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Volumn 48, Issue , 2017, Pages 77-84

Exploring the potential of Saccharomyces cerevisiae for biopharmaceutical protein production

Author keywords

[No Author keywords available]

Indexed keywords

BIOLOGY; FUNCTIONS; MACHINERY; METABOLIC ENGINEERING; RECOMBINANT PROTEINS; THROUGHPUT; YEAST;

EID: 85017308782     PISSN: 09581669     EISSN: 18790429     Source Type: Journal    
DOI: 10.1016/j.copbio.2017.03.017     Document Type: Review
Times cited : (83)

References (53)
  • 1
    • 85017299934 scopus 로고    scopus 로고
    • Global biopharmaceuticals market growth, trends & forecasts
    • (2016–2021).
    • 1 Intelligence M: Global biopharmaceuticals market growth, trends & forecasts (2016–2021). 2016. https://www.mordorintelligence.com/industry-reports/global-biopharmaceuticals-market-industry.
    • (2016)
    • Intelligence, M.1
  • 2
    • 84920502297 scopus 로고    scopus 로고
    • Biopharmaceutical benchmarks 2014
    • A systematic report on the recombinant biologics approved from January 2010 to July 2014.
    • 2• Walsh, G., Biopharmaceutical benchmarks 2014. Nat. Biotechnol. 32 (2014), 992–1000 A systematic report on the recombinant biologics approved from January 2010 to July 2014.
    • (2014) Nat. Biotechnol. , vol.32 , pp. 992-1000
    • Walsh, G.1
  • 3
    • 8344271025 scopus 로고    scopus 로고
    • Advances in the production of human therapeutic proteins in yeasts and filamentous fungi
    • 3 Gerngross, T.U., Advances in the production of human therapeutic proteins in yeasts and filamentous fungi. Nat. Biotechnol. 22 (2004), 1409–1414.
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1409-1414
    • Gerngross, T.U.1
  • 4
    • 84877131240 scopus 로고    scopus 로고
    • Production of biopharmaceutical proteins by yeast: advances through metabolic engineering
    • 4 Nielsen, J., Production of biopharmaceutical proteins by yeast: advances through metabolic engineering. Bioengineered 4 (2013), 207–211.
    • (2013) Bioengineered , vol.4 , pp. 207-211
    • Nielsen, J.1
  • 6
    • 84870946443 scopus 로고    scopus 로고
    • A bacterial glycosidase enables mannose-6-phosphate modification and improved cellular uptake of yeast-produced recombinant human lysosomal enzymes
    • 6 Tiels, P., Baranova, E., Piens, K., De Visscher, C., Pynaert, G., Nerinckx, W., Stout, J., Fudalej, F., Hulpiau, P., Tannler, S., et al. A bacterial glycosidase enables mannose-6-phosphate modification and improved cellular uptake of yeast-produced recombinant human lysosomal enzymes. Nat. Biotechnol. 30 (2012), 1225–1231.
    • (2012) Nat. Biotechnol. , vol.30 , pp. 1225-1231
    • Tiels, P.1    Baranova, E.2    Piens, K.3    De Visscher, C.4    Pynaert, G.5    Nerinckx, W.6    Stout, J.7    Fudalej, F.8    Hulpiau, P.9    Tannler, S.10
  • 8
    • 84877156944 scopus 로고    scopus 로고
    • Cells and cell lysates: a direct approach for engineering antibodies against membrane proteins using yeast surface display
    • 8 Tillotson, B.J., Cho, Y.K., Shusta, E.V., Cells and cell lysates: a direct approach for engineering antibodies against membrane proteins using yeast surface display. Methods 60 (2013), 27–37.
    • (2013) Methods , vol.60 , pp. 27-37
    • Tillotson, B.J.1    Cho, Y.K.2    Shusta, E.V.3
  • 9
    • 84978645964 scopus 로고    scopus 로고
    • Production, purification and characterization of recombinant human antithrombin III by Saccharomyces cerevisiae
    • 9 Mallu, M.R., Vemula, S., Ronda, S.R., Production, purification and characterization of recombinant human antithrombin III by Saccharomyces cerevisiae. Electron. J. Biotechnol. 22 (2016), 81–89.
    • (2016) Electron. J. Biotechnol. , vol.22 , pp. 81-89
    • Mallu, M.R.1    Vemula, S.2    Ronda, S.R.3
  • 10
    • 84911398453 scopus 로고    scopus 로고
    • Engineering the oxygen sensing regulation results in an enhanced recombinant human hemoglobin production by Saccharomyces cerevisiae
    • 10 Martinez, J.L., Liu, L., Petranovic, D., Nielsen, J., Engineering the oxygen sensing regulation results in an enhanced recombinant human hemoglobin production by Saccharomyces cerevisiae. Biotechnol. Bioeng. 112 (2015), 181–188.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 181-188
    • Martinez, J.L.1    Liu, L.2    Petranovic, D.3    Nielsen, J.4
  • 12
    • 84861799596 scopus 로고    scopus 로고
    • Expression, purification and characterization of recombinant human interleukin-2-serum albumin (rhIL-2-HSA) fusion protein in Pichia pastoris
    • 12 Lei, J.Y., Guan, B., Li, B., Duan, Z.Y., Chen, Y., Li, H.Z., Jin, J., Expression, purification and characterization of recombinant human interleukin-2-serum albumin (rhIL-2-HSA) fusion protein in Pichia pastoris. Protein Expr. Purif. 84 (2012), 154–160.
    • (2012) Protein Expr. Purif. , vol.84 , pp. 154-160
    • Lei, J.Y.1    Guan, B.2    Li, B.3    Duan, Z.Y.4    Chen, Y.5    Li, H.Z.6    Jin, J.7
  • 13
    • 85017305146 scopus 로고    scopus 로고
    • High-level secretory expression, purification, and characterization of an anti-human Her II monoclonal antibody, trastuzumab, in the methylotrophic yeast Pichia pastoris
    • 13 Shibui, T., Bando, K., Misawa, S., High-level secretory expression, purification, and characterization of an anti-human Her II monoclonal antibody, trastuzumab, in the methylotrophic yeast Pichia pastoris. Adv. Biosci. Biotechnol. 4 (2013), 640–646.
    • (2013) Adv. Biosci. Biotechnol. , vol.4 , pp. 640-646
    • Shibui, T.1    Bando, K.2    Misawa, S.3
  • 14
    • 84855212712 scopus 로고    scopus 로고
    • Optimization of erythropoietin production with controlled glycosylation-PEGylated erythropoietin produced in glycoengineered Pichia pastoris
    • 14 Nett, J.H., Gomathinayagam, S., Hamilton, S.R., Gong, B., Davidson, R.C., Du, M., Hopkins, D., Mitchell, T., Mallem, M.R., Nylen, A., et al. Optimization of erythropoietin production with controlled glycosylation-PEGylated erythropoietin produced in glycoengineered Pichia pastoris. J. Biotechnol. 157 (2012), 198–206.
    • (2012) J. Biotechnol. , vol.157 , pp. 198-206
    • Nett, J.H.1    Gomathinayagam, S.2    Hamilton, S.R.3    Gong, B.4    Davidson, R.C.5    Du, M.6    Hopkins, D.7    Mitchell, T.8    Mallem, M.R.9    Nylen, A.10
  • 15
    • 84978229862 scopus 로고    scopus 로고
    • The vitamin-sensitive promoter PTHI11 enables pre-defined autonomous induction of recombinant protein production in Pichia pastoris
    • 15 Landes, N., Gasser, B., Vorauer-Uhl, K., Lhota, G., Mattanovich, D., Maurer, M., The vitamin-sensitive promoter PTHI11 enables pre-defined autonomous induction of recombinant protein production in Pichia pastoris. Biotechnol. Bioeng. 113 (2016), 2633–2643.
    • (2016) Biotechnol. Bioeng. , vol.113 , pp. 2633-2643
    • Landes, N.1    Gasser, B.2    Vorauer-Uhl, K.3    Lhota, G.4    Mattanovich, D.5    Maurer, M.6
  • 16
    • 84863629890 scopus 로고    scopus 로고
    • Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae
    • 16 Hou, J., Tyo, K.E., Liu, Z., Petranovic, D., Nielsen, J., Metabolic engineering of recombinant protein secretion by Saccharomyces cerevisiae. FEMS Yeast Res. 12 (2012), 491–510.
    • (2012) FEMS Yeast Res. , vol.12 , pp. 491-510
    • Hou, J.1    Tyo, K.E.2    Liu, Z.3    Petranovic, D.4    Nielsen, J.5
  • 17
    • 84863610089 scopus 로고    scopus 로고
    • Enhancing the copy number of episomal plasmids in Saccharomyces cerevisiae for improved protein production
    • 17 Chen, Y., Partow, S., Scalcinati, G., Siewers, V., Nielsen, J., Enhancing the copy number of episomal plasmids in Saccharomyces cerevisiae for improved protein production. FEMS Yeast Res. 12 (2012), 598–607.
    • (2012) FEMS Yeast Res. , vol.12 , pp. 598-607
    • Chen, Y.1    Partow, S.2    Scalcinati, G.3    Siewers, V.4    Nielsen, J.5
  • 18
    • 84862807811 scopus 로고    scopus 로고
    • Different expression systems for production of recombinant proteins in Saccharomyces cerevisiae
    • This study systematically evaluates factors influencing recombinant protein secretion, including protein type, expression vector and leader peptide, and demonstrates a generally applicable strategy for initial optimization of key factors for rational engineering cell factory for novel proteins.
    • 18•• Liu, Z., Tyo, K.E., Martinez, J.L., Petranovic, D., Nielsen, J., Different expression systems for production of recombinant proteins in Saccharomyces cerevisiae. Biotechnol. Bioeng. 109 (2012), 1259–1268 This study systematically evaluates factors influencing recombinant protein secretion, including protein type, expression vector and leader peptide, and demonstrates a generally applicable strategy for initial optimization of key factors for rational engineering cell factory for novel proteins.
    • (2012) Biotechnol. Bioeng. , vol.109 , pp. 1259-1268
    • Liu, Z.1    Tyo, K.E.2    Martinez, J.L.3    Petranovic, D.4    Nielsen, J.5
  • 19
    • 84989940494 scopus 로고    scopus 로고
    • A new set of rDNA-NTS-based multiple integrative cassettes for the development of antibiotic-marker-free recombinant yeasts
    • 19 Moon, H.Y., Lee, D.W., Sim, G.H., Kim, H.J., Hwang, J.Y., Kwon, M.G., Kang, B.K., Kim, J.M., Kang, H.A., A new set of rDNA-NTS-based multiple integrative cassettes for the development of antibiotic-marker-free recombinant yeasts. J. Biotechnol. 233 (2016), 190–199.
    • (2016) J. Biotechnol. , vol.233 , pp. 190-199
    • Moon, H.Y.1    Lee, D.W.2    Sim, G.H.3    Kim, H.J.4    Hwang, J.Y.5    Kwon, M.G.6    Kang, B.K.7    Kim, J.M.8    Kang, H.A.9
  • 21
    • 84947279264 scopus 로고    scopus 로고
    • A highly efficient single-step, markerless strategy for multi-copy chromosomal integration of large biochemical pathways in Saccharomyces cerevisiae
    • 21 Shi, S., Liang, Y., Zhang, M.M., Ang, E.L., Zhao, H., A highly efficient single-step, markerless strategy for multi-copy chromosomal integration of large biochemical pathways in Saccharomyces cerevisiae. Metab. Eng. 33 (2016), 19–27.
    • (2016) Metab. Eng. , vol.33 , pp. 19-27
    • Shi, S.1    Liang, Y.2    Zhang, M.M.3    Ang, E.L.4    Zhao, H.5
  • 23
    • 68149137106 scopus 로고    scopus 로고
    • Directed evolution of a secretory leader for the improved expression of heterologous proteins and full-length antibodies in Saccharomyces cerevisiae
    • 23 Rakestraw, J.A., Sazinsky, S.L., Piatesi, A., Antipov, E., Wittrup, K.D., Directed evolution of a secretory leader for the improved expression of heterologous proteins and full-length antibodies in Saccharomyces cerevisiae. Biotechnol. Bioeng. 103 (2009), 1192–1201.
    • (2009) Biotechnol. Bioeng. , vol.103 , pp. 1192-1201
    • Rakestraw, J.A.1    Sazinsky, S.L.2    Piatesi, A.3    Antipov, E.4    Wittrup, K.D.5
  • 24
    • 85017303021 scopus 로고    scopus 로고
    • Method for producing heterologous protein using yeast with disruption of VPS gene
    • EP Patent, EP2684948 A1.
    • 24 Nishiyama T, Sakai Y: Method for producing heterologous protein using yeast with disruption of VPS gene. EP Patent 2015, EP2684948 A1.
    • Nishiyama, T.1    Sakai, Y.2
  • 25
    • 84920063141 scopus 로고    scopus 로고
    • Blocking endocytotic mechanisms to improve heterologous protein titers in Saccharomyces cerevisiae
    • 25 Rodriguez-Limas, W.A., Tannenbaum, V., Tyo, K.E., Blocking endocytotic mechanisms to improve heterologous protein titers in Saccharomyces cerevisiae. Biotechnol. Bioeng. 112 (2015), 376–385.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 376-385
    • Rodriguez-Limas, W.A.1    Tannenbaum, V.2    Tyo, K.E.3
  • 26
    • 84876676018 scopus 로고    scopus 로고
    • Heat shock response improves heterologous protein secretion in Saccharomyces cerevisiae
    • 26 Hou, J., Osterlund, T., Liu, Z., Petranovic, D., Nielsen, J., Heat shock response improves heterologous protein secretion in Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 97 (2013), 3559–3568.
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 3559-3568
    • Hou, J.1    Osterlund, T.2    Liu, Z.3    Petranovic, D.4    Nielsen, J.5
  • 27
    • 84909983203 scopus 로고    scopus 로고
    • Multivariate modular engineering of the protein secretory pathway for production of heterologous glucose oxidase in Pichia pastoris
    • 27 Gu, L., Zhang, J., Du, G., Chen, J., Multivariate modular engineering of the protein secretory pathway for production of heterologous glucose oxidase in Pichia pastoris. Enzyme Microb. Technol. 68 (2015), 33–42.
    • (2015) Enzyme Microb. Technol. , vol.68 , pp. 33-42
    • Gu, L.1    Zhang, J.2    Du, G.3    Chen, J.4
  • 28
    • 84937737494 scopus 로고    scopus 로고
    • Engineering protein folding and translocation improves heterologous protein secretion in Saccharomyces cerevisiae
    • This study demonstrates combinatorial strengthening of protein folding and translocation important for heterologous protein production in  S. cerevisiae.
    • 28• Tang, H., Bao, X., Shen, Y., Song, M., Wang, S., Wang, C., Hou, J., Engineering protein folding and translocation improves heterologous protein secretion in Saccharomyces cerevisiae. Biotechnol. Bioeng. 112 (2015), 1872–1882 This study demonstrates combinatorial strengthening of protein folding and translocation important for heterologous protein production in  S. cerevisiae.
    • (2015) Biotechnol. Bioeng. , vol.112 , pp. 1872-1882
    • Tang, H.1    Bao, X.2    Shen, Y.3    Song, M.4    Wang, S.5    Wang, C.6    Hou, J.7
  • 29
    • 84952989800 scopus 로고    scopus 로고
    • Overexpression of native Saccharomyces cerevisiae ER-to-Golgi SNARE genes increased heterologous cellulase secretion
    • 29 Van Zyl, J.H., Den Haan, R., Van Zyl, W.H., Overexpression of native Saccharomyces cerevisiae ER-to-Golgi SNARE genes increased heterologous cellulase secretion. Appl. Microbiol. Biotechnol. 100 (2016), 505–518.
    • (2016) Appl. Microbiol. Biotechnol. , vol.100 , pp. 505-518
    • Van Zyl, J.H.1    Den Haan, R.2    Van Zyl, W.H.3
  • 30
    • 84862781268 scopus 로고    scopus 로고
    • Engineering of vesicle trafficking improves heterologous protein secretion in Saccharomyces cerevisiae
    • 30 Hou, J., Tyo, K., Liu, Z., Petranovic, D., Nielsen, J., Engineering of vesicle trafficking improves heterologous protein secretion in Saccharomyces cerevisiae. Metab. Eng. 14 (2012), 120–127.
    • (2012) Metab. Eng. , vol.14 , pp. 120-127
    • Hou, J.1    Tyo, K.2    Liu, Z.3    Petranovic, D.4    Nielsen, J.5
  • 31
    • 84879345901 scopus 로고    scopus 로고
    • Rate-limiting steps in yeast protein translation
    • The authors establish a detailed computational model based on sequencing data and identify the fast initiation or high codon bias important for protein yield of a transgene in  S. cerevisiae.
    • 31• Shah, P., Ding, Y., Niemczyk, M., Kudla, G., Plotkin, J.B., Rate-limiting steps in yeast protein translation. Cell 153 (2013), 1589–1601 The authors establish a detailed computational model based on sequencing data and identify the fast initiation or high codon bias important for protein yield of a transgene in  S. cerevisiae.
    • (2013) Cell , vol.153 , pp. 1589-1601
    • Shah, P.1    Ding, Y.2    Niemczyk, M.3    Kudla, G.4    Plotkin, J.B.5
  • 33
    • 84899550455 scopus 로고    scopus 로고
    • Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources
    • 33 Li, G.W., Burkhardt, D., Gross, C., Weissman, J.S., Quantifying absolute protein synthesis rates reveals principles underlying allocation of cellular resources. Cell 157 (2014), 624–635.
    • (2014) Cell , vol.157 , pp. 624-635
    • Li, G.W.1    Burkhardt, D.2    Gross, C.3    Weissman, J.S.4
  • 34
    • 84959149884 scopus 로고    scopus 로고
    • Improved ribosome-footprint and mRNA measurements provide insights into dynamics and regulation of yeast translation
    • This study provides improved ribosome-footprint profiles and mRNA abundances confirming the slow translation of the beginning of coding regions and codons matching rare tRNAs in  S. cerevisiae.
    • 34• Weinberg, D.E., Shah, P., Eichhorn, S.W., Hussmann, J.A., Plotkin, J.B., Bartel, D.P., Improved ribosome-footprint and mRNA measurements provide insights into dynamics and regulation of yeast translation. Cell Rep 14 (2016), 1787–1799 This study provides improved ribosome-footprint profiles and mRNA abundances confirming the slow translation of the beginning of coding regions and codons matching rare tRNAs in  S. cerevisiae.
    • (2016) Cell Rep , vol.14 , pp. 1787-1799
    • Weinberg, D.E.1    Shah, P.2    Eichhorn, S.W.3    Hussmann, J.A.4    Plotkin, J.B.5    Bartel, D.P.6
  • 35
    • 84876309308 scopus 로고    scopus 로고
    • Anaerobic alpha-amylase production and secretion with fumarate as the final electron acceptor in Saccharomyces cerevisiae
    • 35 Liu, Z., Osterlund, T., Hou, J., Petranovic, D., Nielsen, J., Anaerobic alpha-amylase production and secretion with fumarate as the final electron acceptor in Saccharomyces cerevisiae. Appl. Environ. Microbiol. 79 (2013), 2962–2967.
    • (2013) Appl. Environ. Microbiol. , vol.79 , pp. 2962-2967
    • Liu, Z.1    Osterlund, T.2    Hou, J.3    Petranovic, D.4    Nielsen, J.5
  • 36
    • 18444378154 scopus 로고    scopus 로고
    • Transcriptome analysis of recombinant protein secretion by Aspergillus nidulans and the unfolded-protein response in vivo
    • 36 Sims, A.H., Gent, M.E., Lanthaler, K., Dunn-Coleman, N.S., Oliver, S.G., Robson, G.D., Transcriptome analysis of recombinant protein secretion by Aspergillus nidulans and the unfolded-protein response in vivo. Appl. Environ. Microbiol. 71 (2005), 2737–2747.
    • (2005) Appl. Environ. Microbiol. , vol.71 , pp. 2737-2747
    • Sims, A.H.1    Gent, M.E.2    Lanthaler, K.3    Dunn-Coleman, N.S.4    Oliver, S.G.5    Robson, G.D.6
  • 37
    • 84885387427 scopus 로고    scopus 로고
    • Correlation of cell growth and heterologous protein production by Saccharomyces cerevisiae
    • 37 Liu, Z., Hou, J., Martinez, J.L., Petranovic, D., Nielsen, J., Correlation of cell growth and heterologous protein production by Saccharomyces cerevisiae. Appl. Microbiol. Biotechnol. 97 (2013), 8955–8962.
    • (2013) Appl. Microbiol. Biotechnol. , vol.97 , pp. 8955-8962
    • Liu, Z.1    Hou, J.2    Martinez, J.L.3    Petranovic, D.4    Nielsen, J.5
  • 38
    • 84863380845 scopus 로고    scopus 로고
    • Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress
    • 38 Tyo, K.E., Liu, Z., Petranovic, D., Nielsen, J., Imbalance of heterologous protein folding and disulfide bond formation rates yields runaway oxidative stress. BMC Biol., 10, 2012, 16.
    • (2012) BMC Biol. , vol.10 , pp. 16
    • Tyo, K.E.1    Liu, Z.2    Petranovic, D.3    Nielsen, J.4
  • 39
    • 35448965117 scopus 로고    scopus 로고
    • Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts
    • 39 Gasser, B., Sauer, M., Maurer, M., Stadlmayr, G., Mattanovich, D., Transcriptomics-based identification of novel factors enhancing heterologous protein secretion in yeasts. Appl. Environ. Microbiol. 73 (2007), 6499–6507.
    • (2007) Appl. Environ. Microbiol. , vol.73 , pp. 6499-6507
    • Gasser, B.1    Sauer, M.2    Maurer, M.3    Stadlmayr, G.4    Mattanovich, D.5
  • 40
    • 84922471043 scopus 로고    scopus 로고
    • Engineering the supply chain for protein production/secretion in yeasts and mammalian cells
    • An excellent review on optimization of supply chain for building blocks and energy for protein production.
    • 40•• Klein, T., Niklas, J., Heinzle, E., Engineering the supply chain for protein production/secretion in yeasts and mammalian cells. J. Ind. Microbiol. Biotechnol. 42 (2015), 453–464 An excellent review on optimization of supply chain for building blocks and energy for protein production.
    • (2015) J. Ind. Microbiol. Biotechnol. , vol.42 , pp. 453-464
    • Klein, T.1    Niklas, J.2    Heinzle, E.3
  • 42
    • 84961654631 scopus 로고    scopus 로고
    • Increasing pentose phosphate pathway flux enhances recombinant protein production in Pichia pastoris
    • The authors combinatorially overexpress genes involved in pentose phosphate pathway (PPP), enhancing the PPP flux ratio and recombinant hSOD production in  P. pastoris.
    • 42• Nocon, J., Steiger, M., Mairinger, T., Hohlweg, J., Russmayer, H., Hann, S., Gasser, B., Mattanovich, D., Increasing pentose phosphate pathway flux enhances recombinant protein production in Pichia pastoris. Appl. Microbiol. Biotechnol. 100 (2016), 5955–5963 The authors combinatorially overexpress genes involved in pentose phosphate pathway (PPP), enhancing the PPP flux ratio and recombinant hSOD production in  P. pastoris.
    • (2016) Appl. Microbiol. Biotechnol. , vol.100 , pp. 5955-5963
    • Nocon, J.1    Steiger, M.2    Mairinger, T.3    Hohlweg, J.4    Russmayer, H.5    Hann, S.6    Gasser, B.7    Mattanovich, D.8
  • 43
    • 77952585767 scopus 로고    scopus 로고
    • Metabolomics-driven approach for the improvement of Chinese hamster ovary cell growth: overexpression of malate dehydrogenase II
    • 43 Chong, W.P., Reddy, S.G., Yusufi, F.N., Lee, D.Y., Wong, N.S., Heng, C.K., Yap, M.G., Ho, Y.S., Metabolomics-driven approach for the improvement of Chinese hamster ovary cell growth: overexpression of malate dehydrogenase II. J. Biotechnol. 147 (2010), 116–121.
    • (2010) J. Biotechnol. , vol.147 , pp. 116-121
    • Chong, W.P.1    Reddy, S.G.2    Yusufi, F.N.3    Lee, D.Y.4    Wong, N.S.5    Heng, C.K.6    Yap, M.G.7    Ho, Y.S.8
  • 44
    • 84866487453 scopus 로고    scopus 로고
    • Integration of expression data in genome-scale metabolic network reconstructions
    • 44 Blazier, A.S., Papin, J.A., Integration of expression data in genome-scale metabolic network reconstructions. Front. Physiol., 3, 2012, 299.
    • (2012) Front. Physiol. , vol.3 , pp. 299
    • Blazier, A.S.1    Papin, J.A.2
  • 45
    • 84901621407 scopus 로고    scopus 로고
    • Model based engineering of Pichia pastoris central metabolism enhances recombinant protein production
    • The authors utilized genome scale metabolic modeling to predict targets for enhancing recombinant protein production in  P. pastoris. A high accuracy in the positive target prediction demonstrates the promising application of model guided strain development.
    • 45•• Nocon, J., Steiger, M.G., Pfeffer, M., Sohn, S.B., Kim, T.Y., Maurer, M., Russmayer, H., Pflugl, S., Ask, M., Haberhauer-Troyer, C., et al. Model based engineering of Pichia pastoris central metabolism enhances recombinant protein production. Metab. Eng. 24 (2014), 129–138 The authors utilized genome scale metabolic modeling to predict targets for enhancing recombinant protein production in  P. pastoris. A high accuracy in the positive target prediction demonstrates the promising application of model guided strain development.
    • (2014) Metab. Eng. , vol.24 , pp. 129-138
    • Nocon, J.1    Steiger, M.G.2    Pfeffer, M.3    Sohn, S.B.4    Kim, T.Y.5    Maurer, M.6    Russmayer, H.7    Pflugl, S.8    Ask, M.9    Haberhauer-Troyer, C.10
  • 46
    • 84949257152 scopus 로고    scopus 로고
    • Genome-scale metabolic model of Pichia pastoris with native and humanized glycosylation of recombinant proteins
    • 46 Irani, Z.A., Kerkhoven, E.J., Shojaosadati, S.A., Nielsen, J., Genome-scale metabolic model of Pichia pastoris with native and humanized glycosylation of recombinant proteins. Biotechnol. Bioeng. 113 (2016), 961–969.
    • (2016) Biotechnol. Bioeng. , vol.113 , pp. 961-969
    • Irani, Z.A.1    Kerkhoven, E.J.2    Shojaosadati, S.A.3    Nielsen, J.4
  • 47
    • 84877119088 scopus 로고    scopus 로고
    • Genome-scale modeling of the protein secretory machinery in yeast
    • The authors construct a genome-scale model for protein secretion in  S. cerevisiae using a bottom-up approach. This model covers the entire secretory process to provide a more detailed comprehensive view of the secretory machinery.
    • 47•• Feizi, A., Osterlund, T., Petranovic, D., Bordel, S., Nielsen, J., Genome-scale modeling of the protein secretory machinery in yeast. PLoS One, 8, 2013, e63284 The authors construct a genome-scale model for protein secretion in  S. cerevisiae using a bottom-up approach. This model covers the entire secretory process to provide a more detailed comprehensive view of the secretory machinery.
    • (2013) PLoS One , vol.8 , pp. e63284
    • Feizi, A.1    Osterlund, T.2    Petranovic, D.3    Bordel, S.4    Nielsen, J.5
  • 50
    • 84893020696 scopus 로고    scopus 로고
    • High-throughput screening for industrial enzyme production hosts by droplet microfluidics
    • 50 Sjostrom, S.L., Bai, Y.P., Huang, M.T., Liu, Z.H., Nielsen, J., Joensson, H.N., Svahn, H.A., High-throughput screening for industrial enzyme production hosts by droplet microfluidics. Lab Chip 14 (2014), 806–813.
    • (2014) Lab Chip , vol.14 , pp. 806-813
    • Sjostrom, S.L.1    Bai, Y.P.2    Huang, M.T.3    Liu, Z.H.4    Nielsen, J.5    Joensson, H.N.6    Svahn, H.A.7
  • 51
    • 84940521020 scopus 로고    scopus 로고
    • Microfluidic screening and whole-genome sequencing identifies mutations associated with improved protein secretion by yeast
    • The authors isolate yeast mutant strains with significantly improved amylase production through microfluidic screening and systematical analysis of mutations and biological processes associated with improved protein secretion.
    • 51•• Huang, M., Bai, Y., Sjostrom, S.L., Hallstrom, B.M., Liu, Z., Petranovic, D., Uhlen, M., Joensson, H.N., Andersson-Svahn, H., Nielsen, J., Microfluidic screening and whole-genome sequencing identifies mutations associated with improved protein secretion by yeast. Proc. Natl. Acad. Sci. U. S. A. 112 (2015), E4689–4696 The authors isolate yeast mutant strains with significantly improved amylase production through microfluidic screening and systematical analysis of mutations and biological processes associated with improved protein secretion.
    • (2015) Proc. Natl. Acad. Sci. U. S. A. , vol.112 , pp. E4689-4696
    • Huang, M.1    Bai, Y.2    Sjostrom, S.L.3    Hallstrom, B.M.4    Liu, Z.5    Petranovic, D.6    Uhlen, M.7    Joensson, H.N.8    Andersson-Svahn, H.9    Nielsen, J.10
  • 52
    • 84952682854 scopus 로고    scopus 로고
    • CRISPR/Cas9 advances engineering of microbial cell factories
    • 52 Jakociunas, T., Jensen, M.K., Keasling, J.D., CRISPR/Cas9 advances engineering of microbial cell factories. Metab. Eng. 34 (2016), 44–59.
    • (2016) Metab. Eng. , vol.34 , pp. 44-59
    • Jakociunas, T.1    Jensen, M.K.2    Keasling, J.D.3
  • 53
    • 84925607864 scopus 로고    scopus 로고
    • RNAi-assisted genome evolution in Saccharomyces cerevisiae for complex phenotype engineering
    • 53 Si, T., Luo, Y., Bao, Z., Zhao, H., RNAi-assisted genome evolution in Saccharomyces cerevisiae for complex phenotype engineering. ACS Synth. Biol. 4 (2015), 283–291.
    • (2015) ACS Synth. Biol. , vol.4 , pp. 283-291
    • Si, T.1    Luo, Y.2    Bao, Z.3    Zhao, H.4


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