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Journal articles on the topic 'Heterologous expression'

Author: Grafiati

Published: 4 June 2021

Last updated: 26 July 2025

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1

Knox, Barry E., Ernesto Salcedo, Katherine Mathiesz, et al. "Heterologous Expression ofLimulusRhodopsin." Journal of Biological Chemistry 278, no. 42 (2003): 40493–502. http://dx.doi.org/10.1074/jbc.m304567200.

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2

Fricker, M. D., and K. J. Oparka. "using heterologous expression systems." Journal of Experimental Botany 50, Special_Issue (1999): 1089–100. http://dx.doi.org/10.1093/jxb/50.special_issue.1089.

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3

Zayed, A., and R. Ulber. "Heterologous Expression of Heteropolysaccharides." Chemie Ingenieur Technik 88, no. 9 (2016): 1399. http://dx.doi.org/10.1002/cite.201650230.

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4

Zheng, Xin, Wei Wei Fan, Ling Jian Meng, Shuang Shuang Li, Ying Ying Liu, and Ling Hua Zhang. "Efficient Expression of Mussel Adhesive Protein in Pichia pastoris GS115 Promoted by Ectoine." Advanced Materials Research 581-582 (October 2012): 1137–40. http://dx.doi.org/10.4028/www.scientific.net/amr.581-582.1137.

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Mussel adhesive protein has significant potential application in the field of medical adhesion. Genetic engineering method is gaining more and more attention, by which mussel adhesive protein can be heterologously expressed. In order to improve the expression efficiency of mussel adhesive protein with heterologous recombinant, it is reported that the compatible solutes Ectoine promoted to expression of adhesive protein on Pichia pastoris GS115. In this study, the adhesive protein gene msfp-1 from Mytilus sp. JHX-2002 was transformed into P. pastoris GS115. Inducement expression of adhesive pro

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5

Cameron, Caroline E., Janelle M. Y. Kuroiwa, Mitsunori Yamada, Teresa Francescutti, Bo Chi, and Howard K. Kuramitsu. "Heterologous Expression of the Treponema pallidum Laminin-Binding Adhesin Tp0751 in the Culturable Spirochete Treponema phagedenis." Journal of Bacteriology 190, no. 7 (2008): 2565–71. http://dx.doi.org/10.1128/jb.01537-07.

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ABSTRACT Treponema pallidum subsp. pallidum, the causative agent of syphilis, is an unculturable, genetically intractable bacterium. Here we report the use of the shuttle vector pKMR4PEMCS for the expression of a previously identified T. pallidum laminin-binding adhesin, Tp0751, in the nonadherent, culturable spirochete Treponema phagedenis. Heterologous expression of Tp0751 in T. phagedenis was confirmed via reverse transcriptase PCR analysis with tp0751 gene-specific primers and immunofluorescence analysis with Tp0751-specific antibodies; the latter assay verified the expression of the lamin

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6

Norkiene, Milda, and Alma Gedvilaite. "Influence of Codon Bias on Heterologous Production of Human Papillomavirus Type 16 Major Structural Protein L1 in Yeast." Scientific World Journal 2012 (2012): 1–6. http://dx.doi.org/10.1100/2012/979218.

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Heterologous gene expression is dependent on multistep processes involving regulation at the level of transcription, mRNA turnover, protein translation, and posttranslational modifications. Codon bias has a significant influence on protein yields. However, sometimes it is not clear which parameter causes observed differences in heterologous gene expression as codon adaptation typically optimizes many sequence properties at once. In the current study, we evaluated the influence of codon bias on heterologous production of human papillomavirus type 16 (HPV-16) major structural protein L1 in yeast

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Salmanian Tabasi, N., A. Gholizadeh, and B. Baghban Kohnehrouz. "Designing, docking and heterologous expression of an anti-HER2 affibody molecule." Ukrainian Biochemical Journal 90, no. 1 (2018): 68–76. http://dx.doi.org/10.15407/ubj90.01.068.

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8

Fazal, Asif, Divya Thankachan, Ellie Harris, and Ryan F. Seipke. "A chromatogram-simplified Streptomyces albus host for heterologous production of natural products." Antonie van Leeuwenhoek 113, no. 4 (2019): 511–20. http://dx.doi.org/10.1007/s10482-019-01360-x.

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AbstractCloning natural product biosynthetic gene clusters from cultured or uncultured sources and their subsequent expression by genetically tractable heterologous hosts is an essential strategy for the elucidation and characterisation of novel microbial natural products. The availability of suitable expression hosts is a critical aspect of this workflow. In this work, we mutagenised five endogenous biosynthetic gene clusters from Streptomyces albus S4, which reduced the complexity of chemical extracts generated from the strain and eliminated antifungal and antibacterial bioactivity. We showe

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9

Popova, Larissa G., Dmitrii E. Khramov, Olga I. Nedelyaeva, and Vadim S. Volkov. "Yeast Heterologous Expression Systems for the Study of Plant Membrane Proteins." International Journal of Molecular Sciences 24, no. 13 (2023): 10768. http://dx.doi.org/10.3390/ijms241310768.

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Researchers are often interested in proteins that are present in cells in small ratios compared to the total amount of proteins. These proteins include transcription factors, hormones and specific membrane proteins. However, sufficient amounts of well-purified protein preparations are required for functional and structural studies of these proteins, including the creation of artificial proteoliposomes and the growth of protein 2D and 3D crystals. This aim can be achieved by the expression of the target protein in a heterologous system. This review describes the applications of yeast heterologo

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10

Nagy, Katalin, Zita Kovács, Pál Salamon, Csongor-Kálmán Orbán, Szabolcs Lányi, and Beáta Albert. "Enhanced heterologous expression in E.coli." Studia Universitatis Babeș-Bolyai Chemia 64, no. 2 T1 (2019): 101–10. http://dx.doi.org/10.24193/subbchem.2019.2.09.

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11

Kurland, Charles, and Jonathan Gallant. "Errors of heterologous protein expression." Current Opinion in Biotechnology 7, no. 5 (1996): 489–93. http://dx.doi.org/10.1016/s0958-1669(96)80050-4.

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12

Santhosh, PK, Deng Yuhua, Gu Weidong, and Chen Xiaoguang. "Heterologous expression in transgenic mosquitoes." Asian Pacific Journal of Tropical Medicine 3, no. 3 (2010): 244–50. http://dx.doi.org/10.1016/s1995-7645(10)60019-3.

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13

Schenk, Gerhard, Ronald G. Duggleby, and Peter F. Nixon. "Heterologous expression of human transketolase." International Journal of Biochemistry & Cell Biology 30, no. 3 (1998): 369–78. http://dx.doi.org/10.1016/s1357-2725(97)00154-4.

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14

PELKONEN, O., H. RAUNIO, and P. SALONPAA. "Heterologous expression systems — current possibilities." Pharmacological Research 31 (1995): 170. http://dx.doi.org/10.1016/1043-6618(95)86940-9.

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15

Kingsman, Susan M., Alan J. Kingsman, Melanie J. Dobson, Jane Mellor, and Nicola A. Roberts. "Heterologous Gene Expression inSaccharomyces cerevisiae." Biotechnology and Genetic Engineering Reviews 3, no. 1 (1985): 377–416. http://dx.doi.org/10.1080/02648725.1985.10647819.

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16

Marchant, Jonathan S. "Heterologous Protein Expression in theXenopusOocyte." Cold Spring Harbor Protocols 2018, no. 4 (2017): pdb.prot096990. http://dx.doi.org/10.1101/pdb.prot096990.

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17

Steffensen, Lotte, and Per Amstrup Pedersen. "Heterologous Expression of Membrane and Soluble Proteins Derepresses GCN4 mRNA Translation in the Yeast Saccharomyces cerevisiae." Eukaryotic Cell 5, no. 2 (2006): 248–61. http://dx.doi.org/10.1128/ec.5.2.248-261.2006.

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ABSTRACT This paper describes the first physiological response at the translational level towards heterologous protein production in Saccharomyces cerevisiae. In yeast, the phosphorylation of eukaryotic initiation factor 2α (eIF-2α) by Gcn2p protein kinase mediates derepression of GCN4 mRNA translation. Gcn4p is a transcription factor initially found to be required for transcriptional induction of genes responsible for amino acid or purine biosynthesis. Using various GCN4-lacZ fusions, knockout yeast strains, and anti-eIF-2α-P/anti-eIF-2α antibodies, we observed that heterologous expression of

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18

Markina, N. M., A. A. Kotlobay, and A. S. Tsarkova. "Heterologous Metabolic Pathways: Strategies for Optimal Expression in Eukaryotic Hosts." Acta Naturae 12, no. 2 (2020): 28–39. http://dx.doi.org/10.32607/actanaturae.10966.

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Heterologous pathways are linked series of biochemical reactions occurring in a host organism after the introduction of foreign genes. Incorporation of metabolic pathways into host organisms is a major strategy used to increase the production of valuable secondary metabolites. Unfortunately, simple introduction of the pathway genes into the heterologous host in most cases does not result in successful heterologous expression. Extensive modification of heterologous genes and the corresponding enzymes on many different levels is required to achieve high target metabolite production rates. This r

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19

Markina, N. M., A. A. Kotlobay, and A. S. Tsarkova. "Heterologous Metabolic Pathways: Strategies for Optimal Expression in Eukaryotic Hosts." Acta Naturae 12, no. 2 (2020): 28–39. http://dx.doi.org/10.32607/actanaturae.11153.

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Heterologous pathways are linked series of biochemical reactions occurring in a host organism after the introduction of foreign genes. Incorporation of metabolic pathways into host organisms is a major strategy used to increase the production of valuable secondary metabolites. Unfortunately, simple introduction of the pathway genes into the heterologous host in most cases does not result in successful heterologous expression. Extensive modification of heterologous genes and the corresponding enzymes on many different levels is required to achieve high target metabolite production rates. This r

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20

Huo, Liujie, Joachim J. Hug, Chengzhang Fu, Xiaoying Bian, Youming Zhang, and Rolf Müller. "Heterologous expression of bacterial natural product biosynthetic pathways." Natural Product Reports 36, no. 10 (2019): 1412–36. http://dx.doi.org/10.1039/c8np00091c.

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The review highlights the 2013–2018 literature on the heterologous expression of bacterial natural product biosynthetic pathways and emphasises new techniques, heterologous hosts, and novel chemistry.

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21

Zhang, Hongyu, Zixuan Zhou, Tingting Lou, et al. "Advance in Heterologous Expression of Biomass-Degrading Auxiliary Activity 10 Family of Lytic Polysaccharide Monooxygenases." Fermentation 9, no. 9 (2023): 795. http://dx.doi.org/10.3390/fermentation9090795.

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AA10 family lytic polysaccharide monooxygenases (AA10 LPMOs) are mainly distributed in bacteria. Because of their characteristics of oxidative degradation of crystalline polysaccharides, such as cellulose and chitin, they have great application potential in industrial biomass conversion and have attracted wide attention. Efficient heterologous expression of LPMOs by recombinant engineering bacteria has become the main strategy for the industrial production of enzymes. The research progress of AA10 LPMOs’ heterologous expression systems was reviewed in this paper. The construction strategies of

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22

Fondi, Marco, Stefano Gonzi, Mikolaj Dziurzynski, et al. "Modelling hCDKL5 Heterologous Expression in Bacteria." Metabolites 11, no. 8 (2021): 491. http://dx.doi.org/10.3390/metabo11080491.

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hCDKL5 refers to the human cyclin-dependent kinase like 5 that is primarily expressed in the brain. Mutations in its coding sequence are often causative of hCDKL5 deficiency disorder, a devastating neurodevelopmental disorder currently lacking a cure. The large-scale recombinant production of hCDKL5 is desirable to boost the translation of preclinical therapeutic approaches into the clinic. However, this is hampered by the intrinsically disordered nature of almost two-thirds of the hCDKL5 sequence, making this region more susceptible to proteolytic attack, and the observed toxicity when the en

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23

Martínez-Alarcón, Dania, Alejandro Blanco-Labra, and Teresa García-Gasca. "Expression of Lectins in Heterologous Systems." International Journal of Molecular Sciences 19, no. 2 (2018): 616. http://dx.doi.org/10.3390/ijms19020616.

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24

Lilly, Mariska, Henri-Pierre Fierobe, Willem H. van Zyl, and Heinrich Volschenk. "Heterologous expression of aClostridiumminicellulosome inSaccharomyces cerevisiae." FEMS Yeast Research 9, no. 8 (2009): 1236–49. http://dx.doi.org/10.1111/j.1567-1364.2009.00564.x.

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25

Fujii, Isao. "Heterologous expression systems for polyketide synthases." Nat. Prod. Rep. 26, no. 2 (2009): 155–69. http://dx.doi.org/10.1039/b817092b.

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26

Spooner, R. K., K. M. A. G. Mahmoud, S. Deacon, and M. J. McPherson. "Heterologous expression hosts for galactose oxidase." Biochemical Society Transactions 28, no. 3 (2000): A71. http://dx.doi.org/10.1042/bst028a071b.

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27

Tuori, Robert P., Thomas J. Wolpert, and Lynda M. Ciuffetti. "Heterologous Expression of Functional Ptr ToxA." Molecular Plant-Microbe Interactions® 13, no. 4 (2000): 456–64. http://dx.doi.org/10.1094/mpmi.2000.13.4.456.

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Ptr ToxA, a proteinaceous host-selective toxin (HST) produced by the fungus Pyrenophora tritici-repentis, was expressed in Escherichia coli and purified as a polyhistidine-tagged, fusion protein (NC-FP). NC-FP, consisting of both the N and C domains of the ToxA open reading frame (ORF), is produced as an insoluble protein in E. coli at approximately 10 to 16 mg per liter of culture. Following in vitro refolding, NC-FP elicits cultivar-specific necrosis in wheat, with a specific activity similar to that of native Ptr ToxA. A fusion protein consisting of only the C domain has approximately 10 to

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28

Gustafsson, Claes, Sridhar Govindarajan, and Jeremy Minshull. "Codon bias and heterologous protein expression." Trends in Biotechnology 22, no. 7 (2004): 346–53. http://dx.doi.org/10.1016/j.tibtech.2004.04.006.

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29

Nevalainen, K. M. Helena, Valentino S. J. Te'o, and Peter L. Bergquist. "Heterologous protein expression in filamentous fungi." Trends in Biotechnology 23, no. 9 (2005): 468–74. http://dx.doi.org/10.1016/j.tibtech.2005.06.002.

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30

Binnie, Craig, J. Douglas Cossar, and Donald I. H. Stewart. "Heterologous biopharmaceutical protein expression in Streptomyces." Trends in Biotechnology 15, no. 8 (1997): 315–20. http://dx.doi.org/10.1016/s0167-7799(97)01062-7.

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31

SAUNDERS, G. "Heterologous gene expression in filamentous fungi." Trends in Biotechnology 7, no. 10 (1989): 283–87. http://dx.doi.org/10.1016/0167-7799(89)90048-6.

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32

Devchand, Medha, and David I. Gwynne. "Expression of heterologous proteins in Aspergillus." Journal of Biotechnology 17, no. 1 (1991): 3–9. http://dx.doi.org/10.1016/0168-1656(91)90022-n.

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33

Dziga, Dariusz, Benedykt Wladyka, Gabriela Zielińska, Jussi Meriluoto, and Marcin Wasylewski. "Heterologous expression and characterisation of microcystinase." Toxicon 59, no. 5 (2012): 578–86. http://dx.doi.org/10.1016/j.toxicon.2012.01.001.

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34

Zwick, Friederike, Rahmi Lale, and Svein Valla. "Combinatorial engineering for heterologous gene expression." Bioengineered 4, no. 6 (2013): 431–34. http://dx.doi.org/10.4161/bioe.24703.

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35

Crossman, L. C., J. W. B. Moir, J. J. Enticknap, D. J. Richardson, and S. Spiro. "Heterologous expression of heterotrophic nitrification genes." Microbiology 143, no. 12 (1997): 3775–83. http://dx.doi.org/10.1099/00221287-143-12-3775.

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36

Keniya, Mikhail V., Richard D. Cannon, ẤnBình Nguyễn, Joel D. A. Tyndall, and Brian C. Monk. "Heterologous expression ofCandida albicansPma1p inSaccharomyces cerevisiae." FEMS Yeast Research 13, no. 3 (2013): 302–11. http://dx.doi.org/10.1111/1567-1364.12035.

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37

Glick, Bernard R. "Metabolic load and heterologous gene expression." Biotechnology Advances 13, no. 2 (1995): 247–61. http://dx.doi.org/10.1016/0734-9750(95)00004-a.

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38

Smith, C. Jeffrey, Marc B. Rogers, and Marian L. Mckee. "Heterologous gene expression in Bacteroides fragilis." Plasmid 27, no. 2 (1992): 141–54. http://dx.doi.org/10.1016/0147-619x(92)90014-2.

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39

Dickschat, Jeroen S., Jan Rinkel, Patrick Rabe, Arman Beyraghdar Kashkooli, and Harro J. Bouwmeester. "18-Hydroxydolabella-3,7-diene synthase – a diterpene synthase from Chitinophaga pinensis." Beilstein Journal of Organic Chemistry 13 (August 23, 2017): 1770–80. http://dx.doi.org/10.3762/bjoc.13.171.

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The product obtained in vitro from a diterpene synthase encoded in the genome of the bacterium Chitinophaga pinensis, an enzyme previously reported to have germacrene A synthase activity during heterologous expression in Escherichia coli, was identified by extensive NMR-spectroscopic methods as 18-hydroxydolabella-3,7-diene. The absolute configuration of this diterpene alcohol and the stereochemical course of the terpene synthase reaction were addressed by isotopic labelling experiments. Heterologous expression of the diterpene synthase in Nicotiana benthamiana resulted in the production of 18

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40

Katoch, Meenu, Rabia Mazmouz, Rocky Chau, Leanne A. Pearson, Russell Pickford, and Brett A. Neilan. "Heterologous Production of Cyanobacterial Mycosporine-Like Amino Acids Mycosporine-Ornithine and Mycosporine-Lysine in Escherichia coli." Applied and Environmental Microbiology 82, no. 20 (2016): 6167–73. http://dx.doi.org/10.1128/aem.01632-16.

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ABSTRACTMycosporine-like amino acids (MAAs) are an important class of secondary metabolites known for their protection against UV radiation and other stress factors. Cyanobacteria produce a variety of MAAs, including shinorine, the active ingredient in many sunscreen creams. Bioinformatic analysis of the genome of the soil-dwelling cyanobacteriumCylindrospermum stagnalePCC 7417 revealed a new gene cluster with homology to MAA synthase fromNostoc punctiforme. This newly identified gene cluster is unusual because it has five biosynthesis genes (mylAtomylE), compared to the four found in other MA

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41

Gladilina, Yu A., A. N. Shishparenok, and D. D. Zhdanov. "Approaches for improving L-asparaginase expression in heterologous systems." Biomeditsinskaya Khimiya 69, no. 1 (2023): 19–38. http://dx.doi.org/10.18097/pbmc20236901019.

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L-asparaginase (EC 3.5.1.1) is one of the most demanded enzymes used in the pharmaceutical industry as a drug and in the food industry to prevent the formation of toxic acrylamide. Researchers aimed to improve specific activity and reduce side effects to create safer and more potent enzyme products. However, protein modifications and heterologous expression remain problematic in the production of asparaginases from different species. Heterologous expression in optimized producer strains is rationally organized; therefore, modified and heterologous protein expression is enhanced, which is the m

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42

Morlino, Giovanni B., Lorenza Tizzani, Reinhard Fleer, Laura Frontali, and Michele M. Bianchi. "Inducible Amplification of Gene Copy Number and Heterologous Protein Production in the Yeast Kluyveromyces lactis." Applied and Environmental Microbiology 65, no. 11 (1999): 4808–13. http://dx.doi.org/10.1128/aem.65.11.4808-4813.1999.

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ABSTRACT Heterologous protein production can be doubled by increasing the copy number of the corresponding heterologous gene. We constructed a host-vector system in the yeast Kluyveromyces lactis that was able to induce copy number amplification of pKD1 plasmid-based vectors upon expression of an integrated copy of the plasmid recombinase gene. We increased the production and secretion of two heterologous proteins, glucoamylase from the yeast Arxula adeninivorans and mammalian interleukin-1β, following gene dosage amplification when the heterologous genes were carried by pKD1-based vectors. Th

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43

Fukutani, Yosuke, Yuko Nakamura, Nonoko Muto, et al. "Hot Spot Mutagenesis Improves the Functional Expression of Unique Mammalian Odorant Receptors." International Journal of Molecular Sciences 23, no. 1 (2021): 277. http://dx.doi.org/10.3390/ijms23010277.

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Vertebrate animals detect odors through olfactory receptors (ORs), members of the G protein-coupled receptor (GPCR) family. Due to the difficulty in the heterologous expression of ORs, studies of their odor molecule recognition mechanisms have progressed poorly. Functional expression of most ORs in heterologous cells requires the co-expression of their chaperone proteins, receptor transporting proteins (RTPs). Yet, some ORs were found to be functionally expressed without the support of RTP (RTP-independent ORs). In this study, we investigated whether amino acid residues highly conserved among

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44

Awakawa, Takayoshi, and Ikuro Abe. "Reconstitution of Polyketide-Derived Meroterpenoid Biosynthetic Pathway in Aspergillus oryzae." Journal of Fungi 7, no. 6 (2021): 486. http://dx.doi.org/10.3390/jof7060486.

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The heterologous gene expression system with Aspergillus oryzae as the host is an effective method to investigate fungal secondary metabolite biosynthetic pathways for reconstruction to produce un-natural molecules due to its high productivity and genetic tractability. In this review, we focus on biosynthetic studies of fungal polyketide-derived meroterpenoids, a group of bioactive natural products, by means of the A. oryzae heterologous expression system. The heterologous expression methods and the biosynthetic reactions are described in detail for future prospects to create un-natural molecu

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45

Wu, Shuyan, David Hooks, and Gale Brightwell. "Current Understanding on the Heterogenous Expression of Plastic Depolymerising Enzymes in Pichia pastoris." Bioengineering 12, no. 1 (2025): 68. https://doi.org/10.3390/bioengineering12010068.

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Enzymatic depolymerisation is increasingly recognised as a reliable and environmentally friendly method. The development of this technology hinges on the availability of high-quality enzymes and associated bioreaction systems for upscaling biodegradation. Microbial heterologous expression systems have been studied for meeting this demand. Among these systems, the Pichia pastoris expression system has emerged as a widely used platform for producing secreted heterologous proteins. This article provides an overview of studies involving the recombinant expression of polymer-degrading enzymes using

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46

Stevens, D. Cole, Michael R. Henry, Kimberly A. Murphy, and Christopher N. Boddy. "Heterologous Expression of the Oxytetracycline Biosynthetic Pathway in Myxococcus xanthus." Applied and Environmental Microbiology 76, no. 8 (2010): 2681–83. http://dx.doi.org/10.1128/aem.02841-09.

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ABSTRACT New natural products for drug discovery may be accessed by heterologous expression of bacterial biosynthetic pathways in metagenomic DNA libraries. However, a “universal” host is needed for this experiment. Herein, we show that Myxococcus xanthus is a potential “universal” host for heterologous expression of polyketide biosynthetic gene clusters.

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47

Xu, Yushan, Xinhua Du, Xionghui Yu, et al. "Recent Advances in the Heterologous Expression of Biosynthetic Gene Clusters for Marine Natural Products." Marine Drugs 20, no. 6 (2022): 341. http://dx.doi.org/10.3390/md20060341.

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Marine natural products (MNPs) are an important source of biologically active metabolites, particularly for therapeutic agent development after terrestrial plants and nonmarine microorganisms. Sequencing technologies have revealed that the number of biosynthetic gene clusters (BGCs) in marine microorganisms and the marine environment is much higher than expected. Unfortunately, the majority of them are silent or only weakly expressed under traditional laboratory culture conditions. Furthermore, the large proportion of marine microorganisms are either uncultivable or cannot be genetically manip

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48

Borschevskaya, L. N., T. V. Feday, A. A. Tkachenko, and S. P. Sineoky. "The Expression Potential of New Yeast Strains of the Komagataella Genus." Biotekhnologiya 37, no. 4 (2021): 5–13. http://dx.doi.org/10.21519/0234-2758-2021-37-4-5-13.

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The expression potential of various strains from the Collection of the National Bio-Resource Center (BRC VKPM) collection belonging to the species Komagataella kurtzmanii, K. phaffii, K. mondaviorum has been assessed by the level of production of the heterologous enzyme Citrobacter freundii phytase. Heterologous expression in the K. mondaviorum strains was observed for the first time. The strains of K. phaffii Y-4288, K. mondaviorum Y-4331 and K. phaffii Y-4287 were identified with a high level production of the heterologous enzyme, a high growth rate, the ability to accumulate a large amount

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49

Kruszewska, J. S. "Heterologous expression of genes in filamentous fungi." Acta Biochimica Polonica 46, no. 1 (1999): 181–95. http://dx.doi.org/10.18388/abp.1999_4196.

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Isolation of some biologically important proteins from natural sources was found to be too expensive or scarcely possible (human proteins). The problem could be solved by expression of heterologous genes. Many biologically active proteins have been successfully expressed in filamentous fungi, some of them, however, at a low level. Thus, improvement of this technique appears to be a very important task. The process comprises several steps. Some of them, such as efficient transformation, vector construction, processing of signal sequences, post-translational modifications and secretion of the ex

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50

Kashi, Lila, Katharina Yandrofski, Renae J. Preston, et al. "Heterologous recombinant expression of non-originator NISTmAb." mAbs 10, no. 6 (2018): 922–33. http://dx.doi.org/10.1080/19420862.2018.1486355.

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