메뉴 건너뛰기




Volumn 122, Issue , 2017, Pages 2-19

The state-of-play and future of antibody therapeutics

Author keywords

Antibody drug conjugates (ADC); Antibody engineering; Biobetters; Biologicals; Biosimilars; Bispecific antibodies; Degradation; Formulation; Manufacture; Monoclonal antibodies (mAbs); Stability; Therapeutic antibodies

Indexed keywords

CELL CULTURE; COMMERCE; CONVERGENCE OF NUMERICAL METHODS; COST EFFECTIVENESS; DEGRADATION; DEVELOPING COUNTRIES; MANUFACTURE; MONOCLONAL ANTIBODIES; SURFACE PLASMON RESONANCE;

EID: 85008199343     PISSN: 0169409X     EISSN: 18728294     Source Type: Journal    
DOI: 10.1016/j.addr.2016.11.004     Document Type: Review
Times cited : (238)

References (230)
  • 1
    • 84921352030 scopus 로고    scopus 로고
    • The therapeutic monoclonal antibody market
    • Ecker, D.M., Jones, S.D., Levine, H.L., The therapeutic monoclonal antibody market. MAbs 7 (2015), 9–14.
    • (2015) MAbs , vol.7 , pp. 9-14
    • Ecker, D.M.1    Jones, S.D.2    Levine, H.L.3
  • 3
    • 84940838464 scopus 로고    scopus 로고
    • An emerging playbook for antibody-drug conjugates: lessons from the laboratory and clinic suggest a strategy for improving efficacy and safety
    • Drake, P.M., Rabuka, D., An emerging playbook for antibody-drug conjugates: lessons from the laboratory and clinic suggest a strategy for improving efficacy and safety. Curr. Opin. Chem. Biol. 28 (2015), 174–180.
    • (2015) Curr. Opin. Chem. Biol. , vol.28 , pp. 174-180
    • Drake, P.M.1    Rabuka, D.2
  • 4
    • 0016756272 scopus 로고
    • Continuous cultures of fused cells secreting antibody of predefined specificity
    • Kohler, G., Milstein, C., Continuous cultures of fused cells secreting antibody of predefined specificity. Nature 256 (1975), 495–497.
    • (1975) Nature , vol.256 , pp. 495-497
    • Kohler, G.1    Milstein, C.2
  • 5
    • 0017135663 scopus 로고
    • Derivation of specific antibody-producing tissue culture and tumor lines by cell fusion
    • Kohler, G., Milstein, C., Derivation of specific antibody-producing tissue culture and tumor lines by cell fusion. Eur. J. Immunol. 6 (1976), 511–519.
    • (1976) Eur. J. Immunol. , vol.6 , pp. 511-519
    • Kohler, G.1    Milstein, C.2
  • 6
    • 76649127063 scopus 로고    scopus 로고
    • New perspective for phage display as an efficient and versatile technology of functional proteomics
    • Li, W., Caberoy, N.B., New perspective for phage display as an efficient and versatile technology of functional proteomics. Appl. Microbiol. Biotechnol. 85 (2010), 909–919.
    • (2010) Appl. Microbiol. Biotechnol. , vol.85 , pp. 909-919
    • Li, W.1    Caberoy, N.B.2
  • 7
    • 0022558297 scopus 로고
    • Replacing the complementarity-determining regions in a human antibody with those from a mouse
    • Jones, P.T., Dear, P.H., Foote, J., Neuberger, M.S., Winter, G., Replacing the complementarity-determining regions in a human antibody with those from a mouse. Nature 321 (1986), 522–525.
    • (1986) Nature , vol.321 , pp. 522-525
    • Jones, P.T.1    Dear, P.H.2    Foote, J.3    Neuberger, M.S.4    Winter, G.5
  • 8
    • 0023911111 scopus 로고
    • Reshaping human antibodies for therapy
    • Riechmann, L., Clark, M., Waldmann, H., Winter, G., Reshaping human antibodies for therapy. Nature 332 (1988), 323–327.
    • (1988) Nature , vol.332 , pp. 323-327
    • Riechmann, L.1    Clark, M.2    Waldmann, H.3    Winter, G.4
  • 9
    • 27144532832 scopus 로고    scopus 로고
    • Human antibodies from transgenic animals
    • Lonberg, N., Human antibodies from transgenic animals. Nat. Biotechnol. 23 (2005), 1117–1125.
    • (2005) Nat. Biotechnol. , vol.23 , pp. 1117-1125
    • Lonberg, N.1
  • 10
    • 35148866620 scopus 로고    scopus 로고
    • Mice with a human touch
    • Scott, C.T., Mice with a human touch. Nat. Biotechnol. 25 (2007), 1075–1077.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1075-1077
    • Scott, C.T.1
  • 11
    • 35148851643 scopus 로고    scopus 로고
    • From XenoMouse technology to panitumumab, the first fully human antibody product from transgenic mice
    • Jakobovits, A., Amado, R., Yang, X., Roskos, L., Schwab, G., From XenoMouse technology to panitumumab, the first fully human antibody product from transgenic mice. Nat. Biotechnol. 25 (2007), 1134–1143.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 1134-1143
    • Jakobovits, A.1    Amado, R.2    Yang, X.3    Roskos, L.4    Schwab, G.5
  • 13
    • 0025226085 scopus 로고
    • Phage antibodies: filamentous phage displaying antibody variable domains
    • McCafferty, J., Griffiths, A.D., Winter, G., Chiswell, D.J., Phage antibodies: filamentous phage displaying antibody variable domains. Nature 348 (1990), 552–554.
    • (1990) Nature , vol.348 , pp. 552-554
    • McCafferty, J.1    Griffiths, A.D.2    Winter, G.3    Chiswell, D.J.4
  • 14
    • 0025838021 scopus 로고
    • Assembly of combinatorial antibody libraries on phage surfaces: the gene III site
    • Barbas, C.F. III, Kang, A.S., Lerner, R.A., Benkovic, S.J., Assembly of combinatorial antibody libraries on phage surfaces: the gene III site. Proc. Natl. Acad. Sci. 88 (1991), 7978–7982.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 7978-7982
    • Barbas, C.F.1    Kang, A.S.2    Lerner, R.A.3    Benkovic, S.J.4
  • 17
    • 0026563253 scopus 로고
    • Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem
    • Barbas, C.F.I., Bain, J.D., Hoekstra, D.M., Lerner, R.A., Semisynthetic combinatorial antibody libraries: a chemical solution to the diversity problem. Proc. Natl. Acad. Sci. 89 (1992), 4457–4461.
    • (1992) Proc. Natl. Acad. Sci. , vol.89 , pp. 4457-4461
    • Barbas, C.F.I.1    Bain, J.D.2    Hoekstra, D.M.3    Lerner, R.A.4
  • 18
    • 0026673067 scopus 로고
    • By-passing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro
    • Hoogenboom, H.R., Winter, G., By-passing immunisation. Human antibodies from synthetic repertoires of germline VH gene segments rearranged in vitro. J. Mol. Biol. 227 (1992), 381–388.
    • (1992) J. Mol. Biol. , vol.227 , pp. 381-388
    • Hoogenboom, H.R.1    Winter, G.2
  • 19
    • 0025740577 scopus 로고
    • Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains
    • Hoogenboom, H.R., Griffiths, A.D., Johnson, K.S., Chiswell, D.J., Hudson, P., Winter, G., Multi-subunit proteins on the surface of filamentous phage: methodologies for displaying antibody (Fab) heavy and light chains. Nucleic Acids Res. 19 (1991), 4133–4137.
    • (1991) Nucleic Acids Res. , vol.19 , pp. 4133-4137
    • Hoogenboom, H.R.1    Griffiths, A.D.2    Johnson, K.S.3    Chiswell, D.J.4    Hudson, P.5    Winter, G.6
  • 20
    • 0029562955 scopus 로고
    • An antibody variable heavy domain with a lox-Cre site integrated into its coding region: bacterial recombination within a single polypeptide chain
    • Davies, J., Riechmann, L., An antibody variable heavy domain with a lox-Cre site integrated into its coding region: bacterial recombination within a single polypeptide chain. FEBS Lett. 377 (1995), 92–96.
    • (1995) FEBS Lett. , vol.377 , pp. 92-96
    • Davies, J.1    Riechmann, L.2
  • 21
    • 35348819390 scopus 로고    scopus 로고
    • Properties, production, and applications of camelid single-domain antibody fragments
    • Harmsen, M.M., De Haard, H.J., Properties, production, and applications of camelid single-domain antibody fragments. Appl. Microbiol. Biotechnol. 77 (2007), 13–22.
    • (2007) Appl. Microbiol. Biotechnol. , vol.77 , pp. 13-22
    • Harmsen, M.M.1    De Haard, H.J.2
  • 24
    • 34249680261 scopus 로고    scopus 로고
    • Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli
    • Mazor, Y., Van Blarcom, T., Mabry, R., Iverson, B.L., Georgiou, G., Isolation of engineered, full-length antibodies from libraries expressed in Escherichia coli. Nat. Biotechnol. 25 (2007), 563–565.
    • (2007) Nat. Biotechnol. , vol.25 , pp. 563-565
    • Mazor, Y.1    Van Blarcom, T.2    Mabry, R.3    Iverson, B.L.4    Georgiou, G.5
  • 25
    • 0028141993 scopus 로고
    • Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen
    • Jespers, L.S., Roberts, A., Mahler, S.M., Winter, G., Hoogenboom, H.R., Guiding the selection of human antibodies from phage display repertoires to a single epitope of an antigen. Biotechnology (N Y) 12 (1994), 899–903.
    • (1994) Biotechnology (N Y) , vol.12 , pp. 899-903
    • Jespers, L.S.1    Roberts, A.2    Mahler, S.M.3    Winter, G.4    Hoogenboom, H.R.5
  • 26
    • 84892591532 scopus 로고    scopus 로고
    • Drugs derived from phage display: from candidate identification to clinical practice
    • Nixon, A.E., Sexton, D.J., Ladner, R.C., Drugs derived from phage display: from candidate identification to clinical practice. MAbs 6 (2014), 73–85.
    • (2014) MAbs , vol.6 , pp. 73-85
    • Nixon, A.E.1    Sexton, D.J.2    Ladner, R.C.3
  • 30
    • 0033664270 scopus 로고    scopus 로고
    • Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display
    • Hanes, J., Schaffitzel, C., Knappik, A., Pluckthun, A., Picomolar affinity antibodies from a fully synthetic naive library selected and evolved by ribosome display. Nat. Biotechnol. 18 (2000), 1287–1292.
    • (2000) Nat. Biotechnol. , vol.18 , pp. 1287-1292
    • Hanes, J.1    Schaffitzel, C.2    Knappik, A.3    Pluckthun, A.4
  • 33
    • 84885969631 scopus 로고    scopus 로고
    • The application of next generation sequencing to the understanding of antibody repertoires
    • Mathonet, P., Ullman, C.G., The application of next generation sequencing to the understanding of antibody repertoires. Front. Immunol., 4, 2013.
    • (2013) Front. Immunol. , vol.4
    • Mathonet, P.1    Ullman, C.G.2
  • 38
    • 84866996247 scopus 로고    scopus 로고
    • Antibody isolation from immunized animals: comparison of phage display and antibody discovery via V gene repertoire mining
    • Saggy, I., Wine, Y., Shefet-Carasso, L., Nahary, L., Georgiou, G., Benhar, I., Antibody isolation from immunized animals: comparison of phage display and antibody discovery via V gene repertoire mining. Protein Eng. Des. Sel. 25 (2012), 539–549.
    • (2012) Protein Eng. Des. Sel. , vol.25 , pp. 539-549
    • Saggy, I.1    Wine, Y.2    Shefet-Carasso, L.3    Nahary, L.4    Georgiou, G.5    Benhar, I.6
  • 39
    • 84879288884 scopus 로고    scopus 로고
    • Targeting B cells in the treatment of multiple sclerosis: recent advances and remaining challenges
    • Lehmann-Horn, K., Kronsbein, H.C., Weber, M.S., Targeting B cells in the treatment of multiple sclerosis: recent advances and remaining challenges. Ther. Adv. Neurol. Disord. 6 (2013), 161–173.
    • (2013) Ther. Adv. Neurol. Disord. , vol.6 , pp. 161-173
    • Lehmann-Horn, K.1    Kronsbein, H.C.2    Weber, M.S.3
  • 44
    • 80053562430 scopus 로고    scopus 로고
    • Clinical programs in the development of similar biotherapeutic products: rationale and general principles
    • Berghout, A., Clinical programs in the development of similar biotherapeutic products: rationale and general principles. Biologicals 39 (2011), 293–296.
    • (2011) Biologicals , vol.39 , pp. 293-296
    • Berghout, A.1
  • 45
    • 84921609595 scopus 로고    scopus 로고
    • Case studies on clinical evaluation of biosimilar monoclonal antibody: scientific considerations for regulatory approval
    • Kudrin, A., Knezevic, I., Joung, J., Kang, H.-N., Case studies on clinical evaluation of biosimilar monoclonal antibody: scientific considerations for regulatory approval. Biologicals 43 (2015), 1–10.
    • (2015) Biologicals , vol.43 , pp. 1-10
    • Kudrin, A.1    Knezevic, I.2    Joung, J.3    Kang, H.-N.4
  • 47
    • 77951471928 scopus 로고    scopus 로고
    • Guideline on Developement, Production, Characterisation and Specification for Monoclonal Antibodies and Related Products
    • European Medicines Agency London (UK)
    • European Medicines Agency, Committee for Medicinal Products for Human Use (CHMP), Guideline on Developement, Production, Characterisation and Specification for Monoclonal Antibodies and Related Products. 2008, European Medicines Agency, London (UK).
    • (2008)
    • European Medicines Agency1
  • 48
    • 84870858362 scopus 로고    scopus 로고
    • Guideline on Similar Biological Medicinal Products Containing Monoclonal Antibodies—Non-clinical and Clinical Issues
    • European Medicines Agency London (UK)
    • Committee for Medicinal Products for Human Use, Guideline on Similar Biological Medicinal Products Containing Monoclonal Antibodies—Non-clinical and Clinical Issues. 2012, European Medicines Agency, London (UK).
    • (2012)
    • Committee for Medicinal Products for Human Use1
  • 49
    • 84870560304 scopus 로고    scopus 로고
    • Guideline on Immunogenicity Assessment of Monoclonal Antibodies Intended for In Vivo Clinical Use
    • European Medicines Agency London (UK)
    • Committee for Medicinal Products for Human Use, Guideline on Immunogenicity Assessment of Monoclonal Antibodies Intended for In Vivo Clinical Use. 2012, European Medicines Agency, London (UK).
    • (2012)
    • Committee for Medicinal Products for Human Use1
  • 50
    • 42049123626 scopus 로고    scopus 로고
    • Guideline on Similar Biological Medicinal Products Containing Biotechnology-derived Proteins as Active Substance: Non-clinical and Clinical Issues
    • European Medicines Agency London (UK)
    • Committee for Medicinal Products for Human Use, Guideline on Similar Biological Medicinal Products Containing Biotechnology-derived Proteins as Active Substance: Non-clinical and Clinical Issues. 2014, European Medicines Agency, London (UK).
    • (2014)
    • Committee for Medicinal Products for Human Use1
  • 51
    • 33644952525 scopus 로고    scopus 로고
    • Guideline on Similar Biological Medicinal Products
    • European Medicines Agency London (UK)
    • Committee for Medicinal Products for Human Use, Guideline on Similar Biological Medicinal Products. 2014, European Medicines Agency, London (UK).
    • (2014)
    • Committee for Medicinal Products for Human Use1
  • 52
    • 42049123626 scopus 로고    scopus 로고
    • Guideline on Similar Biological Medicinal Products Containing Biotechnology-derived Proteins as Active Substance: Quality Issues (Revision 1)
    • European Medicines Agency London (UK)
    • Committee for Medicinal Products for Human Use, Guideline on Similar Biological Medicinal Products Containing Biotechnology-derived Proteins as Active Substance: Quality Issues (Revision 1). 2014, European Medicines Agency, London (UK).
    • (2014)
    • Committee for Medicinal Products for Human Use1
  • 53
    • 84946092617 scopus 로고    scopus 로고
    • Scientific Considerations in Demonstrating Biosimilarity to a Reference Product
    • Guidance for Industry Silver Spring (MD)
    • Food and Drug Administration, Scientific Considerations in Demonstrating Biosimilarity to a Reference Product. 2015, Guidance for Industry, Silver Spring (MD).
    • (2015)
    • Food and Drug Administration1
  • 54
    • 84946035221 scopus 로고    scopus 로고
    • Quality Considerations in Demonstrating Biosimilarity of a Therapeutic Protein Product to a Reference Product
    • Guidance for Industry Silver Spring (MD)
    • Food and Drug Administration, Quality Considerations in Demonstrating Biosimilarity of a Therapeutic Protein Product to a Reference Product. 2015, Guidance for Industry, Silver Spring (MD).
    • (2015)
    • Food and Drug Administration1
  • 55
    • 84908185442 scopus 로고    scopus 로고
    • Clinical Pharmacology Data to Support a Demonstration of Biosimilarity to a Reference Product (Draft Guidance)
    • Food and Drug Administration, Guidance for Industry, Clinical Pharmacology Data to Support a Demonstration of Biosimilarity to a Reference Product (Draft Guidance). 2014.
    • (2014)
    • Food and Drug Administration, Guidance for Industry,1
  • 56
    • 85014204942 scopus 로고    scopus 로고
    • Legislations on biosimilar interchangeability in the US and EU – developments far from visibility
    • Thimmaraju, P.K., Rakshambikai, R., Farista, R., Juluru, K., Legislations on biosimilar interchangeability in the US and EU – developments far from visibility. Generics Biosimilars Initiative, 2015 http://www.gabionline.net/Sponsored-Articles/Legislations-on-biosimilar-interchangeability-in-the-US-and-EU-developments-far-from-visibility.
    • (2015) Generics Biosimilars Initiative
    • Thimmaraju, P.K.1    Rakshambikai, R.2    Farista, R.3    Juluru, K.4
  • 57
    • 85012255168 scopus 로고    scopus 로고
    • Clinical outcomes following a switch from remicade to the biosimilar CT-P13 in inflammatory bowel disease patients: a prospective observational cohort study
    • Smits, L.J., Derikx, L.A., de Jong, D.J., Boshuizen, R.S., van Esch, A.A., Drenth, J.P., Hoentjen, F., Clinical outcomes following a switch from remicade to the biosimilar CT-P13 in inflammatory bowel disease patients: a prospective observational cohort study. J. Crohns Colitis 10 (2016), 1287–1293.
    • (2016) J. Crohns Colitis , vol.10 , pp. 1287-1293
    • Smits, L.J.1    Derikx, L.A.2    de Jong, D.J.3    Boshuizen, R.S.4    van Esch, A.A.5    Drenth, J.P.6    Hoentjen, F.7
  • 58
    • 84964608856 scopus 로고    scopus 로고
    • Switching to biosimilar infliximab (CT-P13): evidence of clinical safety, effectiveness and impact on public health
    • Brown, J., Kudrin, A., Switching to biosimilar infliximab (CT-P13): evidence of clinical safety, effectiveness and impact on public health. Biologicals 44 (2016), 257–266.
    • (2016) Biologicals , vol.44 , pp. 257-266
    • Brown, J.1    Kudrin, A.2
  • 61
    • 62149129236 scopus 로고    scopus 로고
    • Therapeutic antibodies: successes, limitations and hopes for the future
    • Chames, P., Van Regenmortel, M., Weiss, E., Baty, D., Therapeutic antibodies: successes, limitations and hopes for the future. Br. J. Pharmacol. 157 (2009), 220–233.
    • (2009) Br. J. Pharmacol. , vol.157 , pp. 220-233
    • Chames, P.1    Van Regenmortel, M.2    Weiss, E.3    Baty, D.4
  • 62
    • 84922807192 scopus 로고    scopus 로고
    • The current status and prospects of antibody engineering for therapeutic use: focus on glycoengineering technology
    • Niwa, R., Satoh, M., The current status and prospects of antibody engineering for therapeutic use: focus on glycoengineering technology. J. Pharm. Sci. 104 (2015), 930–941.
    • (2015) J. Pharm. Sci. , vol.104 , pp. 930-941
    • Niwa, R.1    Satoh, M.2
  • 63
    • 84901933767 scopus 로고    scopus 로고
    • From the analyst's couch: next-generation antibodies
    • Evans, J.B., Syed, B.A., From the analyst's couch: next-generation antibodies. Nat. Rev. Drug Discov. 13 (2014), 413–414.
    • (2014) Nat. Rev. Drug Discov. , vol.13 , pp. 413-414
    • Evans, J.B.1    Syed, B.A.2
  • 64
    • 84884587259 scopus 로고    scopus 로고
    • Subcutaneous administration of rituximab (MabThera) and trastuzumab (Herceptin) using hyaluronidase
    • Shpilberg, O., Jackisch, C., Subcutaneous administration of rituximab (MabThera) and trastuzumab (Herceptin) using hyaluronidase. Br. J. Cancer 109 (2013), 1556–1561.
    • (2013) Br. J. Cancer , vol.109 , pp. 1556-1561
    • Shpilberg, O.1    Jackisch, C.2
  • 65
    • 84867835452 scopus 로고    scopus 로고
    • Fc engineering: design, expression, and functional characterization of antibody variants with improved effector function
    • Derer, S., Kellner, C., Berger, S., Valerius, T., Peipp, M., Fc engineering: design, expression, and functional characterization of antibody variants with improved effector function. Methods Mol. Biol. 907 (2012), 519–536.
    • (2012) Methods Mol. Biol. , vol.907 , pp. 519-536
    • Derer, S.1    Kellner, C.2    Berger, S.3    Valerius, T.4    Peipp, M.5
  • 66
    • 84863470971 scopus 로고    scopus 로고
    • Marketing approval of mogamulizumab: a triumph for glyco-engineering
    • Beck, A., Reichert, J.M., Marketing approval of mogamulizumab: a triumph for glyco-engineering. MAbs 4 (2012), 419–425.
    • (2012) MAbs , vol.4 , pp. 419-425
    • Beck, A.1    Reichert, J.M.2
  • 67
    • 84938281268 scopus 로고    scopus 로고
    • Obinutuzumab: a FDA approved monoclonal antibody in the treatment of untreated chronic lymphocytic leukemia
    • Sachdeva, M., Dhingra, S., Obinutuzumab: a FDA approved monoclonal antibody in the treatment of untreated chronic lymphocytic leukemia. Int. J. Appl. Basic Med. Res. 5 (2015), 54–57.
    • (2015) Int. J. Appl. Basic Med. Res. , vol.5 , pp. 54-57
    • Sachdeva, M.1    Dhingra, S.2
  • 68
    • 84903795824 scopus 로고    scopus 로고
    • Genentech's glyco-engineered antibody to succeed Rituxan
    • (6 +)
    • Ratner, M., Genentech's glyco-engineered antibody to succeed Rituxan. Nat. Biotechnol., 32, 2014 (6 +).
    • (2014) Nat. Biotechnol. , vol.32
    • Ratner, M.1
  • 70
    • 84940107983 scopus 로고    scopus 로고
    • Obinutuzumab for chronic lymphocytic leukemia: promise of the first treatment approved with breakthrough therapy designation
    • Kakkar, A.K., Balakrishnan, S., Obinutuzumab for chronic lymphocytic leukemia: promise of the first treatment approved with breakthrough therapy designation. J. Oncol. Pharm. Pract. 21 (2015), 358–363.
    • (2015) J. Oncol. Pharm. Pract. , vol.21 , pp. 358-363
    • Kakkar, A.K.1    Balakrishnan, S.2
  • 71
    • 84940450182 scopus 로고    scopus 로고
    • Afucosylated antibodies increase activation of FcgammaRIIIa-dependent signaling components to intensify processes promoting ADCC
    • Liu, S.D., Chalouni, C., Young, J.C., Junttila, T.T., Sliwkowski, M.X., Lowe, J.B., Afucosylated antibodies increase activation of FcgammaRIIIa-dependent signaling components to intensify processes promoting ADCC. Cancer Immunol. Res. 3 (2015), 173–183.
    • (2015) Cancer Immunol. Res. , vol.3 , pp. 173-183
    • Liu, S.D.1    Chalouni, C.2    Young, J.C.3    Junttila, T.T.4    Sliwkowski, M.X.5    Lowe, J.B.6
  • 73
    • 30344434022 scopus 로고    scopus 로고
    • High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G
    • Preithner, S., Elm, S., Lippold, S., Locher, M., Wolf, A., da Silva, A.J., Baeuerle, P.A., Prang, N.S., High concentrations of therapeutic IgG1 antibodies are needed to compensate for inhibition of antibody-dependent cellular cytotoxicity by excess endogenous immunoglobulin G. Mol. Immunol. 43 (2006), 1183–1193.
    • (2006) Mol. Immunol. , vol.43 , pp. 1183-1193
    • Preithner, S.1    Elm, S.2    Lippold, S.3    Locher, M.4    Wolf, A.5    da Silva, A.J.6    Baeuerle, P.A.7    Prang, N.S.8
  • 75
    • 0035794194 scopus 로고    scopus 로고
    • High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R
    • Shields, R.L., Namenuk, A.K., Hong, K., Meng, Y.G., Rae, J., Briggs, J., Xie, D., Lai, J., Stadlen, A., Li, B., Fox, J.A., Presta, L.G., High resolution mapping of the binding site on human IgG1 for Fc gamma RI, Fc gamma RII, Fc gamma RIII, and FcRn and design of IgG1 variants with improved binding to the Fc gamma R. J. Biol. Chem. 276 (2001), 6591–6604.
    • (2001) J. Biol. Chem. , vol.276 , pp. 6591-6604
    • Shields, R.L.1    Namenuk, A.K.2    Hong, K.3    Meng, Y.G.4    Rae, J.5    Briggs, J.6    Xie, D.7    Lai, J.8    Stadlen, A.9    Li, B.10    Fox, J.A.11    Presta, L.G.12
  • 77
    • 34548770705 scopus 로고    scopus 로고
    • Fc optimization of therapeutic antibodies enhances their ability to kill tumor cells in vitro and controls tumor expansion in vivo via low-affinity activating Fcgamma receptors
    • Stavenhagen, J.B., Gorlatov, S., Tuaillon, N., Rankin, C.T., Li, H., Burke, S., Huang, L., Vijh, S., Johnson, S., Bonvini, E., Koenig, S., Fc optimization of therapeutic antibodies enhances their ability to kill tumor cells in vitro and controls tumor expansion in vivo via low-affinity activating Fcgamma receptors. Cancer Res. 67 (2007), 8882–8890.
    • (2007) Cancer Res. , vol.67 , pp. 8882-8890
    • Stavenhagen, J.B.1    Gorlatov, S.2    Tuaillon, N.3    Rankin, C.T.4    Li, H.5    Burke, S.6    Huang, L.7    Vijh, S.8    Johnson, S.9    Bonvini, E.10    Koenig, S.11
  • 78
    • 76249100176 scopus 로고    scopus 로고
    • Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells
    • Jung, S.T., Reddy, S.T., Kang, T.H., Borrok, M.J., Sandlie, I., Tucker, P.W., Georgiou, G., Aglycosylated IgG variants expressed in bacteria that selectively bind FcgammaRI potentiate tumor cell killing by monocyte-dendritic cells. Proc. Natl. Acad. Sci. 107 (2010), 604–609.
    • (2010) Proc. Natl. Acad. Sci. , vol.107 , pp. 604-609
    • Jung, S.T.1    Reddy, S.T.2    Kang, T.H.3    Borrok, M.J.4    Sandlie, I.5    Tucker, P.W.6    Georgiou, G.7
  • 80
    • 84867836578 scopus 로고    scopus 로고
    • Revisiting the role of glycosylation in the structure of human IgG Fc
    • Borrok, M.J., Jung, S.T., Kang, T.H., Monzingo, A.F., Georgiou, G., Revisiting the role of glycosylation in the structure of human IgG Fc. ACS Chem. Biol. 7 (2012), 1596–1602.
    • (2012) ACS Chem. Biol. , vol.7 , pp. 1596-1602
    • Borrok, M.J.1    Jung, S.T.2    Kang, T.H.3    Monzingo, A.F.4    Georgiou, G.5
  • 82
    • 78651275679 scopus 로고    scopus 로고
    • Glycosylation influences on the aggregation propensity of therapeutic monoclonal antibodies
    • Kayser, V., Chennamsetty, N., Voynov, V., Forrer, K., Helk, B., Trout, B.L., Glycosylation influences on the aggregation propensity of therapeutic monoclonal antibodies. Biotechnol. J. 6 (2011), 38–44.
    • (2011) Biotechnol. J. , vol.6 , pp. 38-44
    • Kayser, V.1    Chennamsetty, N.2    Voynov, V.3    Forrer, K.4    Helk, B.5    Trout, B.L.6
  • 83
    • 0035081693 scopus 로고    scopus 로고
    • The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms
    • Mimura, Y., Church, S., Ghirlando, R., Ashton, P.R., Dong, S., Goodall, M., Lund, J., Jefferis, R., The influence of glycosylation on the thermal stability and effector function expression of human IgG1-Fc: properties of a series of truncated glycoforms. Mol. Immunol. 37 (2000), 697–706.
    • (2000) Mol. Immunol. , vol.37 , pp. 697-706
    • Mimura, Y.1    Church, S.2    Ghirlando, R.3    Ashton, P.R.4    Dong, S.5    Goodall, M.6    Lund, J.7    Jefferis, R.8
  • 84
    • 85081150297 scopus 로고    scopus 로고
    • Mylotarg: revisiting its clinical potential post-withdrawal
    • J. Wang W.-C. Shen J.L. Zaro Springer International Publishing
    • Zaro, J.L., Mylotarg: revisiting its clinical potential post-withdrawal. Wang, J., Shen, W.-C., Zaro, J.L., (eds.) Antibody-Drug Conjugates, 2015, Springer International Publishing, 179–190.
    • (2015) Antibody-Drug Conjugates , pp. 179-190
    • Zaro, J.L.1
  • 85
    • 0027368441 scopus 로고
    • Eradication of large solid tumors in mice with an immunotoxin directed against tumor vasculature
    • Burrows, F.J., Thorpe, P.E., Eradication of large solid tumors in mice with an immunotoxin directed against tumor vasculature. Proc. Natl. Acad. Sci. 90 (1993), 8996–9000.
    • (1993) Proc. Natl. Acad. Sci. , vol.90 , pp. 8996-9000
    • Burrows, F.J.1    Thorpe, P.E.2
  • 89
    • 84887444879 scopus 로고    scopus 로고
    • Microenvironmental regulation of tumor progression and metastasis
    • Quail, D., Joyce, J., Microenvironmental regulation of tumor progression and metastasis. Nat. Med. 19 (2013), 1423–1437.
    • (2013) Nat. Med. , vol.19 , pp. 1423-1437
    • Quail, D.1    Joyce, J.2
  • 93
    • 38949192547 scopus 로고    scopus 로고
    • Targeted cancer therapy: conferring specificity to cytotoxic drugs
    • Chari, R.V., Targeted cancer therapy: conferring specificity to cytotoxic drugs. Acc. Chem. Res. 41 (2008), 98–107.
    • (2008) Acc. Chem. Res. , vol.41 , pp. 98-107
    • Chari, R.V.1
  • 95
    • 84960902961 scopus 로고    scopus 로고
    • Antibody-drug conjugates: a clinical pharmacy perspective on an emerging cancer therapy
    • Jerjian, T.V., Glode, A.E., Thompson, L.A., O'Bryant, C.L., Antibody-drug conjugates: a clinical pharmacy perspective on an emerging cancer therapy. Pharmacotherapy 36 (2016), 99–116.
    • (2016) Pharmacotherapy , vol.36 , pp. 99-116
    • Jerjian, T.V.1    Glode, A.E.2    Thompson, L.A.3    O'Bryant, C.L.4
  • 97
    • 79955867207 scopus 로고    scopus 로고
    • The development of pyrrolobenzodiazepines as antitumour agents
    • Hartley, J.A., The development of pyrrolobenzodiazepines as antitumour agents. Expert Opin. Investig. Drugs 20 (2011), 733–744.
    • (2011) Expert Opin. Investig. Drugs , vol.20 , pp. 733-744
    • Hartley, J.A.1
  • 98
    • 0034651996 scopus 로고    scopus 로고
    • Unraveling the role of proteases in cancer
    • Koblinski, J.E., Ahram, M., Sloane, B.F., Unraveling the role of proteases in cancer. Clin. Chim. Acta 291 (2000), 113–135.
    • (2000) Clin. Chim. Acta , vol.291 , pp. 113-135
    • Koblinski, J.E.1    Ahram, M.2    Sloane, B.F.3
  • 100
    • 84993726247 scopus 로고    scopus 로고
    • Safety and efficacy of brentuximab vedotin in patients with Hodgkin lymphoma or systemic anaplastic large cell lymphoma
    • Vaklavas, C., Forero-Torres, A., Safety and efficacy of brentuximab vedotin in patients with Hodgkin lymphoma or systemic anaplastic large cell lymphoma. Ther. Adv. Hematol. 3 (2012), 209–225.
    • (2012) Ther. Adv. Hematol. , vol.3 , pp. 209-225
    • Vaklavas, C.1    Forero-Torres, A.2
  • 102
    • 33645500289 scopus 로고    scopus 로고
    • Antibody-maytansinoid conjugates are activated in targeted cancer cells by lysosomal degradation and linker-dependent intracellular processing
    • Erickson, H.K., Park, P.U., Widdison, W.C., Kovtun, Y.V., Garrett, L.M., Hoffman, K., Lutz, R.J., Goldmacher, V.S., Blattler, W.A., Antibody-maytansinoid conjugates are activated in targeted cancer cells by lysosomal degradation and linker-dependent intracellular processing. Cancer Res. 66 (2006), 4426–4433.
    • (2006) Cancer Res. , vol.66 , pp. 4426-4433
    • Erickson, H.K.1    Park, P.U.2    Widdison, W.C.3    Kovtun, Y.V.4    Garrett, L.M.5    Hoffman, K.6    Lutz, R.J.7    Goldmacher, V.S.8    Blattler, W.A.9
  • 107
    • 84855379223 scopus 로고    scopus 로고
    • Conjugation of anticancer drugs through endogenous monoclonal antibody cysteine residues
    • Lyon, R.P., Meyer, D.L., Setter, J.R., Senter, P.D., Conjugation of anticancer drugs through endogenous monoclonal antibody cysteine residues. Methods Enzymol. 502 (2012), 123–138.
    • (2012) Methods Enzymol. , vol.502 , pp. 123-138
    • Lyon, R.P.1    Meyer, D.L.2    Setter, J.R.3    Senter, P.D.4
  • 108
    • 84934441628 scopus 로고    scopus 로고
    • Protocols for lysine conjugation
    • Brun, M.P., Gauzy-Lazo, L., Protocols for lysine conjugation. Methods Mol. Biol. 1045 (2013), 173–187.
    • (2013) Methods Mol. Biol. , vol.1045 , pp. 173-187
    • Brun, M.P.1    Gauzy-Lazo, L.2
  • 113
    • 84939263374 scopus 로고    scopus 로고
    • Current methods for the synthesis of homogeneous antibody-drug conjugates
    • Sochaj, A.M., Swiderska, K.W., Otlewski, J., Current methods for the synthesis of homogeneous antibody-drug conjugates. Biotechnol. Adv. 33 (2015), 775–784.
    • (2015) Biotechnol. Adv. , vol.33 , pp. 775-784
    • Sochaj, A.M.1    Swiderska, K.W.2    Otlewski, J.3
  • 114
    • 84945366854 scopus 로고    scopus 로고
    • Chemoenzymatic conjugation of toxic payloads to the globally conserved N-glycan of native mAbs provides homogeneous and highly efficacious antibody-drug conjugates
    • van Geel, R., Wijdeven, M.A., Heesbeen, R., Verkade, J.M., Wasiel, A.A., van Berkel, S.S., van Delft, F.L., Chemoenzymatic conjugation of toxic payloads to the globally conserved N-glycan of native mAbs provides homogeneous and highly efficacious antibody-drug conjugates. Bioconjug. Chem. 26 (2015), 2233–2242.
    • (2015) Bioconjug. Chem. , vol.26 , pp. 2233-2242
    • van Geel, R.1    Wijdeven, M.A.2    Heesbeen, R.3    Verkade, J.M.4    Wasiel, A.A.5    van Berkel, S.S.6    van Delft, F.L.7
  • 115
    • 0001303221 scopus 로고
    • Recombination of a mixture of univalent antibody fragments of different specificity
    • Nisonoff, A., Rivers, M.M., Recombination of a mixture of univalent antibody fragments of different specificity. Arch. Biochem. Biophys. 93 (1961), 460–462.
    • (1961) Arch. Biochem. Biophys. , vol.93 , pp. 460-462
    • Nisonoff, A.1    Rivers, M.M.2
  • 116
    • 0022508883 scopus 로고
    • Hybrid hybridoma producing a bispecific monoclonal antibody that can focus effector T-cell activity
    • Staerz, U.D., Bevan, M.J., Hybrid hybridoma producing a bispecific monoclonal antibody that can focus effector T-cell activity. Proc. Natl. Acad. Sci. 83 (1986), 1453–1457.
    • (1986) Proc. Natl. Acad. Sci. , vol.83 , pp. 1453-1457
    • Staerz, U.D.1    Bevan, M.J.2
  • 120
    • 0029946383 scopus 로고    scopus 로고
    • ‘Knobs-into-holes’ engineering of antibody CH3 domains for heavy chain heterodimerization
    • Ridgway, J.B., Presta, L.G., Carter, P., ‘Knobs-into-holes’ engineering of antibody CH3 domains for heavy chain heterodimerization. Protein Eng. Des. Sel. 9 (1996), 617–621.
    • (1996) Protein Eng. Des. Sel. , vol.9 , pp. 617-621
    • Ridgway, J.B.1    Presta, L.G.2    Carter, P.3
  • 122
    • 33646477258 scopus 로고    scopus 로고
    • Stably tethered multifunctional structures of defined composition made by the dock and lock method for use in cancer targeting
    • Rossi, E.A., Goldenberg, D.M., Cardillo, T.M., McBride, W.J., Sharkey, R.M., Chang, C.H., Stably tethered multifunctional structures of defined composition made by the dock and lock method for use in cancer targeting. Proc. Natl. Acad. Sci. 103 (2006), 6841–6846.
    • (2006) Proc. Natl. Acad. Sci. , vol.103 , pp. 6841-6846
    • Rossi, E.A.1    Goldenberg, D.M.2    Cardillo, T.M.3    McBride, W.J.4    Sharkey, R.M.5    Chang, C.H.6
  • 123
    • 84863337696 scopus 로고    scopus 로고
    • The dock-and-lock method combines recombinant engineering with site-specific covalent conjugation to generate multifunctional structures
    • Rossi, E.A., Goldenberg, D.M., Chang, C.H., The dock-and-lock method combines recombinant engineering with site-specific covalent conjugation to generate multifunctional structures. Bioconjug. Chem. 23 (2012), 309–323.
    • (2012) Bioconjug. Chem. , vol.23 , pp. 309-323
    • Rossi, E.A.1    Goldenberg, D.M.2    Chang, C.H.3
  • 124
    • 77954628740 scopus 로고    scopus 로고
    • SEED bodies: fusion proteins based on strand-exchange engineered domain (SEED) CH3 heterodimers in an Fc analogue platform for asymmetric binders or immunofusions and bispecific antibodies
    • Davis, J.H., Aperlo, C., Li, Y., Kurosawa, E., Lan, Y., Lo, K.M., Huston, J.S., SEED bodies: fusion proteins based on strand-exchange engineered domain (SEED) CH3 heterodimers in an Fc analogue platform for asymmetric binders or immunofusions and bispecific antibodies. Protein Eng. Des. Sel. 23 (2010), 195–202.
    • (2010) Protein Eng. Des. Sel. , vol.23 , pp. 195-202
    • Davis, J.H.1    Aperlo, C.2    Li, Y.3    Kurosawa, E.4    Lan, Y.5    Lo, K.M.6    Huston, J.S.7
  • 125
    • 0034051390 scopus 로고    scopus 로고
    • The Fc-region of a new class of intact bispecific antibody mediates activation of accessory cells and NK cells and induces direct phagocytosis of tumour cells
    • Zeidler, R., Mysliwietz, J., Csanady, M., Walz, A., Ziegler, I., Schmitt, B., Wollenberg, B., Lindhofer, H., The Fc-region of a new class of intact bispecific antibody mediates activation of accessory cells and NK cells and induces direct phagocytosis of tumour cells. Br. J. Cancer 83 (2000), 261–266.
    • (2000) Br. J. Cancer , vol.83 , pp. 261-266
    • Zeidler, R.1    Mysliwietz, J.2    Csanady, M.3    Walz, A.4    Ziegler, I.5    Schmitt, B.6    Wollenberg, B.7    Lindhofer, H.8
  • 126
    • 84855586532 scopus 로고    scopus 로고
    • Humoral response to catumaxomab correlates with clinical outcome: results of the pivotal phase II/III study in patients with malignant ascites
    • Ott, M.G., Marme, F., Moldenhauer, G., Lindhofer, H., Hennig, M., Spannagl, R., Essing, M.M., Linke, R., Seimetz, D., Humoral response to catumaxomab correlates with clinical outcome: results of the pivotal phase II/III study in patients with malignant ascites. Int. J. Cancer 130 (2012), 2195–2203.
    • (2012) Int. J. Cancer , vol.130 , pp. 2195-2203
    • Ott, M.G.1    Marme, F.2    Moldenhauer, G.3    Lindhofer, H.4    Hennig, M.5    Spannagl, R.6    Essing, M.M.7    Linke, R.8    Seimetz, D.9
  • 128
    • 58849085569 scopus 로고    scopus 로고
    • BiTE: teaching antibodies to engage T-cells for cancer therapy
    • Baeuerle, P.A., Kufer, P., Bargou, R., BiTE: teaching antibodies to engage T-cells for cancer therapy. Curr. Opin. Mol. Ther. 11 (2009), 22–30.
    • (2009) Curr. Opin. Mol. Ther. , vol.11 , pp. 22-30
    • Baeuerle, P.A.1    Kufer, P.2    Bargou, R.3
  • 129
    • 84975474128 scopus 로고    scopus 로고
    • A review of blinatumomab, a novel immunotherapy
    • Newman, M.J., Benani, D.J., A review of blinatumomab, a novel immunotherapy. J. Oncol. Pharm. Pract. 22 (2016), 639–645.
    • (2016) J. Oncol. Pharm. Pract. , vol.22 , pp. 639-645
    • Newman, M.J.1    Benani, D.J.2
  • 134
    • 84863650195 scopus 로고    scopus 로고
    • RECRUIT-TandAbs: harnessing the immune system to kill cancer cells
    • McAleese, F., Eser, M., RECRUIT-TandAbs: harnessing the immune system to kill cancer cells. Future Oncol. 8 (2012), 687–695.
    • (2012) Future Oncol. , vol.8 , pp. 687-695
    • McAleese, F.1    Eser, M.2
  • 139
    • 77952063094 scopus 로고    scopus 로고
    • CMC Activities for Development of MAbs
    • Contract Pharma
    • Jones, S.D., Seymour, P., Levine, H.L., CMC Activities for Development of MAbs. 2010, Contract Pharma, 60–63.
    • (2010) , pp. 60-63
    • Jones, S.D.1    Seymour, P.2    Levine, H.L.3
  • 140
    • 60849120154 scopus 로고    scopus 로고
    • Development and production of commercial therapeutic monoclonal antibodies in Mammalian cell expression systems: an overview of the current upstream technologies
    • Chartrain, M., Chu, L., Development and production of commercial therapeutic monoclonal antibodies in Mammalian cell expression systems: an overview of the current upstream technologies. Curr. Pharm. Biotechnol. 9 (2008), 447–467.
    • (2008) Curr. Pharm. Biotechnol. , vol.9 , pp. 447-467
    • Chartrain, M.1    Chu, L.2
  • 142
    • 84874101229 scopus 로고    scopus 로고
    • Effective phagocytosis of low Her2 tumor cell lines with engineered, aglycosylated IgG displaying high FcgammaRIIa affinity and selectivity
    • Jung, S.T., Kelton, W., Kang, T.H., Ng, D.T., Andersen, J.T., Sandlie, I., Sarkar, C.A., Georgiou, G., Effective phagocytosis of low Her2 tumor cell lines with engineered, aglycosylated IgG displaying high FcgammaRIIa affinity and selectivity. ACS Chem. Biol. 8 (2013), 368–375.
    • (2013) ACS Chem. Biol. , vol.8 , pp. 368-375
    • Jung, S.T.1    Kelton, W.2    Kang, T.H.3    Ng, D.T.4    Andersen, J.T.5    Sandlie, I.6    Sarkar, C.A.7    Georgiou, G.8
  • 146
    • 0028031827 scopus 로고
    • Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants
    • Ma, J.K., Lehner, T., Stabila, P., Fux, C.I., Hiatt, A., Assembly of monoclonal antibodies with IgG1 and IgA heavy chain domains in transgenic tobacco plants. Eur. J. Immunol. 24 (1994), 131–138.
    • (1994) Eur. J. Immunol. , vol.24 , pp. 131-138
    • Ma, J.K.1    Lehner, T.2    Stabila, P.3    Fux, C.I.4    Hiatt, A.5
  • 147
    • 77953999126 scopus 로고    scopus 로고
    • Production of antibodies in plants: status after twenty years
    • De Muynck, B., Navarre, C., Boutry, M., Production of antibodies in plants: status after twenty years. Plant Biotechnol. J. 8 (2010), 529–563.
    • (2010) Plant Biotechnol. J. , vol.8 , pp. 529-563
    • De Muynck, B.1    Navarre, C.2    Boutry, M.3
  • 148
    • 84945922782 scopus 로고    scopus 로고
    • Production of monoclonal antibodies in plants for cancer immunotherapy
    • Moussavou, G., Ko, K., Lee, J.H., Choo, Y.K., Production of monoclonal antibodies in plants for cancer immunotherapy. Biomed. Res. Int., 2015, 2015, 306164.
    • (2015) Biomed. Res. Int. , vol.2015 , pp. 306164
    • Moussavou, G.1    Ko, K.2    Lee, J.H.3    Choo, Y.K.4
  • 150
    • 84892367415 scopus 로고    scopus 로고
    • Recent advances in mammalian protein production
    • Bandaranayake, A.D., Almo, S.C., Recent advances in mammalian protein production. FEBS Lett. 588 (2014), 253–260.
    • (2014) FEBS Lett. , vol.588 , pp. 253-260
    • Bandaranayake, A.D.1    Almo, S.C.2
  • 151
    • 35548990601 scopus 로고    scopus 로고
    • Selection methods for high-producing mammalian cell lines
    • Browne, S.M., Al-Rubeai, M., Selection methods for high-producing mammalian cell lines. Trends Biotechnol. 25 (2007), 425–432.
    • (2007) Trends Biotechnol. , vol.25 , pp. 425-432
    • Browne, S.M.1    Al-Rubeai, M.2
  • 152
    • 80053916832 scopus 로고    scopus 로고
    • A high-throughput automated platform for the development of manufacturing cell lines for protein therapeutics
    • Shi, S., Condon, R.G., Deng, L., Saunders, J., Hung, F., Tsao, Y.S., Liu, Z., A high-throughput automated platform for the development of manufacturing cell lines for protein therapeutics. J. Vis. Exp., 55, 2011, e3010, 10.3791/3010.
    • (2011) J. Vis. Exp. , vol.55
    • Shi, S.1    Condon, R.G.2    Deng, L.3    Saunders, J.4    Hung, F.5    Tsao, Y.S.6    Liu, Z.7
  • 153
    • 0035313635 scopus 로고    scopus 로고
    • Industrial choices for protein production by large-scale cell culture
    • Chu, L., Robinson, D.K., Industrial choices for protein production by large-scale cell culture. Curr. Opin. Biotechnol. 12 (2001), 180–187.
    • (2001) Curr. Opin. Biotechnol. , vol.12 , pp. 180-187
    • Chu, L.1    Robinson, D.K.2
  • 154
    • 77958589701 scopus 로고    scopus 로고
    • Recovery and purification process development for monoclonal antibody production
    • Liu, H.F., Ma, J., Winter, C., Bayer, R., Recovery and purification process development for monoclonal antibody production. MAbs 2 (2010), 480–499.
    • (2010) MAbs , vol.2 , pp. 480-499
    • Liu, H.F.1    Ma, J.2    Winter, C.3    Bayer, R.4
  • 157
    • 0035951331 scopus 로고    scopus 로고
    • Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies
    • Schwart, W., Judd, D., Wysocki, M., Guerrier, L., Birck-Wilson, E., Boschetti, E., Comparison of hydrophobic charge induction chromatography with affinity chromatography on protein A for harvest and purification of antibodies. J. Chromatogr. A 908 (2001), 251–263.
    • (2001) J. Chromatogr. A , vol.908 , pp. 251-263
    • Schwart, W.1    Judd, D.2    Wysocki, M.3    Guerrier, L.4    Birck-Wilson, E.5    Boschetti, E.6
  • 159
    • 48449091706 scopus 로고    scopus 로고
    • Application of high-performance tangential flow filtration (HPTFF) to the purification of a human pharmaceutical antibody fragment expressed in Escherichia coli
    • Lebreton, B., Brown, A., van Reis, R., Application of high-performance tangential flow filtration (HPTFF) to the purification of a human pharmaceutical antibody fragment expressed in Escherichia coli. Biotechnol. Bioeng. 100 (2008), 964–974.
    • (2008) Biotechnol. Bioeng. , vol.100 , pp. 964-974
    • Lebreton, B.1    Brown, A.2    van Reis, R.3
  • 161
    • 0031444874 scopus 로고    scopus 로고
    • Single-step purification of bispecific monoclonal antibodies for immunotherapeutic use by hydrophobic interaction chromatography
    • Manzke, O., Tesch, H., Diehl, V., Bohlen, H., Single-step purification of bispecific monoclonal antibodies for immunotherapeutic use by hydrophobic interaction chromatography. J. Immunol. Methods 208 (1997), 65–73.
    • (1997) J. Immunol. Methods , vol.208 , pp. 65-73
    • Manzke, O.1    Tesch, H.2    Diehl, V.3    Bohlen, H.4
  • 163
    • 84864133435 scopus 로고    scopus 로고
    • Challenges in the development and manufacturing of antibody-drug conjugates
    • Ducry, L., Challenges in the development and manufacturing of antibody-drug conjugates. Methods Mol. Biol. 899 (2012), 489–497.
    • (2012) Methods Mol. Biol. , vol.899 , pp. 489-497
    • Ducry, L.1
  • 164
    • 85038014670 scopus 로고    scopus 로고
    • Bioprocessing Challenges of Antibody–Drug Conjugates
    • BioProcess International
    • Rader, R.A., Bioprocessing Challenges of Antibody–Drug Conjugates. 2014, BioProcess International.
    • (2014)
    • Rader, R.A.1
  • 167
    • 3042761213 scopus 로고    scopus 로고
    • Structure-immunogenicity relationships of therapeutic proteins
    • Hermeling, S., Crommelin, D.J., Schellekens, H., Jiskoot, W., Structure-immunogenicity relationships of therapeutic proteins. Pharm. Res. 21 (2004), 897–903.
    • (2004) Pharm. Res. , vol.21 , pp. 897-903
    • Hermeling, S.1    Crommelin, D.J.2    Schellekens, H.3    Jiskoot, W.4
  • 169
    • 33747488943 scopus 로고    scopus 로고
    • Formulation and delivery issues for monoclonal antibody therapeutics
    • Daugherty, A.L., Mrsny, R.J., Formulation and delivery issues for monoclonal antibody therapeutics. Adv. Drug Deliv. Rev. 58 (2006), 686–706.
    • (2006) Adv. Drug Deliv. Rev. , vol.58 , pp. 686-706
    • Daugherty, A.L.1    Mrsny, R.J.2
  • 170
    • 84958191421 scopus 로고    scopus 로고
    • Isomerization and oxidation in the complementarity-determining regions of a monoclonal antibody: a study of the modification–structure–function correlations by hydrogen–deuterium exchange mass spectrometry
    • Yan, Y., Wei, H., Fu, Y., Jusuf, S., Zeng, M., Ludwig, R., Krystek, S.R., Chen, G., Tao, L., Das, T.K., Isomerization and oxidation in the complementarity-determining regions of a monoclonal antibody: a study of the modification–structure–function correlations by hydrogen–deuterium exchange mass spectrometry. Anal. Chem. 88 (2016), 2041–2050.
    • (2016) Anal. Chem. , vol.88 , pp. 2041-2050
    • Yan, Y.1    Wei, H.2    Fu, Y.3    Jusuf, S.4    Zeng, M.5    Ludwig, R.6    Krystek, S.R.7    Chen, G.8    Tao, L.9    Das, T.K.10
  • 173
    • 77952467953 scopus 로고    scopus 로고
    • Prediction of aggregation prone regions of therapeutic proteins
    • Chennamsetty, N., Voynov, V., Kayser, V., Helk, B., Trout, B.L., Prediction of aggregation prone regions of therapeutic proteins. J. Phys. Chem. B 114 (2010), 6614–6624.
    • (2010) J. Phys. Chem. B , vol.114 , pp. 6614-6624
    • Chennamsetty, N.1    Voynov, V.2    Kayser, V.3    Helk, B.4    Trout, B.L.5
  • 178
    • 78049249356 scopus 로고    scopus 로고
    • Comparative effects of pH and ionic strength on protein–protein interactions, unfolding, and aggregation for IgG1 antibodies
    • Sahin, E., Grillo, A.O., Perkins, M.D., Roberts, C.J., Comparative effects of pH and ionic strength on protein–protein interactions, unfolding, and aggregation for IgG1 antibodies. J. Pharm. Sci. 99 (2010), 4830–4848.
    • (2010) J. Pharm. Sci. , vol.99 , pp. 4830-4848
    • Sahin, E.1    Grillo, A.O.2    Perkins, M.D.3    Roberts, C.J.4
  • 179
    • 84878893050 scopus 로고    scopus 로고
    • Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: from oligomers to larger aggregates
    • Arosio, P., Rima, S., Morbidelli, M., Aggregation mechanism of an IgG2 and two IgG1 monoclonal antibodies at low pH: from oligomers to larger aggregates. Pharm. Res. 30 (2013), 641–654.
    • (2013) Pharm. Res. , vol.30 , pp. 641-654
    • Arosio, P.1    Rima, S.2    Morbidelli, M.3
  • 181
    • 84876023989 scopus 로고    scopus 로고
    • Inhaled proteins: challenges and perspectives
    • Depreter, F., Pilcer, G., Amighi, K., Inhaled proteins: challenges and perspectives. Int. J. Pharm. 447 (2013), 251–280.
    • (2013) Int. J. Pharm. , vol.447 , pp. 251-280
    • Depreter, F.1    Pilcer, G.2    Amighi, K.3
  • 182
    • 79955591497 scopus 로고    scopus 로고
    • Evaluation of a non-Arrhenius model for therapeutic monoclonal antibody aggregation
    • Kayser, V., Chennamsetty, N., Voynov, V., Helk, B., Forrer, K., Trout, B.L., Evaluation of a non-Arrhenius model for therapeutic monoclonal antibody aggregation. J. Pharm. Sci. 100 (2011), 2526–2542.
    • (2011) J. Pharm. Sci. , vol.100 , pp. 2526-2542
    • Kayser, V.1    Chennamsetty, N.2    Voynov, V.3    Helk, B.4    Forrer, K.5    Trout, B.L.6
  • 183
    • 84873886259 scopus 로고    scopus 로고
    • Aggregation of anti-streptavidin immunoglobulin gamma-1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration
    • Kim, N., Remmele, R.L. Jr., Liu, D., Razinkov, V.I., Fernandez, E.J., Roberts, C.J., Aggregation of anti-streptavidin immunoglobulin gamma-1 involves Fab unfolding and competing growth pathways mediated by pH and salt concentration. Biophys. Chem. 172 (2013), 26–36.
    • (2013) Biophys. Chem. , vol.172 , pp. 26-36
    • Kim, N.1    Remmele, R.L.2    Liu, D.3    Razinkov, V.I.4    Fernandez, E.J.5    Roberts, C.J.6
  • 185
    • 84901453181 scopus 로고    scopus 로고
    • Partial unfolding of a monoclonal antibody: role of a single domain in driving protein aggregation
    • Mehta, S.B., Bee, J.S., Randolph, T.W., Carpenter, J.F., Partial unfolding of a monoclonal antibody: role of a single domain in driving protein aggregation. Biochemistry 53 (2014), 3367–3377.
    • (2014) Biochemistry , vol.53 , pp. 3367-3377
    • Mehta, S.B.1    Bee, J.S.2    Randolph, T.W.3    Carpenter, J.F.4
  • 186
    • 84925761458 scopus 로고    scopus 로고
    • Accelerated formulation development of monoclonal antibodies (mAbs) and mAb-based modalities: review of methods and tools
    • Razinkov, V.I., Treuheit, M.J., Becker, G.W., Accelerated formulation development of monoclonal antibodies (mAbs) and mAb-based modalities: review of methods and tools. J. Biomol. Screen. 20 (2015), 468–483.
    • (2015) J. Biomol. Screen. , vol.20 , pp. 468-483
    • Razinkov, V.I.1    Treuheit, M.J.2    Becker, G.W.3
  • 187
    • 33744466598 scopus 로고    scopus 로고
    • Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature
    • Liu, H., Gaza-Bulseco, G., Sun, J., Characterization of the stability of a fully human monoclonal IgG after prolonged incubation at elevated temperature. J. Chromatogr. B 837 (2006), 35–43.
    • (2006) J. Chromatogr. B , vol.837 , pp. 35-43
    • Liu, H.1    Gaza-Bulseco, G.2    Sun, J.3
  • 188
    • 79955656236 scopus 로고    scopus 로고
    • Fragmentation of monoclonal antibodies
    • Vlasak, J., Ionescu, R., Fragmentation of monoclonal antibodies. MAbs 3 (2011), 253–263.
    • (2011) MAbs , vol.3 , pp. 253-263
    • Vlasak, J.1    Ionescu, R.2
  • 190
    • 60149093608 scopus 로고    scopus 로고
    • Glutamine deamidation of a recombinant monoclonal antibody
    • Liu, H., Gaza-Bulseco, G., Chumsae, C., Glutamine deamidation of a recombinant monoclonal antibody. Rapid Commun. Mass Spectrom. 22 (2008), 4081–4088.
    • (2008) Rapid Commun. Mass Spectrom. , vol.22 , pp. 4081-4088
    • Liu, H.1    Gaza-Bulseco, G.2    Chumsae, C.3
  • 191
    • 84903711520 scopus 로고    scopus 로고
    • Characterization of asparagine 330 deamidation in an Fc-fragment of IgG1 using cation exchange chromatography and peptide mapping
    • Zhang, Y.T., Hu, J., Pace, A.L., Wong, R., Wang, Y.J., Kao, Y.-H., Characterization of asparagine 330 deamidation in an Fc-fragment of IgG1 using cation exchange chromatography and peptide mapping. J. Chromatogr. B 965 (2014), 65–71.
    • (2014) J. Chromatogr. B , vol.965 , pp. 65-71
    • Zhang, Y.T.1    Hu, J.2    Pace, A.L.3    Wong, R.4    Wang, Y.J.5    Kao, Y.-H.6
  • 192
    • 84877926248 scopus 로고    scopus 로고
    • Asparagine deamidation dependence on buffer type, pH, and temperature
    • Pace, A.L., Wong, R.L., Zhang, Y.T., Kao, Y.-H., Wang, Y.J., Asparagine deamidation dependence on buffer type, pH, and temperature. J. Pharm. Sci. 102 (2013), 1712–1723.
    • (2013) J. Pharm. Sci. , vol.102 , pp. 1712-1723
    • Pace, A.L.1    Wong, R.L.2    Zhang, Y.T.3    Kao, Y.-H.4    Wang, Y.J.5
  • 193
    • 84878146568 scopus 로고    scopus 로고
    • Isomerization of Asp–Asp motif in model peptides and a monoclonal antibody fab fragment
    • Yi, L., Beckley, N., Gikanga, B., Zhang, J., Wang, Y.J., Chih, H.-W., Sharma, V.K., Isomerization of Asp–Asp motif in model peptides and a monoclonal antibody fab fragment. J. Pharm. Sci. 102 (2013), 947–959.
    • (2013) J. Pharm. Sci. , vol.102 , pp. 947-959
    • Yi, L.1    Beckley, N.2    Gikanga, B.3    Zhang, J.4    Wang, Y.J.5    Chih, H.-W.6    Sharma, V.K.7
  • 194
    • 77449103392 scopus 로고    scopus 로고
    • Identification and characterization of oxidation and deamidation sites in monoclonal rat/mouse hybrid antibodies
    • Timm, V., Gruber, P., Wasiliu, M., Lindhofer, H., Chelius, D., Identification and characterization of oxidation and deamidation sites in monoclonal rat/mouse hybrid antibodies. J. Chromatogr. B 878 (2010), 777–784.
    • (2010) J. Chromatogr. B , vol.878 , pp. 777-784
    • Timm, V.1    Gruber, P.2    Wasiliu, M.3    Lindhofer, H.4    Chelius, D.5
  • 195
    • 14744268457 scopus 로고    scopus 로고
    • In vivo deamidation characterization of monoclonal antibody by LC/MS/MS
    • Huang, L., Lu, J., Wroblewski, V.J., Beals, J.M., Riggin, R.M., In vivo deamidation characterization of monoclonal antibody by LC/MS/MS. Anal. Chem. 77 (2005), 1432–1439.
    • (2005) Anal. Chem. , vol.77 , pp. 1432-1439
    • Huang, L.1    Lu, J.2    Wroblewski, V.J.3    Beals, J.M.4    Riggin, R.M.5
  • 198
    • 84895502551 scopus 로고    scopus 로고
    • Oxidation of therapeutic proteins and peptides: structural and biological consequences
    • Torosantucci, R., Schöneich, C., Jiskoot, W., Oxidation of therapeutic proteins and peptides: structural and biological consequences. Pharm. Res. 31 (2014), 541–553.
    • (2014) Pharm. Res. , vol.31 , pp. 541-553
    • Torosantucci, R.1    Schöneich, C.2    Jiskoot, W.3
  • 200
    • 33846140780 scopus 로고    scopus 로고
    • Antibody structure, instability, and formulation
    • Wang, W., Singh, S., Zeng, D.L., King, K., Nema, S., Antibody structure, instability, and formulation. J. Pharm. Sci. 96 (2007), 1–26.
    • (2007) J. Pharm. Sci. , vol.96 , pp. 1-26
    • Wang, W.1    Singh, S.2    Zeng, D.L.3    King, K.4    Nema, S.5
  • 201
    • 72149086122 scopus 로고    scopus 로고
    • Human IgG1 hinge fragmentation as the result of H2O2-mediated radical cleavage
    • Yan, B., Yates, Z., Balland, A., Kleemann, G.R., Human IgG1 hinge fragmentation as the result of H2O2-mediated radical cleavage. J. Biol. Chem. 284 (2009), 35390–35402.
    • (2009) J. Biol. Chem. , vol.284 , pp. 35390-35402
    • Yan, B.1    Yates, Z.2    Balland, A.3    Kleemann, G.R.4
  • 202
    • 34247125652 scopus 로고    scopus 로고
    • Identification of a single tryptophan residue as critical for binding activity in a humanized monoclonal antibody against respiratory syncytial virus
    • Wei, Z., Feng, J., Lin, H.-Y., Mullapudi, S., Bishop, E., Tous, G.I., Casas-Finet, J., Hakki, F., Strouse, R., Schenerman, M.A., Identification of a single tryptophan residue as critical for binding activity in a humanized monoclonal antibody against respiratory syncytial virus. Anal. Chem. 79 (2007), 2797–2805.
    • (2007) Anal. Chem. , vol.79 , pp. 2797-2805
    • Wei, Z.1    Feng, J.2    Lin, H.-Y.3    Mullapudi, S.4    Bishop, E.5    Tous, G.I.6    Casas-Finet, J.7    Hakki, F.8    Strouse, R.9    Schenerman, M.A.10
  • 203
    • 84927158354 scopus 로고    scopus 로고
    • Rational protein design: developing next-generation biological therapeutics and nanobiotechnological tools
    • Wilson, C.J., Rational protein design: developing next-generation biological therapeutics and nanobiotechnological tools. Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. 7 (2015), 330–341.
    • (2015) Wiley Interdiscip. Rev. Nanomed. Nanobiotechnol. , vol.7 , pp. 330-341
    • Wilson, C.J.1
  • 204
    • 33846565857 scopus 로고    scopus 로고
    • Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates
    • Cerda-Costa, N., Esteras-Chopo, A., Aviles, F.X., Serrano, L., Villegas, V., Early kinetics of amyloid fibril formation reveals conformational reorganisation of initial aggregates. J. Mol. Biol., 366, 2007, 1351.
    • (2007) J. Mol. Biol. , vol.366 , pp. 1351
    • Cerda-Costa, N.1    Esteras-Chopo, A.2    Aviles, F.X.3    Serrano, L.4    Villegas, V.5
  • 207
    • 45749102914 scopus 로고    scopus 로고
    • The Zyggregator method for predicting protein aggregation propensities
    • Tartaglia, G.G., Vendruscolo, M., The Zyggregator method for predicting protein aggregation propensities. Chem. Soc. Rev. 37 (2008), 1395–1401.
    • (2008) Chem. Soc. Rev. , vol.37 , pp. 1395-1401
    • Tartaglia, G.G.1    Vendruscolo, M.2
  • 209
    • 25844466604 scopus 로고    scopus 로고
    • Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences
    • Tartaglia, G.G., Cavalli, A., Pellarin, R., Caflisch, A., Prediction of aggregation rate and aggregation-prone segments in polypeptide sequences. Protein Sci. 14 (2005), 2723–2734.
    • (2005) Protein Sci. , vol.14 , pp. 2723-2734
    • Tartaglia, G.G.1    Cavalli, A.2    Pellarin, R.3    Caflisch, A.4
  • 210
    • 77953655331 scopus 로고    scopus 로고
    • Potential aggregation prone regions in biotherapeutics
    • Wang, X., Das, T.K., Singh, S.K., Kumar, S., Potential aggregation prone regions in biotherapeutics. MAbs 1 (2009), 254–267.
    • (2009) MAbs , vol.1 , pp. 254-267
    • Wang, X.1    Das, T.K.2    Singh, S.K.3    Kumar, S.4
  • 211
    • 84868117563 scopus 로고    scopus 로고
    • Protein dynamics governed by interfaces of high polarity and low packing density
    • Angarica, V.E., Sancho, J., Protein dynamics governed by interfaces of high polarity and low packing density. PLoS ONE, 7, 2012, e48212.
    • (2012) PLoS ONE , vol.7
    • Angarica, V.E.1    Sancho, J.2
  • 212
    • 84979865185 scopus 로고    scopus 로고
    • AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures
    • Zambrano, R., Jamroz, M., Szczasiuk, A., Pujols, J., Kmiecik, S., Ventura, S., AGGRESCAN3D (A3D): server for prediction of aggregation properties of protein structures. Nucleic Acids Res. 43 (2015), W306–W313.
    • (2015) Nucleic Acids Res. , vol.43 , pp. W306-W313
    • Zambrano, R.1    Jamroz, M.2    Szczasiuk, A.3    Pujols, J.4    Kmiecik, S.5    Ventura, S.6
  • 214
    • 84875954486 scopus 로고    scopus 로고
    • Buffer capacity of biologics - from buffer salts to buffering by antibodies
    • Karow, A.R., Bahrenburg, S., Garidel, P., Buffer capacity of biologics - from buffer salts to buffering by antibodies. Biotechnol. Prog. 29 (2013), 480–492.
    • (2013) Biotechnol. Prog. , vol.29 , pp. 480-492
    • Karow, A.R.1    Bahrenburg, S.2    Garidel, P.3
  • 215
    • 23844461800 scopus 로고    scopus 로고
    • Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: Implications for the mechanism of protein stabilization in the solid state
    • Chang, L., Shepherd, D., Sun, J., Tang, X., Pikal, M.J., Effect of sorbitol and residual moisture on the stability of lyophilized antibodies: Implications for the mechanism of protein stabilization in the solid state. J. Pharm. Sci. 94 (2005), 1445–1455.
    • (2005) J. Pharm. Sci. , vol.94 , pp. 1445-1455
    • Chang, L.1    Shepherd, D.2    Sun, J.3    Tang, X.4    Pikal, M.J.5
  • 216
    • 84963978439 scopus 로고    scopus 로고
    • Controlling protein stability: mechanisms revealed using formulations of arginine, glycine and guanidinium HCl with three globular proteins
    • Platts, L., Falconer, R.J., Controlling protein stability: mechanisms revealed using formulations of arginine, glycine and guanidinium HCl with three globular proteins. Int. J. Pharm. 486 (2015), 131–135.
    • (2015) Int. J. Pharm. , vol.486 , pp. 131-135
    • Platts, L.1    Falconer, R.J.2
  • 217
    • 80054758768 scopus 로고    scopus 로고
    • Interactions of formulation excipients with proteins in solution and in the dried state
    • Ohtake, S., Kita, Y., Arakawa, T., Interactions of formulation excipients with proteins in solution and in the dried state. Adv. Drug Deliv. Rev. 63 (2011), 1053–1073.
    • (2011) Adv. Drug Deliv. Rev. , vol.63 , pp. 1053-1073
    • Ohtake, S.1    Kita, Y.2    Arakawa, T.3
  • 219
    • 84872508710 scopus 로고    scopus 로고
    • Protein-polyanion interactions for the controlled release of monoclonal antibodies
    • Schweizer, D., Schonhammer, K., Jahn, M., Gopferich, A., Protein-polyanion interactions for the controlled release of monoclonal antibodies. Biomacromolecules 14 (2013), 75–83.
    • (2013) Biomacromolecules , vol.14 , pp. 75-83
    • Schweizer, D.1    Schonhammer, K.2    Jahn, M.3    Gopferich, A.4
  • 220
    • 3142738681 scopus 로고    scopus 로고
    • Controlled-release and local delivery of therapeutic antibodies
    • Grainger, D.W., Controlled-release and local delivery of therapeutic antibodies. Expert. Opin. Biol. Ther. 4 (2004), 1029–1044.
    • (2004) Expert. Opin. Biol. Ther. , vol.4 , pp. 1029-1044
    • Grainger, D.W.1
  • 221
    • 0027664833 scopus 로고
    • Encapsulation of chicken egg yolk immunoglobulin G (IgY) by liposomes
    • Shimizu, M., Miwa, Y., Hashimoto, K., Goto, A., Encapsulation of chicken egg yolk immunoglobulin G (IgY) by liposomes. Biosci. Biotechnol. Biochem. 57 (1993), 1445–1449.
    • (1993) Biosci. Biotechnol. Biochem. , vol.57 , pp. 1445-1449
    • Shimizu, M.1    Miwa, Y.2    Hashimoto, K.3    Goto, A.4
  • 223
    • 84878855642 scopus 로고    scopus 로고
    • Nanoparticles for oral delivery: targeted nanoparticles with peptidic ligands for oral protein delivery
    • Yun, Y., Cho, Y.W., Park, K., Nanoparticles for oral delivery: targeted nanoparticles with peptidic ligands for oral protein delivery. Adv. Drug Deliv. Rev. 65 (2013), 822–832.
    • (2013) Adv. Drug Deliv. Rev. , vol.65 , pp. 822-832
    • Yun, Y.1    Cho, Y.W.2    Park, K.3
  • 224
    • 33748885429 scopus 로고    scopus 로고
    • Topical application of the tumour necrosis factor-alpha antibody infliximab improves healing of chronic wounds
    • Streit, M., Beleznay, Z., Braathen, L.R., Topical application of the tumour necrosis factor-alpha antibody infliximab improves healing of chronic wounds. Int. Wound J. 3 (2006), 171–179.
    • (2006) Int. Wound J. , vol.3 , pp. 171-179
    • Streit, M.1    Beleznay, Z.2    Braathen, L.R.3
  • 225
    • 67649970063 scopus 로고    scopus 로고
    • Nanocarriers as pulmonary drug delivery systems to treat and to diagnose respiratory and non respiratory diseases
    • Smola, M., Vandamme, T., Sokolowski, A., Nanocarriers as pulmonary drug delivery systems to treat and to diagnose respiratory and non respiratory diseases. Int. J. Nanomedicine 3 (2008), 1–19.
    • (2008) Int. J. Nanomedicine , vol.3 , pp. 1-19
    • Smola, M.1    Vandamme, T.2    Sokolowski, A.3
  • 227
    • 1542404791 scopus 로고    scopus 로고
    • Rational design of solid aerosols for immunoglobulin delivery by modulation of aerodynamic and release characteristics
    • Dellamary, L., Smith, D.J., Bloom, A., Bot, S., Guo, G.R., Deshmuk, H., Costello, M., Bot, A., Rational design of solid aerosols for immunoglobulin delivery by modulation of aerodynamic and release characteristics. J. Control. Release 95 (2004), 489–500.
    • (2004) J. Control. Release , vol.95 , pp. 489-500
    • Dellamary, L.1    Smith, D.J.2    Bloom, A.3    Bot, S.4    Guo, G.R.5    Deshmuk, H.6    Costello, M.7    Bot, A.8
  • 228
    • 0034001190 scopus 로고    scopus 로고
    • Novel lipid-based hollow-porous microparticles as a platform for immunoglobulin delivery to the respiratory tract
    • Bot, A.I., Tarara, T.E., Smith, D.J., Bot, S.R., Woods, C.M., Weers, J.G., Novel lipid-based hollow-porous microparticles as a platform for immunoglobulin delivery to the respiratory tract. Pharm. Res. 17 (2000), 275–283.
    • (2000) Pharm. Res. , vol.17 , pp. 275-283
    • Bot, A.I.1    Tarara, T.E.2    Smith, D.J.3    Bot, S.R.4    Woods, C.M.5    Weers, J.G.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.