2    Breneman, C.M.3    Cramer, S.M.4
  • 52
    • 0023789366 scopus 로고
    • Polyethylene glycol precipitation for recovery of pathogenic viruses, including hepatitis a virus and human rotavirus, from oyster, water, and sediment samples
    • Lewis G.D., Metcalf T.G. Polyethylene glycol precipitation for recovery of pathogenic viruses, including hepatitis a virus and human rotavirus, from oyster, water, and sediment samples. Appl Environ Microbiol 1988, 54:1983-1988.
    • (1988) Appl Environ Microbiol , vol.54 , pp. 1983-1988
    • Lewis, G.D.1    Metcalf, T.G.2
  • 53
    • 80053457078 scopus 로고    scopus 로고
    • Development of a platform process for the purification of therapeutic monoclonal antibodies
    • John Wiley & Sons, U. Gottschalk (Ed.)
    • Li Y., Kahn D.W., Galperina O., Blatter E., Luo R., Wu Y., et al. Development of a platform process for the purification of therapeutic monoclonal antibodies. Process scale purification of antibodies 2009, 187-201. John Wiley & Sons. U. Gottschalk (Ed.).
    • (2009) Process scale purification of antibodies , pp. 187-201
    • Li, Y.1    Kahn, D.W.2    Galperina, O.3    Blatter, E.4    Luo, R.5    Wu, Y.6
  • 55
    • 16344377051 scopus 로고    scopus 로고
    • Good manufacturing practice production of adenoviral vectors for clinical trials
    • Lusky M. Good manufacturing practice production of adenoviral vectors for clinical trials. Hum Gene Ther 2005, 16:281-291.
    • (2005) Hum Gene Ther , vol.16 , pp. 281-291
    • Lusky, M.1
  • 56
    • 0036536992 scopus 로고    scopus 로고
    • Process chromatography: current constraints and future options for the adsorptive recovery of bioproducts
    • Lyddiatt A. Process chromatography: current constraints and future options for the adsorptive recovery of bioproducts. Curr Opin Biotechnol 2002, 13:95-103.
    • (2002) Curr Opin Biotechnol , vol.13 , pp. 95-103
    • Lyddiatt, A.1
  • 57
    • 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., Luo Z., Jansen K.U., et al. 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.4    Luo, Z.5    Jansen, K.U.6
  • 60
    • 70350492883 scopus 로고    scopus 로고
    • Impact of physicochemical parameters on in vitro assembly and disassembly kinetics of recombinant triple-layered rotavirus-like particles
    • Mellado M.C.M., Mena J.A., Lopes A., Ramírez O.T., Carrondo M.J.T., Palomares L.A., et al. Impact of physicochemical parameters on in vitro assembly and disassembly kinetics of recombinant triple-layered rotavirus-like particles. Biotechnol Bioeng 2009, 104:674-686.
    • (2009) Biotechnol Bioeng , vol.104 , pp. 674-686
    • Mellado, M.C.M.1    Mena, J.A.2    Lopes, A.3    Ramírez, O.T.4    Carrondo, M.J.T.5    Palomares, L.A.6
  • 61
    • 27544445072 scopus 로고    scopus 로고
    • Current issues in adeno-associated viral vector production
    • Merten O.W., Geny-Fiamma C., Douar A.M. Current issues in adeno-associated viral vector production. Gene Ther 2005, 12:S51-S61.
    • (2005) Gene Ther , vol.12
    • Merten, O.W.1    Geny-Fiamma, C.2    Douar, A.M.3
  • 62
    • 37349120092 scopus 로고    scopus 로고
    • Quality by design - thermodynamic modelling of chromatographic separation of proteins
    • Mollerup J.M., Hansen T.B., Kidal S., Staby A. Quality by design - thermodynamic modelling of chromatographic separation of proteins. J Chromatogr A 2008, 1177:200-206.
    • (2008) J Chromatogr A , vol.1177 , pp. 200-206
    • Mollerup, J.M.1    Hansen, T.B.2    Kidal, S.3    Staby, A.4
  • 63
    • 27544467262 scopus 로고    scopus 로고
    • Downstream processing of viral vectors and vaccines
    • Morenweiser R. Downstream processing of viral vectors and vaccines. Gene Ther 2005, 12(Suppl. 1):S103-S110.
    • (2005) Gene Ther , vol.12 , Issue.SUPPL. 1
    • Morenweiser, R.1
  • 64
    • 0029149328 scopus 로고
    • Enhanced transduction efficiency of retroviral vectors coprecipitated with calcium phosphate
    • Morling F., Russell S. Enhanced transduction efficiency of retroviral vectors coprecipitated with calcium phosphate. Gene Ther 1995, 2:504-508.
    • (1995) Gene Ther , vol.2 , pp. 504-508
    • Morling, F.1    Russell, S.2
  • 67
    • 0034328476 scopus 로고    scopus 로고
    • Scaleable chromatographic purification process for recombinant adeno-associated virus (raav)
    • O'Riordan C.R., Lachapelle A.L., Vincent K.A., Wadsworth S.C. Scaleable chromatographic purification process for recombinant adeno-associated virus (raav). J Gene Med 2000, 2:444-454.
    • (2000) J Gene Med , vol.2 , pp. 444-454
    • O'Riordan, C.R.1    Lachapelle, A.L.2    Vincent, K.A.3    Wadsworth, S.C.4
  • 68
    • 70349129594 scopus 로고    scopus 로고
    • Scalable purification of adeno-associated virus serotype 1 (aav1) and aav8 vectors, using dual ion-exchange adsorptive membranes
    • Okada T., Nonaka-Sarukawa M., Uchibori R., Kinoshita K., Hayashita-Kinoh H., Nitahara-Kasahara Y., et al. Scalable purification of adeno-associated virus serotype 1 (aav1) and aav8 vectors, using dual ion-exchange adsorptive membranes. Hum Gene Ther 2009, 20:1013-1021.
    • (2009) Hum Gene Ther , vol.20 , pp. 1013-1021
    • Okada, T.1    Nonaka-Sarukawa, M.2    Uchibori, R.3    Kinoshita, K.4    Hayashita-Kinoh, H.5    Nitahara-Kasahara, Y.6
  • 69
    • 33845197089 scopus 로고    scopus 로고
    • Lectin-affinity chromatography for downstream processing of mdck cell culture derived human influenza a viruses
    • Opitz L., Salaklang J., Buttner H., Reichl U., Wolff M.W. Lectin-affinity chromatography for downstream processing of mdck cell culture derived human influenza a viruses. Vaccine 2007, 25:939-947.
    • (2007) Vaccine , vol.25 , pp. 939-947
    • Opitz, L.1    Salaklang, J.2    Buttner, H.3    Reichl, U.4    Wolff, M.W.5
  • 70
    • 56249102761 scopus 로고    scopus 로고
    • Capture of cell culture-derived influenza virus by lectins: strain independent, but host cell dependent
    • Opitz L., Zimmermann A., Lehmann S., Genzel Y., Lübben H., Reichl U., et al. Capture of cell culture-derived influenza virus by lectins: strain independent, but host cell dependent. J Virol Methods 2008, 154:61-68.
    • (2008) J Virol Methods , vol.154 , pp. 61-68
    • Opitz, L.1    Zimmermann, A.2    Lehmann, S.3    Genzel, Y.4    Lübben, H.5    Reichl, U.6
  • 71
    • 32344445016 scopus 로고    scopus 로고
    • Purification of adenoviral vectors using expanded bed chromatography
    • Peixoto C., Ferreira T., Carrondo M., Cruz P., Alves P. Purification of adenoviral vectors using expanded bed chromatography. J Virol Methods 2006, 132:121-126.
    • (2006) J Virol Methods , vol.132 , pp. 121-126
    • Peixoto, C.1    Ferreira, T.2    Carrondo, M.3    Cruz, P.4    Alves, P.5
  • 74
    • 33747886682 scopus 로고    scopus 로고
    • Depth filtration: cell clarification of bioreactor offloads
    • Prashad M., Tarrach K. Depth filtration: cell clarification of bioreactor offloads. Filtr Sep 2006, 43:28-30.
    • (2006) Filtr Sep , vol.43 , pp. 28-30
    • Prashad, M.1    Tarrach, K.2
  • 75
    • 4744342353 scopus 로고    scopus 로고
    • Alternative bioseparation operations: life beyond packed-bed chromatography
    • Przybycien T.M., Pujar N.S., Steele L.M. Alternative bioseparation operations: life beyond packed-bed chromatography. Curr Opin Biotechnol 2004, 15:469-478.
    • (2004) Curr Opin Biotechnol , vol.15 , pp. 469-478
    • Przybycien, T.M.1    Pujar, N.S.2    Steele, L.M.3
  • 76
    • 0032548914 scopus 로고    scopus 로고
    • Electrostatic effects on protein partitioning in size-exclusion chromatography and membrane ultrafiltration
    • Pujar N.S., Zydney A.L. Electrostatic effects on protein partitioning in size-exclusion chromatography and membrane ultrafiltration. J Chromatogr A 1998, 796:229-238.
    • (1998) J Chromatogr A , vol.796 , pp. 229-238
    • Pujar, N.S.1    Zydney, A.L.2
  • 77
    • 33644908243 scopus 로고    scopus 로고
    • High-throughput process development for recombinant protein purification
    • Rege K., Pepsin M., Falcon B., Steele L., Heng M. High-throughput process development for recombinant protein purification. Biotechnol Bioeng 2006, 93:618-630.
    • (2006) Biotechnol Bioeng , vol.93 , pp. 618-630
    • Rege, K.1    Pepsin, M.2    Falcon, B.3    Steele, L.4    Heng, M.5
  • 79
    • 34248526597 scopus 로고    scopus 로고
    • Purification of retroviral vectors for clinical application: biological implications and technological challenges
    • Rodrigues T., Carrondo M.J.T., Alves P.M., Cruz P.E. Purification of retroviral vectors for clinical application: biological implications and technological challenges. J Biotechnol 2007, 127:520-541.
    • (2007) J Biotechnol , vol.127 , pp. 520-541
    • Rodrigues, T.1    Carrondo, M.J.T.2    Alves, P.M.3    Cruz, P.E.4
  • 81
    • 58749085714 scopus 로고    scopus 로고
    • Removal of envelope protein-free retroviral vectors by anion-exchange chromatography to improve product quality
    • Rodrigues T., Alves A., Lopes A., Carrondo M.J., Alves P.M., Cruz P.E. Removal of envelope protein-free retroviral vectors by anion-exchange chromatography to improve product quality. J Sep Sci 2008, 31:3509-3518.
    • (2008) J Sep Sci , vol.31 , pp. 3509-3518
    • Rodrigues, T.1    Alves, A.2    Lopes, A.3    Carrondo, M.J.4    Alves, P.M.5    Cruz, P.E.6
  • 84
    • 33847170529 scopus 로고    scopus 로고
    • Determining surface plasmon resonance response factors for deposition onto three-dimensional surfaces
    • Roper D.K. Determining surface plasmon resonance response factors for deposition onto three-dimensional surfaces. Chem Eng Sci 2007, 62:1988-1996.
    • (2007) Chem Eng Sci , vol.62 , pp. 1988-1996
    • Roper, D.K.1
  • 85
    • 29144506003 scopus 로고    scopus 로고
    • Adenovirus type 5 intrinsic adsorption rates measured by surface plasmon resonance
    • Roper D.K., Nakra S. Adenovirus type 5 intrinsic adsorption rates measured by surface plasmon resonance. Anal Biochem 2006, 348:75-83.
    • (2006) Anal Biochem , vol.348 , pp. 75-83
    • Roper, D.K.1    Nakra, S.2
  • 86
    • 0028203818 scopus 로고
    • A simple method for obtaining highly viable virus from culture supernatant
    • Saha K., Lin Y.C., Wong P.K. A simple method for obtaining highly viable virus from culture supernatant. J Virol Methods 1994, 46:349-352.
    • (1994) J Virol Methods , vol.46 , pp. 349-352
    • Saha, K.1    Lin, Y.C.2    Wong, P.K.3
  • 87
    • 28244447670 scopus 로고    scopus 로고
    • The influence of ionic strength on the interaction of viruses with charged surfaces under environmental conditions
    • Schaldach C.M., Bourcier W.L., Shaw H.F., Viani B.E., Wilson W.D. The influence of ionic strength on the interaction of viruses with charged surfaces under environmental conditions. J Colloid Interface Sci 2006, 294:1-10.
    • (2006) J Colloid Interface Sci , vol.294 , pp. 1-10
    • Schaldach, C.M.1    Bourcier, W.L.2    Shaw, H.F.3    Viani, B.E.4    Wilson, W.D.5
  • 88
    • 63449086888 scopus 로고    scopus 로고
    • Investigation of the interaction mechanism of the recombinant human antibody mdj8 and its fragments with chromatographic apatite phases
    • Schubert S., Freitag R. Investigation of the interaction mechanism of the recombinant human antibody mdj8 and its fragments with chromatographic apatite phases. J Chromatogr A 2009, 1216:3831-3840.
    • (2009) J Chromatogr A , vol.1216 , pp. 3831-3840
    • Schubert, S.1    Freitag, R.2
  • 89
    • 84890713207 scopus 로고    scopus 로고
    • Harvest and recovery of monoclonal antibodies: cell removal and clarification
    • John Wiley & Sons, U. Gottschalk (Ed.)
    • Shukla A., Kandula J. Harvest and recovery of monoclonal antibodies: cell removal and clarification. Process scale purification of antibodies 2009, 53-78. John Wiley & Sons. U. Gottschalk (Ed.).
    • (2009) Process scale purification of antibodies , pp. 53-78
    • Shukla, A.1    Kandula, J.2
  • 91
    • 84934442168 scopus 로고    scopus 로고
    • Chromatography-based purification of adeno-associated virus
    • Smith R.H., Yang L., Kotin R.M. Chromatography-based purification of adeno-associated virus. Methods Mol Biol 2008, 434:37-54.
    • (2008) Methods Mol Biol , vol.434 , pp. 37-54
    • Smith, R.H.1    Yang, L.2    Kotin, R.M.3
  • 93
    • 33846580009 scopus 로고    scopus 로고
    • Sorption processes in ion-exchange chromatography of viruses
    • Trilisky E.I., Lenhoff A.M. Sorption processes in ion-exchange chromatography of viruses. J Chromatogr A 2007, 1142:2-12.
    • (2007) J Chromatogr A , vol.1142 , pp. 2-12
    • Trilisky, E.I.1    Lenhoff, A.M.2
  • 94
    • 69249090586 scopus 로고    scopus 로고
    • Flow-dependent entrapment of large bioparticles in porous process media
    • Trilisky E.I., Lenhoff A.M. Flow-dependent entrapment of large bioparticles in porous process media. Biotechnol Bioeng 2009, 104:127-133.
    • (2009) Biotechnol Bioeng , vol.104 , pp. 127-133
    • Trilisky, E.I.1    Lenhoff, A.M.2
  • 95
    • 68549088976 scopus 로고    scopus 로고
    • Relation of structure to performance characteristics of monolithic and perfusive stationary phases
    • Trilisky E.I., Koku H., Czymmek K.J., Lenhoff A.M. Relation of structure to performance characteristics of monolithic and perfusive stationary phases. J Chromatogr A 2009, 1216:6365-6376.
    • (2009) J Chromatogr A , vol.1216 , pp. 6365-6376
    • Trilisky, E.I.1    Koku, H.2    Czymmek, K.J.3    Lenhoff, A.M.4
  • 96
    • 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.T., Titchener-Hooker N.J., Hoare M. 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.T.3    Titchener-Hooker, N.J.4    Hoare, M.5
  • 97
    • 34248591731 scopus 로고    scopus 로고
    • Bioprocess membrane technology
    • van Reis R., Zydney A. Bioprocess membrane technology. J Membr Sci 2007, 297:16-50.
    • (2007) J Membr Sci , vol.297 , pp. 16-50
    • van Reis, R.1    Zydney, A.2
  • 101
    • 67449098368 scopus 로고    scopus 로고
    • Purification of recombinant baculoviruses for gene therapy using membrane processes
    • Vicente T., Peixoto C., Carrondo M.J.T., Alves P.M. Purification of recombinant baculoviruses for gene therapy using membrane processes. Gene Ther 2009, 16:766-775.
    • (2009) Gene Ther , vol.16 , pp. 766-775
    • Vicente, T.1    Peixoto, C.2    Carrondo, M.J.T.3    Alves, P.M.4
  • 103
    • 77955054815 scopus 로고    scopus 로고
    • Analysis of adsorption of a baculovirus bioreaction bulk on an ion-exchange surface by surface plasmon resonance
    • Vicente T., Mota J.P.B., Peixoto C., Alves P.M., Carrondo M.J.T. Analysis of adsorption of a baculovirus bioreaction bulk on an ion-exchange surface by surface plasmon resonance. J Biotechnol 2010, 148:171-181.
    • (2010) J Biotechnol , vol.148 , pp. 171-181
    • Vicente, T.1    Mota, J.P.B.2    Peixoto, C.3    Alves, P.M.4    Carrondo, M.J.T.5
  • 104
    • 77349088483 scopus 로고    scopus 로고
    • Modeling protein binding and elution over a chromatographic surface probed by surface plasmon resonance
    • Vicente T., Mota J.P.B., Peixoto C., Alves P.M., Carrondo M.J.T. Modeling protein binding and elution over a chromatographic surface probed by surface plasmon resonance. J Chromatogr A 2010, 1217:2032-2041.
    • (2010) J Chromatogr A , vol.1217 , pp. 2032-2041
    • Vicente, T.1    Mota, J.P.B.2    Peixoto, C.3    Alves, P.M.4    Carrondo, M.J.T.5
  • 105
    • 77953022811 scopus 로고    scopus 로고
    • Modeling electrostatic interactions of baculovirus vectors for ion-exchange process development
    • Vicente T., Peixoto C., Alves P.M., Carrondo M.J.T. Modeling electrostatic interactions of baculovirus vectors for ion-exchange process development. J Chromatogr A 2010, 1217:3754-3764.
    • (2010) J Chromatogr A , vol.1217 , pp. 3754-3764
    • Vicente, T.1    Peixoto, C.2    Alves, P.M.3    Carrondo, M.J.T.4
  • 106
    • 79954488461 scopus 로고    scopus 로고
    • Impact of ligand density on the optimization of ion-exchange membrane chromatography for viral vector purification
    • Vicente T., Faber R., Alves P.M., Carrondo M.J.T., Mota J.P.B. Impact of ligand density on the optimization of ion-exchange membrane chromatography for viral vector purification. Biotechnol Bioeng 2011, 108:1347-1359.
    • (2011) Biotechnol Bioeng , vol.108 , pp. 1347-1359
    • Vicente, T.1    Faber, R.2    Alves, P.M.3    Carrondo, M.J.T.4    Mota, J.P.B.5
  • 107
    • 25644448228 scopus 로고    scopus 로고
    • Triple layered rotavirus vlp production: kinetics of vector replication, mRNA stability and recombinant protein production
    • Vieira H.L.A., Estevao C., Roldao A., Peixoto C.C., Sousa M.F.Q., Cruz P.E., et al. Triple layered rotavirus vlp production: kinetics of vector replication, mRNA stability and recombinant protein production. J Biotechnol 2005, 120:72-82.
    • (2005) J Biotechnol , vol.120 , pp. 72-82
    • Vieira, H.L.A.1    Estevao, C.2    Roldao, A.3    Peixoto, C.C.4    Sousa, M.F.Q.5    Cruz, P.E.6
  • 108
    • 46249087945 scopus 로고    scopus 로고
    • High-throughput screening of chromatographic separations: Iii. monoclonal antibodies on ceramic hydroxyapatite
    • Wensel D.L., Kelley B.D., Coffman J.L. High-throughput screening of chromatographic separations: Iii. monoclonal antibodies on ceramic hydroxyapatite. Biotechnol Bioeng 2008, 100:839-854.
    • (2008) Biotechnol Bioeng , vol.100 , pp. 839-854
    • Wensel, D.L.1    Kelley, B.D.2    Coffman, J.L.3
  • 109
    • 61449223007 scopus 로고    scopus 로고
    • Rapid high-performance liquid chromatographic analysis of adenovirus type 5 particles with a prototype anion-exchange analytical monolith column
    • Whitfield R.J., Battom S.E., Barut M., Gilham D.E., Ball P.D. Rapid high-performance liquid chromatographic analysis of adenovirus type 5 particles with a prototype anion-exchange analytical monolith column. J Chromatogr A 2009, 1216:2725-2729.
    • (2009) J Chromatogr A , vol.1216 , pp. 2725-2729
    • Whitfield, R.J.1    Battom, S.E.2    Barut, M.3    Gilham, D.E.4    Ball, P.D.5
  • 110
    • 33746680446 scopus 로고    scopus 로고
    • Characterizing solute binding to macroporous ion exchange membrane adsorbers using confocal laser scanning microscopy
    • Wickramasinghe S.R., Carlson J.O., Teske C., Hubbuch J., Ulbricht M. Characterizing solute binding to macroporous ion exchange membrane adsorbers using confocal laser scanning microscopy. J Membr Sci 2006, 281:609-618.
    • (2006) J Membr Sci , vol.281 , pp. 609-618
    • Wickramasinghe, S.R.1    Carlson, J.O.2    Teske, C.3    Hubbuch, J.4    Ulbricht, M.5
  • 112
    • 78149252754 scopus 로고    scopus 로고
    • Purification of cell culture-derived modified vaccinia ankara virus by pseudo-affinity membrane adsorbers and hydrophobic interaction chromatography
    • Wolff M.W., Siewert C., Hansen S.P., Faber R., Reichl U. Purification of cell culture-derived modified vaccinia ankara virus by pseudo-affinity membrane adsorbers and hydrophobic interaction chromatography. Biotechnol Bioeng 2010, 107:312-320.
    • (2010) Biotechnol Bioeng , vol.107 , pp. 312-320
    • Wolff, M.W.1    Siewert, C.2    Hansen, S.P.3    Faber, R.4    Reichl, U.5
  • 113
    • 20844434555 scopus 로고    scopus 로고
    • Identification of factors that contribute to recombinant aav2 particle aggregation and methods to prevent its occurrence during vector purification and formulation
    • Wright J.F., Le T., Prado J., Bahr-Davidson J., Smith P.H., Zhen Z., et al. Identification of factors that contribute to recombinant aav2 particle aggregation and methods to prevent its occurrence during vector purification and formulation. Mol Ther 2005, 12:171-178.
    • (2005) Mol Ther , vol.12 , pp. 171-178
    • Wright, J.F.1    Le, T.2    Prado, J.3    Bahr-Davidson, J.4    Smith, P.H.5    Zhen, Z.6
  • 114
    • 34547496345 scopus 로고    scopus 로고
    • Ion-exchange membrane chromatography method for rapid and efficient purification of recombinant baculovirus and baculovirus gp64 protein
    • Wu C., Soh K.Y., Wang S. Ion-exchange membrane chromatography method for rapid and efficient purification of recombinant baculovirus and baculovirus gp64 protein. Hum Gene Ther 2007, 18:665-672.
    • (2007) Hum Gene Ther , vol.18 , pp. 665-672
    • Wu, C.1    Soh, K.Y.2    Wang, S.3
  • 115
    • 0038666499 scopus 로고    scopus 로고
    • Lentivirus vector purification using anion exchange hplc leads to improved gene transfer
    • 1080
    • Yamada K., McCarty D.M., Madden V.J., Walsh C.E. Lentivirus vector purification using anion exchange hplc leads to improved gene transfer. Biotechniques 2003, 34:1074-1078. 1080.
    • (2003) Biotechniques , vol.34 , pp. 1074-1078
    • Yamada, K.1    McCarty, D.M.2    Madden, V.J.3    Walsh, C.E.4
  • 116
    • 4444351653 scopus 로고    scopus 로고
    • Tagging retrovirus vectors with a metal binding peptide and one-step purification by immobilized metal affinity chromatography
    • Ye K., Jin S., Ataai M.M., Schultz J.S., Ibeh J. Tagging retrovirus vectors with a metal binding peptide and one-step purification by immobilized metal affinity chromatography. J Virol 2004, 78:9820-9827.
    • (2004) J Virol , vol.78 , pp. 9820-9827
    • Ye, K.1    Jin, S.2    Ataai, M.M.3    Schultz, J.S.4    Ibeh, J.5


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