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Volumn 35, Issue 12, 2013, Pages 1961-1969

A systems biology approach to optimising hosts for industrial protein production

Author keywords

Chaperones; Enzyme production; Industrial proteins; Mathematical modelling; Molecular toolboxes; Recombinant protein production; Synthetic biology

Indexed keywords

CHAPERONES; ENZYME PRODUCTION; INDUSTRIAL PROTEINS; MOLECULAR TOOLBOXES; RECOMBINANT PROTEIN PRODUCTIONS; SYNTHETIC BIOLOGY;

EID: 84887318841     PISSN: 01415492     EISSN: 15736776     Source Type: Journal    
DOI: 10.1007/s10529-013-1297-0     Document Type: Review
Times cited : (6)

References (44)
  • 1
    • 84870949388 scopus 로고    scopus 로고
    • What's fueling the biotech engine-2011 to 2012
    • Aggarwal S (2012) What's fueling the biotech engine-2011 to 2012. Nat Biotechnol 30: 1191-1197.
    • (2012) Nat Biotechnol , vol.30 , pp. 1191-1197
    • Aggarwal, S.1
  • 2
    • 79959936732 scopus 로고    scopus 로고
    • Empirical model and in vivo characterization of the bacterial response to synthetic gene expression show that ribosome allocation limits growth rate
    • Carrera J, Rodrigo G, Singh V, Kirov B, Jaramillo A (2011) Empirical model and in vivo characterization of the bacterial response to synthetic gene expression show that ribosome allocation limits growth rate. Biotechnol J 6: 773-783.
    • (2011) Biotechnol J , vol.6 , pp. 773-783
    • Carrera, J.1    Rodrigo, G.2    Singh, V.3    Kirov, B.4    Jaramillo, A.5
  • 3
    • 58949086663 scopus 로고    scopus 로고
    • The effect of Fc glycan forms on human IgG2 antibody clearance in humans
    • Chen X, Liu YD, Flynn GC (2009) The effect of Fc glycan forms on human IgG2 antibody clearance in humans. Glycobiology 19: 240-249.
    • (2009) Glycobiology , vol.19 , pp. 240-249
    • Chen, X.1    Liu, Y.D.2    Flynn, G.C.3
  • 4
    • 84862908629 scopus 로고    scopus 로고
    • Robust design of biological circuits: evolutionary systems biology approach
    • Chen BS, Hsu CY, Liou JJ (2011) Robust design of biological circuits: evolutionary systems biology approach. J Biomed Biotechnol 2011: 304236.
    • (2011) J Biomed Biotechnol , vol.2011 , pp. 304236
    • Chen, B.S.1    Hsu, C.Y.2    Liou, J.J.3
  • 6
    • 61349178501 scopus 로고    scopus 로고
    • Production of recombinant proteins by microbes and higher organisms
    • Demain AL, Vaishnav P (2009) Production of recombinant proteins by microbes and higher organisms. Biotechnol Adv 27: 297-306.
    • (2009) Biotechnol Adv , vol.27 , pp. 297-306
    • Demain, A.L.1    Vaishnav, P.2
  • 8
    • 66149172363 scopus 로고    scopus 로고
    • Diversity-based, model-guided construction of synthetic gene networks with predicted functions
    • Ellis T, Wang X, Collins JJ (2009) Diversity-based, model-guided construction of synthetic gene networks with predicted functions. Nat Biotechnol 27: 465-471.
    • (2009) Nat Biotechnol , vol.27 , pp. 465-471
    • Ellis, T.1    Wang, X.2    Collins, J.J.3
  • 9
    • 84874010654 scopus 로고    scopus 로고
    • A mathematical model of the unfolded protein stress response reveals the decision mechanism for recovery, adaptation and apoptosis
    • Erguler K, Pieri M, Deltas C (2013) A mathematical model of the unfolded protein stress response reveals the decision mechanism for recovery, adaptation and apoptosis. BMC Syst Biol 7: 16.
    • (2013) BMC Syst Biol , vol.7 , pp. 16
    • Erguler, K.1    Pieri, M.2    Deltas, C.3
  • 11
    • 73949123429 scopus 로고    scopus 로고
    • Considerations for the design and construction of a synthetic platform cell for biotechnological applications
    • Foley PL, Shuler ML (2010) Considerations for the design and construction of a synthetic platform cell for biotechnological applications. Biotechnol Bioeng 105: 26-36.
    • (2010) Biotechnol Bioeng , vol.105 , pp. 26-36
    • Foley, P.L.1    Shuler, M.L.2
  • 12
    • 80053369081 scopus 로고    scopus 로고
    • Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response
    • Gardner BM, Walter P (2011) Unfolded proteins are Ire1-activating ligands that directly induce the unfolded protein response. Science 333: 1891-1894.
    • (2011) Science , vol.333 , pp. 1891-1894
    • Gardner, B.M.1    Walter, P.2
  • 13
    • 79960652801 scopus 로고    scopus 로고
    • Molecular chaperones in protein folding and proteostasis
    • Hartl FU, Bracher A, Hayer-Hartl M (2011) Molecular chaperones in protein folding and proteostasis. Nature 475: 324-332.
    • (2011) Nature , vol.475 , pp. 324-332
    • Hartl, F.U.1    Bracher, A.2    Hayer-Hartl, M.3
  • 14
    • 84861744439 scopus 로고    scopus 로고
    • Yeast 5-an expanded reconstruction of the Saccharomyces cerevisiae metabolic network
    • Heavner B, Smallbone K, Barker B, Mendes P, Walker L (2012) Yeast 5-an expanded reconstruction of the Saccharomyces cerevisiae metabolic network. BMC Syst Biol 6: 55.
    • (2012) BMC Syst Biol , vol.6 , pp. 55
    • Heavner, B.1    Smallbone, K.2    Barker, B.3    Mendes, P.4    Walker, L.5
  • 15
    • 56049116692 scopus 로고    scopus 로고
    • A top-down approach to mechanistic biological modeling: application to the single-chain antibody folding pathway
    • Hildebrandt S, Raden D, Petzold L, Robinson AS, Doyle FJ (2008) A top-down approach to mechanistic biological modeling: application to the single-chain antibody folding pathway. Biophys J 95: 3535-3558.
    • (2008) Biophys J , vol.95 , pp. 3535-3558
    • Hildebrandt, S.1    Raden, D.2    Petzold, L.3    Robinson, A.S.4    Doyle, F.J.5
  • 16
    • 33644976621 scopus 로고    scopus 로고
    • Enhancement of protein secretion in Pichia pastoris by overexpression of protein disulfide isomerase
    • Inan M, Aryasomayajula D, Sinha J, Meagher MM (2006) Enhancement of protein secretion in Pichia pastoris by overexpression of protein disulfide isomerase. Biotechnol Bioeng 93: 771-778.
    • (2006) Biotechnol Bioeng , vol.93 , pp. 771-778
    • Inan, M.1    Aryasomayajula, D.2    Sinha, J.3    Meagher, M.M.4
  • 17
    • 82955237386 scopus 로고    scopus 로고
    • A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus
    • Jimenez del Val I, Nagy JM, Kontoravdi C (2011) A dynamic mathematical model for monoclonal antibody N-linked glycosylation and nucleotide sugar donor transport within a maturing Golgi apparatus. Biotechnol Prog 27: 1730-1743.
    • (2011) Biotechnol Prog , vol.27 , pp. 1730-1743
    • Jimenez del Val, I.1    Nagy, J.M.2    Kontoravdi, C.3
  • 18
    • 79954426601 scopus 로고    scopus 로고
    • Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells
    • Kimata Y, Kohno K (2011) Endoplasmic reticulum stress-sensing mechanisms in yeast and mammalian cells. Curr Opin Cell Biol 23: 135-142.
    • (2011) Curr Opin Cell Biol , vol.23 , pp. 135-142
    • Kimata, Y.1    Kohno, K.2
  • 20
    • 8444250981 scopus 로고    scopus 로고
    • A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1
    • Kimata Y, Oikawa D, Shimizu Y, Ishiwata-Kimata Y, Kohno K (2004) A role for BiP as an adjustor for the endoplasmic reticulum stress-sensing protein Ire1. J Cell Biol 167: 445-456.
    • (2004) J Cell Biol , vol.167 , pp. 445-456
    • Kimata, Y.1    Oikawa, D.2    Shimizu, Y.3    Ishiwata-Kimata, Y.4    Kohno, K.5
  • 22
    • 64849114915 scopus 로고    scopus 로고
    • Coding-sequence determinants of gene expression in Escherichia coli
    • Kudla G, Murray AW, Tollervey D, Plotkin JB (2009) Coding-sequence determinants of gene expression in Escherichia coli. Science 324: 255-258.
    • (2009) Science , vol.324 , pp. 255-258
    • Kudla, G.1    Murray, A.W.2    Tollervey, D.3    Plotkin, J.B.4
  • 23
    • 84862006007 scopus 로고    scopus 로고
    • Systematic single-cell analysis of Pichia pastoris reveals secretory capacity limits productivity
    • Love KR, Politano TJ, Panagiotou V, Jiang B, Stadheim TA, Love JC (2012) Systematic single-cell analysis of Pichia pastoris reveals secretory capacity limits productivity. PLoS ONE 7: e37915.
    • (2012) PLoS ONE , vol.7
    • Love, K.R.1    Politano, T.J.2    Panagiotou, V.3    Jiang, B.4    Stadheim, T.A.5    Love, J.C.6
  • 25
    • 84874619884 scopus 로고    scopus 로고
    • Transferring a synthetic gene circuit from yeast to mammalian cells
    • Nevozhay D, Zal T, Balazsi G (2013) Transferring a synthetic gene circuit from yeast to mammalian cells. Nat Commun 4: 1451.
    • (2013) Nat Commun , vol.4 , pp. 1451
    • Nevozhay, D.1    Zal, T.2    Balazsi, G.3
  • 26
    • 84866449925 scopus 로고    scopus 로고
    • Prediction of variable translation rate effects on cotranslational protein folding
    • O'Brien EP, Vendruscolo M, Dobson CM (2012) Prediction of variable translation rate effects on cotranslational protein folding. Nat Commun 3: 868.
    • (2012) Nat Commun , vol.3 , pp. 868
    • O'Brien, E.P.1    Vendruscolo, M.2    Dobson, C.M.3
  • 27
    • 84870868447 scopus 로고    scopus 로고
    • Direct association of unfolded proteins with mammalian ER stress sensor, Ire1β
    • Oikawa D, Kitamura A, Kinjo M, Iwawaki T (2012) Direct association of unfolded proteins with mammalian ER stress sensor, Ire1β. PLoS ONE 7: e51290.
    • (2012) PLoS ONE , vol.7
    • Oikawa, D.1    Kitamura, A.2    Kinjo, M.3    Iwawaki, T.4
  • 29
    • 84861161529 scopus 로고    scopus 로고
    • FoldEco: a model for proteostasis in E. coli
    • Powers ET, Powers DL, Gierasch LM (2012) FoldEco: a model for proteostasis in E. coli. Cell Rep 1: 265-276.
    • (2012) Cell Rep , vol.1 , pp. 265-276
    • Powers, E.T.1    Powers, D.L.2    Gierasch, L.M.3
  • 30
    • 84862666301 scopus 로고    scopus 로고
    • A computational framework for the design of optimal protein synthesis
    • Racle J, Overney J, Hatzimanikatis V (2012) A computational framework for the design of optimal protein synthesis. Biotechnol Bioeng 109: 2127-2133.
    • (2012) Biotechnol Bioeng , vol.109 , pp. 2127-2133
    • Racle, J.1    Overney, J.2    Hatzimanikatis, V.3
  • 32
    • 84866621300 scopus 로고    scopus 로고
    • Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system
    • Sekhar A, Lam HN, Cavagnero S (2012) Protein folding rates and thermodynamic stability are key determinants for interaction with the Hsp70 chaperone system. Protein Sci 21: 1489-1502.
    • (2012) Protein Sci , vol.21 , pp. 1489-1502
    • Sekhar, A.1    Lam, H.N.2    Cavagnero, S.3
  • 33
    • 77649272553 scopus 로고    scopus 로고
    • Slowing bacterial translation speed enhances eukaryotic protein folding efficiency
    • Siller E, DeZwaan DC, Anderson JF, Freeman BC, Barral JM (2010) Slowing bacterial translation speed enhances eukaryotic protein folding efficiency. J Mol Biol 396: 1310-1318.
    • (2010) J Mol Biol , vol.396 , pp. 1310-1318
    • Siller, E.1    DeZwaan, D.C.2    Anderson, J.F.3    Freeman, B.C.4    Barral, J.M.5
  • 34
    • 84864301147 scopus 로고    scopus 로고
    • Self-cycling operation increases productivity of recombinant protein in Escherichia coli
    • Storms ZJ, Brown T, Sauvageau D, Cooper DG (2012) Self-cycling operation increases productivity of recombinant protein in Escherichia coli. Biotechnol Bioeng 109: 2262-2270.
    • (2012) Biotechnol Bioeng , vol.109 , pp. 2262-2270
    • Storms, Z.J.1    Brown, T.2    Sauvageau, D.3    Cooper, D.G.4
  • 35
    • 77949566751 scopus 로고    scopus 로고
    • Strategies for the enhancement of recombinant protein production from mammalian cells by growth arrest
    • Sunley K, Butler M (2010) Strategies for the enhancement of recombinant protein production from mammalian cells by growth arrest. Biotechnol Adv 28: 385-394.
    • (2010) Biotechnol Adv , vol.28 , pp. 385-394
    • Sunley, K.1    Butler, M.2
  • 38
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: from stress pathway to homeostatic regulation
    • Walter P, Ron D (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science 334: 1081-1086.
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 39
    • 61849145185 scopus 로고    scopus 로고
    • Development and crystallization of a minimal thermostabilised G protein-coupled receptor
    • Warne T, Serrano-Vega MJ, Tate CG, Schertler GFX (2009) Development and crystallization of a minimal thermostabilised G protein-coupled receptor. Protein Expr Purif 65: 204-213.
    • (2009) Protein Expr Purif , vol.65 , pp. 204-213
    • Warne, T.1    Serrano-Vega, M.J.2    Tate, C.G.3    Schertler, G.F.X.4
  • 41
    • 79960867411 scopus 로고    scopus 로고
    • Native-state stability determines the extent of degradation relative to secretion of protein variants from Pichia pastoris
    • Whyteside G, Alcocer MJC, Kumita JR, Dobson CM, Lazarou M, Pleass RJ, Archer DB (2011) Native-state stability determines the extent of degradation relative to secretion of protein variants from Pichia pastoris. PLoS ONE 6: e22692.
    • (2011) PLoS ONE , vol.6
    • Whyteside, G.1    Alcocer, M.J.C.2    Kumita, J.R.3    Dobson, C.M.4    Lazarou, M.5    Pleass, R.J.6    Archer, D.B.7
  • 42
    • 36049032748 scopus 로고    scopus 로고
    • An adaptable standard for protein export from the endoplasmic reticulum
    • Wiseman RL, Powers ET, Buxbaum JN, Kelly JW, Balch WE (2007) An adaptable standard for protein export from the endoplasmic reticulum. Cell 131: 809-821.
    • (2007) Cell , vol.131 , pp. 809-821
    • Wiseman, R.L.1    Powers, E.T.2    Buxbaum, J.N.3    Kelly, J.W.4    Balch, W.E.5
  • 43
    • 24044505375 scopus 로고    scopus 로고
    • Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding
    • Xu P, Raden D, Doyle FJ III, Robinson AS (2005) Analysis of unfolded protein response during single-chain antibody expression in Saccaromyces cerevisiae reveals different roles for BiP and PDI in folding. Metab Eng 7: 269-279.
    • (2005) Metab Eng , vol.7 , pp. 269-279
    • Xu, P.1    Raden, D.2    Doyle III, F.J.3    Robinson, A.S.4
  • 44
    • 84874683740 scopus 로고    scopus 로고
    • Non-optimal codon usage affects expression, structure and function of clock protein FRQ
    • Zhou M, Guo J, Cha J, Chae M, Chen S, Barral JM, Sachs MS, Liu Y (2013) Non-optimal codon usage affects expression, structure and function of clock protein FRQ. Nature 495: 111-115.
    • (2013) Nature , vol.495 , pp. 111-115
    • Zhou, M.1    Guo, J.2    Cha, J.3    Chae, M.4    Chen, S.5    Barral, J.M.6    Sachs, M.S.7    Liu, Y.8


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.