Cited by 133Microbial Metabolic Engineering and BioproductionViral Infectious Diseases and Gene Expression in InsectsFungal and yeast genetics research

The DOI matches its Crossref record; 259 of the 266 references it cites were found in a registry or an index.

Unconventional microbial systems for the cost-efficient production of high-quality protein therapeutics

Corchero, José Luis, Gasser, Brigitte, Resina, David, Smith, Wesley, Parrilli, Ermenegilda, Vázquez, Felícitas, Abasolo, Ibane, Giuliani, Maria, Jäntti, Jussi, Ferrer, Pau, Saloheimo, Markku, Mattanovich, Diethard, Schwartz, Simó, Tutino, Maria Luisa, Villaverde, Antonio·2013·Biotechnology Advances

DOI 10.1016/j.biotechadv.2012.09.001

Open this paper in CoChat — free account

Abstract

Both conventional and innovative biomedical approaches require cost-effective protein drugs with high therapeutic potency, improved bioavailability, biocompatibility, stability and pharmacokinetics. The growing longevity of the human population, the increasing incidence and prevalence of age-related diseases and the better comprehension of genetic-linked disorders prompt to develop natural and engineered drugs addressed to fulfill emerging therapeutic demands. Conventional microbial systems have been for long time exploited to produce biotherapeutics, competing with animal cells due to easier operation and lower process costs. However, both biological platforms exhibit important drawbacks (mainly associated to intracellular retention of the product, lack of post-translational modifications and conformational stresses), that cannot be overcome through further strain optimization merely due to physiological constraints. The metabolic diversity among microorganisms offers a spectrum of unconventional hosts, that, being able to bypass some of these weaknesses, are under progressive incorporation into production pipelines. In this review we describe the main biological traits and potentials of emerging bacterial, yeast, fungal and microalgae systems, by comparing selected leading species with well established conventional organisms with a long run in protein drug production.

Integrity signals

Registry

Crossref · 10.1016/j.biotechadv.2012.09.001

Cites

259 of 259 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

Commercial Applications of Microalgae
Spolaore, P., Joannis-Cassan, C., Duran, E., & Isambert, A. (2006) · Journal of Bioscience and Bioengineering · doi:10.1263/jbb.101.87 · Cited by 4,285
Aggresomes: A Cellular Response to Misfolded Proteins
Johnston, J. A., Ward, C. L., & Kopito, R. R. (1998) · The Journal of Cell Biology · doi:10.1083/jcb.143.7.1883 · Cited by 2,148
Production of recombinant protein therapeutics in cultivated mammalian cells
Wurm, F. M. (2004) · Nature Biotechnology · doi:10.1038/nbt1026 · Cited by 2,032
Aggresomes, inclusion bodies and protein aggregation
Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,942
Recombinant protein folding and misfolding in Escherichia coli
Baneyx, F., & Mujacic, M. (2004) · Nature Biotechnology · doi:10.1038/nbt1029 · Cited by 1,497
Microbial Ecology: Fundamentals and Applications
Atlas, R. M., & Bartha, R. (1978) · Cited by 1,261
Protein drug stability: a formulation challenge
Frøkjær, S., & Otzen, D. E. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1695 · Cited by 1,116
Microbial Ecology: Fundamentals and Applications.
Swift, M. J., Atlas, R. M., & Bartha, R. (1982) · Journal of Ecology · doi:10.2307/2259932 · Cited by 1,113
Production of recombinant proteins by microbes and higher organisms
Demain, A. L., & Vaishnav, P. (2009) · Biotechnology Advances · doi:10.1016/j.biotechadv.2009.01.008 · Cited by 1,043
High-level and high-throughput recombinant protein production by transient transfection of suspension-growing human 293-EBNA1 cells
Durocher, Y. (2002) · Nucleic Acids Research · doi:10.1093/nar/30.2.e9 · Cited by 1,037
Chloroplast Transformation in Chlamydomonas with High Velocity Microprojectiles
Boynton, J. E., Gillham, N. W., Harris, E. H., Hosler, J. P., Johnson, A. M., Jones, A. R., Randolph-Anderson, B. L., Robertson, D., Klein, T. M., Shark, K. B., et al. (1988) · Science · doi:10.1126/science.2897716 · Cited by 963
Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
Sørensen, H. P., & Mortensen, K. K. (2005) · Microbial Cell Factories · doi:10.1186/1475-2859-4-1 · Cited by 841
The purification of eukaryotic polypeptides synthesized in Escherichia coli
Marston, F. A. O. (1986) · Biochemical Journal · doi:10.1042/bj2400001 · Cited by 837
N-Linked Glycosylation in Campylobacter jejuni and Its Functional Transfer into E. coli
Wacker, M., Linton, D., Hitchen, P. G., Lazar, M. N., Haslam, S. M., North, S. J., Panico, M., Morris, H. R., Dell, A., Wren, B. W., et al. (2002) · Science · doi:10.1126/science.298.5599.1790 · Cited by 780
Directed evolution of industrial enzymes: an update.
Cherry, J., & Fidantsef, A. (2003) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(03)00099-5 · Cited by 778
Biopharmaceutical benchmarks 2010
Walsh, G. (2010) · Nature Biotechnology · doi:10.1038/nbt0910-917 · Cited by 755
Human hepatitis B vaccine from recombinant yeast
McAleer, W. J., Buynak, E. B., Maigetter, R. Z., Wampler, D. E., Miller, W. J. W., & Hilleman, M. R. (1984) · Nature · doi:10.1038/307178a0 · Cited by 740
Microalgal biofactories: A promising approach towards sustainable omega-3 fatty acid production
Adarme-Vega, T. C., Lim, D. K. Y., Timmins, M., Vernen, F., Li, Y., & Schenk, P. M. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-96 · Cited by 641
A green light for engineered algae: redirecting metabolism to fuel a biotechnology revolution
Rosenberg, J. N., Oyler, G. A., Wilkinson, L., & Betenbaugh, M. J. (2008) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2008.07.008 · Cited by 631
Formation of high molecular weight complexes of mutant Cu,Zn-superoxide dismutase in a mouse model for familial amyotrophic lateral sclerosis
Johnston, J. A., Dalton, M. J., Gurney, M. E., & Kopito, R. R. (2000) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.220417997 · Cited by 616
Characterization and Dynamics of Aggresome Formation by a Cytosolic Gfp-Chimera✪
García‐Mata, R., Bebők, Z., Sorscher, E. J., & Sztul, E. S. (1999) · The Journal of Cell Biology · doi:10.1083/jcb.146.6.1239 · Cited by 597
Immunogenicity of protein therapeutics
Groot, A. S. D., & Scott, D. W. (2007) · Trends in Immunology · doi:10.1016/j.it.2007.07.011 · Cited by 544
Humanization of yeast to produce complex terminally sialylated glycoproteins
Hamilton, S. R., Davidson, R. C., Sethuraman, N., Nett, J. H., Jiang, Y., Rios, S., Bobrowicz, P., Stadheim, T. A., Li, H., Choi, B.-K., et al. (2006) · Science · doi:10.1126/science.1130256 · Cited by 511
Enhancement of therapeutic protein in vivo activities through glycoengineering
Elliott, S., Lorenzini, T., Asher, S., Aoki, K., Brankow, D. W., Buck, L., Busse, L. A., Chang, D., Fuller, J., Grant, J. R., et al. (2003) · Nature Biotechnology · doi:10.1038/nbt799 · Cited by 510
Strategies for optimizing heterologous protein expression in Escherichia coli
Hannig, G., & Makrides, S. C. (1998) · Trends in biotechnology · doi:10.1016/s0167-7799(97)01155-4 · Cited by 495
Animal cell cultures: recent achievements and perspectives in the production of biopharmaceuticals
Butler, M. (2005) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-005-1980-8 · Cited by 493
Bacillus subtilis as cell factory for pharmaceutical proteins: a biotechnological approach to optimize the host organism
Westers, L., Westers, H., & Quax, W. J. (2004) · Biochimica et Biophysica Acta (BBA) - Molecular Cell Research · doi:10.1016/j.bbamcr.2004.02.011 · Cited by 491
Introduction to current and future protein therapeutics: A protein engineering perspective
Carter, P. J. (2011) · Experimental Cell Research · doi:10.1016/j.yexcr.2011.02.013 · Cited by 489
Recombinant protein secretion in Escherichia coli
Mergulhão, F. J. M., Summers, D. K., & Monteiro, G. A. (2005) · Biotechnology Advances · doi:10.1016/j.biotechadv.2004.11.003 · Cited by 485
Microbial factories for recombinant pharmaceuticals
Ferrer‐Miralles, N., Domingo‐Espín, J., Corchero, J. L., Vázquez, E., & Villaverde, A. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-17 · Cited by 465
Self-citation
Enclosed outdoor photobioreactors: Light regime, photosynthetic efficiency, scale‐up, and future prospects
Janssen, M., Tramper, J., Mur, L. R., & Wijffels, R. H. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10468 · Cited by 464
The argininosuccinate lyase gene of Chlamydomonas reinhardtii: an important tool for nuclear transformation and for correlating the genetic and molecular maps of the ARG7 locus.
Debuchy, R., Purton, S., & Rochaix, J. (1989) · The EMBO Journal · doi:10.1002/j.1460-2075.1989.tb08426.x · Cited by 411
Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
Gerngross, T. U. (2004) · Nature Biotechnology · doi:10.1038/nbt1028 · Cited by 409
A perspective on the biotechnological potential of microalgae
Raja, R., Hemaiswarya, S., Kumar, N. A., Sridhar, S., & Rengasamy, R. (2008) · Critical Reviews in Microbiology · doi:10.1080/10408410802086783 · Cited by 404
COMMERCIAL DEVELOPMENTS IN MICROALGAL BIOTECHNOLOGY
Apt, K. E., & Behrens, P. W. (1999) · Journal of Phycology · doi:10.1046/j.1529-8817.1999.3520215.x · Cited by 402
Process economics of industrial monoclonal antibody manufacture
Farid, S. S. (2006) · Journal of Chromatography B · doi:10.1016/j.jchromb.2006.07.037 · Cited by 394
Coping with cold: The genome of the versatile marine Antarctica bacterium Pseudoalteromonas haloplanktis TAC125Preprint
Médigue, C., Krin, E., Pascal, G., Barbe, V., Bernsel, A., Bertin, P. N., Cheung, F., Cruveiller, S., D’Amico, S., Duilio, A., et al. (2005) · Genome Research · doi:10.1101/gr.4126905 · Cited by 390
Self-citation
Hassles with Taking Out the Garbage: Aggravating Aggresomes
García‐Mata, R., Gao, Y., & Sztul, E. S. (2002) · Traffic · doi:10.1034/j.1600-0854.2002.30602.x · Cited by 387
Antibodies and Genetically Engineered Related Molecules: Production and Purification
Roque, A., Lowe, C. R., & Taipa, M. (2004) · Biotechnology progress (Print) · doi:10.1021/bp030070k · Cited by 368
Recombinant Protein Production in Yeasts
Mattanovich, D., Branduardi, P., Dato, L., Gasser, B., Sauer, M., & Porro, D. (2011) · Methods in molecular biology · doi:10.1007/978-1-61779-433-9_17 · Cited by 365
Self-citation
Protein aggregation in recombinant bacteria: biological role of inclusion bodies
Villaverde, A., & Carrió, M. (2003) · Biotechnology Letters · doi:10.1023/a:1025024104862 · Cited by 359
Self-citation
Protein folding and conformational stress in microbial cells producing recombinant proteins: a host comparative overview
Gasser, B., Saloheimo, M., Rinas, U., Dragosits, M., Rodríguez‐Carmona, E., Baumann, K., Giuliani, M., Parrilli, E., Branduardi, P., Lang, C., et al. (2008) · Microbial Cell Factories · doi:10.1186/1475-2859-7-11 · Cited by 347
Self-citation
Expression and assembly of a fully active antibody in algae
Mayfield, S. P., Franklin, S. E., & Lerner, R. A. (2003) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.0237108100 · Cited by 345
Engineering of protein secretion in yeast: strategies and impact on protein production
Idiris, A., Tohda, H., Kumagai, H., & Takegawa, K. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2447-0 · Cited by 333
Formulation and manufacturability of biologics
Shire, S. J. (2009) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2009.10.006 · Cited by 331
Recombinant protein production by large-scale transient gene expression in mammalian cells: state of the art and future perspectives
Baldi, L., Hacker, D. L., Adam, M., & Wurm, F. M. (2007) · Biotechnology Letters · doi:10.1007/s10529-006-9297-y · Cited by 328
Therapeutic application of peptides and proteins: parenteral forever?
Antošová, Z., Macková, M., Král, V., & Macek, T. (2009) · Trends in biotechnology · doi:10.1016/j.tibtech.2009.07.009 · Cited by 325
Expression of a human gene for interferon in yeast
Hitzeman, R. A., Hagie, F. E., Levine, H. L., Goeddel, D. V., Ammerer, G., & Hall, B. D. (1981) · Nature · doi:10.1038/293717a0 · Cited by 323
Specific aggregation of partially folded polypeptide chains: The molecular basis of inclusion body composition
Speed, M. A., Wang, D. I. C., & King, J. (1996) · Nature Biotechnology · doi:10.1038/nbt1096-1283 · Cited by 313
Strategies for the recovery of active proteins through refolding of bacterial inclusion body proteins
Vallejo, L. F., & Rinas, U. (2004) · Microbial Cell Factories · doi:10.1186/1475-2859-3-11 · Cited by 311
Micro-algae come of age as a platform for recombinant protein production
Specht, E. A., Miyake-Stoner, S. J., & Mayfield, S. P. (2010) · Biotechnology Letters · doi:10.1007/s10529-010-0326-5 · Cited by 304
Microalgae as bioreactors
Walker, T. L., Purton, S., Becker, D. K., & Collet, C. (2005) · Plant Cell Reports · doi:10.1007/s00299-005-0004-6 · Cited by 302
Genomic Diversity and Versatility of Lactobacillus plantarum, a Natural Metabolic Engineer
Siezen, R. J., & van Hylckama Vlieg, J. E. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-s1-s3 · Cited by 294
Chaperone-based procedure to increase yields of soluble recombinant proteins produced in E. coli
de Marco, A., Deuerling, E., Mogk, A., Tomoyasu, T., & Bukau, B. (2007) · BMC Biotechnology · doi:10.1186/1472-6750-7-32 · Cited by 291
Current Perspectives on Stability of Protein Drug Products during Formulation, Fill and Finish Operations
Rathore, N., & Rajan, R. S. (2008) · Biotechnology Progress · doi:10.1021/bp070462h · Cited by 290
Delivery of peptide and protein drugs over the blood–brain barrier
Brasnjevic, I., Steinbusch, H. W. M., Schmitz, C., & Martinez-Martinez, P. (2009) · Progress in Neurobiology · doi:10.1016/j.pneurobio.2008.12.002 · Cited by 279
Microalgae as bioreactors for bioplastic production
Hempel, F., Bozarth, A., Lindenkamp, N., Klingl, A., Zauner, S., Linne, U., Steinbüchel, A., & Maier, U. G. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-81 · Cited by 274
Production of therapeutic proteins in algae, analysis of expression of seven human proteins in the chloroplast of Chlamydomonas reinhardtii
Rasala, B. A., Muto, M., Lee, P. A., Jager, M., Cardoso, R. M. F., Behnke, C. A., Kirk, P. B., Hokanson, C. A., Crea, R., Mendez, M. J., et al. (2010) · Plant Biotechnology Journal · doi:10.1111/j.1467-7652.2010.00503.x · Cited by 271
Engineering complex-type N-glycosylation in Pichia pastoris using GlycoSwitch technology
Jacobs, P. P., Geysens, S., Vervecken, W., Contreras, R., & Callewaert, N. (2008) · Nature Protocols · doi:10.1038/nprot.2008.213 · Cited by 271
OCH1 encodes a novel membrane bound mannosyltransferase: outer chain elongation of asparagine‐linked oligosaccharides.
Nakayama, K.-I., Nagasu, T., Shimma, Y., Kuromitsu, J., & Jigami, Y. (1992) · The EMBO Journal · doi:10.1002/j.1460-2075.1992.tb05316.x · Cited by 260
Amyloid-like Properties of Bacterial Inclusion Bodies
Carrió, M., González‐Montalbán, N., Vera, A., Villaverde, A., & Ventura, S. (2005) · Journal of Molecular Biology · doi:10.1016/j.jmb.2005.02.030 · Cited by 254
Self-citation
Challenges in therapeutic glycoprotein production
Sethuraman, N., & Stadheim, T. A. (2006) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2006.06.010 · Cited by 252
Lactococci and lactobacilli as mucosal delivery vectors for therapeutic proteins and DNA vaccines
Bermúdez‐Humarán, L. G., Kharrat, P., Chatel, J., & Langella, P. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-s1-s4 · Cited by 244
Lactococcus lactis, an Efficient Cell Factory for Recombinant Protein Production and Secretion
Morello, E., Bermúdez‐Humarán, L. G., Llull, D., Solé-Jamault, V., Miraglio, N., Langella, P., & Poquet, I. (2007) · Microbial Physiology · doi:10.1159/000106082 · Cited by 243
Large-Scale transfection of mammalian cells for the fast production of recombinant protein
Pham, P. L., Kamen, A., & Durocher, Y. (2006) · Molecular Biotechnology · doi:10.1385/mb:34:2:225 · Cited by 236
A new method for quantitative determination of polysaccharides in the yeast cell wall. Application to the cell wall defective mutants ofSaccharomyces cerevisiae
Dallies, N., François, J., & Paquet, V. (1998) · Yeast · doi:10.1002/(sici)1097-0061(1998100)14:14 · Cited by 236
Aggresomes and Russell bodies
Kopito, R. R., & Sitia, R. (2000) · EMBO Reports · doi:10.1093/embo-reports/kvd052 · Cited by 234
Quality Attributes of Recombinant Therapeutic Proteins: An Assessment of Impact on Safety and Efficacy as Part of a Quality by Design Development Approach
Eon‐Duval, A., Broly, H., & Gleixner, R. (2012) · Biotechnology Progress · doi:10.1002/btpr.1548 · Cited by 234
Isolation and characterization of the nitrate reductase structural gene of Chlamydomonas reinhardtii.
Fernández, E. M., Schnell, R., Ranum, L. P. W., Hussey, S. C., Silflow, C. D., & Lefebvre, P. A. (1989) · Proceedings of the National Academy of Sciences · doi:10.1073/pnas.86.17.6449 · Cited by 232
Stability of protein production from recombinant mammalian cells
Barnes, L. M., Bentley, C. M., & Dickson, A. J. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10517 · Cited by 226
Protein secretion in Lactococcus lactis: an efficient way to increase the overall heterologous protein production
Loir, Y. L., Azevedo, V., Oliveira, S. C., Freitas, D., Miyoshi, A., Bermúdez‐Humarán, L. G., Nouaille, S., Ribeiro, L. A., Leclercq, S., Gabriel, J. E., et al. (2005) · Microbial Cell Factories · doi:10.1186/1475-2859-4-2 · Cited by 216
Strain engineering for improved expression of recombinant proteins in bacteria
Makino, T., Σκρέτας, Γ., & Georgiou, G. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-32 · Cited by 207
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 205
Large-scale transient expression in mammalian cells for recombinant protein production
Wurm, F. M., & Bernard, A. (1999) · Current Opinion in Biotechnology · doi:10.1016/s0958-1669(99)80027-5 · Cited by 205
Serum‐free large‐scale transient transfection of CHO cells
Derouazi, M., Girard, P., Tilborgh, F. V., Iglesias, K., Müller, N., Bertschinger, M., & Wurm, F. M. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.20161 · Cited by 205
Engineering of Pichia pastoris for improved production of antibody fragments
Gasser, B., Maurer, M., Gach, J. S., Kunert, R., & Mattanovich, D. (2006) · Biotechnology and Bioengineering · doi:10.1002/bit.20851 · Cited by 203
Self-citation
Transient gene expression: Recombinant protein production with suspension‐adapted HEK293‐EBNA cells
Meissner, P., Pick, H. M., Kulangara, A., Chatellard, P., Friedrich, K., & Wurm, F. M. (2001) · Biotechnology and Bioengineering · doi:10.1002/bit.1179 · Cited by 200
Not just for Eukarya anymore: protein glycosylation in Bacteria and Archaea
Abu‐Qarn, M., Eichler, J., & Sharon, N. (2008) · Current Opinion in Structural Biology · doi:10.1016/j.sbi.2008.06.010 · Cited by 198
Modifications of the metabolic pathways of lipid and triacylglycerol production in microalgae
Yu, W.-L., Ansari, W. S., Schoepp, N. G., Hannon, M. J., Mayfield, S. P., & Burkart, M. D. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-91 · Cited by 198
Development of a GFP reporter gene for Chlamydomonas reinhardtii chloroplast
Franklin, S. E., Ngo, B. X., Efuet, E. T., & Mayfield, S. P. (2002) · The Plant Journal · doi:10.1046/j.1365-313x.2002.01319.x · Cited by 194
Live bacterial vaccines--a review and identification of potential hazards.
Detmer, A. M., & Glenting, J. (2006) · Microbial Cell Factories · doi:10.1186/1475-2859-5-23 · Cited by 191
Strategies for high-level recombinant protein expression in transgenic microalgae: A review
Potvin, G., & Zhang, Z. (2010) · Biotechnology Advances · doi:10.1016/j.biotechadv.2010.08.006 · Cited by 191
Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures
Jahic, M., Wållberg, F., Bollók, M., García, P. G. M., & Enfors, S. (2003) · Microbial Cell Factories · doi:10.1186/1475-2859-2-6 · Cited by 190
Synthesis and assembly of a full‐length human monoclonal antibody in algal chloroplasts
Tran, M., Zhou, B., Pettersson, P. L., González, M. J., & Mayfield, S. P. (2009) · Biotechnology and Bioengineering · doi:10.1002/bit.22446 · Cited by 183
Causes of proteolytic degradation of secreted recombinant proteins produced in methylotrophic yeast Pichia pastoris: Case study with recombinant ovine interferon‐τ
Sinha, J., Plantz, B. A., İnan, M., & Meagher, M. M. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.20318 · Cited by 182
Engineering of Therapeutic Proteins Production in Escherichia coli
Kamionka, M. (2011) · Current Pharmaceutical Biotechnology · doi:10.2174/138920111794295693 · Cited by 179
Immunogenicity of aggregates of recombinant human growth hormone in mouse models
Fradkin, A. H., Carpenter, J. F., & Randolph, T. W. (2009) · Journal of Pharmaceutical Sciences · doi:10.1002/jps.21834 · Cited by 173
The Effects of Drugs Inhibiting Protein Secretion in the Filamentous Fungus Trichoderma reesei
Pakula, T., Laxell, M., Huuskonen, A., Uusitalo, J. M., Saloheimo, M., & Penttilä, M. E. (2003) · Journal of Biological Chemistry · doi:10.1074/jbc.m302372200 · Cited by 171
Self-citation
Microalgae as platforms for production of recombinant proteins and valuable compounds: progress and prospects
Gong, Y., Hu, H., Gao, Y., Xu, X., & Gao, H. C. (2011) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-011-1032-6 · Cited by 168
Structure of the N-linked oligosaccharides that show the complete loss of alpha-1,6-polymannose outer chain from och1, och1 mnn1, and och1 mnn1 alg3 mutants of Saccharomyces cerevisiae.
Nakanishi-Shindo, Y., Nakayama, K.-I., Tanaka, A., Toda, Y., & Jigami, Y. (1993) · Journal of Biological Chemistry · doi:10.1016/s0021-9258(19)74320-8 · Cited by 167
Engineering of glycosylation in yeast and other fungi: current state and perspectives
Pourcq, K. D., Schutter, K. D., & Callewaert, N. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-2721-1 · Cited by 167
Bench to batch: advances in plant cell culture for producing useful products
Weathers, P. J., Towler, M. J., & Xu, J. (2009) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-009-2354-4 · Cited by 165
Genomic analysis of the secretion stress response in the enzyme-producing cell factory Aspergillus niger
Guillemette, T., van Peij, N. N. M. E., Goosen, T., Lanthaler, K., Robson, G. D., van den Hondel, C. A. M. J. J., Stam, H., & Archer, D. B. (2007) · BMC Genomics · doi:10.1186/1471-2164-8-158 · Cited by 158
Cooverexpression of chaperones for enhanced secretion of a single-chain antibody fragment in Pichia pastoris
Damasceno, L. M., Anderson, K. A., Ritter, G., Cregg, J. M., Old, L. J., & Batt, C. A. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0652-7 · Cited by 157
Identification and characterisation of novel Pichia pastoris promoters for heterologous protein production
Stadlmayr, G., MecklenbrÃ¤uker, A., Rothmüller, M., Maurer, M., Sauer, M., Mattanovich, D., & Gasser, B. (2010) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2010.09.957 · Cited by 155
Self-citation
Lactococcus lactis as a live vector: Heterologous protein production and DNA delivery systems
Pontes, D. S., de Azevedo, M. S. P., Chatel, J., Langella, P., Azevedo, V., & Miyoshi, A. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.06.005 · Cited by 154
Parkin Accumulation in Aggresomes Due to Proteasome Impairment
Junn, E., Lee, S. S., Suhr, U. T., & Mouradian, M. M. (2002) · Journal of Biological Chemistry · doi:10.1074/jbc.m203159200 · Cited by 144
Activation mechanisms of the HACI‐mediated unfolded protein response in filamentous fungi
Saloheimo, M., Valkonen, M. J., & Penttilä, M. E. (2003) · Molecular Microbiology · doi:10.1046/j.1365-2958.2003.03363.x · Cited by 144
Self-citation
Production of Human Compatible High Mannose-type (Man5GlcNAc2) Sugar Chains in Saccharomyces cerevisiae
Chiba, Y., Suzuki, M., Yoshida, S., Yoshida, A., Ikenaga, H., Takeuchi, M., Jigami, Y., & Ichishima, E. (1998) · Journal of Biological Chemistry · doi:10.1074/jbc.273.41.26298 · Cited by 140
Eukaryotic protein production in designed storage organelles
Torrent, M., Llompart, B., Lasserre-Ramassamy, S., Llop-Tous, I., Bastida, M., Marzábal, P., Westerholm‐Parvinen, A., Saloheimo, M., Heifetz, P. B., & Ludevid, M. D. (2009) · BMC Biology · doi:10.1186/1741-7007-7-5 · Cited by 138
Self-citation
A Novel Fungal Expression System: Secretion of Active Calf Chymosin from the Filamentous Fungus Trichoderma Reesei
Harkki, A. M., Uusitalo, J. M., Bailey, M., Penttilä, M. E., & Knowles, J. K. C. (1989) · Nature Biotechnology · doi:10.1038/nbt0689-596 · Cited by 136
Localization of Chaperones DnaK and GroEL in Bacterial Inclusion Bodies
Carrió, M., & Villaverde, A. (2005) · Journal of Bacteriology · doi:10.1128/jb.187.10.3599-3601.2005 · Cited by 136
Self-citation
Factors influencing glycosylation of Trichoderma reesei cellulases. I: Postsecretorial changes of the O- and N-glycosylation pattern of Cel7A
Stals, I. (2004) · Glycobiology · doi:10.1093/glycob/cwh080 · Cited by 134
Recent trends in stabilising peptides and proteins in pharmaceutical formulation – considerations in the choice of excipients
Jørgensen, L., Hostrup, S., Moeller, E. H., & Grohganz, H. (2009) · Expert Opinion on Drug Delivery · doi:10.1517/17425240903199143 · Cited by 133
Genome‐scale metabolic model of methylotrophic yeast Pichia pastoris and its use for in silico analysis of heterologous protein production
Sohn, S. B., Graf, A. B., Kim, T. Y., Gasser, B., Maurer, M., Ferrer, P., Mattanovich, D., & Lee, S. Y. (2010) · Biotechnology Journal · doi:10.1002/biot.201000078 · Cited by 133
Self-citation
Enzyme production by filamentous fungi: analysis of the secretome of Trichoderma reesei grown on unconventional carbon source
Jun, H., Kieselbach, T., & Jönsson, L. J. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-68 · Cited by 133
The pro‐sequence facilitates folding of human nerve growth factor fromEscherichia coliinclusion bodies
Rattenholl, A., Lilie, H., Grossmann, A., Stern, A., Schwarz, E., & Rudolph, R. (2001) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2001.02232.x · Cited by 132
Large‐scale transient transfection of serum‐free suspension‐growing HEK293 EBNA1 cells: Peptone additives improve cell growth and transfection efficiency
Pham, P. L., Perret, S., Doan, H. C., Cass, B., St‐Laurent, G., Kamen, A., & Durocher, Y. (2003) · Biotechnology and Bioengineering · doi:10.1002/bit.10774 · Cited by 131
Characterization of the aggregates formed during recombinant protein expression in bacteria
Schrödel, A., & de Marco, A. (2005) · BMC Biochemistry · doi:10.1186/1471-2091-6-10 · Cited by 131
Transgenic microalgae as a non-antibiotic bactericide producer to defend against bacterial pathogen infection in the fish digestive tract
Li, S.-S., & Tsai, H.-J. (2009) · Fish & Shellfish Immunology · doi:10.1016/j.fsi.2008.07.004 · Cited by 130
Recombinant protein solubility—does more mean better?
González‐Montalbán, N., García‐Fruitós, E., & Villaverde, A. (2007) · Nature Biotechnology · doi:10.1038/nbt0707-718 · Cited by 130
Self-citation
Directed gene copy number amplification inPichia pastorisby vector integration into the ribosomal DNA locus
Marx, H., MecklenbrÃ¤uker, A., Gasser, B., Sauer, M., & Mattanovich, D. (2009) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2009.00561.x · Cited by 127
Self-citation
Bioproduction of Therapeutic Proteins in the 21st Century and the Role of Plants and Plant Cells as Production Platforms
Boehm, R. (2007) · Annals of the New York Academy of Sciences · doi:10.1196/annals.1408.009 · Cited by 123
Side effects of chaperone gene co-expression in recombinant protein production
Martínez‐Alonso, M., García‐Fruitós, E., Ferrer‐Miralles, N., Rinas, U., & Villaverde, A. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-64 · Cited by 123
Self-citation
Employing epigenetics to augment the expression of therapeutic proteins in mammalian cells
Kwaks, T., & Otte, A. P. (2006) · Trends in biotechnology · doi:10.1016/j.tibtech.2006.01.007 · Cited by 121
Efficient Production of Antibody Fragments by the Filamentous Fungus Trichoderma reesei
Nyyssönen, E., Penttilä, M. E., Harkki, A. M., Saloheimo, A., Knowles, J. K. C., & Keränen, S. (1993) · Nature Biotechnology · doi:10.1038/nbt0593-591 · Cited by 120
Novel insights into the unfolded protein response using Pichia pastoris specific DNA microarrays
Graf, A. B., Gasser, B., Dragosits, M., Sauer, M., Leparc, G., Tüchler, T., Kreil, D. P., & Mattanovich, D. (2008) · BMC Genomics · doi:10.1186/1471-2164-9-390 · Cited by 117
Self-citation
Nanostructured bacterial materials for innovative medicines
Rodríguez‐Carmona, E., & Villaverde, A. (2010) · Trends in Microbiology · doi:10.1016/j.tim.2010.06.007 · Cited by 116
Self-citation
Use of folding modulators to improve heterologous protein production in Escherichia coli
Kolaj‐Robin, O., Spada, S., Robin, S., & Wall, J. G. (2009) · University of Limerick Institutional Repository (University of Limerick) · doi:10.34961/2685 · Cited by 116
Heterologous Protein Secretion by Bacillus Species
Pohl, S., & Harwood, C. R. (2010) · Advances in applied microbiology · doi:10.1016/s0065-2164(10)73001-x · Cited by 115
100-liter transient transfection
Girard, P., Derouazi, M., Baumgartner, G., Bourgeois, M., Jordan, M., Jacko, B., & Wurm, F. M. (2002) · Cytotechnology · doi:10.1023/a:1021173124640 · Cited by 115
Fed‐batch methanol feeding strategy for recombinant protein production by Pichia pastoris in the presence of co‐substrate sorbitol
Çelik, E., Çalı́k, P., & Oliver, S. G. (2009) · Yeast · doi:10.1002/yea.1679 · Cited by 115
Production of recombinant proteins and metabolites in yeasts
Porro, D., Gasser, B., Fossati, T., Maurer, M., Branduardi, P., Sauer, M., & Mattanovich, D. (2010) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-010-3019-z · Cited by 112
Self-citation
Transient gene expression in HEK293 cells: Peptone addition posttransfection improves recombinant protein synthesis
Pham, P. L., Perret, S., Cass, B., Carpentier, E., St‐Laurent, G., Bisson, L., Kamen, A., & Durocher, Y. (2005) · Biotechnology and Bioengineering · doi:10.1002/bit.20428 · Cited by 112
Mild Hypothermia Improves Transient Gene Expression Yields Several Fold in Chinese Hamster Ovary Cells
Wulhfard, S., Tissot, S., Bouchet, S., Cevey, J., de Jesus, M., Hacker, D. L., & Wurm, F. M. (2008) · Biotechnology Progress · doi:10.1021/bp070286c · Cited by 110
Decision-Support Tool for Assessing Biomanufacturing Strategies under Uncertainty: Stainless Steel versus Disposable Equipment for Clinical Trial Material Preparation
Farid, S. S., Washbrook, J., & Titchener-Hooker, N. J. (2005) · Biotechnology Progress · doi:10.1021/bp049692b · Cited by 109
Current achievements in the production of complex biopharmaceuticals with moss bioreactors
Decker, E. L., & Reski, R. (2007) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-007-0151-y · Cited by 107
A Gene Optimization Strategy that Enhances Production of Fully Functional P-Glycoprotein in Pichia pastoris
Bai, J., Swartz, D. J., Protasevich, I. I., Brouillette, C. G., Harrell, P. M., Hildebrandt, E. F., Gasser, B., Mattanovich, D., Ward, A. B., Chang, G. A., et al. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022577 · Cited by 106
Self-citation
Yeast expression platforms
Böer, E., Steinborn, G., Kunze, G., & Gellissen, G. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1209-0 · Cited by 105
Contribution of 5′- and 3′-untranslated regions of plastid mRNAs to the expression of Chlamydomonas reinhardtii chloroplast genes
Barnes, D., Franklin, S. E., Schultz, J., Henry, R. E., Brown, E. C., Coragliotti, A., & Mayfield, S. P. (2005) · Molecular Genetics and Genomics · doi:10.1007/s00438-005-0055-y · Cited by 105
Lactococcus lactis Expressing either Staphylococcus aureus Fibronectin-Binding Protein A or Listeria monocytogenes Internalin A Can Efficiently Internalize and Deliver DNA in Human Epithelial Cells
Innocentin, S., Guimarães, V., Miyoshi, A., Azevedo, V., Langella, P., Chatel, J., & Lefèvre, F. (2009) · Applied and Environmental Microbiology · doi:10.1128/aem.00825-09 · Cited by 105
E. coli Transports Aggregated Proteins to the Poles by a Specific and Energy-Dependent Process
Rokney, A., Shagan, M., Kessel, M., Smith, Y., Rosenshine, I., & Oppenheim, A. B. (2009) · Journal of Molecular Biology · doi:10.1016/j.jmb.2009.07.009 · Cited by 104
Analysis of the heat capacity dependence of protein folding
Yang, A., Sharp, K. A., & Honig, B. H. (1992) · Journal of Molecular Biology · doi:10.1016/0022-2836(92)90229-d · Cited by 102
Simple high-cell density fed-batch technique for high-level recombinant protein production with Pichia pastoris: Application to intracellular production of Hepatitis B surface antigen
Gurramkonda, C., Adnan, A., Gäbel, T., Lünsdorf, H., Roß, A., Nemani, S. K., Swaminathan, S., Khanna, N., & Rinas, U. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-13 · Cited by 99
Common features and interesting differences in transcriptional responses to secretion stress in the fungi Trichoderma reesei and Saccharomyces cerevisiae
Arvas, M., Pakula, T., Lanthaler, K., Saloheimo, M., Valkonen, M. J., Suortti, T., Robson, G., & Penttilä, M. E. (2006) · BMC Genomics · doi:10.1186/1471-2164-7-32 · Cited by 98
Self-citation
Low Molecular Weight High–Mannose Type Glycans in a Secreted Protein of the Filamentous Fungus Trichoderma Reesei
Salovuori, I., Makarow, M., Rauvala, H., Knowles, J., & Kääriäinen, L. (1987) · Nature Biotechnology · doi:10.1038/nbt0287-152 · Cited by 98
Enzyme production by recombinant Trichoderma reesei strains
Uusitalo, J. M., Nevalainen, H. K. M., Harkki, A. M., Knowles, J. K. C., & Penttilä, M. E. (1991) · Journal of Biotechnology · doi:10.1016/0168-1656(91)90025-q · Cited by 97
Development of a luciferase reporter gene, luxCt, for Chlamydomonas reinhardtii chloroplast
Mayfield, S. P., & Schultz, J. (2004) · The Plant Journal · doi:10.1046/j.1365-313x.2003.01965.x · Cited by 95
Triggering Aggresome Formation
Zaarur, N., Meriin, A. B., Gabai, V. L., & Sherman, M. Y. (2008) · Journal of Biological Chemistry · doi:10.1074/jbc.m802216200 · Cited by 95
Proteomics of life at low temperatures: trigger factor is the primary chaperone in the Antarctic bacterium Pseudoalteromonas haloplanktis TAC125
Piette, F., D’Amico, S., Struvay, C., Mazzucchelli, G., Renaut, J., Tutino, M. L., Danchin, A., Leprince, P., & Feller, G. (2010) · Molecular Microbiology · doi:10.1111/j.1365-2958.2010.07084.x · Cited by 95
Self-citation
The yeast Golgi apparatus: Insights and mysteries
Papanikou, E., & Glick, B. S. (2009) · FEBS Letters · doi:10.1016/j.febslet.2009.10.072 · Cited by 94
Recombinant lactic acid bacteria as mucosal biotherapeutic agents
Daniel, C., Roussel, Y., Kleerebezem, M., & Pot, B. (2011) · Trends in biotechnology · doi:10.1016/j.tibtech.2011.05.002 · Cited by 93
A novel expression platform for the production of diabetes-associated autoantigen human glutamic acid decarboxylase (hGAD65)
Wang, X., Brandsma, M. E., Tremblay, R., Maxwell, D. P., Jevnikar, A. M., Hüner, N. P. A., & Ma, S. (2008) · BMC Biotechnology · doi:10.1186/1472-6750-8-87 · Cited by 93
Divergent Genetic Control of Protein Solubility and Conformational Quality in Escherichia coli
García‐Fruitós, E., Martínez‐Alonso, M., González‐Montalbán, N., Valli, M., Mattanovich, D., & Villaverde, A. (2007) · Journal of Molecular Biology · doi:10.1016/j.jmb.2007.09.004 · Cited by 92
Self-citation
Blood–brain barrier delivery of protein and non-viral gene therapeutics with molecular Trojan horses
Pardridge, W. M. (2007) · Journal of Controlled Release · doi:10.1016/j.jconrel.2007.04.001 · Cited by 92
Virus-like particle production with yeast: ultrastructural and immunocytochemical insights into Pichia pastoris producing high levels of the Hepatitis B surface antigen
Lünsdorf, H., Gurramkonda, C., Adnan, A., Khanna, N., & Rinas, U. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-48 · Cited by 92
Moss bioreactors producing improved biopharmaceuticals
Decker, E. L., & Reski, R. (2007) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2007.07.012 · Cited by 92
Recent developments in the production of human therapeutic proteins in eukaryotic algae
Franklin, S. E., & Mayfield, S. P. (2005) · Expert Opinion on Biological Therapy · doi:10.1517/14712598.5.2.225 · Cited by 92
Highly phosphomannosylated enzyme replacement therapy for GM2 gangliosidosis
Tsuji, D., Akeboshi, H., Matsuoka, K., Yasuoka, H., Miyasaki, E., Kasahara, Y., Kawashima, I., Chiba, Y., Jigami, Y., Taki, T., et al. (2010) · Annals of Neurology · doi:10.1002/ana.22262 · Cited by 91
Vaccines based on whole recombinant Saccharomyces cerevisiae cells
Ardiani, A., Higgins, J. P., & Hodge, J. W. (2010) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2010.00665.x · Cited by 90
Antibody production with yeasts and filamentous fungi: on the road to large scale?
Gasser, B., & Mattanovich, D. (2006) · Biotechnology Letters · doi:10.1007/s10529-006-9237-x · Cited by 86
Self-citation
Chlamydomonas reinhardtii: A Protein Expression System for Pharmaceutical and Biotechnological Proteins
Griesbeck, C., Kobl, I., & Heitzer, M. (2006) · Molecular Biotechnology · doi:10.1385/mb:34:2:213 · Cited by 85
Food‐grade gene expression in lactic acid bacteria
Peterbauer, C., Maischberger, T., & Haltrich, D. (2011) · Biotechnology Journal · doi:10.1002/biot.201100034 · Cited by 83
Isolation of cell-free bacterial inclusion bodies
Rodríguez‐Carmona, E., Cano‐Garrido, O., Seras‐Franzoso, J., Villaverde, A., & García‐Fruitós, E. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-71 · Cited by 83
Self-citation
A novel replication element from an Antarctic plasmid as a tool for the expression of proteins at low temperature
Tutino, M. L., Duilio, A., Parrilli, E., Remaut, E., Sannia, G., & Marino, G. (2001) · Extremophiles · doi:10.1007/s007920100203 · Cited by 82
Self-citation
Aspartate aminotransferase from the Antarctic bacterium Pseudoalteromonas haloplanktis TAC 125
Birolo, L., Tutino, M. L., Fontanella, B., Gerday, C., Mainolfi, K., Pascarella, S., Sannia, G., Vinci, F., & Marino, G. (2000) · European Journal of Biochemistry · doi:10.1046/j.1432-1327.2000.01299.x · Cited by 81
Self-citation
Removal of N‐terminal methionine from recombinant proteins by engineered E. coli methionine aminopeptidase
Liao, Y., Jeng, J., Wang, C., Wang, S., & Chang, S. (2004) · Protein Science · doi:10.1110/ps.04679104 · Cited by 81
Learning about protein solubility from bacterial inclusion bodies
Martínez‐Alonso, M., González‐Montalbán, N., García‐Fruitós, E., & Villaverde, A. (2009) · Microbial Cell Factories · doi:10.1186/1475-2859-8-4 · Cited by 80
Self-citation
High-Yield Intra- and Extracellular Protein Production Using Bacillus megaterium
Stammen, S., Müller, B. K., Korneli, C., Biedendieck, R., Gamer, M., Franco‐Lara, E., & Jahn, D. (2010) · Applied and Environmental Microbiology · doi:10.1128/aem.00431-10 · Cited by 80
Transferrin Fusion Technology: A Novel Approach to Prolonging Biological Half-Life of Insulinotropic Peptides
Kim, B.-J., Zhou, J., Martin, B., Carlson, O. D., Maudsley, S. R., Greig, N. H., Mattson, M. P., Ladenheim, E. E., Wustner, J., Turner, A., et al. (2010) · Journal of Pharmacology and Experimental Therapeutics · doi:10.1124/jpet.110.166470 · Cited by 78
Inclusion bodies: a new concept
García‐Fruitós, E. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-80 · Cited by 78
Pharmacokinetics of IgG1 monoclonal antibodies produced in humanized Pichia pastoris with specific glycoforms: A comparative study with CHO produced materials
Liu, L., Stadheim, A., Hamuro, L., Pittman, T. J., Wang, W., Zha, D., Hochman, J. H., & Prueksaritanont, T. (2011) · Biologicals · doi:10.1016/j.biologicals.2011.06.002 · Cited by 76
Towards universal systems for recombinant gene expression
Sørensen, H. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-27 · Cited by 74
TatABC Overexpression Improves Corynebacterium glutamicum Tat-Dependent Protein Secretion
Kikuchi, Y., Itaya, H., Date, M., Matsui, K., & Wu, L. (2008) · Applied and Environmental Microbiology · doi:10.1128/aem.01874-08 · Cited by 72
Advancing mammalian cell culture engineering using genome-scale technologies
Griffin, T. J., Seth, G., Xie, H., Bandhakavi, S., & Hu, W. (2007) · Trends in biotechnology · doi:10.1016/j.tibtech.2007.07.004 · Cited by 71
Recombinant protein vaccines against the asexual blood-stages ofPlasmodium falciparum
Anders, R. F., Adda, C. G., Foley, M., & Norton, R. S. (2010) · Human Vaccines · doi:10.4161/hv.6.1.10712 · Cited by 71
The protein disulphide isomerase gene of the fungus Trichoderma reesei is induced by endoplasmic reticulum stress and regulated by the carbon source
Saloheimo, M., Lund, M., & Penttilä, M. E. (1999) · Molecular and General Genetics MGG · doi:10.1007/s004380051057 · Cited by 68
Self-citation
Transient transfection of CHO-K1-S using serum-free medium in suspension: a rapid mammalian protein expression system
Rosser, M. P., Xia, W., Hartsell, S., McCaman, M., Zhu, Y., Wang, S., Harvey, S., Bringmann, P., & Cobb, R. R. (2005) · Protein Expression and Purification · doi:10.1016/j.pep.2004.07.015 · Cited by 68
Glycan Engineering and Production of 'Humanized' Glycoprotein in Yeast Cells
Chiba, Y., & Akeboshi, H. (2009) · Biological and Pharmaceutical Bulletin · doi:10.1248/bpb.32.786 · Cited by 67
Protein trafficking, ergosterol biosynthesis and membrane physics impact recombinant protein secretion in Pichia pastoris
Baumann, K., Adelantado, N., Lang, C., Mattanovich, D., & Ferrer, P. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-93 · Cited by 65
Self-citation
Nanotechnology, bionanotechnology and microbial cell factories
Villaverde, A. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-53 · Cited by 63
Self-citation
Production of Chryseobacterium proteolyticum protein-glutaminase using the twin-arginine translocation pathway in Corynebacterium glutamicum
Kikuchi, Y., Itaya, H., Date, M., Matsui, K., & Wu, L. (2007) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-007-1283-3 · Cited by 62
Systems biology of lactic acid bacteria: a critical review
Teusink, B., Bachmann, H., & Molenaar, D. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-s1-s11 · Cited by 62
Packaging protein drugs as bacterial inclusion bodies for therapeutic applications
Villaverde, A., García‐Fruitós, E., Rinas, U., Seras‐Franzoso, J., Kosoy, A., Corchero, J. L., & Vázquez, E. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-76 · Cited by 61
Self-citation
Longer action means better drug: Tuning up protein therapeutics
Szlachcic, A., Zakrzewska, M., & Otlewski, J. (2011) · Biotechnology Advances · doi:10.1016/j.biotechadv.2011.03.005 · Cited by 61
Improvement of cell viability and hirudin production by ascorbic acid in Pichia pastoris fermentation
Xiao, A., Zhou, X., Zhou, L., & Zhang, Y. (2006) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-006-0338-1 · Cited by 60
Influence of growth temperature on the production of antibody Fab fragments in different microbes: A host comparative analysis
Dragosits, M., Frascotti, G., Bernard‐Granger, L., Vázquez, F., Giuliani, M., Baumann, K., Rodríguez‐Carmona, E., Tokkanen, J., Parrilli, E., Wiebe, M. G., et al. (2011) · Biotechnology Progress · doi:10.1002/btpr.524 · Cited by 59
Self-citation
Heterologous protein display on the cell surface of lactic acid bacteria mediated by the s-layer protein
Hu, S.-M., Kong, J., Sun, Z., Han, L., Kong, W.-T., & Yang, P. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-86 · Cited by 59
Recombinant Protein Production in Antarctic Gram-Negative Bacteria
Duilio, A., Tutino, M. L., & Marino, G. (2004) · Humana Press eBooks · doi:10.1385/1-59259-774-2:225 · Cited by 59
Self-citation
The impact of oxygen on the transcriptome of recombinant S. cerevisiae and P. pastoris - a comparative analysis
Baumann, K., Dato, L., Graf, A. B., Frascotti, G., Dragosits, M., Porro, D., Mattanovich, D., Ferrer, P., & Branduardi, P. (2011) · BMC Genomics · doi:10.1186/1471-2164-12-218 · Cited by 56
Self-citation
High-throughput screening and selection of yeast cell lines expressing monoclonal antibodies
Barnard, G. C., Kull, A. R., Sharkey, N., Shaikh, S. S., Rittenhour, A. M., Burnina, I., Jiang, Y., Li, F., Lynaugh, H., Mitchell, T., et al. (2010) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-010-0746-1 · Cited by 55
A new plasmid vector for DNA delivery using lactococci
Guimarães, V., Innocentin, S., Chatel, J., Lefèvre, F., Langella, P., Azevedo, V., & Miyoshi, A. (2009) · Genetic Vaccines and Therapy · doi:10.1186/1479-0556-7-4 · Cited by 55
Highly efficient production of phosphorylated hepatitis B core particles in yeast Pichia pastoris
Freivalds, J., Dišlers, A., Ose, V., Pumpens, P., Tārs, K., & Kazāks, A. (2010) · Protein Expression and Purification · doi:10.1016/j.pep.2010.09.010 · Cited by 55
Evaluation of Mut+ and MutS Pichia pastoris Phenotypes for High Level Extracellular scFv Expression under Feedback Control of the Methanol Concentration
Pla, I., Damasceno, L. M., Vannelli, T., Ritter, G., Batt, C. A., & Shuler, M. L. (2006) · Biotechnology Progress · doi:10.1021/bp060012+ · Cited by 54
Expression of human soluble TRAIL in Chlamydomonas reinhardtii chloroplast
Yang, Z., Li, Y., Chen, F., Li, D., Zhang, Z., Liu, Y., Zheng, D., Wang, Y., & Shen, G. (2006) · Chinese Science Bulletin · doi:10.1007/s11434-006-2041-0 · Cited by 53
An effective cold inducible expression system developed in Pseudoalteromonas haloplanktis TAC125
Papa, R., Rippa, V., Sannia, G., Marino, G., & Duilio, A. (2006) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2006.07.003 · Cited by 52
Next-generation protein drugs
Tomlinson, I. M. (2004) · Nature Biotechnology · doi:10.1038/nbt0504-521 · Cited by 51
PK–PD Modeling of Protein Drugs: Implications in Assay Development
Roskos, L. K., Schneider, A. K., Vainshtein, I., Schwickart, M., Lee, R., Lu, H. L., Faggioni, R., & Liang, M. (2011) · Bioanalysis · doi:10.4155/bio.11.28 · Cited by 51
Native-State Stability Determines the Extent of Degradation Relative to Secretion of Protein Variants from Pichia pastoris
Whyteside, G., Alcocer, M. J. C., Kumita, J. R., Dobson, C. M., Lazarou, M., Pleass, R. J., & Archer, D. B. (2011) · PLoS ONE · doi:10.1371/journal.pone.0022692 · Cited by 51
Role of the chaperone DnaK in protein solubility and conformational quality in inclusion body-formingEscherichia colicells
Martínez‐Alonso, M., Vera, A., & Villaverde, A. (2007) · FEMS Microbiology Letters · doi:10.1111/j.1574-6968.2007.00788.x · Cited by 50
Self-citation
Development of a generic transient transfection process at 100 L scale
Tuvesson, O., Uhe, C., Rozkov, A., & Lüllau, E. (2008) · Cytotechnology · doi:10.1007/s10616-008-9135-2 · Cited by 50
Engineering of a mammalian O-glycosylation pathway in the yeast Saccharomyces cerevisiae: production of O-fucosylated epidermal growth factor domains
Chigira, Y., Oka, T., Okajima, T., & Jigami, Y. (2008) · Glycobiology · doi:10.1093/glycob/cwn008 · Cited by 50
Recombinant dengue virus-like particles from Pichia pastoris: efficient production and immunological properties
Liu, W., Jiang, H., Zhou, J., Yang, X., Tang, Y., Fang, D., & Jiang, L. (2009) · Virus Genes · doi:10.1007/s11262-009-0418-2 · Cited by 49
Formulation Development for Hydrophobic Therapeutic Proteins
Hawe, A., & Frieß, W. (2007) · Pharmaceutical Development and Technology · doi:10.1080/10837450701247350 · Cited by 49
Recombinant Gene Expression
(2011) · Methods in molecular biology · doi:10.1007/978-1-61779-433-9 · Cited by 49
N-Linked glycoengineering for human therapeutic proteins in bacteria
Pandhal, J., & Wright, P. C. (2010) · Biotechnology Letters · doi:10.1007/s10529-010-0289-6 · Cited by 46
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
Protein production and induction of the unfolded protein response in Trichoderma reesei strain Rut‐C30 and its transformant expressing endoglucanase I with a hydrophobic tag
Collén, A., Saloheimo, M., Bailey, M., Penttilä, M. E., & Pakula, T. (2004) · Biotechnology and Bioengineering · doi:10.1002/bit.20350 · Cited by 46
Self-citation
Post-production protein stability: trouble beyond the cell factory
Vázquez, E., Corchero, J. L., & Villaverde, A. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-60 · Cited by 46
Self-citation
Development of an improved Pseudoalteromonas haloplanktis TAC125 strain for recombinant protein secretion at low temperature
Parrilli, E., Vizio, D. D., Cirulli, C., & Tutino, M. L. (2008) · Microbial Cell Factories · doi:10.1186/1475-2859-7-2 · Cited by 45
Self-citation

Flagged first, then by citations

7 of the 266 references couldn’t be matched to a known paper.

Research works printed but not linked: 2

Evans, 2009, Method of controlling O-linked glycosylation of antibodies, Novozymes Biopharm
Meyer, 2008, An emerging star for therapeutic and catalytic protein production, BioProcess Int, 6, 10

Sorted by citations

Adaptive laboratory evolution—Principles and applications for biotechnology
Dragosits, M., & Mattanovich, D. (2013) · Microbial Cell Factories · doi:10.1186/1475-2859-12-64 · Cited by 827
Self-citation
Recombinant pharmaceuticals from microbial cells: a 2015 update
Sánchez‐García, L., Martín, L., Mangues, R., Ferrer‐Miralles, N., Vázquez, E., & Villaverde, A. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0437-3 · Cited by 341
Self-citation
Photosynthetic biomanufacturing in green algae; production of recombinant proteins for industrial, nutritional, and medical uses
Rasala, B. A., & Mayfield, S. P. (2014) · Photosynthesis Research · doi:10.1007/s11120-014-9994-7 · Cited by 296
The Potential for Microalgae as Bioreactors to Produce Pharmaceuticals
Yan, N. J., Fan, C., Chen, Y., & Hu, Z. (2016) · International Journal of Molecular Sciences · doi:10.3390/ijms17060962 · Cited by 264
Pichia Pastoris : Protein Production Host and Model Organism for Biomedical Research
Gasser, B., Prielhofer, R., Marx, H., Maurer, M., Nocon, J., Steiger, M. G., Puxbaum, V., Sauer, M., & Mattanovich, D. (2013) · Future Microbiology · doi:10.2217/fmb.12.133 · Cited by 237
Self-citation

See all 133

Authors: Corchero, J. L., Gasser, B., Resina, D., Smith, W., Parrilli, E., Vázquez, F., Abasolo, I., Giuliani, M., Jäntti, J., Ferrer, P., Saloheimo, M., Mattanovich, D., Schwartz, S., Tutino, M. L., & Villaverde, A.
Affiliations: Austrian Centre of Industrial Biotechnology (Austria) (AT)
Parc Científic de Barcelona (ES)
VTT Technical Research Centre of Finland (FI)
University of Naples Federico II (IT)
Universitat Autònoma de Barcelona (ES)
Corresponding author: Villaverde, Antonio
ORCID: Gasser, Brigitte
Parrilli, Ermenegilda
Abasolo, Ibane
Jäntti, Jussi
Ferrer, Pau
Mattanovich, Diethard
Schwartz, Simó
Tutino, Maria Luisa
Villaverde, Antonio
Venue: Biotechnology Advances
Publisher: Elsevier BV
Published: 2013-03
Volume: 31
Issue: 2
Pages: 140-153
ISSN: 0734-9750 (ISSN-L)
DOI: 10.1016/j.biotechadv.2012.09.001
OpenAlex: W2069940872
Cited by: 133
References: 266
Citations by year: 2026: 8 · 2025: 4 · 2024: 6 · 2023: 6 · 2022: 10 · 2021: 7 · 2020: 6 · 2019: 8 · 2018: 3 · 2017: 11 · 2016: 20 · 2015: 14 · 2014: 17 · 2013: 11
FWCI: 1.25
Type: journal article
Language: en
Open access: closed
Licence: www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations: Biotechnology Advances (publishedVersion)
PubMed (publishedVersion)
Funders: Institució Catalana de Recerca i Estudis Avançats
Steirische Wirtschaftsförderungsgesellschaft
Instituto de Salud Carlos III
European Regional Development Fund
Topics: Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Microbial Metabolic Engineering and Bioproduction
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Viral Infectious Diseases and Gene Expression in Insects
Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Fungal and yeast genetics research
Keywords: therapeutic proteins, recombinant protein expression, microbial cell factories, post-translational modification, intracellular retention, recombinant yeast, recombinant bacteria
MeSH terms: Animals, Cost-Benefit Analysis, Escherichia coli, Industrial Microbiology, Mammals, Pichia, Protein Processing, Post-Translational, Recombinant Proteins, Saccharomyces cerevisiae, Trichoderma, Protein Engineering, Chlamydomonas reinhardtii, Protein Folding, Pseudoalteromonas

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review

Unconventional microbial systems for the cost-efficient production of high-quality protein therapeutics

Abstract

Overview

Integrity signals

Verification

Claims the paper makes

Claims other papers make about this one

Citations

Cites

Cited by

Related

Metadata

Record

About these checks