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

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 · see citing works

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 · see citing works

Production of recombinant protein therapeutics in cultivated mammalian cells

Wurm, F. M. (2004) · Nature Biotechnology · doi:10.1038/nbt1026 · Cited by 2,032 · see citing works

Aggresomes, inclusion bodies and protein aggregation

Kopito, R. R. (2000) · Trends in Cell Biology · doi:10.1016/s0962-8924(00)01852-3 · Cited by 1,906 · see citing works

Recombinant protein folding and misfolding in Escherichia coli

Baneyx, F., & Mujacic, M. (2004) · Nature Biotechnology · doi:10.1038/nbt1029 · Cited by 1,488 · see citing works

Microbial Ecology: Fundamentals and Applications

Atlas, R. M., & Bartha, R. (1978) · Cited by 1,261 · see citing works

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 · see citing works

Protein drug stability: a formulation challenge

Frøkjær, S., & Otzen, D. E. (2005) · Nature Reviews Drug Discovery · doi:10.1038/nrd1695 · Cited by 1,102 · see citing works

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 · see citing works

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 1,041 · see citing works

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 · see citing works

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 · see citing works

The purification of eukaryotic polypeptides synthesized in Escherichia coli

Marston, F. A. O. (1986) · Biochemical Journal · doi:10.1042/bj2400001 · Cited by 837 · see citing works

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 · see citing works

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 · see citing works

Biopharmaceutical benchmarks 2010

Walsh, G. (2010) · Nature Biotechnology · doi:10.1038/nbt0910-917 · Cited by 755 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 607 · see citing works

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 · see citing works

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 545 · see citing works

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 · see citing works

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 · see citing works

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 494 · see citing works

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 · see citing works

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 · see citing works

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 469 · see citing works

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 467 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 396 · see citing works

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 393 · see citing works

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 · see citing works

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 · see citing works

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 377 · see citing works

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 · see citing works

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 · see citing works

Protein aggregation in recombinant bacteria: biological role of inclusion bodies

Villaverde, A., & Carrió, M. (2003) · Biotechnology Letters · doi:10.1023/a:1025024104862 · Cited by 346 · see citing works

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 · see citing works

Formulation and manufacturability of biologics

Shire, S. J. (2009) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2009.10.006 · Cited by 331 · see citing works

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 327 · see citing works

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 · see citing works

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 324 · see citing works

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 · see citing works

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 312 · see citing works

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 311 · see citing works

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 · see citing works

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 297 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 271 · see citing works

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 · see citing works

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 250 · see citing works

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 247 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Aggresomes and Russell bodies

Kopito, R. R., & Sitia, R. (2000) · EMBO Reports · doi:10.1093/embo-reports/kvd052 · Cited by 230 · see citing works

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 223 · see citing works

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 218 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 204 · see citing works

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 · see citing works

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 200 · see citing works

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 · see citing works

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 200 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 188 · see citing works

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 · see citing works

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 · see citing works

Engineering of Therapeutic Proteins Production in Escherichia coli

Kamionka, M. (2011) · Current Pharmaceutical Biotechnology · doi:10.2174/138920111794295693 · Cited by 177 · see citing works

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 · see citing works

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 170 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 160 · see citing works

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 · see citing works

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 · see citing works

Identification and characterisation of novel Pichia pastoris promoters for heterologous protein production

Stadlmayr, G., Mecklenbräuker, 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 · see citing works

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 147 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Characterization of the aggregates formed during recombinant protein expression in bacteria

Schrodel, A., & de Marco, A. (2005) · BMC Biochemistry · doi:10.1186/1471-2091-6-10 · Cited by 138 · see citing works

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 137 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 130 · see citing works

Directed gene copy number amplification inPichia pastorisby vector integration into the ribosomal DNA locus

Marx, H., Mecklenbräuker, A., Gasser, B., Sauer, M., & Mattanovich, D. (2009) · FEMS Yeast Research · doi:10.1111/j.1567-1364.2009.00561.x · Cited by 127 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 118 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 106 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 104 · see citing works

Current achievements in the production of complex biopharmaceuticals with moss bioreactors

Decker, E. L., & Ralf Reski, A. (2007) · Bioprocess and Biosystems Engineering · doi:10.1007/s00449-007-0151-y · Cited by 104 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 94 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Moss bioreactors producing improved biopharmaceuticals

Decker, E. L., & Ralf Reski, A. (2007) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2007.07.012 · Cited by 90 · see citing works

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 84 · see citing works

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 84 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Inclusion bodies: a new concept

García‐Fruitós, E. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-80 · Cited by 78 · see citing works

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 77 · see citing works

Towards universal systems for recombinant gene expression

Sørensen, H. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-27 · Cited by 74 · see citing works

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 73 · see citing works

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 · see citing works

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 · see citing works

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 70 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Nanotechnology, bionanotechnology and microbial cell factories

Villaverde, A. (2010) · Microbial Cell Factories · doi:10.1186/1475-2859-9-53 · Cited by 63 · see citing works

Systems biology of lactic acid bacteria: a critical review

Teusink, B., Bachmann, H., & Douwe Molenaar, B. (2011) · Microbial Cell Factories · doi:10.1186/1475-2859-10-s1-s11 · Cited by 63 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Reliable protein production in a Pseudomonas fluorescens expression system

Retallack, D. M., Jin, H., & Chew, L. (2011) · Protein Expression and Purification · doi:10.1016/j.pep.2011.09.010 · Cited by 55 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 52 · see citing works

Next-generation protein drugs

Tomlinson, I. M. (2004) · Nature Biotechnology · doi:10.1038/nbt0504-521 · Cited by 51 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Recombinant Gene Expression

(2011) · Methods in molecular biology · doi:10.1007/978-1-61779-433-9 · Cited by 49 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

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 · see citing works

Efficient Antibody Production upon Suppression of O Mannosylation in the Yeast Ogataea minuta

Kuroda, K., Kobayashi, K., Kitagawa, Y., Nakagawa, T., Tsumura, H., Komeda, T., Shinmi, D., Mori, E., Motoki, K., Fuju, K., et al. (2007) · Applied and Environmental Microbiology · doi:10.1128/aem.02106-07 · Cited by 45 · see citing works

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 · see citing works

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 · see citing works

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 289 · see citing works

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 255 · see citing works

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 231 · see citing works

Challenges and opportunities for non-antibody scaffold drugs

Vazquez-Lombardi, R., Phan, T. G., Zimmermann, C., Lowe, D., Jermutus, L., & Christ, D. (2015) · Drug Discovery Today · doi:10.1016/j.drudis.2015.09.004 · Cited by 226 · see citing works

Microalgae and cyanobacteria as enzyme biofactories

Brasil, B. S. A. F., de Siqueira, F. G., Salum, T. F. C., Zanette, C. M., & Spier, M. R. (2017) · Algal Research · doi:10.1016/j.algal.2017.04.035 · Cited by 199 · see citing works

Towards systems metabolic engineering in Pichia pastoris

Schwarzhans, J.-P., Luttermann, T., Geier, M., Kalinowski, J., & Friehs, K. (2017) · Biotechnology Advances · doi:10.1016/j.biotechadv.2017.07.009 · Cited by 169 · see citing works

An improved secretion signal enhances the secretion of model proteins from Pichia pastoris

Barrero, J. J., Casler, J. C., Valero, F., Ferrer, P., & Glick, B. S. (2018) · Microbial Cell Factories · doi:10.1186/s12934-018-1009-5 · Cited by 157 · see citing works

Emerging Trends in Genetic Engineering of Microalgae for Commercial Applications

Grama, S. B., Liu, Z., & Li, J. (2022) · Marine Drugs · doi:10.3390/md20050285 · Cited by 157 · see citing works

Industrial Production of Proteins with Pichia pastoris—Komagataella phaffii

Barone, G. D., Emmerstorfer-Augustin, A., Biundo, A., Pisano, I., Coccetti, P., Mapelli, V., & Camattari, A. (2023) · Biomolecules · doi:10.3390/biom13030441 · Cited by 138 · see citing works

New biorefineries and sustainable agriculture: Increased food, biofuels, and ecosystem security

Chen, H., & Zhang, Y. ‐. P. (2015) · Renewable and Sustainable Energy Reviews · doi:10.1016/j.rser.2015.02.048 · Cited by 120 · see citing works

Challenges and progress towards industrial recombinant protein production in yeasts: A review

Brabander, P. D., Uitterhaegen, E., Delmulle, T., Winter, K. D., & Soetaert, W. (2023) · Biotechnology Advances · doi:10.1016/j.biotechadv.2023.108121 · Cited by 119 · see citing works

Recombinant protein production in Pichia pastoris under glyceraldehyde-3-phosphate dehydrogenase promoter: From carbon source metabolism to bioreactor operation parameters

Çalı́k, P., Ata, Ö., Güneş, H., Massahi, A., Boy, E., Keskin, A., Öztürk, S., Zerze, G. H., & Özdamar, T. H. (2014) · Biochemical Engineering Journal · doi:10.1016/j.bej.2014.12.003 · Cited by 111 · see citing works

Comparative genomics and transcriptomics of Pichia pastoris

Love, K. R., Shah, K., Whittaker, C. A., Wu, J., Matthews, C. B., Ma, D., Leeson, R. L., Priest, M., Borowsky, J. H., Young, S., et al. (2016) · BMC Genomics · doi:10.1186/s12864-016-2876-y · Cited by 110 · see citing works

Bacterial inclusion bodies are industrially exploitable amyloids

de Marco, A., Ferrer‐Miralles, N., García‐Fruitós, E., Mitraki, A., Peternel, Š., Rinas, U., Trujillo‐Roldán, M. A., Valdez‐Cruz, N. A., Vázquez, E., & Villaverde, A. (2018) · FEMS Microbiology Reviews · doi:10.1093/femsre/fuy038 · Cited by 109 · see citing works

The art of adapting to extreme environments: The model system Pseudoalteromonas

Parrilli, E., Tedesco, P., Fondi, M., Tutino, M. L., Giudice, A. L., de Pascale, D., & Fani, R. (2019) · Physics of Life Reviews · doi:10.1016/j.plrev.2019.04.003 · Cited by 106 · see citing works

Bacterial cell factories for recombinant protein production; expanding the catalogue

Ferrer‐Miralles, N., & Villaverde, A. (2013) · Microbial Cell Factories · doi:10.1186/1475-2859-12-113 · Cited by 105 · see citing works

Multifunctional Click Hyaluronic Acid Nanogels for Targeted Protein Delivery and Effective Cancer Treatment in Vivo

Chen, J., Zou, Y., Deng, C., Meng, F., Zhang, J., & Zhong, Z. (2016) · Chemistry of Materials · doi:10.1021/acs.chemmater.6b04404 · Cited by 99 · see citing works

The yeast stands alone: the future of protein biologic production

Love, K. R., Dalvie, N. C., & Love, J. C. (2017) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2017.12.010 · Cited by 97 · see citing works

Synthetic promoters capable of driving robust nuclear gene expression in the green alga Chlamydomonas reinhardtii

Scranton, M. A., Ostrand, J. T., Georgianna, D. R., Lofgren, S., Li, D. D., Ellis, R. C., Carruthers, D. N., Dräger, A., Masica, D. L., & Mayfield, S. P. (2016) · Algal Research · doi:10.1016/j.algal.2016.02.011 · Cited by 93 · see citing works

Fine‐tuning the P. pastoris iMT1026 genome‐scale metabolic model for improved prediction of growth on methanol or glycerol as sole carbon sources

Tomàs‐Gamisans, M., Ferrer, P., & Albiol, J. (2017) · Microbial Biotechnology · doi:10.1111/1751-7915.12871 · Cited by 92 · see citing works

ASA3P: An automatic and scalable pipeline for the assembly, annotation and higher-level analysis of closely related bacterial isolates

Schwengers, O., Hoek, A., Fritzenwanker, M., Falgenhauer, L., Hain, T., Chakraborty, T., & Goesmann, A. (2020) · PLoS Computational Biology · doi:10.1371/journal.pcbi.1007134 · Cited by 87 · see citing works

Fed-batch operational strategies for recombinant Fab production with Pichia pastoris using the constitutive GAP promoter

Garcia-Ortega, X., Ferrer, P., Montesinos, J. L., & Valero, F. (2013) · Biochemical Engineering Journal · doi:10.1016/j.bej.2013.07.013 · Cited by 79 · see citing works

Towards protein-based viral mimetics for cancer therapies

Unzueta, U., Céspedes, M. V., Vázquez, E., Ferrer‐Miralles, N., Mangues, R., & Villaverde, A. (2015) · Trends in biotechnology · doi:10.1016/j.tibtech.2015.02.007 · Cited by 78 · see citing works

Systems metabolic engineering, industrial biotechnology and microbial cell factories

Lee, S. Y., Mattanovich, D., & Villaverde, A. (2012) · Microbial Cell Factories · doi:10.1186/1475-2859-11-156 · Cited by 78 · see citing works

Ecology of cold environments: new insights of bacterial metabolic adaptation through an integrated genomic-phenomic approach

Mocali, S., Chiellini, C., Fabiani, A., Decuzzi, S., de Pascale, D., Parrilli, E., Tutino, M. L., Perrin, E., Bosi, E., Fondi, M., et al. (2017) · Scientific Reports · doi:10.1038/s41598-017-00876-4 · Cited by 75 · see citing works

BBB-targeting, protein-based nanomedicines for drug and nucleic acid delivery to the CNS

Peluffo, H., Unzueta, U., Negro‐Demontel, M. L., Xu, Z., Váquez, E., Ferrer‐Miralles, N., & Villaverde, A. (2015) · Biotechnology Advances · doi:10.1016/j.biotechadv.2015.02.004 · Cited by 76 · see citing works

Enabling Low Cost Biopharmaceuticals: A Systematic Approach to Delete Proteases from a Well-Known Protein Production Host Trichoderma reesei

Landowski, C. P., Huuskonen, A., Wahl, R., Westerholm‐Parvinen, A., Kanerva, A., Hänninen, A., Salovuori, N., Penttilä, M. E., Natunen, J., Ostermeier, C., et al. (2015) · PLoS ONE · doi:10.1371/journal.pone.0134723 · Cited by 76 · see citing works

Engineering protein self-assembling in protein-based nanomedicines for drug delivery and gene therapy

Ferrer-Miralles, N., Rodríguez‐Carmona, E., Corchero, J., García-Fruitós, E., Vázquez, E., & Villaverde, A. (2015) · Critical Reviews in Biotechnology · doi:10.3109/07388551.2013.833163 · Cited by 63 · see citing works

Rational development of bioprocess engineering strategies for recombinant protein production in Pichia pastoris (Komagataella phaffii) using the methanol-free GAP promoter. Where do we stand?

Garcia‐Ortega, X., Cámara, E., Ferrer, P., Albiol, J., Montesinos, J. L. G., & Valero, F. (2019) · New Biotechnology · doi:10.1016/j.nbt.2019.06.002 · Cited by 70 · see citing works

Integration and Validation of the Genome-Scale Metabolic Models of Pichia pastoris: A Comprehensive Update of Protein Glycosylation Pathways, Lipid and Energy Metabolism

Tomàs‐Gamisans, M., Ferrer, P., & Albiol, J. (2016) · PLoS ONE · doi:10.1371/journal.pone.0148031 · Cited by 68 · see citing works

Efficient Transient Expression of Recombinant Proteins Using DNA Viral Vectors in Freshwater Microalgal Species

Malla, A., Rosales‐Mendoza, S., Phoolcharoen, W., & Vimolmangkang, S. (2021) · Frontiers in Plant Science · doi:10.3389/fpls.2021.650820 · Cited by 67 · see citing works

Anti-biofilm activity of the Antarctic marine bacterium Pseudoalteromonas haloplanktis TAC125

Papa, R., Parrilli, E., Sannino, F., Barbato, G., Tutino, M. L., Artini, M., & Selan, L. (2013) · Research in Microbiology · doi:10.1016/j.resmic.2013.01.010 · Cited by 67 · see citing works

Pichia pastoris secretes recombinant proteins less efficiently than Chinese hamster ovary cells but allows higher space‐time yields for less complex proteins

Maccani, A., Landes, N., Stadlmayr, G., Maresch, D., Leitner, C., Maurer, M., Gasser, B., Ernst, W., Kunert, R., & Mattanovich, D. (2014) · Biotechnology Journal · doi:10.1002/biot.201300305 · Cited by 66 · see citing works

Unraveling the potential of non-conventional yeasts in biotechnology

Geijer, C., Ledesma‐Amaro, R., & Tomás‐Pejó, E. (2022) · FEMS Yeast Research · doi:10.1093/femsyr/foab071 · Cited by 64 · see citing works

Dynamic genome-scale metabolic modeling of the yeast Pichia pastoris

Saitua, F., Torres, P., Pérez‐Correa, J. R., & Agosin, E. E. (2017) · BMC Systems Biology · doi:10.1186/s12918-017-0408-2 · Cited by 62 · see citing works

Harnessing genetic engineering to drive economic bioproduct production in algae

Gupta, A., Kang, K., Pathania, R., Saxton, L., Saucedo, B., Malik, A., Torres-Tiji, Y., Diaz, C. J., Dutra Molino, J. V., & Mayfield, S. P. (2024) · Frontiers in Bioengineering and Biotechnology · doi:10.3389/fbioe.2024.1350722 · Cited by 60 · see citing works

Recombinant vaccines in 2022: a perspective from the cell factory

Favaro, M. T. D. P., Atienza-Garriga, J., Martínez-Torró, C., Parladé, E., Vázquez, E., Corchero, J. L., Ferrer‐Miralles, N., & Villaverde, A. (2022) · Microbial Cell Factories · doi:10.1186/s12934-022-01929-8 · Cited by 58 · see citing works

Comprehensive clone screening and evaluation of fed-batch strategies in a microbioreactor and lab scale stirred tank bioreactor system: application on Pichia pastoris producing Rhizopus oryzae lipase

Hemmerich, J., Adelantado, N., Barrigón, J. M., Ponte, X., Hörmann, A., Ferrer, P., Kensy, F., & Valero, F. (2014) · Microbial Cell Factories · doi:10.1186/1475-2859-13-36 · Cited by 57 · see citing works

Engineering Secretory Amyloids for Remote and Highly Selective Destruction of Metastatic Foci

Céspedes, M. V., Cano‐Garrido, O., Álamo, P., Sala, R., Gallardo, A., Serna, N., Falgàs, A., Voltà‐Durán, E., Casanova, I., Sánchez‐Chardi, A., et al. (2019) · Advanced Materials · doi:10.1002/adma.201907348 · Cited by 56 · see citing works

Production of functional inclusion bodies in endotoxin-free Escherichia coli

Rueda, F. L., Cano‐Garrido, O., Mamat, U., Wilke, K., Seras‐Franzoso, J., García‐Fruitós, E., & Villaverde, A. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-6008-9 · Cited by 54 · see citing works

Quantitative Metabolomics and Instationary 13C-Metabolic Flux Analysis Reveals Impact of Recombinant Protein Production on Trehalose and Energy Metabolism in Pichia pastoris

Jordà, J., Cueto-Rojas, H. F., Carnicer, M., Wahl, A., Ferrer, P., & Albiol, J. (2014) · Metabolites · doi:10.3390/metabo4020281 · Cited by 52 · see citing works

Familiar Stranger

Druzhinina, I. S., & Kubicek, C. P. (2016) · Advances in applied microbiology · doi:10.1016/bs.aambs.2016.02.001 · Cited by 52 · see citing works

Functional Protein Aggregates: Just the Tip of the Iceberg

Villaverde, A., Corchero, J. L., Seras‐Franzoso, J., & García‐Fruitós, E. (2015) · Nanomedicine · doi:10.2217/nnm.15.125 · Cited by 51 · see citing works

Genome‐scale metabolic reconstruction and constraint‐based modelling of the Antarctic bacterium P seudoalteromonas haloplanktis TAC 125

Fondi, M., Maida, I., Perrin, E., Mellera, A., Mocali, S., Parrilli, E., Tutino, M. L., Lió, P., & Fani, R. (2014) · Environmental Microbiology · doi:10.1111/1462-2920.12513 · Cited by 50 · see citing works

A rapid, modular and marker-free chloroplast expression system for the green alga Chlamydomonas reinhardtii

Bertalan, I., Munder, M. C., Weiß, C., Kopf, J., Fischer, D., & Johanningmeier, U. (2014) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2014.12.017 · Cited by 49 · see citing works

Going beyond the limit: Increasing global translation activity leads to increased productivity of recombinant secreted proteins in Pichia pastoris

Staudacher, J., Rebnegger, C., Dohnal, T., Landes, N., Mattanovich, D., & Gasser, B. (2022) · Metabolic Engineering · doi:10.1016/j.ymben.2022.01.010 · Cited by 47 · see citing works

Improved expression of single-chain antibodies in Ustilago maydis

Sarkari, P., Reindl, M., Stock, J., Müller, O., Kahmann, R., Feldbrügge, M., & Schipper, K. (2014) · Journal of Biotechnology · doi:10.1016/j.jbiotec.2014.06.028 · Cited by 44 · see citing works

Endophytic Yeasts: Biology and Applications

Doty, S. (2013) · Soil biology · doi:10.1007/978-3-642-39317-4_17 · Cited by 40 · see citing works

A brief overview on the application and sources of α‐amylase and expression hosts properties in order to production of recombinant α‐amylase

Movahedpour, A., Asadi, M., Khatami, S. H., Taheri‐Anganeh, M., Adelipour, M., Shabaninejad, Z., Ahmadi, N., Irajie, C., & Mousavi, P. (2021) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.2140 · Cited by 37 · see citing works

Biofabrication of functional protein nanoparticles through simple His-tag engineering

López‐Laguna, H., Sánchez, J. M., Carratalá, J. V., Rojas-Peña, M., Sánchez‐García, L., Parladé, E., Sánchez‐Chardi, A., Voltà‐Durán, E., Serna, N., Cano‐Garrido, O., et al. (2021) · ACS Sustainable Chemistry & Engineering · doi:10.1021/acssuschemeng.1c04256 · Cited by 37 · see citing works

Recombinant Protein Materials for Bioengineering and Nanomedicine

Corchero, J. L., Vázquez, E., García‐Fruitós, E., Ferrer‐Miralles, N., & Villaverde, A. (2014) · Nanomedicine · doi:10.2217/nnm.14.153 · Cited by 35 · see citing works

A novel synthetic medium and expression system for subzero growth and recombinant protein production in Pseudoalteromonas haloplanktis TAC125

Sannino, F., Giuliani, M., Salvatore, U., Apuzzo, G. A., de Pascale, D., Fani, R., Fondi, M., Marino, G., Tutino, M. L., & Parrilli, E. (2016) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-016-7942-5 · Cited by 35 · see citing works

Engineering the supply chain for protein production/secretion in yeasts and mammalian cells

Klein, T., Niklas, J., & Heinzle, E. (2015) · Journal of Industrial Microbiology & Biotechnology · doi:10.1007/s10295-014-1569-2 · Cited by 31 · see citing works

Expanding the recombinant protein quality in Lactococcus lactis

Cano‐Garrido, O., Rueda, F. L., Sánchez‐García, L., Ruíz-Ávila, L., Bosser, R., Villaverde, A., & García‐Fruitós, E. (2014) · Microbial Cell Factories · doi:10.1186/s12934-014-0167-3 · Cited by 31 · see citing works

Bioreactor-scale cell performance and protein production can be substantially increased by using a secretion signal that drives co-translational translocation in Pichia pastoris

Barrero, J. J., Pagazartaundua, A., Glick, B. S., Valero, F., & Ferrer, P. (2020) · New Biotechnology · doi:10.1016/j.nbt.2020.09.001 · Cited by 30 · see citing works

A Nanostructured Bacterial Bioscaffold for The Sustained Bottom-Up Delivery of Protein Drugs

Seras‐Franzoso, J., Peebo, K., Corchero, J. L., Tsimbouri, P. M., Unzueta, U., Rinas, U., Dalby, M. J., Vázquez, E., García‐Fruitós, E., & Villaverde, A. (2013) · Nanomedicine · doi:10.2217/nnm.12.188 · Cited by 30 · see citing works

Improving recombinant protein production in the Chlamydomonas reinhardtii chloroplast using vivid Verde Fluorescent Protein as a reporter

Braun‐Galleani, S., Baganz, F., & Purton, S. (2015) · Biotechnology Journal · doi:10.1002/biot.201400566 · Cited by 28 · see citing works

Deregulation of methanol metabolism reverts transcriptional limitations of recombinant Pichia pastoris ( Komagataella spp) with multiple expression cassettes under control of the AOX1 promoter

Cámara, E., Monforte, S., Albiol, J., & Ferrer, P. (2019) · Biotechnology and Bioengineering · doi:10.1002/bit.26947 · Cited by 27 · see citing works

A novel salt-inducible CrGPDH3 promoter of the microalga Chlamydomonas reinhardtii for transgene overexpression

Beltran-Aguilar, A. G., Peraza-Echeverría, S., López-Ochoa, L., Borges-Argáez, I. C., & Herrera-Valencia, V. A. (2019) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-019-09733-y · Cited by 27 · see citing works

Nanotechnology‐based approaches for treating lysosomal storage disorders, a focus on Fabry disease

Abasolo, I., Seras‐Franzoso, J., Moltó‐Abad, M., Díaz‐Riascos, V., Corchero, J. L., Pintos‐Morell, G., & Schwartz, S. (2020) · Wiley Interdisciplinary Reviews Nanomedicine and Nanobiotechnology · doi:10.1002/wnan.1684 · Cited by 27 · see citing works

Human recombinant lysosomal enzymes produced in microorganisms

Espejo-Mojica, A. J., Alméciga-Díaz, C. J., Rodríguez‐López, A., Mosquera, Á., Díaz, D., Beltrán, L., Díaz, S., Pimentel, N., Moreno, J., Sánchez, J., et al. (2015) · Molecular Genetics and Metabolism · doi:10.1016/j.ymgme.2015.06.001 · Cited by 27 · see citing works

Microbial Biofabrication for Nanomedicine: Biomaterials, Nanoparticles and Beyond

Vázquez, E., & Villaverde, A. (2013) · Nanomedicine · doi:10.2217/nnm.13.164 · Cited by 26 · see citing works

Production, secretion and purification of a correctly folded staphylococcal antigen in Lactococcus lactis

Samazan, F., Rokbi, B., Seguin, D., Telles, F., Gautier, V., Richarme, G., Chevret, D., Varela, P. F., Velours, C., & Poquet, I. (2015) · Microbial Cell Factories · doi:10.1186/s12934-015-0271-z · Cited by 24 · see citing works

Release of functional fibroblast growth factor-2 from artificial inclusion bodies

Serna, N., Cano‐Garrido, O., Sánchez, J. M., Sánchez‐Chardi, A., Sánchez‐García, L., López‐Laguna, H., Fernández, E., Vázquez, E., & Villaverde, A. (2020) · Journal of Controlled Release · doi:10.1016/j.jconrel.2020.08.007 · Cited by 24 · see citing works

Biosynthesis of protein-based drugs using eukaryotic microalgae

Xie, Z., He, J., Peng, S., Zhang, X., & Kong, W. (2023) · Algal Research · doi:10.1016/j.algal.2023.103219 · Cited by 20 · see citing works

Conformational and functional variants of CD44-targeted protein nanoparticles bio-produced in bacteria

Pesarrodona, M., Fernández, Y., Foradada, L., Sánchez‐Chardi, A., Conchillo‐Solé, O., Unzueta, U., Xu, Z., Roldán, M., Villegas, S., Ferrer‐Miralles, N., et al. (2016) · Biofabrication · doi:10.1088/1758-5090/8/2/025001 · Cited by 20 · see citing works

Towards a synthetic nuclear transcription system in green algae: Characterization of Chlamydomonas reinhardtii nuclear transcription factors and identification of targeted promoters

Anderson, M. S., Muff, T. J., Georgianna, D. R., & Mayfield, S. P. (2016) · Algal Research · doi:10.1016/j.algal.2016.12.002 · Cited by 20 · see citing works

Protein scaffolds in human clinics

Cano‐Garrido, O., Serna, N., Unzueta, U., Parladé, E., Mangues, R., Villaverde, A., & Vázquez, E. (2022) · Biotechnology Advances · doi:10.1016/j.biotechadv.2022.108032 · Cited by 20 · see citing works

Genomics and transcriptomics analysis reveals the mechanism of isobutanol tolerance of a laboratory evolved Lactococcus lactis strain

Gupta, J. A., Thapa, S., Verma, M., Som, R., & Mukherjee, K. J. (2020) · Scientific Reports · doi:10.1038/s41598-020-67635-w · Cited by 19 · see citing works

Sequential Release of Proteins from Structured Multishell Microcapsules

Shimanovich, U., Michaels, T. C. T., Genst, E. D., Matak‐Vinković, D., Dobson, C. M., & Knowles, T. P. J. (2017) · Biomacromolecules · doi:10.1021/acs.biomac.7b00351 · Cited by 19 · see citing works

Gene expression engineering in fungi

Mojžita, D., Rantasalo, A., & Jäntti, J. (2019) · Current Opinion in Biotechnology · doi:10.1016/j.copbio.2019.04.007 · Cited by 19 · see citing works

Structural and functional features of self-assembling protein nanoparticles produced in endotoxin-free Escherichia coli

Rueda, F. L., Céspedes, M. V., Sánchez‐Chardi, A., Seras‐Franzoso, J., Pesarrodona, M., Ferrer‐Miralles, N., Vázquez, E., Rinas, U., Unzueta, U., Mamat, U., et al. (2016) · Microbial Cell Factories · doi:10.1186/s12934-016-0457-z · Cited by 17 · see citing works

Modelling microbial metabolic rewiring during growth in a complex medium

Fondi, M., Bosi, E., Presta, L., Natoli, D., & Fani, R. (2016) · BMC Genomics · doi:10.1186/s12864-016-3311-0 · Cited by 17 · see citing works

A Stochastic Landscape Approach for Protein Folding State Classification

Faran, M., Ray, D., Nag, S., Raucci, U., Parrinello, M., & Bisker, G. (2024) · Journal of Chemical Theory and Computation · doi:10.1021/acs.jctc.4c00464 · Cited by 14 · see citing works

Genome-scale phylogenetic and DNA composition analyses of Antarctic Pseudoalteromonas bacteria reveal inconsistencies in current taxonomic affiliation

Bosi, E., Fondi, M., Maida, I., Perrin, E., de Pascale, D., Tutino, M. L., Parrilli, E., Giudice, A. L., Filloux, A., & Fani, R. (2015) · Hydrobiologia · doi:10.1007/s10750-015-2396-9 · Cited by 16 · see citing works

Recombinant production of a single-chain antibody fragment in Pseudoalteromonas haloplanktis TAC125

Giuliani, M., Parrilli, E., Sannino, F., Apuzzo, G. A., Marino, G., & Tutino, M. L. (2014) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-014-5582-1 · Cited by 16 · see citing works

Magnetic nanoparticle mediated-gene delivery for simpler and more effective transformation of Pichia pastoris

Arslan, Ş. Y., Solak, K., Acar, M., Mavi, A., & Ünver, Y. (2021) · Nanoscale Advances · doi:10.1039/d1na00079a · Cited by 15 · see citing works

Comparison of intracellular and secretion-based strategies for production of human α-galactosidase A in the filamentous fungus Trichoderma reesei

Smith, W., Jäntti, J., Oja, M., & Saloheimo, M. (2014) · BMC Biotechnology · doi:10.1186/s12896-014-0091-y · Cited by 15 · see citing works

Combined metabolic and enzymatic engineering for de novo biosynthesis of δ-tocotrienol in Yarrowia lipolytica

Xiang, J., Liu, M., Wang, X., Yue, M., Qin, Z., & Zhou, J. (2025) · Synthetic and Systems Biotechnology · doi:10.1016/j.synbio.2025.02.011 · Cited by 13 · see citing works

Development of a novel platform for recombinant protein production in Corynebacterium glutamicum on ethanol

Yu, X.-Y., Liu, X.-X., Gao, X., Luo, X.-X., Yang, Y.-K., Li, Y., Liu, C.-L., Zhang, C., & Bai, Z. (2022) · Synthetic and Systems Biotechnology · doi:10.1016/j.synbio.2022.03.004 · Cited by 12 · see citing works

Autoinduction as Means for Optimization of the Heterologous Expression of Recombinant Single-Chain Fv (scFv) Antibodies

Nikolova, G., Georgieva, Y., Atanasova, A., Radulova, G., Kapogianni, A., & Tsacheva, I. (2021) · Molecular Biotechnology · doi:10.1007/s12033-021-00363-2 · Cited by 12 · see citing works

Secretome-based screening of fusion partners and their application in recombinant protein secretion in Saccharomyces cerevisiae

Bae, J., Yun, S., Kim, M. J., Kim, H., Sung, B. H., Kim, S. I., & Sohn, J. (2021) · Applied Microbiology and Biotechnology · doi:10.1007/s00253-021-11750-9 · Cited by 12 · see citing works

Self-assembled calcium pyrophosphate nanostructures for targeted molecular delivery

Bassett, D. C., Robinson, T. E., Hill, R. J., Grover, L. M., & Barralet, J. E. (2022) · Biomaterials Advances · doi:10.1016/j.bioadv.2022.213086 · Cited by 12 · see citing works

Yeast Suspension Culture

Mattanovich, D., Jungo, C., Wenger, J., Dabros, M., & Maurer, M. (2014) · doi:10.1002/9783527683321.ch02 · Cited by 12 · see citing works

CXCR4 + -Targeted Protein Nanoparticles Produced in the Food-Grade Bacterium Lactococcus Lactis

Cano‐Garrido, O., Céspedes, M. V., Unzueta, U., Saccardo, P., Roldán, M., Sánchez‐Chardi, A., Cubarsí, R., Vázquez, E., Mangues, R., García‐Fruitós, E., et al. (2016) · Nanomedicine · doi:10.2217/nnm-2016-0200 · Cited by 11 · see citing works

Recombinant Proteins for Assembling as Nano- and Micro-Scale Materials for Drug Delivery: A Host Comparative Overview

Corchero, J. L., Favaro, M. T. D. P., Márquez-Martínez, M., Lascorz, J., Martínez-Torró, C., Sánchez, J. M., López‐Laguna, H., Ferreira, L. C. D. S., Vázquez, E., Ferrer‐Miralles, N., et al. (2023) · Pharmaceutics · doi:10.3390/pharmaceutics15041197 · Cited by 11 · see citing works

Thermostable α‐amylase immobilization: Enhanced stability and performance for starch biocatalysis

Kumar, G. S., Rather, G. M., Gurramkonda, C., & Reddy, B. R. (2015) · Biotechnology and Applied Biochemistry · doi:10.1002/bab.1350 · Cited by 11 · see citing works

Algae as Crop Plants Being a Source of Bioactive Ingredients of Pharmaceutical and Dietary Importance

Jabłońska‐Trypuć, A. (2024) · Agronomy · doi:10.3390/agronomy14050895 · Cited by 10 · see citing works

Noncanonical Amino Acid Incorporation in Animals and Animal Cells

Kim, J., Kim, Y., Cho, S., & Park, H. (2024) · Chemical Reviews · doi:10.1021/acs.chemrev.3c00955 · Cited by 11 · see citing works

Production of Recombinant Trichoderma reesei Cellobiohydrolase II in a New Expression System Based on Wickerhamomyces anomalus

Díaz‐Rincón, D. J., Duque, I., Osorio, E., Rodríguez‐López, A., Espejo-Mojica, A. J., Parra‐Giraldo, C. M., Poutou‐Piñales, R. A., Alméciga-Díaz, C. J., & Quevedo-Hidalgo, B. E. (2017) · Enzyme Research · doi:10.1155/2017/6980565 · Cited by 10 · see citing works

Precision fermentation of sustainable products in the food industry

Prasath, C. S. S., Sivadas, C. A., Chandran, C. H., & Suchithra, T. V. (2024) · Elsevier eBooks · doi:10.1016/b978-0-443-19049-0.00020-7 · Cited by 9 · see citing works

Heterologous Protein Expression in Pseudoalteromonas haloplanktis TAC125

Parrilli, E., & Tutino, M. L. (2017) · Springer eBooks · doi:10.1007/978-3-319-57057-0_21 · Cited by 9 · see citing works

Soluble Recombinant Protein Production in Pseudoalteromonas haloplanktis TAC125: The Case Study of the Full-Length Human CDKL5 Protein

Calvanese, M., Colarusso, A., Lauro, C., Parrilli, E., & Tutino, M. L. (2022) · Methods in molecular biology · doi:10.1007/978-1-0716-1859-2_13 · Cited by 9 · see citing works

Microalgae as a Vaccine Delivery System to Aquatic Organisms

Abidin, A. A. Z., Suntarajh, M., & Yusof, Z. N. B. (2020) · Springer eBooks · doi:10.1007/978-981-15-0169-2_10 · Cited by 8 · see citing works

An In Silico Methodology That Facilitates Decision Making in the Engineering of Nanoscale Protein Materials

Parladé, E., Voltà‐Durán, E., Cano‐Garrido, O., Sánchez, J. M., Unzueta, U., López‐Laguna, H., Serna, N., Cano, M., Rodríguez-Mariscal, M., Vázquez, E., et al. (2022) · International Journal of Molecular Sciences · doi:10.3390/ijms23094958 · Cited by 8 · see citing works

The Corn Smut Fungus Ustilago maydis as an Alternative Expression System for Biopharmaceuticals

Sarkari, P., Feldbrügge, M., & Schipper, K. (2016) · Fungal biology · doi:10.1007/978-3-319-27951-0_7 · Cited by 7 · see citing works

A Systems Biology View on Bacterial Response to Temperature Shift

Fondi, M., Bosi, E., Giudice, A. L., & Fani, R. (2016) · Grand challenges in biology and biotechnology · doi:10.1007/978-3-319-13521-2_21 · Cited by 7 · see citing works

Molecular engineering of a cryptic epitope in Spike RBD improves manufacturability and neutralizing breadth against SARS-CoV-2 variants

Rodriguez‐Aponte, S. A., Dalvie, N. C., Wong, T. Y., Johnston, R. S., Naranjo, C. A., Bajoria, S., Kumru, O. S., Kaur, K., Russ, B. P., Lee, K. S., et al. (2022) · Vaccine · doi:10.1016/j.vaccine.2022.12.062 · Cited by 7 · see citing works

Microbial protein cell factories fight back?

Rettenbacher, L. A., Arauzo-Aguilera, K., Buscajoni, L., Castillo-Corujo, A., Ferrero-Bordera, B., Kostopoulou, A., Moran-Torres, R., Núñez-Nepomuceno, D., Öktem, A., Palma, A., et al. (2021) · Trends in Biotechnology · doi:10.1016/j.tibtech.2021.10.003 · Cited by 59 · see citing works

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 · see citing works

Unveiling microbial and microalgal chassis for therapeutic and diagnostic protein expression

Bhandari, L., Kulkarni, S., & Prakash, G. (2026) · Biotechnology Progress · doi:10.1002/btpr.70098

Non-conventional expression systems for the production of vaccine proteins and immunotherapeutic molecules

Legastelois, I., Buffin, S., Peubez, I., Mignon, C., Sodoyer, R., & Werle, B. (2016) · Human Vaccines & Immunotherapeutics · doi:10.1080/21645515.2016.1260795 · Cited by 76 · see citing works

Towards a new avenue for producing therapeutic proteins: Microalgae as a tempting green biofactory

Dehghani, J., Adibkia, K., Movafeghi, A., Maleki, H., Saeedi, N., & Omidi, Y. (2019) · Biotechnology Advances · doi:10.1016/j.biotechadv.2019.107499 · Cited by 51 · see citing works