메뉴 건너뛰기




Volumn 6, Issue 6, 2017, Pages 1016-1025

A Modular Toolkit for Generating Pichia pastoris Secretion Libraries

Author keywords

high throughput; Pichia pastoris; secretion; synthetic biology; yeast

Indexed keywords

CELL PROTEIN; ENHANCED GREEN FLUORESCENT PROTEIN; RED FLUORESCENT PROTEIN; REGULATOR PROTEIN; RECOMBINANT PROTEIN; SIGNAL PEPTIDE;

EID: 85020843976     PISSN: None     EISSN: 21615063     Source Type: Journal    
DOI: 10.1021/acssynbio.6b00337     Document Type: Article
Times cited : (78)

References (61)
  • 1
    • 84947998665 scopus 로고    scopus 로고
    • Industrial systems biology and its impact on synthetic biology of yeast cell factories
    • Fletcher, E., Krivoruchko, A., and Nielsen, J. (2016) Industrial systems biology and its impact on synthetic biology of yeast cell factories Biotechnol. Bioeng. 103, 1164-1170 10.1002/bit.25870
    • (2016) Biotechnol. Bioeng. , vol.103 , pp. 1164-1170
    • Fletcher, E.1    Krivoruchko, A.2    Nielsen, J.3
  • 3
    • 84960124110 scopus 로고    scopus 로고
    • Synthetic biology and molecular genetics in non-conventional yeasts: Current tools and future advances
    • Wagner, J. M. and Alper, H. S. (2015) Synthetic biology and molecular genetics in non-conventional yeasts: Current tools and future advances Fungal Genet. Biol. 89, 126-136 10.1016/j.fgb.2015.12.001
    • (2015) Fungal Genet. Biol. , vol.89 , pp. 126-136
    • Wagner, J.M.1    Alper, H.S.2
  • 4
    • 33845579099 scopus 로고    scopus 로고
    • Fast, cheap and somewhat in control
    • Arkin, A. P. and Fletcher, D. a. (2006) Fast, cheap and somewhat in control Genome Biol. 7, 114 10.1186/gb-2006-7-8-114
    • (2006) Genome Biol. , vol.7 , pp. 114
    • Arkin, A.P.1    Fletcher, D.A.2
  • 5
    • 84878854426 scopus 로고    scopus 로고
    • Next generation biofuel engineering in prokaryotes
    • Gronenberg, L. S., Marcheschi, R. J., and Liao, J. C. (2013) Next generation biofuel engineering in prokaryotes Curr. Opin. Chem. Biol. 17, 462-471 10.1016/j.cbpa.2013.03.037
    • (2013) Curr. Opin. Chem. Biol. , vol.17 , pp. 462-471
    • Gronenberg, L.S.1    Marcheschi, R.J.2    Liao, J.C.3
  • 7
    • 84975780687 scopus 로고    scopus 로고
    • Biosynthesis of therapeutic natural products using synthetic biology
    • Awan, A. R., Shaw, W. M., and Ellis, T. (2016) Biosynthesis of therapeutic natural products using synthetic biology Adv. Drug Delivery Rev. 105, 96-106 10.1016/j.addr.2016.04.010
    • (2016) Adv. Drug Delivery Rev. , vol.105 , pp. 96-106
    • Awan, A.R.1    Shaw, W.M.2    Ellis, T.3
  • 9
    • 66249088017 scopus 로고    scopus 로고
    • The second wave of synthetic biology: From modules to systems
    • Purnick, P. E. M. and Weiss, R. (2009) The second wave of synthetic biology: from modules to systems Nat. Rev. Mol. Cell Biol. 10, 410-422 10.1038/nrm2698
    • (2009) Nat. Rev. Mol. Cell Biol. , vol.10 , pp. 410-422
    • Purnick, P.E.M.1    Weiss, R.2
  • 11
    • 85027954689 scopus 로고    scopus 로고
    • The synthetic biology toolbox for tuning gene expression in yeast
    • Redden, H., Morse, N., and Alper, H. S. (2015) The synthetic biology toolbox for tuning gene expression in yeast FEMS Yeast Res. 15, 1-10 10.1111/1567-1364.12188
    • (2015) FEMS Yeast Res. , vol.15 , pp. 1-10
    • Redden, H.1    Morse, N.2    Alper, H.S.3
  • 13
    • 84949231588 scopus 로고    scopus 로고
    • Methanol regulated yeast promoters: Production vehicles and toolbox for synthetic biology
    • Gasser, B., Steiger, M. G., and Mattanovich, D. (2015) Methanol regulated yeast promoters: production vehicles and toolbox for synthetic biology Microb. Cell Fact. 14, 196 10.1186/s12934-015-0387-1
    • (2015) Microb. Cell Fact. , vol.14 , pp. 196
    • Gasser, B.1    Steiger, M.G.2    Mattanovich, D.3
  • 15
    • 84879681227 scopus 로고    scopus 로고
    • Characterization of 582 natural and synthetic terminators and quantification of their design constraints
    • Chen, Y.-J., Liu, P., Nielsen, A. a K., Brophy, J. a N., Clancy, K., Peterson, T., and Voigt, C. a. (2013) Characterization of 582 natural and synthetic terminators and quantification of their design constraints Nat. Methods 10, 659-64 10.1038/nmeth.2515
    • (2013) Nat. Methods , vol.10 , pp. 659-664
    • Chen, Y.-J.1    Liu, P.2    Nielsen, A.A.K.3    Brophy, J.A.N.4    Clancy, K.5    Peterson, T.6    Voigt, C.A.7
  • 16
    • 84930667107 scopus 로고    scopus 로고
    • Ribosome binding site libraries and pathway modules for shikimic acid synthesis with Corynebacterium glutamicum
    • Zhang, B., Zhou, N., Liu, Y.-M., Liu, C., Lou, C.-B., Jiang, C.-Y., and Liu, S.-J. (2015) Ribosome binding site libraries and pathway modules for shikimic acid synthesis with Corynebacterium glutamicum Microb. Cell Fact. 14, 71 10.1186/s12934-015-0254-0
    • (2015) Microb. Cell Fact. , vol.14 , pp. 71
    • Zhang, B.1    Zhou, N.2    Liu, Y.-M.3    Liu, C.4    Lou, C.-B.5    Jiang, C.-Y.6    Liu, S.-J.7
  • 17
    • 84863634266 scopus 로고    scopus 로고
    • Construction of synthetic regulatory networks in yeast
    • Blount, B. A., Weenink, T., and Ellis, T. (2012) Construction of synthetic regulatory networks in yeast FEBS Lett. 586, 2112-2121 10.1016/j.febslet.2012.01.053
    • (2012) FEBS Lett. , vol.586 , pp. 2112-2121
    • Blount, B.A.1    Weenink, T.2    Ellis, T.3
  • 18
    • 85028224726 scopus 로고    scopus 로고
    • Yeast synthetic biology for the production of recombinant therapeutic proteins
    • Kim, H., Yoo, S. J., and Kang, H. A. (2015) Yeast synthetic biology for the production of recombinant therapeutic proteins FEMS Yeast Res. 15, 1-16 10.1111/1567-1364.12195
    • (2015) FEMS Yeast Res. , vol.15 , pp. 1-16
    • Kim, H.1    Yoo, S.J.2    Kang, H.A.3
  • 19
    • 77249147339 scopus 로고    scopus 로고
    • Engineering of protein secretion in yeast: Strategies and impact on protein production
    • Idiris, A., Tohda, H., Kumagai, H., and Takegawa, K. (2010) Engineering of protein secretion in yeast: strategies and impact on protein production Appl. Microbiol. Biotechnol. 86, 403-17 10.1007/s00253-010-2447-0
    • (2010) Appl. Microbiol. Biotechnol. , vol.86 , pp. 403-417
    • Idiris, A.1    Tohda, H.2    Kumagai, H.3    Takegawa, K.4
  • 20
    • 84897950795 scopus 로고    scopus 로고
    • Playing catch-up with Escherichia coli: Using yeast to increase success rates in recombinant protein production experiments
    • Bill, R. M. (2014) Playing catch-up with escherichia coli: Using yeast to increase success rates in recombinant protein production experiments Front. Microbiol. 5, 1-5 10.3389/fmicb.2014.00085
    • (2014) Front. Microbiol. , vol.5 , pp. 1-5
    • Bill, R.M.1
  • 21
    • 84887626949 scopus 로고    scopus 로고
    • New opportunities by synthetic biology for biopharmaceutical production in Pichia pastoris
    • Vogl, T., Hartner, F. S., and Glieder, A. (2013) New opportunities by synthetic biology for biopharmaceutical production in Pichia pastoris Curr. Opin. Biotechnol. 24, 1094-1101 10.1016/j.copbio.2013.02.024
    • (2013) Curr. Opin. Biotechnol. , vol.24 , pp. 1094-1101
    • Vogl, T.1    Hartner, F.S.2    Glieder, A.3
  • 22
    • 77955558145 scopus 로고    scopus 로고
    • Engineering of glycosylation in yeast and other fungi: Current state and perspectives
    • De Pourcq, K., De Schutter, K., and Callewaert, N. (2010) Engineering of glycosylation in yeast and other fungi: current state and perspectives Appl. Microbiol. Biotechnol. 87, 1617-31 10.1007/s00253-010-2721-1
    • (2010) Appl. Microbiol. Biotechnol. , vol.87 , pp. 1617-1631
    • De Pourcq, K.1    De Schutter, K.2    Callewaert, N.3
  • 23
    • 36149001292 scopus 로고    scopus 로고
    • Glycosylation engineering in yeast: The advent of fully humanized yeast
    • Hamilton, S. R. and Gerngross, T. U. (2007) Glycosylation engineering in yeast: the advent of fully humanized yeast Curr. Opin. Biotechnol. 18, 387-392 10.1016/j.copbio.2007.09.001
    • (2007) Curr. Opin. Biotechnol. , vol.18 , pp. 387-392
    • Hamilton, S.R.1    Gerngross, T.U.2
  • 25
    • 84863090270 scopus 로고    scopus 로고
    • Deletion of the pichia pastoris ku70 homologue facilitates platform strain generation for gene expression and synthetic biology
    • Näätsaari, L., Mistlberger, B., Ruth, C., Hajek, T., Hartner, F. S., and Glieder, A. (2012) Deletion of the pichia pastoris ku70 homologue facilitates platform strain generation for gene expression and synthetic biology PLoS One 7, e39720 10.1371/journal.pone.0039720
    • (2012) PLoS One , vol.7 , pp. e39720
    • Näätsaari, L.1    Mistlberger, B.2    Ruth, C.3    Hajek, T.4    Hartner, F.S.5    Glieder, A.6
  • 26
    • 4644348208 scopus 로고    scopus 로고
    • Recombinant expression systems in the pharmaceutical industry
    • Schmidt, F. R. (2004) Recombinant expression systems in the pharmaceutical industry Appl. Microbiol. Biotechnol. 65, 363-372 10.1007/s00253-004-1656-9
    • (2004) Appl. Microbiol. Biotechnol. , vol.65 , pp. 363-372
    • Schmidt, F.R.1
  • 27
    • 84977998177 scopus 로고    scopus 로고
    • Pichia pastoris: A workhorse for recombinant protein production
    • Fickers, P. (2014) Pichia pastoris: a workhorse for recombinant protein production Curr. Res. Microbiol. Biotechnol. 2, 354-363
    • (2014) Curr. Res. Microbiol. Biotechnol. , vol.2 , pp. 354-363
    • Fickers, P.1
  • 28
    • 84925491299 scopus 로고    scopus 로고
    • Quo vadis? the challenges of recombinant protein folding and secretion in Pichia pastoris
    • Puxbaum, V., Mattanovich, D., and Gasser, B. (2015) Quo vadis? The challenges of recombinant protein folding and secretion in Pichia pastoris Appl. Microbiol. Biotechnol. 99, 2925-2938 10.1007/s00253-015-6470-z
    • (2015) Appl. Microbiol. Biotechnol. , vol.99 , pp. 2925-2938
    • Puxbaum, V.1    Mattanovich, D.2    Gasser, B.3
  • 29
    • 0026232555 scopus 로고
    • Gene expression in yeast: Protein secretion
    • Shuster, J. R. (1991) Gene expression in yeast: protein secretion Curr. Opin. Biotechnol. 2, 685-90 10.1016/0958-1669(91)90035-4
    • (1991) Curr. Opin. Biotechnol. , vol.2 , pp. 685-690
    • Shuster, J.R.1
  • 30
    • 84862006007 scopus 로고    scopus 로고
    • Systematic Single-Cell Analysis of Pichia pastoris Reveals Secretory Capacity Limits Productivity
    • Love, K. R., Politano, T. J., Panagiotou, V., Jiang, B., Stadheim, T. A., and Love, C. (2012) Systematic Single-Cell Analysis of Pichia pastoris Reveals Secretory Capacity Limits Productivity PLoS One 7, 1-11 10.1371/journal.pone.0037915
    • (2012) PLoS One , vol.7 , pp. 1-11
    • Love, K.R.1    Politano, T.J.2    Panagiotou, V.3    Jiang, B.4    Stadheim, T.A.5    Love, C.6
  • 31
    • 84897546101 scopus 로고    scopus 로고
    • Engineering of protein folding and secretion-strategies to overcome bottlenecks for efficient production of recombinant proteins
    • Delic, M., Göngrich, R., Mattanovich, D., and Gasser, B. (2014) Engineering of protein folding and secretion-strategies to overcome bottlenecks for efficient production of recombinant proteins Antioxid. Redox Signaling 21, 414-37 10.1089/ars.2014.5844
    • (2014) Antioxid. Redox Signaling , vol.21 , pp. 414-437
    • Delic, M.1    Göngrich, R.2    Mattanovich, D.3    Gasser, B.4
  • 32
    • 84942013003 scopus 로고    scopus 로고
    • A Highly Characterized Yeast Toolkit for Modular, Multipart Assembly
    • Lee, M. E., DeLoache, W. C., Cervantes, B., and Dueber, J. E. (2015) A Highly Characterized Yeast Toolkit for Modular, Multipart Assembly ACS Synth. Biol. 4, 975-986 10.1021/sb500366v
    • (2015) ACS Synth. Biol. , vol.4 , pp. 975-986
    • Lee, M.E.1    DeLoache, W.C.2    Cervantes, B.3    Dueber, J.E.4
  • 33
    • 84863322344 scopus 로고    scopus 로고
    • Contextualizing context for synthetic biology - Identifying causes of failure of synthetic biological systems
    • Cardinale, S. and Arkin, A. P. (2012) Contextualizing context for synthetic biology-identifying causes of failure of synthetic biological systems Biotechnol. J. 7, 856-866 10.1002/biot.201200085
    • (2012) Biotechnol. J. , vol.7 , pp. 856-866
    • Cardinale, S.1    Arkin, A.P.2
  • 34
    • 70349964350 scopus 로고    scopus 로고
    • Automated design of synthetic ribosome binding sites to control protein expression
    • Salis, H. M., Mirsky, E. A., and Voigt, C. A. (2009) Automated design of synthetic ribosome binding sites to control protein expression Nat. Biotechnol. 27, 946-50 10.1038/nbt.1568
    • (2009) Nat. Biotechnol. , vol.27 , pp. 946-950
    • Salis, H.M.1    Mirsky, E.A.2    Voigt, C.A.3
  • 35
    • 56649114274 scopus 로고    scopus 로고
    • A one pot, one step, precision cloning method with high throughput capability
    • Engler, C., Kandzia, R., and Marillonnet, S. (2008) A one pot, one step, precision cloning method with high throughput capability PLoS One 3, e3647 10.1371/journal.pone.0003647
    • (2008) PLoS One , vol.3 , pp. e3647
    • Engler, C.1    Kandzia, R.2    Marillonnet, S.3
  • 36
    • 79951997641 scopus 로고    scopus 로고
    • A Modular Cloning System for Standardized Assembly of Multigene Constructs
    • Weber, E., Engler, C., Gruetzner, R., Werner, S., and Marillonnet, S. (2011) A Modular Cloning System for Standardized Assembly of Multigene Constructs PLoS One 6, e16765 10.1371/journal.pone.0016765
    • (2011) PLoS One , vol.6 , pp. e16765
    • Weber, E.1    Engler, C.2    Gruetzner, R.3    Werner, S.4    Marillonnet, S.5
  • 37
    • 84877832640 scopus 로고    scopus 로고
    • Regulation of Pichia pastoris promoters and its consequences for protein production
    • Vogl, T. and Glieder, A. (2013) Regulation of Pichia pastoris promoters and its consequences for protein production New Biotechnol. 30, 385-404 10.1016/j.nbt.2012.11.010
    • (2013) New Biotechnol. , vol.30 , pp. 385-404
    • Vogl, T.1    Glieder, A.2
  • 38
    • 78649447147 scopus 로고    scopus 로고
    • Identification and characterisation of novel Pichia pastoris promoters for heterologous protein production
    • Stadlmayr, G., Mecklenbräuker, A., Rothmüller, M., Maurer, M., Sauer, M., Mattanovich, D., and Gasser, B. (2010) Identification and characterisation of novel Pichia pastoris promoters for heterologous protein production J. Biotechnol. 150, 519-529 10.1016/j.jbiotec.2010.09.957
    • (2010) J. Biotechnol. , vol.150 , pp. 519-529
    • Stadlmayr, G.1    Mecklenbräuker, A.2    Rothmüller, M.3    Maurer, M.4    Sauer, M.5    Mattanovich, D.6    Gasser, B.7
  • 39
    • 84890395226 scopus 로고    scopus 로고
    • Expression-level optimization of a multi-enzyme pathway in the absence of a high-throughput assay
    • Lee, M. E., Aswani, A., Han, A. S., Tomlin, C. J., and Dueber, J. E. (2013) Expression-level optimization of a multi-enzyme pathway in the absence of a high-throughput assay Nucleic Acids Res. 41, 10668-10678 10.1093/nar/gkt809
    • (2013) Nucleic Acids Res. , vol.41 , pp. 10668-10678
    • Lee, M.E.1    Aswani, A.2    Han, A.S.3    Tomlin, C.J.4    Dueber, J.E.5
  • 40
    • 0022395208 scopus 로고
    • Pichia pastoris as a host system for transformations
    • Cregg, J. and Barringer, K. (1985) Pichia pastoris as a host system for transformations Mol. Cell. Biol. 5, 3376-3385 10.1128/MCB.5.12.3376
    • (1985) Mol. Cell. Biol. , vol.5 , pp. 3376-3385
    • Cregg, J.1    Barringer, K.2
  • 41
    • 0023948010 scopus 로고
    • High efficiency transformation of E. Coli by high voltage electroporation
    • Dower, W. J., Miller, J. F., and Ragsdale, C. W. (1988) High efficiency transformation of E. coli by high voltage electroporation Nucleic Acids Res. 16, 6127-45 10.1093/nar/16.13.6127
    • (1988) Nucleic Acids Res. , vol.16 , pp. 6127-6145
    • Dower, W.J.1    Miller, J.F.2    Ragsdale, C.W.3
  • 42
  • 43
    • 84982702468 scopus 로고    scopus 로고
    • Synthetic biology and microbioreactor platforms for programmable production of biologics at the point-of-care
    • Perez-Pinera, P., Han, N., Cleto, S., Cao, J., Purcell, O., Shah, K. A., Lee, K., Ram, R., and Lu, T. K. (2016) Synthetic biology and microbioreactor platforms for programmable production of biologics at the point-of-care Nat. Commun. 7, 12211 10.1038/ncomms12211
    • (2016) Nat. Commun. , vol.7 , pp. 12211
    • Perez-Pinera, P.1    Han, N.2    Cleto, S.3    Cao, J.4    Purcell, O.5    Shah, K.A.6    Lee, K.7    Ram, R.8    Lu, T.K.9
  • 44
    • 84963593243 scopus 로고    scopus 로고
    • Combinatorial optimization of CRISPR/Cas9 expression enables precision genome engineering in the methylotrophic yeast Pichia pastoris
    • Weninger, A., Hatzl, A.-M., Schmid, C., Vogl, T., and Glieder, A. (2016) Combinatorial optimization of CRISPR/Cas9 expression enables precision genome engineering in the methylotrophic yeast Pichia pastoris J. Biotechnol. 235, 139 10.1016/j.jbiotec.2016.03.027
    • (2016) J. Biotechnol. , vol.235 , pp. 139
    • Weninger, A.1    Hatzl, A.-M.2    Schmid, C.3    Vogl, T.4    Glieder, A.5
  • 46
    • 84870607828 scopus 로고    scopus 로고
    • Endogenous signal peptides efficiently mediate the secretion of recombinant proteins in Pichia pastoris
    • Liang, S., Li, C., Ye, Y., and Lin, Y. (2013) Endogenous signal peptides efficiently mediate the secretion of recombinant proteins in Pichia pastoris Biotechnol. Lett. 35, 97-105 10.1007/s10529-012-1055-8
    • (2013) Biotechnol. Lett. , vol.35 , pp. 97-105
    • Liang, S.1    Li, C.2    Ye, Y.3    Lin, Y.4
  • 47
    • 0023088363 scopus 로고
    • Many random sequences functionally replace the secretion signal sequence of yeast invertase
    • Kaiser, C. a, Preuss, D., Grisafi, P., and Botstein, D. (1987) Many random sequences functionally replace the secretion signal sequence of yeast invertase Science 235, 312-317 10.1126/science.3541205
    • (1987) Science , vol.235 , pp. 312-317
    • Kaiser, C.A.1    Preuss, D.2    Grisafi, P.3    Botstein, D.4
  • 48
    • 33748937555 scopus 로고    scopus 로고
    • The surprising complexity of signal sequences
    • Hegde, R. S. and Bernstein, H. D. (2006) The surprising complexity of signal sequences Trends Biochem. Sci. 31, 563-571 10.1016/j.tibs.2006.08.004
    • (2006) Trends Biochem. Sci. , vol.31 , pp. 563-571
    • Hegde, R.S.1    Bernstein, H.D.2
  • 50
    • 84903814380 scopus 로고    scopus 로고
    • Protein expression in Pichia pastoris: Recent achievements and perspectives for heterologous protein production
    • Ahmad, M., Hirz, M., Pichler, H., and Schwab, H. (2014) Protein expression in Pichia pastoris: recent achievements and perspectives for heterologous protein production Appl. Microbiol. Biotechnol. 98, 5301-17 10.1007/s00253-014-5732-5
    • (2014) Appl. Microbiol. Biotechnol. , vol.98 , pp. 5301-5317
    • Ahmad, M.1    Hirz, M.2    Pichler, H.3    Schwab, H.4
  • 52
    • 0033753671 scopus 로고    scopus 로고
    • Recombinant protein expression in Pichia pastoris
    • Cregg, J., Cereghino, J., Shi, J., and Higgins, D. (2000) Recombinant protein expression in Pichia pastoris Mol. Biotechnol. 16, 23-52 10.1385/MB:16:1:23
    • (2000) Mol. Biotechnol. , vol.16 , pp. 23-52
    • Cregg, J.1    Cereghino, J.2    Shi, J.3    Higgins, D.4
  • 54
    • 84860649085 scopus 로고    scopus 로고
    • Metabolic flux profiling of recombinant protein secreting Pichia pastoris growing on glucose:methanol mixtures
    • Jordà, J., Jouhten, P., Cámara, E., Maaheimo, H., Albiol, J., and Ferrer, P. (2012) Metabolic flux profiling of recombinant protein secreting Pichia pastoris growing on glucose:methanol mixtures Microb. Cell Fact. 11, 57 10.1186/1475-2859-11-57
    • (2012) Microb. Cell Fact. , vol.11 , pp. 57
    • Jordà, J.1    Jouhten, P.2    Cámara, E.3    Maaheimo, H.4    Albiol, J.5    Ferrer, P.6
  • 55
    • 33646042890 scopus 로고    scopus 로고
    • Impact of methanol concentration on secreted protein production in oxygen-limited cultures of recombinant Pichia pastoris
    • Khatri, N. K. and Hoffmann, F. (2006) Impact of methanol concentration on secreted protein production in oxygen-limited cultures of recombinant Pichia pastoris Biotechnol. Bioeng. 93, 871-879 10.1002/bit.20773
    • (2006) Biotechnol. Bioeng. , vol.93 , pp. 871-879
    • Khatri, N.K.1    Hoffmann, F.2
  • 56
    • 84928327289 scopus 로고    scopus 로고
    • Pichia pastoris regulates its gene-specific response to different carbon sources at the transcriptional, rather than the translational, level
    • Prielhofer, R., Cartwright, S. P., Graf, A. B., Valli, M., Bill, R. M., Mattanovich, D., and Gasser, B. (2015) Pichia pastoris regulates its gene-specific response to different carbon sources at the transcriptional, rather than the translational, level BMC Genomics 16, 167 10.1186/s12864-015-1393-8
    • (2015) BMC Genomics , vol.16 , pp. 167
    • Prielhofer, R.1    Cartwright, S.P.2    Graf, A.B.3    Valli, M.4    Bill, R.M.5    Mattanovich, D.6    Gasser, B.7
  • 58
    • 2942627936 scopus 로고    scopus 로고
    • Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures
    • Jahic, M., Wallberg, F., Bollok, M., Garcia, P., and Enfors, S.-O. (2003) Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures Microb. Cell Fact. 2, 6 10.1186/1475-2859-2-6
    • (2003) Microb. Cell Fact. , vol.2 , pp. 6
    • Jahic, M.1    Wallberg, F.2    Bollok, M.3    Garcia, P.4    Enfors, S.-O.5
  • 60
    • 79955970114 scopus 로고    scopus 로고
    • Reliable high-throughput approach for screening of engineered constitutive promoters in the yeast Pichia pastoris
    • Qin, X., Qian, J., Xiao, C., Zhuang, Y., Zhang, S., and Chu, J. (2011) Reliable high-throughput approach for screening of engineered constitutive promoters in the yeast Pichia pastoris Lett. Appl. Microbiol. 52, 634-641 10.1111/j.1472-765X.2011.03051.x
    • (2011) Lett. Appl. Microbiol. , vol.52 , pp. 634-641
    • Qin, X.1    Qian, J.2    Xiao, C.3    Zhuang, Y.4    Zhang, S.5    Chu, J.6
  • 61
    • 45449094170 scopus 로고    scopus 로고
    • Secretory expression of interferon-alpha 2b in recombinant Pichia pastoris using three different secretion signals
    • Ghosalkar, A., Sahai, V., and Srivastava, A. (2008) Secretory expression of interferon-alpha 2b in recombinant Pichia pastoris using three different secretion signals Protein Expression Purif. 60, 103-109 10.1016/j.pep.2008.02.006
    • (2008) Protein Expression Purif. , vol.60 , pp. 103-109
    • Ghosalkar, A.1    Sahai, V.2    Srivastava, A.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.