The DOI matches its Crossref record; 100 of the 100 references it cites were found in a registry or an index.
Antibodies and Genetically Engineered Related Molecules: Production and Purification
Abstract
Antibodies and antibody derivatives constitute 20 % of biopharmaceutical products currently in development, and despite early failures of murine products, chimeric and humanized monoclonal antibodies are now viable therapeutics. A number of genetically engineered antibody constructions have emerged, including molecular hybrids or chimeras that can deliver a powerful toxin to a target such as a tumor cell. However, the general use in clinical practice of antibody therapeutics is dependent not only on the availability of products with required efficacy but also on the costs of therapy. As a rule, a significant percentage (50-80%) of the total manufacturing cost of a therapeutic antibody is incurred during downstream processing. The critical challenges posed by the production of novel antibody therapeutics include improving process economics and efficiency, to reduce costs, and fulfilling increasingly demanding quality criteria for Food and Drug Administration (FDA) approval. It is anticipated that novel affinity-based separations will emerge from the development of synthetic ligands tailored to specific biotechnological needs. These synthetic affinity ligands include peptides obtained by synthesis and screening of peptide combinatorial libraries and artificial non-peptidic ligands generated by a de novo process design and synthesis. The exceptional stability, improved selectivity, and low cost of these ligands can lead to more efficient, less expensive, and safer procedures for antibody purification at manufacturing scales. This review aims to highlight the current trends in the design and construction of genetically engineered antibodies and related molecules, the recombinant systems used for their production, and the development of novel affinity-based strategies for antibody recovery and purification.
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Citations
Cites
Reshaping human antibodies for therapy
Riechmann, L., Clark, M., Waldmann, H., & Winter, G. (1988) · Nature · doi:10.1038/332323a0 · Cited by 1,562
Deisenhofer, J. (1981) · PubMed · Cited by 1,422
Houghten, R. A., Pinilla, C., Blondelle, S. E., Appel, J. R., Dooley, C. T., & Cuervo, J. H. (1991) · Nature · doi:10.1038/354084a0 · Cited by 1,326
Winter, G., & Milstein, C. (1991) · Nature · doi:10.1038/349293a0 · Cited by 945
Peptides on phage: a vast library of peptides for identifying ligands.
Cwirla, S. E., Peters, E. A., Barrett, R. W., & Dower, W. J. (1990) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.87.16.6378 · Cited by 928
"Diabodies": small bivalent and bispecific antibody fragments.
Holliger, P., Prospero, T., & Winter, G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.14.6444 · Cited by 874
Zhu, H., & Snyder, M. (2003) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(02)00005-4 · Cited by 870
A synthetic IgG-binding domain based on staphylococcal protein A
Nilsson, B., Moks, T., Jansson, B., Abrahmsén, L., Elmblad, A., Holmgren, E., Henrichson, C., Jones, T. A., & Uhlén, M. (1987) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/1.2.107 · Cited by 759
Knappik, A., Ge, L., Honegger, A., Pack, P., Fischer, M., Wellnhofer, G., Hoess, A., Wölle, J., Plückthun, A., & Virnekäs, B. (2000) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.3444 · Cited by 728
Directed evolution of antibody fragments with monovalent femtomolar antigen-binding affinity
Boder, E. T., Midelfort, K. S., & Wittrup, K. D. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.170297297 · Cited by 673
Binding proteins selected from combinatorial libraries of an α-helical bacterial receptor domain
Nord, K., Gunneriusson, E., Ringdahl, J., Ståhl, S., Uhlén, M., & Nygren, P.-Å. (1997) · Nature Biotechnology · doi:10.1038/nbt0897-772 · Cited by 662
Antibodies, viruses and vaccines
Burton, D. R. (2002) · Nature Reviews Immunology · doi:10.1038/nri891 · Cited by 637
Efficient folding of proteins with multiple disulfide bonds in the Escherichia coli cytoplasm
Bessette, P. H., Åslund, F., Beckwith, J., & Georgiou, G. (1999) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.96.24.13703 · Cited by 633
Stability engineering of antibody single-chain Fv fragments
Wörn, A., & Plückthun, A. (2001) · Journal of Molecular Biology · doi:10.1006/jmbi.2000.4265 · Cited by 616
PEGylated antibodies and antibody fragments for improved therapy: a review
Chapman, A. P. (2002) · Advanced Drug Delivery Reviews · doi:10.1016/s0169-409x(02)00026-1 · Cited by 556
Therapeutic antibodies for human diseases at the dawn of the twenty-first century
Brekke, O. H., & Sandlie, I. (2003) · Nature Reviews Drug Discovery · doi:10.1038/nrd984 · Cited by 550
Advances in refolding of proteins produced in E. coli
Lilie, H., Schwarz, E., & Rudolph, R. (1998) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(98)80035-9 · Cited by 476
A sensitive and specific enzyme-based assay detecting HIV-1 virion fusion in primary T lymphocytes
Cavrois, M., de Noronha, C., & Greene, W. C. (2002) · Nature Biotechnology · doi:10.1038/nbt745 · Cited by 475
Refolding of recombinant proteins
De Bernardez Clark, E. (1998) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(98)80109-2 · Cited by 473
By–Passing Immunization: Building High Affinity Human Antibodies by Chain Shuffling
Marks, J. D., Griffiths, A. D., Malmqvist, M., Clackson, T. P., Bye, J. M., & Winter, G. (1992) · Nature Biotechnology · doi:10.1038/nbt0792-779 · Cited by 404
Hanes, J., Schaffitzel, C., Knappik, A., & Plückthun, A. (2000) · Nature Biotechnology · doi:10.1038/82407 · Cited by 373
Therapeutic antibody fragments with prolonged in vivo half-lives
Chapman, A. P., Antoniw, P., Spitali, M., West, S., Stephens, S., & King, D. J. (1999) · Nature Biotechnology · doi:10.1038/11717 · Cited by 350
Galactose-extended glycans of antibodies produced by transgenic plants
Bakker, H., Bardor, M., Molthoff, J. W., Gomord, V., Elbers, I., Stevens, L. H., Jordi, W., Lommen, A., Faye, L., Lerouge, P., et al. (2001) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.031419998 · Cited by 336
Hu, S., Shively, L., Raubitschek, A. A., Sherman, M. A., Williams, L. E., Wong, J. Y., Shively, J. E., & Wu, A. M. (1996) · PubMed · Cited by 330
[25] Yeast surface display for directed evolution of protein expression, affinity, and stability
Boder, E. T., & Wittrup, K. D. (2000) · Methods in Enzymology · doi:10.1016/s0076-6879(00)28410-3 · Cited by 324
Waibel, R., Alberto, R., Willuda, J., Finnern, R., Schibli, R., Stichelberger, A., Egli, A., Abram, U., Mach, J.-P., Plückthun, A., et al. (1999) · Nature Biotechnology · doi:10.1038/12890 · Cited by 303
Minimizing a binding domain from protein A.
Braisted, A. C., & Wells, J. A. (1996) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.93.12.5688 · Cited by 302
A helper phage to improve single-chain antibody presentation in phage display
Rondot, S., Koch, J., Breitling, F., & Dübel, S. (2001) · Nature Biotechnology · doi:10.1038/83567 · Cited by 300
Design, synthesis, and application of a Protein A mimetic
Li, R., Dowd, V., Stewart, D. J., Burton, S. J., & Lowe, C. R. (1998) · Nature Biotechnology · doi:10.1038/nbt0298-190 · Cited by 297
Self-citationA combinatorial library of an α-helical bacterial receptor domain
Nord, K., Nilsson, J., Nilsson, B., Uhlén, M., & Nygren, P.-Å. (1995) · "Protein Engineering, Design and Selection" · doi:10.1093/protein/8.6.601 · Cited by 285
Cloned transchromosomic calves producing human immunoglobulin
Kuroiwa, Y., Kasinathan, P., Choi, Y. J., Naeem, R., Tomizuka, K., Sullivan, E. J., Knott, J. G., Duteau, A., Goldsby, R. A., Osborne, B. A., et al. (2002) · Nature Biotechnology · doi:10.1038/nbt727 · Cited by 267
Antibody recognition imaging by force microscopy
Raab, A., Han, W., Badt, D., Smith-Gill, S. J., Lindsay, S. M., Schindler, H., & Hinterdorfer, P. (1999) · Nature Biotechnology · doi:10.1038/12898 · Cited by 260
Purification of antibodies by affinity chromatography
Huse, K., Böhme, H., & Scholz, G. H. (2002) · Journal of Biochemical and Biophysical Methods · doi:10.1016/s0165-022x(02)00017-9 · Cited by 254
Francisco, J. A., Campbell, R., Iverson, B. L., & Georgiou, G. (1993) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.90.22.10444 · Cited by 251
Affinity Chromatography: A Review of Clinical Applications
Hage, D. S. (1999) · Clinical Chemistry · doi:10.1093/clinchem/45.5.593 · Cited by 243
In vitro selection from protein and peptide libraries
Clackson, T., & Wells, J. A. (1994) · Trends in Biotechnology · doi:10.1016/0167-7799(94)90079-5 · Cited by 242
Safar, J. G., Scott, M., Monaghan, J., Deering, C., Didorenko, S., Vergara, J., Ball, H., Legname, G., Leclerc, E., Solforosi, L., et al. (2002) · Nature Biotechnology · doi:10.1038/nbt748 · Cited by 240
Green, L. L. (1999) · Journal of Immunological Methods · doi:10.1016/s0022-1759(99)00137-4 · Cited by 229
High avidity scFv multimers; diabodies and triabodies
Hudson, P. J., & Kortt, A. A. (1999) · Journal of Immunological Methods · doi:10.1016/s0022-1759(99)00157-x · Cited by 219
Ribosome display: an in vitro method for selection and evolution of antibodies from libraries
Schaffitzel, C., Hanes, J., Jermutus, L., & Plückthun, A. (1999) · Journal of Immunological Methods · doi:10.1016/s0022-1759(99)00149-0 · Cited by 211
Therapeutic antibody expression technology
Chadd, H. E., & Chamow, S. M. (2001) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(00)00198-1 · Cited by 204
Tomizuka, K., Shinohara, T., Yoshida, H., Uejima, H., Ohguma, A., Tanaka, S., Sato, K., Oshimura, M., & Ishida, I. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.97.2.722 · Cited by 202
Tsumoto, K., Shinoki, K., Kondo, H., Uchikawa, M., Juji, T., & Kumagai, I. (1998) · Journal of Immunological Methods · doi:10.1016/s0022-1759(98)00127-6 · Cited by 195
Dimeric and trimeric antibodies: high avidity scFvs for cancer targeting
Kortt, A. A., Dolezal, O., Power, B. E., & Hudson, P. J. (2001) · Biomolecular Engineering · doi:10.1016/s1389-0344(01)00090-9 · Cited by 173
Monoclonal antibodies in the clinic
Reichert, J. M. (2001) · Nature Biotechnology · doi:10.1038/nbt0901-819 · Cited by 168
Bispecific human IgG by design
Carter, P. (2001) · Journal of Immunological Methods · doi:10.1016/s0022-1759(00)00339-2 · Cited by 167
Factors Influencing the Dimer to Monomer Transition of an Antibody Single-Chain Fv Fragment
Arndt, K. M., Müller, K. M., & Plückthun, A. (1998) · Biochemistry · doi:10.1021/bi9810407 · Cited by 163
Producing proteins in transgenic plants and animals
Larrick, J. W., & Thomas, D. W. (2001) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(00)00236-6 · Cited by 158
Vaughan, T. J., Osbourn, J. K., & Tempest, P. R. (1998) · Nature Biotechnology · doi:10.1038/nbt0698-535 · Cited by 158
High-throughput generation and engineering of recombinant human antibodies
Krebs, B., Rauchenberger, R., Reiffert, S. U., Rothe, C., Tesar, M., Thomassen, E., Cao, M., Dreier, T., Fischer, D., Höss, A., et al. (2001) · Journal of Immunological Methods · doi:10.1016/s0022-1759(01)00398-2 · Cited by 153
The selection of intracellular antibodies
Cattaneo, A., & Biocca, S. (1999) · Trends in biotechnology · doi:10.1016/s0167-7799(98)01268-2 · Cited by 151
Generating improved single-chain Fv molecules for tumor targeting
Adams, G. P., & Schier, R. (1999) · Journal of Immunological Methods · doi:10.1016/s0022-1759(99)00161-1 · Cited by 146
Targeted gene delivery to mammalian cells by filamentous bacteriophage
Poul, M., & Marks, J. D. (1999) · Journal of Molecular Biology · doi:10.1006/jmbi.1999.2678 · Cited by 145
Kortt, A. A., Lah, M. S., Oddie, G. W., Gruen, C. L., Burns, J. E., Pearce, L. A., Atwell, J. L., McCoy, A. J., Howlett, G. J., Metzger, D. W., et al. (1997) · Protein Engineering Design and Selection · doi:10.1093/protein/10.4.423 · Cited by 133
Graille, M., Stura, E. A., Housden, N. G., Beckingham, J. A., Bottomley, S., Beale, D., Taussig, M., Sutton, B. J., Gore, M. G., & Charbonnier, J. (2001) · Structure · doi:10.1016/s0969-2126(01)00630-x · Cited by 131
Novel ligands for the affinity-chromatographic purification of antibodies
Fassina, G., Ruvo, M., Palombo, G., Verdoliva, A., & Marino, M. (2001) · Journal of Biochemical and Biophysical Methods · doi:10.1016/s0165-022x(01)00215-9 · Cited by 128
Epitope discovery using peptide libraries displayed on phage
Cortese, R., Felici, F., Galfré, G., Luzzago, A., Monaci, P., & Nicosia, A. (1994) · Trends in biotechnology · doi:10.1016/0167-7799(94)90137-6 · Cited by 123
Signaling antibodies in cancer therapy
Cragg, M. S., French, R. R., & Glennie, M. J. (1999) · Current Opinion in Immunology · doi:10.1016/s0952-7915(99)00010-2 · Cited by 119
Nord, K., Nord, O., Uhlén, M., Kelley, B. D., Ljungqvist, C., & Nygren, P. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02344.x · Cited by 117
Human antibodies as next generation therapeutics
van Dijk, M. A., & van de Winkel, J. G. J. (2001) · Current Opinion in Chemical Biology · doi:10.1016/s1367-5931(00)00216-7 · Cited by 107
Irving, R. A., Coia, G., Roberts, A., Nuttall, S. D., & Hudson, P. J. (2001) · Journal of Immunological Methods · doi:10.1016/s0022-1759(00)00341-0 · Cited by 96
Surface display of a functional single-chain Fv antibody on staphylococci
Gunneriusson, E., Samuelson, P., Uhlén, M., Nygren, P., & Ståhl, S. (1996) · Journal of Bacteriology · doi:10.1128/jb.178.5.1341-1346.1996 · Cited by 95
Specific killing of lymphoma cells by cytotoxic T-cells mediated by a bispecific diabody
Holliger, P., Brissinck, J., Williams, R. L., Thielemans, K., & Winter, G. P. (1996) · Protein Engineering Design and Selection · doi:10.1093/protein/9.3.299 · Cited by 94
lich, S. G. ⁄. (2000) · Journal of Biotechnology · doi:10.1016/s0168-1656(99)00197-2 · Cited by 87
Affinity purification of immunoglobulins from chicken egg yolk using a new synthetic ligand
Verdoliva, A., Basile, G., & Fassina, G. (2000) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(00)00426-6 · Cited by 86
Pei, X. Y., Holliger, P., Murzin, A. G., & Williams, R. L. (1997) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.94.18.9637 · Cited by 81
Treatment of Human B Cell Lymphoma Xenografts with a CD3 × CD19 Diabody and T Cells
Cochlovius, B., Kipriyanov, S. M., Stassar, M. J. J. G., Christ, O., Schuhmacher, J., Strauß, G., Moldenhauer, G., & Little, M. (2000) · The Journal of Immunology · doi:10.4049/jimmunol.165.2.888 · Cited by 80
Kumar, A., Kamihira, M., Galaev, I. Y., Mattìasson, B., & Iijima, S. (2001) · Biotechnology and Bioengineering · doi:10.1002/bit.10080 · Cited by 79
Retargeting serum immunoglobulin with bispecific diabodies
Holliger, P., Wing, M. G., Pound, J. D., Bohlen, H., & Winter, G. P. (1997) · Nature Biotechnology · doi:10.1038/nbt0797-632 · Cited by 79
Comparison of affinity membranes for the purification of immunoglobulins
Castilho, L. R., Anspach, F. B., & Deckwer, W. (2002) · Journal of Membrane Science · doi:10.1016/s0376-7388(02)00257-0 · Cited by 77
Phage diabody repertoires for selection of large numbers of bispecific antibody fragments
McGuinness, B., Walter, G., FitzGerald, K., Schuler, P., Mahoney, W. C., Duncan, A., & Hoogenboom, H. R. (1996) · Nature Biotechnology · doi:10.1038/nbt0996-1149 · Cited by 75
Knowledge-based Design of Reagentless Fluorescent Biosensors from Recombinant Antibodies
Renard, M., Belkadi, L., Hugo, N., England, P., Altschuh, D., & Bedouelle, H. (2002) · Journal of Molecular Biology · doi:10.1016/s0022-2836(02)00023-2 · Cited by 71
Anastase‐Ravion, S., Ding, Z., Meddahi‐Pellé, A., Hoffman, A. S., & Letourneur, D. (2001) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(01)00336-x · Cited by 68
The affinity‐selection of a minibody polypeptide inhibitor of human interleukin‐6.
Martin, F., Toniatti, C., Salvati, A. L., Venturini, S., Ciliberto, G., Cortese, R., & Sollazzo, M. (1994) · The EMBO Journal · doi:10.1002/j.1460-2075.1994.tb06864.x · Cited by 65
Völkel, T., Korn, T., Bach, M., Müller, R., & Kontermann, R. E. (2001) · Protein Engineering Design and Selection · doi:10.1093/protein/14.10.815 · Cited by 64
Complement recruitment using bispecific diabodies
Kontermann, R. E., Wing, M. G., & Winter, G. P. (1997) · Nature Biotechnology · doi:10.1038/nbt0797-629 · Cited by 63
The roots of antibody diversity
Gearhart, P. J. (2002) · Nature · doi:10.1038/419029a · Cited by 60
Affinity Chromatography with Collapsibly Tethered Ligands
Yamanaka, H., Yoshizako, K., Akiyama, Y., Sota, H., Hasegawa, Y., Shinohara, Y., Kikuchi, A., & Okano, T. (2003) · Analytical Chemistry · doi:10.1021/ac0263768 · Cited by 59
Houghten, R. A., & Dooley, C. T. (1993) · Bioorganic & Medicinal Chemistry Letters · doi:10.1016/s0960-894x(01)80222-5 · Cited by 59
Bispecific antibodies targeting cancer cells
Peipp, M., & Valerius, T. (2002) · Biochemical Society Transactions · doi:10.1042/bst0300507 · Cited by 59
Mapping of the Immunoglobulin Light Chain-binding Site of Protein L
Wikström, M., Sjöbring, U., Drakenberg, T., Forsén, S., & Björck, L. (1995) · Journal of Molecular Biology · doi:10.1006/jmbi.1995.0364 · Cited by 55
Synthesis of high avidity antibody fragments (scFv multimers) for cancer imaging
Power, B. E., & Hudson, P. J. (2000) · Journal of Immunological Methods · doi:10.1016/s0022-1759(00)00201-5 · Cited by 47
Laukkanen, M., Teeri, T. T., & KEINÄNEN, K. P. (1993) · Protein Engineering Design and Selection · doi:10.1093/protein/6.4.449 · Cited by 44
Expression of a bispecific dsFv–dsFv′ antibody fragment in Escherichia coli
Schmiedl, A., Breitling, F., & Dübel, S. (2000) · Protein Engineering Design and Selection · doi:10.1093/protein/13.10.725 · Cited by 43
Antibody design: Beyond the natural limits
Rees, A. R., Staunton, D., Webster, D. M., Searle, S. J., Henry, A. H., & Pedersen, J. T. (1994) · Trends in biotechnology · doi:10.1016/0167-7799(94)90083-3 · Cited by 40
An efficient route to the production of an IgG-like bispecific antibody
Zuo, Z., Jimenez, X., Witte, L., & Zhu, Z. (2000) · Protein Engineering Design and Selection · doi:10.1093/protein/13.5.361 · Cited by 39
Blank, K. G., Lindner, P. J., Diefenbach, B., & Plückthun, A. (2002) · Protein Expression and Purification · doi:10.1006/prep.2001.1575 · Cited by 39
Routes to active proteins from transformed microorganisms
Büchner, J., & Rudolph, R. (1991) · Current Opinion in Biotechnology · doi:10.1016/0958-1669(91)90077-i · Cited by 38
Schmidt, A., Müller, D., Mersmann, M., Wüest, T., Gerlach, E., Garin‐Chesa, P., Rettig, W. J., Pfizenmaier, K., & Moosmayer, D. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02046.x · Cited by 38
Humphreys, D. P. (2003) · PubMed · Cited by 34
Construction of a diabody (small recombinant bispecific antibody) using a refolding system
Takemura, S.-I., Asano, R., Tsumoto, K., et al. (2000) · Protein Engineering Design and Selection · doi:10.1093/protein/13.8.583 · Cited by 33
Willems, A. V., Leœn, J., Schoonooghe, S., Grooten, J., & Mertens, N. (2003) · Journal of Chromatography B · doi:10.1016/s1570-0232(02)00813-9 · Cited by 29
Single-chain Fv with manifold N-glycans as bifunctional scaffolds for immunomolecules
Wang, M., Lee, L. S., Nepomich, A., Yang, J., Conover, C., Whitlow, M. D., & Filpula, D. R. (1998) · Protein Engineering Design and Selection · doi:10.1093/protein/11.12.1277 · Cited by 29
Beckingham, J. A., Housden, N. G., Muir, N. M., Bottomley, S., & Gore, M. G. (2001) · Biochemical Journal · doi:10.1042/0264-6021:3530395 · Cited by 27
Kriangkum, J., Xu, B., Gervais, C., Paquette, D., Jacobs, F. A., Martin, L., & Suresh, M. R. (2000) · Hybridoma · doi:10.1089/027245700315770 · Cited by 24
Engineering therapeutic proteins
McCafferty, J., & Glover, D. R. (2000) · Current Opinion in Structural Biology · doi:10.1016/s0959-440x(00)00108-1 · Cited by 24
Benkovic, S. J. (1996) · Nature · doi:10.1038/383023a0 · Cited by 14
Mergulhão, F. J., Monteiro, G. A., Cabral, J. M. S., & Taipa, M. Â. (2001) · Molecular Biotechnology · doi:10.1385/mb:19:3:239 · Cited by 13
Self-citationMimetic ligand-based affinity purification of immune complexes and immunoconjugates
Xu, D., Leveugle, B., Kreutz, F., & Suresh, M. R. (1998) · Journal of Chromatography B Biomedical Sciences and Applications · doi:10.1016/s0378-4347(97)00441-6 · Cited by 9
Evaluation of affinity filters for protein isolation.
Kasper, C., Reif, O., & Freitag, R. (1996) · PubMed · Cited by 8
Cited by
Future of antibody purification
Low, D., O’Leary, R., & Pujar, N. S. (2007) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.10.033 · Cited by 472
Brockmeier, U., Caspers, M., Freudl, R., Jockwer, A., Noll, T., & Eggert, T. (2006) · Journal of Molecular Biology · doi:10.1016/j.jmb.2006.07.034 · Cited by 272
Corchero, J. L., Gasser, B., Resina, D., Smith, W., Parrilli, E., Vázquez, F., Abasolo, I., Giuliani, M., Jäntti, J., Ferrer, P., et al. (2013) · Biotechnology Advances · doi:10.1016/j.biotechadv.2012.09.001 · Cited by 133
Viral clearance for biopharmaceutical downstream processes
Shukla, A. A., & Aranha, H. (2015) · Pharmaceutical Bioprocessing · doi:10.4155/pbp.14.62 · Cited by 63
Reliable protein production in a Pseudomonas fluorescens expression system
Retallack, D. M., Jin, H., & Chew, L. (2012) · Protein Expression and Purification · doi:10.1016/j.pep.2011.09.010 · Cited by 46
Metadata
- Authors
- Roque, A. C. A., Lowe, C. R., & Taipa, M. A.
- Venue
- Biotechnology Progress
- Publisher
- Wiley
- Published
- 2004-06-04
- Volume
- 20
- Issue
- 3
- Pages
- 639-654
- ISSN
- 1520-6033 (ISSN-L)
- 8756-7938
- OpenAlex
- W2028284841
- Cited by
- 360
- References
- 100
- FWCI
- 7.22
- Type
- journal article
- Language
- en
- Open access
- closed
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