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Volumn 98, Issue 18, 2014, Pages 7671-7698

Overexpression of membrane proteins from higher eukaryotes in yeasts

Author keywords

Heterologous expression; Membrane protein; Protein interactions; Protein structure; Yeast

Indexed keywords

CELL CULTURE; MEMBRANES; YEAST;

EID: 84906951267     PISSN: 01757598     EISSN: 14320614     Source Type: Journal    
DOI: 10.1007/s00253-014-5948-4     Document Type: Short Survey
Times cited : (20)

References (357)
  • 1
    • 79751537491 scopus 로고    scopus 로고
    • Lipid-binding surfaces of membrane proteins: Evidence from evolutionary and structural analysis
    • doi:10.1016/j.bbamem.2010.12.008
    • Adamian L, Naveed H, Liang J (2011) Lipid-binding surfaces of membrane proteins: evidence from evolutionary and structural analysis. Biochim Biophys Acta 1808:1092-1102. doi:10.1016/j.bbamem.2010.12.008
    • (2011) Biochim Biophys Acta , vol.1808 , pp. 1092-1102
    • Adamian, L.1    Naveed, H.2    Liang, J.3
  • 2
    • 34547631962 scopus 로고    scopus 로고
    • Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis
    • DOI 10.1038/nature05936, PII NATURE05936
    • Ago H, Kanaoka Y, Irikura D, Lam BK, Shimamura T, Austen KF, Miyano M (2007) Crystal structure of a human membrane protein involved in cysteinyl leukotriene biosynthesis. Nature 448:609-612. doi:10.1038/nature05936 (Pubitemid 47206929)
    • (2007) Nature , vol.448 , Issue.7153 , pp. 609-612
    • Ago, H.1    Kanaoka, Y.2    Irikura, D.3    Lam, B.K.4    Shimamura, T.5    Austen, K.F.6    Miyano, M.7
  • 3
    • 2542452829 scopus 로고    scopus 로고
    • Cotranslational membrane protein biogenesis at the endoplasmic reticulum
    • DOI 10.1074/jbc.R400002200
    • Alder NN, Johnson AE (2004) Cotranslational membrane protein biogenesis at the endoplasmic reticulum. J Biol Chem 279:22787-22790. doi:10.1074/jbc. R400002200 (Pubitemid 38685576)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.22 , pp. 22787-22790
    • Alder, N.N.1    Johnson, A.E.2
  • 5
    • 84890441641 scopus 로고    scopus 로고
    • G protein modulation of K2P potassium channel TASK-2: A role of basic residues in the C terminus domain
    • doi:10.1007/s00424-013-1314-0
    • Añazco C, Peña-Münzenmayer G, Araya C, Cid LP, Sepúlveda FV, Niemeyer MI (2013) G protein modulation of K2P potassium channel TASK-2 : a role of basic residues in the C terminus domain. Pflugers Arch 465:1715-1726. doi:10.1007/s00424-013-1314-0
    • (2013) Pflugers Arch , vol.465 , pp. 1715-1726
    • Añazco, C.1    Peña-Münzenmayer, G.2    Araya, C.3    Cid, L.P.4    Sepúlveda, F.V.5    Niemeyer, M.I.6
  • 6
    • 33646155331 scopus 로고    scopus 로고
    • Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen
    • doi:10.1110/ps.062098206
    • André N, Cherouati N, Prual C, Steffan T, Zeder-Lutz G, Magnin T, Pattus F, Michel H, Wagner R, Reinhart C (2006) Enhancing functional production of G protein-coupled receptors in Pichia pastoris to levels required for structural studies via a single expression screen. Protein Sci 15:1115-1126. doi:10.1110/ps.062098206
    • (2006) Protein Sci , vol.15 , pp. 1115-1126
    • André, N.1    Cherouati, N.2    Prual, C.3    Steffan, T.4    Zeder-Lutz, G.5    Magnin, T.6    Pattus, F.7    Michel, H.8    Wagner, R.9    Reinhart, C.10
  • 7
    • 84877800939 scopus 로고    scopus 로고
    • Overexpression of membrane proteins in mammalian cells for structural studies
    • doi:10.3109/09687688.2012.703703
    • Andréll J, Tate CG (2013) Overexpression of membrane proteins in mammalian cells for structural studies. Mol Membr Biol 30:52-63. doi:10.3109/09687688.2012.703703
    • (2013) Mol Membr Biol , vol.30 , pp. 52-63
    • Andréll, J.1    Tate, C.G.2
  • 8
    • 58149386641 scopus 로고    scopus 로고
    • Recent advances in artemisinin production through heterologous expression
    • doi:10.2174/092986708786242813
    • Arsenault PR, Wobbe KK, Weathers PJ (2008) Recent advances in artemisinin production through heterologous expression. Curr Med Chem 15:2886-2896. doi:10.2174/092986708786242813
    • (2008) Curr Med Chem , vol.15 , pp. 2886-2896
    • Arsenault, P.R.1    Wobbe, K.K.2    Weathers, P.J.3
  • 9
    • 76749114230 scopus 로고    scopus 로고
    • Expression of zebrafish (Danio rerio) monoamine oxidase (MAO) in Pichia pastoris: Purification and comparison with human MAO A and MAO B
    • doi:10.1016/j.pep.2010.01.005
    • Arslan BK, Edmondson DE (2010) Expression of zebrafish (Danio rerio) monoamine oxidase (MAO) in Pichia pastoris: purification and comparison with human MAO A and MAO B. Protein Expr Purif 70:290-297. doi:10.1016/j.pep.2010.01. 005
    • (2010) Protein Expr Purif , vol.70 , pp. 290-297
    • Arslan, B.K.1    Edmondson, D.E.2
  • 10
    • 79957834961 scopus 로고    scopus 로고
    • Mapping the yeast host cell response to recombinant membrane protein production: Relieving the biological bottlenecks
    • doi:10.1002/biot.201000333
    • Ashe MP, Bill RM (2011) Mapping the yeast host cell response to recombinant membrane protein production: relieving the biological bottlenecks. Biotechnol J 6:707-714. doi:10.1002/biot.201000333
    • (2011) Biotechnol J , vol.6 , pp. 707-714
    • Ashe, M.P.1    Bill, R.M.2
  • 11
    • 84872576383 scopus 로고    scopus 로고
    • 2A receptor-T4 lysozyme fusion protein: A practical route for the structure
    • doi:10.1016/B978-0-12-391861-1.00008-3
    • 2A receptor-T4 lysozyme fusion protein: a practical route for the structure. Methods Enzymol 520:175-198. doi:10.1016/B978-0-12-391861-1.00008-3
    • (2013) Methods Enzymol , vol.520 , pp. 175-198
    • Ashok, Y.1    Nanekar, R.T.2    Jaakola, V.-P.3
  • 12
    • 29444435893 scopus 로고    scopus 로고
    • Creation of GPCR-based chemical sensors by directed evolution in yeast
    • DOI 10.1093/protein/gzi069
    • Ault AD, Broach JR (2006) Creation of GPCR-based chemical sensors by directed evolution in yeast. Protein Eng Des Sel 19:1-8. doi:10.1093/protein/ gzi069 (Pubitemid 43011866)
    • (2006) Protein Engineering, Design and Selection , vol.19 , Issue.1 , pp. 1-8
    • Ault, A.D.1    Broach, J.R.2
  • 13
    • 49449108547 scopus 로고    scopus 로고
    • Characterization of four plasma membrane aquaporins in tulip petals: A putative homolog is regulated by phosphorylation
    • doi:10.1093/pcp/pcn095
    • Azad AK, Katsuhara M, Sawa Y, Ishikawa T, Shibata H (2008) Characterization of four plasma membrane aquaporins in tulip petals: a putative homolog is regulated by phosphorylation. Plant Cell Physiol 49:1196-1208. doi:10.1093/pcp/pcn095
    • (2008) Plant Cell Physiol , vol.49 , pp. 1196-1208
    • Azad, A.K.1    Katsuhara, M.2    Sawa, Y.3    Ishikawa, T.4    Shibata, H.5
  • 14
    • 65549112503 scopus 로고    scopus 로고
    • Heterologous expression of tulip petal plasma membrane aquaporins in Pichia pastoris for water channel analysis
    • doi:10.1128/AEM.02335-08
    • Azad AK, Sawa Y, Ishikawa T, Shibata H (2009) Heterologous expression of tulip petal plasma membrane aquaporins in Pichia pastoris for water channel analysis. Appl Environ Microbiol 75:2792-2797. doi:10.1128/AEM.02335-08
    • (2009) Appl Environ Microbiol , vol.75 , pp. 2792-2797
    • Azad, A.K.1    Sawa, Y.2    Ishikawa, T.3    Shibata, H.4
  • 15
    • 80054093905 scopus 로고    scopus 로고
    • Substitution of a single amino acid residue in the aromatic/arginine selectivity filter alters the transport profiles of tonoplast aquaporin homologs
    • doi:10.1016/j.bbamem.2011.09.014
    • Azad AK, Yoshikawa N, Ishikawa T, Sawa Y, Shibata H (2012) Substitution of a single amino acid residue in the aromatic/arginine selectivity filter alters the transport profiles of tonoplast aquaporin homologs. Biochim Biophys Acta 1818:1-11. doi:10.1016/j.bbamem.2011.09.014
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 1-11
    • Azad, A.K.1    Yoshikawa, N.2    Ishikawa, T.3    Sawa, Y.4    Shibata, H.5
  • 16
    • 0037450548 scopus 로고    scopus 로고
    • The expression of outer membrane proteins for crystallization
    • DOI 10.1016/S0005-2736(02)00711-3
    • Bannwarth M, Schulz GE (2003) The expression of outer membrane proteins for crystallization. Biochim Biophys Acta 1610:37-45 (Pubitemid 36173994)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1610 , Issue.1 , pp. 37-45
    • Bannwarth, M.1    Schulz, G.E.2
  • 18
    • 0036938740 scopus 로고    scopus 로고
    • Targeting and membrane-insertion of a sunflower oleosin in vitro and in Saccharomyces cerevisiae: The central hydrophobic domain contains more than one signal sequence, and directs oleosin insertion into the endoplasmic reticulum membrane using a signal anchor sequence mechanism
    • DOI 10.1007/s00425-002-0737-1
    • Beaudoin F, Napier JA (2002) Targeting and membrane-insertion of a sunflower oleosin in vitro and in Saccharomyces cerevisiae: the central hydrophobic domain contains more than one signal sequence, and directs oleosin insertion into the endoplasmic reticulum membrane using a signal anchor sequence mechanism. Planta 215:293-303. doi:10.1007/s00425-002-0737-1 (Pubitemid 36064979)
    • (2002) Planta , vol.215 , Issue.2 , pp. 293-303
    • Beaudoin, F.1    Napier, J.A.2
  • 19
    • 0033880434 scopus 로고    scopus 로고
    • In vivo targeting of a sunflower oil body protein in yeast secretory (sec) mutants
    • DOI 10.1046/j.1365-313X.2000.00769.x
    • Beaudoin F, Wilkinson BM, Stirling CJ, Napier JA (2000) In vivo targeting of a sunflower oil body protein in yeast secretory (sec) mutants. Plant J 23:159-170. doi:10.1046/j.1365-313x.2000.00769.x (Pubitemid 30597276)
    • (2000) Plant Journal , vol.23 , Issue.2 , pp. 159-170
    • Beaudoin, F.1    Wilkinson, B.M.2    Stirling, C.J.3    Napier, J.A.4
  • 20
    • 27644494426 scopus 로고    scopus 로고
    • Heterologous expression and site-directed mutagenesis of an ascorbate-reducible cytochrome b561
    • DOI 10.1016/j.abb.2005.09.006, PII S0003986105003929
    • Bérczi A, Su D, Lakshminarasimhan M, Vargas A, Asard H (2005) Heterologous expression and site-directed mutagenesis of an ascorbate-reducible cytochrome b561. Arch Biochem Biophys 443:82-92. doi:10.1016/j.abb.2005.09.006 (Pubitemid 41562329)
    • (2005) Archives of Biochemistry and Biophysics , vol.443 , Issue.1-2 , pp. 82-92
    • Berczi, A.1    Su, D.2    Lakshminarasimhan, M.3    Vargas, A.4    Asard, H.5
  • 21
    • 0041589322 scopus 로고    scopus 로고
    • Differential Regulation of nramp and irt Metal Transporter Genes in Wild Type and Iron Uptake Mutants of Tomato
    • DOI 10.1074/jbc.M301365200
    • Bereczky Z, Wang H-Y, Schubert V, Ganal M, Bauer P (2003) Differential regulation of nramp and irt metal transporter genes in wild type and iron uptake mutants of tomato. J Biol Chem 278:24697-24704. doi:10.1074/jbc.M301365200 (Pubitemid 37548626)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.27 , pp. 24697-24704
    • Bereczky, Z.1    Wang, H.-Y.2    Schubert, V.3    Ganal, M.4    Bauer, P.5
  • 23
    • 33744520321 scopus 로고    scopus 로고
    • Cytochromes P450 as versatile biocatalysts
    • doi:10.1016/j.jbiotec.2006.01.026
    • Bernhardt R (2006) Cytochromes P450 as versatile biocatalysts. J Biotechnol 124:128-145. doi:10.1016/j.jbiotec.2006.01.026
    • (2006) J Biotechnol , vol.124 , pp. 128-145
    • Bernhardt, R.1
  • 24
    • 16644366865 scopus 로고    scopus 로고
    • Pharmacological chaperone action on G-protein-coupled receptors
    • DOI 10.1016/j.coph.2004.08.001, PII S1471489204001316
    • Bernier V, Bichet DG, Bouvier M (2004) Pharmacological chaperone action on G-protein-coupled receptors. Curr Opin Pharmacol 4:528-533. doi:10.1016/j.coph.2004.08.001 (Pubitemid 40533016)
    • (2004) Current Opinion in Pharmacology , vol.4 , Issue.5 , pp. 528-533
    • Bernier, V.1    Bichet, D.G.2    Bouvier, M.3
  • 25
    • 84877835636 scopus 로고    scopus 로고
    • Potential use of potassium efflux-deficient yeast for studying trafficking signals and potassium channel functions
    • doi:10.1016/j.fob.2013.04.002
    • Bernstein JD, Okamoto Y, Kim M, Shikano S (2013) Potential use of potassium efflux-deficient yeast for studying trafficking signals and potassium channel functions. FEBS Open Bio 3:196-203. doi:10.1016/j.fob.2013.04.002
    • (2013) FEBS Open Bio , vol.3 , pp. 196-203
    • Bernstein, J.D.1    Okamoto, Y.2    Kim, M.3    Shikano, S.4
  • 27
    • 25144437063 scopus 로고    scopus 로고
    • Techniques: How to boost GPCR mutagenesis studies using yeast
    • DOI 10.1016/j.tips.2005.08.005, PII S0165614705002038
    • Beukers MW, Ijzerman AP (2005) Techniques: how to boost GPCR mutagenesis studies using yeast. Trends Pharmacol Sci 26:533-539. doi:10.1016/j.tips.2005. 08.005 (Pubitemid 41338564)
    • (2005) Trends in Pharmacological Sciences , vol.26 , Issue.10 , pp. 533-539
    • Beukers, M.W.1    Ijzerman, A.P.2
  • 28
    • 77949571450 scopus 로고    scopus 로고
    • Use of oil bodies and oleosins in recombinant protein production and other biotechnological applications
    • doi:10.1016/j.biotechadv.2010.01.001
    • Bhatla SC, Kaushik V, Yadav MK (2010) Use of oil bodies and oleosins in recombinant protein production and other biotechnological applications. Biotechnol Adv 28:293-300. doi:10.1016/j.biotechadv.2010.01.001
    • (2010) Biotechnol Adv , vol.28 , pp. 293-300
    • Bhatla, S.C.1    Kaushik, V.2    Yadav, M.K.3
  • 29
    • 84897950795 scopus 로고    scopus 로고
    • Playing catch-up with Escherichia coli: Using yeast to increase success rates in recombinant protein production experiments
    • doi:10.3389/fmicb.2014.00085
    • Bill RM (2014) Playing catch-up with Escherichia coli: using yeast to increase success rates in recombinant protein production experiments. Front Microbiol 5:85. doi:10.3389/fmicb.2014.00085
    • (2014) Front Microbiol , vol.5 , pp. 85
    • Bill, R.M.1
  • 31
    • 0036140732 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders
    • DOI 10.1038/nsb732
    • Binda C, Newton-Vinson P, Hubálek F, Edmondson DE, Mattevi A (2002) Structure of human monoamine oxidase B, a drug target for the treatment of neurological disorders. Nat Struct Biol 9:22-26. doi:10.1038/nsb732 (Pubitemid 34049174)
    • (2002) Nature Structural Biology , vol.9 , Issue.1 , pp. 22-26
    • Binda, C.1    Newton-Vinson, P.2    Hubalek, F.3    Edmondson, D.E.4    Mattevi, A.5
  • 34
    • 84873694546 scopus 로고    scopus 로고
    • Recombinant production of human Aquaporin-1 to an exceptional high membrane density in Saccharomyces cerevisiae
    • doi:10.1371/journal.pone.0056431
    • Bomholt J, Hélix-Nielsen C, Scharff-Poulsen P, Pedersen PA (2013) Recombinant production of human Aquaporin-1 to an exceptional high membrane density in Saccharomyces cerevisiae. PLoS One 8:e56431. doi:10.1371/journal. pone.0056431
    • (2013) PLoS One , vol.8
    • Bomholt, J.1    Hélix-Nielsen, C.2    Scharff-Poulsen, P.3    Pedersen, P.A.4
  • 35
    • 84859848389 scopus 로고    scopus 로고
    • Optimising yeast as a host for recombinant protein production
    • (review). doi:10.1007/978-1-61779-770-5-1
    • Bonander N, Bill RM (2012) Optimising yeast as a host for recombinant protein production (review). Methods Mol Biol 866:1-9. doi:10.1007/978-1-61779- 770-5-1
    • (2012) Methods Mol Biol , vol.866 , pp. 1-9
    • Bonander, N.1    Bill, R.M.2
  • 36
    • 22244478668 scopus 로고    scopus 로고
    • Design of improved membrane protein production experiments: Quantitation of the host response
    • DOI 10.1110/ps.051435705
    • Bonander N, Hedfalk K, Larsson C, Mostad P, Chang C, Gustafsson L, Bill RM (2005) Design of improved membrane protein production experiments: quantitation of the host response. Protein Sci 14:1729-1740. doi:10.1110/ps.051435705 (Pubitemid 40994143)
    • (2005) Protein Science , vol.14 , Issue.7 , pp. 1729-1740
    • Bonander, N.1    Hedfalk, K.2    Larsson, C.3    Mostad, P.4    Chang, C.5    Gustafsson, L.6    Bill, R.M.7
  • 38
    • 68149161029 scopus 로고    scopus 로고
    • Transport of drugs by proton-coupled peptide transporters: Pearls and pitfalls
    • doi:10.1517/17425250903042292
    • Brandsch M (2009) Transport of drugs by proton-coupled peptide transporters: pearls and pitfalls. Expert Opin Drug Metab Toxicol 5:887-905. doi:10.1517/17425250903042292
    • (2009) Expert Opin Drug Metab Toxicol , vol.5 , pp. 887-905
    • Brandsch, M.1
  • 39
    • 84864682056 scopus 로고    scopus 로고
    • Steroid biotransformations in biphasic systems with Yarrowia lipolytica expressing human liver cytochrome P450 genes
    • doi:10.1186/1475-2859-11-106
    • Braun A, Geier M, Buehler B, Schmid A, Mauersberger S, Glieder A (2012) Steroid biotransformations in biphasic systems with Yarrowia lipolytica expressing human liver cytochrome P450 genes. Microb Cell Factories 11:106. doi:10.1186/1475-2859-11-106
    • (2012) Microb Cell Factories , vol.11 , pp. 106
    • Braun, A.1    Geier, M.2    Buehler, B.3    Schmid, A.4    Mauersberger, S.5    Glieder, A.6
  • 42
    • 84878269745 scopus 로고    scopus 로고
    • Rapid expression screening of eukaryotic membrane proteins in Pichia pastoris
    • doi:10.1002/pro.2223
    • Brooks CL, Morrison M, Joanne Lemieux M (2013) Rapid expression screening of eukaryotic membrane proteins in Pichia pastoris. Protein Sci 22:425-433. doi:10.1002/pro.2223
    • (2013) Protein Sci , vol.22 , pp. 425-433
    • Brooks, C.L.1    Morrison, M.2    Joanne Lemieux, M.3
  • 43
    • 78649475176 scopus 로고    scopus 로고
    • The biosynthesis of artemisinin (Qinghaosu) and the phytochemistry of Artemisia annua L. (Qinghao)
    • doi:10.3390/molecules15117603
    • Brown GD (2010) The biosynthesis of artemisinin (Qinghaosu) and the phytochemistry of Artemisia annua L. (Qinghao). Molecules 15: 7603-7698. doi:10.3390/molecules15117603
    • (2010) Molecules , vol.15 , pp. 7603-7698
    • Brown, G.D.1
  • 44
    • 84892375464 scopus 로고    scopus 로고
    • Identification and characterization of a PutAMT1;1 gene from Puccinellia tenuiflora
    • doi:10.1371/journal.pone.0083111
    • Bu Y, Sun B, Zhou A, Zhang X, Lee I, Liu S (2013) Identification and characterization of a PutAMT1;1 gene from Puccinellia tenuiflora. PLoS One 8:e83111. doi:10.1371/journal.pone.0083111
    • (2013) PLoS One , vol.8
    • Bu, Y.1    Sun, B.2    Zhou, A.3    Zhang, X.4    Lee, I.5    Liu, S.6
  • 45
    • 77955983837 scopus 로고    scopus 로고
    • In and out of the cation pumps: P-type ATPase structure revisited
    • doi:10.1016/j.sbi.2010.06.007
    • Bublitz M, Poulsen H, Morth JP, Nissen P (2010) In and out of the cation pumps: P-type ATPase structure revisited. Curr Opin Struct Biol 20:431-439. doi:10.1016/j.sbi.2010.06.007
    • (2010) Curr Opin Struct Biol , vol.20 , pp. 431-439
    • Bublitz, M.1    Poulsen, H.2    Morth, J.P.3    Nissen, P.4
  • 46
    • 0141533196 scopus 로고    scopus 로고
    • Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast
    • DOI 10.1002/bit.10771
    • Butz JA, Niebauer RT, Robinson AS (2003) Co-expression of molecular chaperones does not improve the heterologous expression of mammalian G-protein coupled receptor expression in yeast. Biotechnol Bioeng 84:292-304. doi:10.1002/bit.10771 (Pubitemid 37221531)
    • (2003) Biotechnology and Bioengineering , vol.84 , Issue.3 , pp. 292-304
    • Butz, J.A.1    Niebauer, R.T.2    Robinson, A.S.3
  • 47
    • 33846403806 scopus 로고    scopus 로고
    • Properties and exploitation of oleosins
    • DOI 10.1016/j.biotechadv.2006.11.006, PII S0734975006001406
    • Capuano F, Beaudoin F, Napier JA, Shewry PR (2007) Properties and exploitation of oleosins. Biotechnol Adv 25:203-206. doi:10.1016/j.biotechadv. 2006.11.006 (Pubitemid 46149226)
    • (2007) Biotechnology Advances , vol.25 , Issue.2 , pp. 203-206
    • Capuano, F.1    Beaudoin, F.2    Napier, J.A.3    Shewry, P.R.4
  • 49
    • 77956203756 scopus 로고    scopus 로고
    • Purified E255L mutant SERCA1a and purified PfATP6 are sensitive to SERCA-type inhibitors but insensitive to artemisinins
    • doi:10.1074/jbc.M109.090340
    • Cardi D, Pozza A, Arnou B, Marchal E, Clausen JD, Andersen JP, Krishna S, Møller JV, le Maire M, Jaxel C (2010b) Purified E255L mutant SERCA1a and purified PfATP6 are sensitive to SERCA-type inhibitors but insensitive to artemisinins. J Biol Chem 285:26406-26416. doi:10.1074/jbc.M109.090340
    • (2010) J Biol Chem , vol.285 , pp. 26406-26416
    • Cardi, D.1    Pozza, A.2    Arnou, B.3    Marchal, E.4    Clausen, J.D.5    Andersen, J.P.6    Krishna, S.7    Møller, J.V.8    Le Maire, M.9    Jaxel, C.10
  • 51
    • 1542650842 scopus 로고    scopus 로고
    • Intensive mutational analysis of Gprotein-coupled receptors in yeast
    • doi:10.1385/1-59259-430-1:105
    • Celić A, Connelly SM, Martin NP, Dumont ME (2004) Intensive mutational analysis of Gprotein-coupled receptors in yeast. Methods Mol Biol 237:105-120. doi:10.1385/1-59259-430-1:105
    • (2004) Methods Mol Biol , vol.237 , pp. 105-120
    • Celić, A.1    Connelly, S.M.2    Martin, N.P.3    Dumont, M.E.4
  • 52
    • 84855720996 scopus 로고    scopus 로고
    • Heterologous production and characterisation of two distinct dihaem-containing membrane integral cytochrome b561 enzymes from Arabidopsis thaliana in Pichia pastoris and Escherichia coli cells
    • doi:10.1016/j.bbamem.2011.10.030
    • Cenacchi L, Busch M, Schleidt PG, Müller FG, Stumpp TVM, Mäntele W, Trost P, Lancaster CRD (2012) Heterologous production and characterisation of two distinct dihaem-containing membrane integral cytochrome b561 enzymes from Arabidopsis thaliana in Pichia pastoris and Escherichia coli cells. Biochim Biophys Acta 1818:679-688. doi:10.1016/j.bbamem.2011.10.030
    • (2012) Biochim Biophys Acta , vol.1818 , pp. 679-688
    • Cenacchi, L.1    Busch, M.2    Schleidt, P.G.3    Müller, F.G.4    Stumpp, T.V.M.5    Mäntele, W.6    Trost, P.7    Lancaster, C.R.D.8
  • 54
    • 0036669602 scopus 로고    scopus 로고
    • Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris
    • DOI 10.1016/S0958-1669(02)00330-0
    • Cereghino GPL, Cereghino JL, Ilgen C, Cregg JM (2002) Production of recombinant proteins in fermenter cultures of the yeast Pichia pastoris. Curr Opin Biotechnol 13:329-332. doi:10.1016/S0958-1669(02)00330-0 (Pubitemid 35254090)
    • (2002) Current Opinion in Biotechnology , vol.13 , Issue.4 , pp. 329-332
    • Cereghino G.P.Lin1    Cereghino, J.L.2    Ilgen, C.3    Cregg, J.M.4
  • 56
    • 77957304743 scopus 로고    scopus 로고
    • Molecular cloning of amphioxus uncoupling protein and assessment of its uncoupling activity using a yeast heterologous expression system
    • doi:10.1016/j.bbrc.2010.08.131
    • Chen K, Sun G, Lv Z, Wang C, Jiang X, Li D, Zhang C (2010a) Molecular cloning of amphioxus uncoupling protein and assessment of its uncoupling activity using a yeast heterologous expression system. Biochem Biophys Res Commun 400:701-706. doi:10.1016/j.bbrc.2010.08.131
    • (2010) Biochem Biophys Res Commun , vol.400 , pp. 701-706
    • Chen, K.1    Sun, G.2    Lv, Z.3    Wang, C.4    Jiang, X.5    Li, D.6    Zhang, C.7
  • 57
    • 77954895219 scopus 로고    scopus 로고
    • Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement
    • doi:10.1073/pnas.1000142107
    • Chen X, Wang Q, Ni F, Ma J (2010b) Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement. Proc Natl Acad Sci U S A 107:11352-11357. doi:10.1073/pnas.1000142107
    • (2010) Proc Natl Acad Sci U S A , vol.107 , pp. 11352-11357
    • Chen, X.1    Wang, Q.2    Ni, F.3    Ma, J.4
  • 58
    • 84870725271 scopus 로고    scopus 로고
    • Uncovering Arabidopsis membrane protein interactome enriched in transporters using mating-based split ubiquitin assays and classification models
    • doi:10.3389/fpls.2012.00124
    • Chen J, Lalonde S, Obrdlik P, Noorani Vatani A, Parsa SA, Vilarino C, Revuelta JL, Frommer WB, Rhee SY (2012) Uncovering Arabidopsis membrane protein interactome enriched in transporters using mating-based split ubiquitin assays and classification models. Front Plant Sci 3:124. doi:10.3389/fpls.2012.00124
    • (2012) Front Plant Sci , vol.3 , pp. 124
    • Chen, J.1    Lalonde, S.2    Obrdlik, P.3    Noorani Vatani, A.4    Parsa, S.A.5    Vilarino, C.6    Revuelta, J.L.7    Frommer, W.B.8    Rhee, S.Y.9
  • 59
    • 84860353068 scopus 로고    scopus 로고
    • Remodeling of the glycosylation pathway in the methylotrophic yeast Hansenula polymorpha to produce human hybrid-type N-glycans
    • doi:10.1007/s12275-012-2097-2
    • Cheon SA, Kim H, Oh D-B, Kwon O, Kang HA (2012) Remodeling of the glycosylation pathway in the methylotrophic yeast Hansenula polymorpha to produce human hybrid-type N-glycans. J Microbiol 50:341-348. doi:10.1007/s12275-012-2097-2
    • (2012) J Microbiol , vol.50 , pp. 341-348
    • Cheon, S.A.1    Kim, H.2    Oh, D.-B.3    Kwon, O.4    Kang, H.A.5
  • 61
    • 84880818178 scopus 로고    scopus 로고
    • Identification and functional characterization of two Δ12-fatty acid desaturases associated with essential linoleic acid biosynthesis in Physcomitrella patens
    • doi:10.1007/s10295-013-1285-3
    • Chodok P, Eiamsa-ard P, Cove DJ, Quatrano RS, Kaewsuwan S (2013) Identification and functional characterization of two Δ12-fatty acid desaturases associated with essential linoleic acid biosynthesis in Physcomitrella patens. J Ind Microbiol Biotechnol 40:901-913. doi:10.1007/s10295-013-1285-3
    • (2013) J Ind Microbiol Biotechnol , vol.40 , pp. 901-913
    • Chodok, P.1    Eiamsa-ard, P.2    Cove, D.J.3    Quatrano, R.S.4    Kaewsuwan, S.5
  • 62
    • 84890859909 scopus 로고    scopus 로고
    • 2+ channel TRPML3 specifically interacts with themammalian ATG8 homologue GATE16 to regulate autophagy
    • doi:10.1016/j.bbrc.2013.11.044
    • 2+ channel TRPML3 specifically interacts with themammalian ATG8 homologue GATE16 to regulate autophagy. Biochem Biophys Res Commun 443:56-61. doi:10.1016/j.bbrc.2013.11.044
    • (2014) Biochem Biophys Res Commun , vol.443 , pp. 56-61
    • Choi, S.1    Kim, H.J.2
  • 63
    • 1642311916 scopus 로고    scopus 로고
    • Kinetic properties of a micronutrient transporter from Pisum sativum indicate a primary function in Fe uptake from the soil
    • DOI 10.1007/s00425-003-1156-7
    • Cohen CK, Garvin DF, Kochian LV (2004) Kinetic properties of a micronutrient transporter from Pisum sativum indicate a primary function in Fe uptake from the soil. Planta 218:784-792. doi:10.1007/s00425-003-1156-7 (Pubitemid 38390498)
    • (2004) Planta , vol.218 , Issue.5 , pp. 784-792
    • Cohen, C.K.1    Garvin, D.F.2    Kochian, L.V.3
  • 64
    • 6344284868 scopus 로고    scopus 로고
    • A search for hyperglycosylation signals in yeast glycoproteins
    • DOI 10.1074/jbc.M406678200
    • Conde R, Cueva R, Pablo G, Polaina J, Larriba G (2004) A search for hyperglycosylation signals in yeast glycoproteins. J Biol Chem 279:43789-43798. doi:10.1074/jbc.M406678200 (Pubitemid 39390684)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.42 , pp. 43789-43798
    • Conde, R.1    Cueva, R.2    Pablo, G.3    Polaina, J.4    Larriba, G.5
  • 65
    • 0033753671 scopus 로고    scopus 로고
    • Recombinant protein expression in Pichia pastoris
    • doi:10.1385/MB:16:1:23
    • Cregg JM, Cereghino JL, Shi J, Higgins DR (2000) Recombinant protein expression in Pichia pastoris. Mol Biotechnol 16:23-52. doi:10.1385/MB:16:1:23
    • (2000) Mol Biotechnol , vol.16 , pp. 23-52
    • Cregg, J.M.1    Cereghino, J.L.2    Shi, J.3    Higgins, D.R.4
  • 67
    • 0033622090 scopus 로고    scopus 로고
    • G(G(olf) complements a GPA1 null mutation in Saccharomyces cerevisiae and functionally couples to the STE2 pheromone receptor
    • Crowe ML, Perry BN, Connerton IF (2000) Golf complements a GPA1 null mutation in Saccharomyces cerevisiae and functionally couples to the STE2 pheromone receptor. J Recept Signal Transduct Res 20: 61-73. doi:10.3109/10799890009150037 (Pubitemid 30123165)
    • (2000) Journal of Receptor and Signal Transduction Research , vol.20 , Issue.1 , pp. 61-73
    • Crowe, M.L.1    Perry, B.N.2    Connerton, I.F.3
  • 68
    • 0034974699 scopus 로고    scopus 로고
    • Human chymotrypsinogen B production with Pichia pastoris by integrated development of fermentation and downstream processing. Part 1. Fermentation
    • DOI 10.1021/bp000164j
    • Curvers S, Brixius P, Klauser T, Thömmes J, Weuster-Botz D, Takors R, Wandrey C (2001) Human chymotrypsinogen B production with Pichia pastoris by integrated development of fermentation and downstream processing. Part 1. Fermentation. Biotechnol Prog 17:495-502. doi:10.1021/bp000164j (Pubitemid 32532778)
    • (2001) Biotechnology Progress , vol.17 , Issue.3 , pp. 495-502
    • Curvers, S.1    Brixius, P.2    Klauser, T.3    Thommes, J.4    Weuster-Botz, D.5    Takors, R.6    Wandrey, C.7
  • 69
    • 19744376674 scopus 로고    scopus 로고
    • Biochemistry: Global topology analysis of the Escherichia coli inner membrane proteome
    • DOI 10.1126/science.1109730
    • Daley DO, Rapp M, Granseth E, Melén K, Drew D, von Heijne G (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308:1321-1323. doi:10.1126/science.1109730 (Pubitemid 40746130)
    • (2005) Science , vol.308 , Issue.5726 , pp. 1321-1323
    • Daley, D.O.1    Rapp, M.2    Granseth, E.3    Melen, K.4    Drew, D.5    Von Heijne, G.6
  • 70
    • 27644442731 scopus 로고    scopus 로고
    • Phosphorylation of aquaporin PvTIP3;1 defined by mass spectrometry and molecular modeling
    • DOI 10.1021/bi050565d
    • Daniels MJ, Yeager M (2005) Phosphorylation of aquaporin PvTIP3;1 defined by mass spectrometry and molecular modeling. Biochemistry 44:14443-14454. doi:10.1021/bi050565d (Pubitemid 41567452)
    • (2005) Biochemistry , vol.44 , Issue.44 , pp. 14443-14454
    • Daniels, M.J.1    Yeager, M.2
  • 71
    • 84859880444 scopus 로고    scopus 로고
    • Which yeast species shall I choose? Saccharomyces cerevisiae versus Pichia pastoris
    • doi:10.1007/978-1-61779-770-5-2
    • Darby RAJ, Cartwright SP, Dilworth MV, Bill RM (2012) Which yeast species shall I choose? Saccharomyces cerevisiae versus Pichia pastoris. Methods Mol Biol 866:11-23. doi:10.1007/978-1-61779-770-5-2
    • (2012) Methods Mol Biol , vol.866 , pp. 11-23
    • Darby, R.A.J.1    Cartwright, S.P.2    Dilworth, M.V.3    Bill, R.M.4
  • 72
    • 80052811600 scopus 로고    scopus 로고
    • Heterologous expression of GPCRs in fission yeast
    • doi:10.1007/978-1-61779-126-0-7
    • Davey J, Ladds G (2011) Heterologous expression of GPCRs in fission yeast. Methods Mol Biol 746:113-131. doi:10.1007/978-1-61779-126-0-7
    • (2011) Methods Mol Biol , vol.746 , pp. 113-131
    • Davey, J.1    Ladds, G.2
  • 75
    • 77955558145 scopus 로고    scopus 로고
    • Engineering of glycosylation in yeast and other fungi: Current state and perspectives
    • doi:10.1007/s00253-010-2721-1
    • De Pourcq K, De Schutter K, Callewaert N (2010) Engineering of glycosylation in yeast and other fungi: current state and perspectives. Appl Microbiol Biotechnol 87:1617-1631. doi: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
  • 77
    • 68649111197 scopus 로고    scopus 로고
    • Heterologous expression of olfactory receptors for targeted chemosensing
    • doi:10.1111/j.1749-6632.2009.04374.x
    • Dhanasekaran DN, Radhika V, Proikas-Cezanne T, Jayaraman M, Ha J (2009) Heterologous expression of olfactory receptors for targeted chemosensing. Ann N Y Acad Sci 1170:157-160. doi:10.1111/j.1749-6632.2009.04374.x
    • (2009) Ann N Y Acad Sci , vol.1170 , pp. 157-160
    • Dhanasekaran, D.N.1    Radhika, V.2    Proikas-Cezanne, T.3    Jayaraman, M.4    Ha, J.5
  • 78
    • 0041315728 scopus 로고    scopus 로고
    • Acyl carriers used as substrates by the desaturases and elongases involved in very long-chain polyunsaturated fatty acids biosynthesis reconstituted in yeast
    • DOI 10.1074/jbc.M305990200
    • Domergue F, Abbadi A, Ott C, Zank TK, Zähringer U, Heinz E (2003a) Acyl carriers used as substrates by the desaturases and elongases involved in very long-chain polyunsaturated fatty acids biosynthesis reconstituted in yeast. J Biol Chem 278:35115-35126. doi:10.1074/jbc.M305990200 (Pubitemid 37102275)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.37 , pp. 35115-35126
    • Domergue, F.1    Abbadi, A.2    Ott, C.3    Zank, T.K.4    Zahringer, U.5    Heinz, E.6
  • 79
    • 0037392456 scopus 로고    scopus 로고
    • New insight into Phaeodactylum tricornutum fatty acid metabolism. Cloning and functional characterization of plastidial and microsomal delta12-fatty acid desaturases
    • doi:10.1104/pp. 102.018317
    • Domergue F, Spiekermann P, Lerchl J, Beckmann C, Kilian O, Kroth PG, Boland W, Zähringer U, Heinz E (2003b) New insight into Phaeodactylum tricornutum fatty acid metabolism. Cloning and functional characterization of plastidial and microsomal delta12-fatty acid desaturases. Plant Physiol 131:1648-1660. doi:10.1104/pp. 102.018317
    • (2003) Plant Physiol , vol.131 , pp. 1648-1660
    • Domergue, F.1    Spiekermann, P.2    Lerchl, J.3    Beckmann, C.4    Kilian, O.5    Kroth, P.G.6    Boland, W.7    Zähringer, U.8    Heinz, E.9
  • 80
    • 0031587763 scopus 로고    scopus 로고
    • Expression and functional characterization of the mammalian intestinal peptide transporter PepT1 in the methylotropic yeast Pichia pastoris
    • DOI 10.1006/bbrc.1997.6351
    • Döring F, Theis S, Daniel H (1997) Expression and functional characterization of the mammalian intestinal peptide transporter PepT1 in the methylotropic yeast Pichia pastoris. Biochem Biophys Res Commun 232:656-662. doi:10.1006/bbrc.1997.6351 (Pubitemid 27214053)
    • (1997) Biochemical and Biophysical Research Communications , vol.232 , Issue.3 , pp. 656-662
    • Doring, F.1    Theis, S.2    Daniel, H.3
  • 81
    • 0031819814 scopus 로고    scopus 로고
    • Expression of the mammalian renal peptide transporter PEPT2 in the yeast Pichia pastoris and applications of the yeast system for functional analysis
    • Döring F, Michel T, Rösel A, Nickolaus M, Daniel H (1998a) Expression of the mammalian renal peptide transporter PEPT2 in the yeast Pichia pastoris and applications of the yeast system for functional analysis. Mol Membr Biol 15:79-88 (Pubitemid 28391077)
    • (1998) Molecular Membrane Biology , vol.15 , Issue.2 , pp. 79-88
    • Doring, F.1    Michel, T.2    Rosel, A.3    Nickolaus, M.4    Daniel, H.5
  • 82
    • 2642602528 scopus 로고    scopus 로고
    • Delta-aminolevulinic acid transport by intestinal and renal peptide transporters and its physiological and clinical implications
    • Döring F, Walter J, Will J, Föcking M, Boll M, Amasheh S, Clauss W, Daniel H (1998b) Delta-aminolevulinic acid transport by intestinal and renal peptide transporters and its physiological and clinical implications. J Clin Invest 101:2761-2767. doi:10.1172/JCI1909 (Pubitemid 28294585)
    • (1998) Journal of Clinical Investigation , vol.101 , Issue.12 , pp. 2761-2767
    • Doring, F.1    Walter, J.2    Will, J.3    Focking, M.4    Boll, M.5    Amasheh, S.6    Clauss, W.7    Daniel, H.8
  • 83
    • 30344441840 scopus 로고    scopus 로고
    • Uncoupling protein 1 affects the yeast mitoproteome and oxygen free radical production
    • DOI 10.1016/j.freeradbiomed.2005.08.024, PII S0891584905004831
    • Douette P, Gerkens P, Navet R, Leprince P, De Pauw E, Sluse FE (2006) Uncoupling protein 1 affects the yeast mitoproteome and oxygen free radical production. Free Radic Biol Med 40:303-315. doi:10.1016/j.freeradbiomed.2005.08. 024 (Pubitemid 43069354)
    • (2006) Free Radical Biology and Medicine , vol.40 , Issue.2 , pp. 303-315
    • Douette, P.1    Gerkens, P.2    Navet, R.3    Leprince, P.4    De Pauw, E.5    Sluse, F.E.6
  • 84
    • 67650410457 scopus 로고    scopus 로고
    • Yeast assays for G protein-coupled receptors
    • doi:10.1007/978-1-60327- 317-6-15
    • Dowell SJ, Brown AJ (2009) Yeast assays for G protein-coupled receptors. Methods Mol Biol 552:213-229. doi:10.1007/978-1-60327- 317-6-15
    • (2009) Methods Mol Biol , vol.552 , pp. 213-229
    • Dowell, S.J.1    Brown, A.J.2
  • 85
    • 15044342928 scopus 로고    scopus 로고
    • Efficient conversion of 11-deoxycortisol to cortisol (hydrocortisone) by recombinant fission yeast Schizosaccharomyces pombe
    • DOI 10.1016/j.femsyr.2004.12.001, Fungal Physiology, Moving Towards Fungal Physionomics
    • Drǎgan C-A, Zearo S, Hannemann F, Bernhardt R, Bureik M (2005) Efficient conversion of 11-deoxycortisol to cortisol (hydrocortisone) by recombinant fission yeast Schizosaccharomyces pombe. FEMS Yeast Res 5:621-625. doi:10.1016/j.femsyr.2004.12.001 (Pubitemid 40380701)
    • (2005) FEMS Yeast Research , vol.5 , Issue.6-7 , pp. 621-625
    • Dragan, C.-A.1    Zearo, S.2    Hannemann, F.3    Bernhardt, R.4    Bureik, M.5
  • 86
    • 76549089845 scopus 로고    scopus 로고
    • N-terminal chimaeras with signal sequences enhance the functional expression and alter the subcellular localization of heterologous membrane-bound inorganic pyrophosphatases in yeast
    • doi:10.1042/BJ20091491
    • Drake R, Serrano A, Pérez-Castiñeira JR (2010) N-terminal chimaeras with signal sequences enhance the functional expression and alter the subcellular localization of heterologous membrane-bound inorganic pyrophosphatases in yeast. Biochem J 426:147-157. doi:10.1042/BJ20091491
    • (2010) Biochem J , vol.426 , pp. 147-157
    • Drake, R.1    Serrano, A.2    Pérez-Castiñeira, J.R.3
  • 87
    • 84859856454 scopus 로고    scopus 로고
    • Large-scale production of membrane proteins in Saccharomyces cerevisiae: Using a green fluorescent protein fusion strategy in the production of membrane proteins
    • doi:10.1007/978-1-61779-770-5-18
    • Drew D, Kim H (2012a) Large-scale production of membrane proteins in Saccharomyces cerevisiae: using a green fluorescent protein fusion strategy in the production of membrane proteins. Methods Mol Biol 866:209-216. doi:10.1007/978-1-61779-770-5-18
    • (2012) Methods Mol Biol , vol.866 , pp. 209-216
    • Drew, D.1    Kim, H.2
  • 88
    • 84859859308 scopus 로고    scopus 로고
    • Optimizing Saccharomyces cerevisiae induction regimes
    • doi:10.1007/978-1-61779-770-5-16
    • Drew D, Kim H (2012b) Optimizing Saccharomyces cerevisiae induction regimes. Methods Mol Biol 866:191-195. doi:10.1007/978-1-61779-770-5-16
    • (2012) Methods Mol Biol , vol.866 , pp. 191-195
    • Drew, D.1    Kim, H.2
  • 89
    • 84859821910 scopus 로고    scopus 로고
    • Screening for high-yielding Saccharomyces cerevisiae clones: Using a green fluorescent protein fusion strategy in the production of membrane proteins
    • doi:10.1007/978-1-61779-770-5-8
    • Drew D, Kim H (2012c) Screening for high-yielding Saccharomyces cerevisiae clones: using a green fluorescent protein fusion strategy in the production of membrane proteins. Methods Mol Biol 866:75-86. doi:10.1007/978-1-61779-770-5-8
    • (2012) Methods Mol Biol , vol.866 , pp. 75-86
    • Drew, D.1    Kim, H.2
  • 91
    • 43149098999 scopus 로고    scopus 로고
    • GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae
    • DOI 10.1038/nprot.2008.44, PII NPROT.2008.44
    • Drew D, Newstead S, Sonoda Y, Kim H, von Heijne G, Iwata S (2008) GFP-based optimization scheme for the overexpression and purification of eukaryotic membrane proteins in Saccharomyces cerevisiae. Nat Protoc 3:784-798. doi:10.1038/nprot.2008.44 (Pubitemid 351639023)
    • (2008) Nature Protocols , vol.3 , Issue.5 , pp. 784-798
    • Drew, D.1    Newstead, S.2    Sonoda, Y.3    Kim, H.4    Von, H.G.5    Iwata, S.6
  • 92
    • 0035029264 scopus 로고    scopus 로고
    • Two iron-regulated cation transporters from tomato complement metal uptake-deficient yeast mutants
    • DOI 10.1023/A:1010620012803
    • Eckhardt U, Mas Marques A, Buckhout TJ (2001) Two iron-regulated cation transporters from tomato complement metal uptake-deficient yeast mutants. Plant Mol Biol 45:437-448 (Pubitemid 32382756)
    • (2001) Plant Molecular Biology , vol.45 , Issue.4 , pp. 437-448
    • Eckhardt, U.1    Mas, M.A.2    Buckhout, T.J.3
  • 93
    • 11244254935 scopus 로고    scopus 로고
    • Transcriptional responses to glucose at different glycolytic rates in Saccharomyces cerevisiae
    • DOI 10.1111/j.1432-1033.2004.04451.x
    • Elbing K, Ståhlberg A, Hohmann S, Gustafsson L (2004) Transcriptional responses to glucose at different glycolytic rates in Saccharomyces cerevisiae. Eur J Biochem 271:4855-4864. doi:10.1111/j.1432-1033. 2004.04451.x (Pubitemid 40065588)
    • (2004) European Journal of Biochemistry , vol.271 , Issue.23-24 , pp. 4855-4864
    • Elbing, K.1    Stahlberg, A.2    Hohmann, S.3    Gustafsson, L.4
  • 94
    • 84875953307 scopus 로고    scopus 로고
    • Detergent screening and purification of the human liver ABC transporters BSEP (ABCB11) and MDR3 (ABCB4) expressed in the yeast Pichia pastoris
    • doi:10.1371/journal.pone.0060620
    • Ellinger P, Kluth M, Stindt J, Smits SHJ, Schmitt L (2013) Detergent screening and purification of the human liver ABC transporters BSEP (ABCB11) and MDR3 (ABCB4) expressed in the yeast Pichia pastoris. PLoS One 8:e60620. doi:10.1371/journal.pone.0060620
    • (2013) PLoS One , vol.8
    • Ellinger, P.1    Kluth, M.2    Stindt, J.3    Smits, S.H.J.4    Schmitt, L.5
  • 96
    • 42549149753 scopus 로고    scopus 로고
    • The endogenous adrenodoxin reductase-like flavoprotein arh1 supports heterologous cytochrome P450-dependent substrate conversions in Schizosaccharomyces pombe
    • DOI 10.1111/j.1567-1364.2008.00360.x
    • Ewen KM, Schiffler B, Uhlmann-Schiffler H, Bernhardt R, Hannemann F (2008) The endogenous adrenodoxin reductase-like flavoprotein arh1 supports heterologous cytochrome P450-dependent substrate conversions in Schizosaccharomyces pombe. FEMS Yeast Res 8: 432-441. doi:10.1111/j.1567-1364. 2008.00360.x (Pubitemid 351579660)
    • (2008) FEMS Yeast Research , vol.8 , Issue.3 , pp. 432-441
    • Ewen, K.M.1    Schiffler, B.2    Uhlmann-Schiffler, H.3    Bernhardt, R.4    Hannemann, F.5
  • 97
    • 77954583237 scopus 로고    scopus 로고
    • Increasing cell biomass in Saccharomyces cerevisiae increases recombinant protein yield: The use of a respiratory strain as a microbial cell factory
    • doi:10.1186/1475-2859-9-47
    • Ferndahl C, Bonander N, Logez C, Wagner R, Gustafsson L, Larsson C, Hedfalk K, Darby RAJ, Bill RM (2010) Increasing cell biomass in Saccharomyces cerevisiae increases recombinant protein yield: the use of a respiratory strain as a microbial cell factory. Microb Cell Factories 9:47. doi:10.1186/1475-2859- 9-47
    • (2010) Microb Cell Factories , vol.9 , pp. 47
    • Ferndahl, C.1    Bonander, N.2    Logez, C.3    Wagner, R.4    Gustafsson, L.5    Larsson, C.6    Hedfalk, K.7    Darby, R.A.J.8    Bill, R.M.9
  • 98
    • 15044365159 scopus 로고    scopus 로고
    • Hydrophobic substrate utilisation by the yeast Yarrowia lipolytica, and its potential applications
    • DOI 10.1016/j.femsyr.2004.09.004, Fungal Physiology, Moving Towards Fungal Physionomics
    • Fickers P, Benetti P-H, Waché Y, Marty A, Mauersberger S, Smit MS, Nicaud J-M (2005) Hydrophobic substrate utilisation by the yeast Yarrowia lipolytica, and its potential applications. FEMS Yeast Res 5:527-543. doi:10.1016/j.femsyr.2004.09.004 (Pubitemid 40385096)
    • (2005) FEMS Yeast Research , vol.5 , Issue.6-7 , pp. 527-543
    • Fickers, P.1    Benetti, P.-H.2    Wache, Y.3    Marty, A.4    Mauersberger, S.5    Smit, M.S.6    Nicaud, J.-M.7
  • 99
    • 0034176255 scopus 로고    scopus 로고
    • Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: High-yield expression and purification of human P-glycoprotein
    • DOI 10.1006/abbi.2000.1712
    • Figler RA, Omote H, Nakamoto RK, Al-Shawi MK (2000) Use of chemical chaperones in the yeast Saccharomyces cerevisiae to enhance heterologous membrane protein expression: high-yield expression and purification of human P-glycoprotein. Arch Biochem Biophys 376:34-46. doi:10.1006/abbi.2000.1712 (Pubitemid 30205112)
    • (2000) Archives of Biochemistry and Biophysics , vol.376 , Issue.1 , pp. 34-46
    • Figler, R.A.1    Omote, H.2    Nakamoto, R.K.3    Al-Shawi, M.K.4
  • 100
    • 33644893341 scopus 로고    scopus 로고
    • Heterologous expression of mammalian Na/H antiporters in Saccharomyces cerevisiae
    • doi:10.1016/j.bbagen.2006.01.014
    • Flegelova H, Haguenauer-Tsapis R, Sychrova H (2006) Heterologous expression of mammalian Na/H antiporters in Saccharomyces cerevisiae. Biochim Biophys Acta 1760:504-516. doi:10.1016/j.bbagen.2006.01.014
    • (2006) Biochim Biophys Acta , vol.1760 , pp. 504-516
    • Flegelova, H.1    Haguenauer-Tsapis, R.2    Sychrova, H.3
  • 101
    • 3342901760 scopus 로고    scopus 로고
    • A rapid in vitro screening for delivery of peptide-derived peptidase inhibitors as potential drug candidates via epithelial peptide transporters
    • DOI 10.1124/jpet.104.066480
    • Foltz M, Meyer A, Theis S, Demuth H-U, Daniel H (2004) A rapid in vitro screening for delivery of peptide-derived peptidase inhibitors as potential drug candidates via epithelial peptide transporters. J Pharmacol Exp Ther 310:695-702. doi:10.1124/jpet.104.066480 (Pubitemid 38988915)
    • (2004) Journal of Pharmacology and Experimental Therapeutics , vol.310 , Issue.2 , pp. 695-702
    • Foltz, M.1    Meyer, A.2    Theis, S.3    Demuth, H.-U.4    Daniel, H.5
  • 102
    • 33747780439 scopus 로고    scopus 로고
    • Expression and functional purification of a glycosylation deficient version of the human adenosine 2a receptor for structural studies
    • doi:10.1016/j.pep.2006.03.006
    • Fraser NJ (2006) Expression and functional purification of a glycosylation deficient version of the human adenosine 2a receptor for structural studies. Protein Expr Purif 49:129-137. doi:10.1016/j.pep.2006.03.006
    • (2006) Protein Expr Purif , vol.49 , pp. 129-137
    • Fraser, N.J.1
  • 103
    • 74549181271 scopus 로고    scopus 로고
    • Tuning microbial hosts for membrane protein production
    • doi:10.1186/1475-2859-8-69
    • Freigassner M, Pichler H, Glieder A (2009) Tuning microbial hosts for membrane protein production. Microb Cell Factories 8:69. doi:10.1186/1475-2859- 8-69
    • (2009) Microb Cell Factories , vol.8 , pp. 69
    • Freigassner, M.1    Pichler, H.2    Glieder, A.3
  • 106
    • 33747375103 scopus 로고    scopus 로고
    • Inositol induces a profound alteration in the pattern and rate of synthesis and turnover of membrane lipids in Saccharomyces cerevisiae
    • doi:10.1074/jbc.M603548200
    • Gaspar ML, Aregullin MA, Jesch SA, Henry SA (2006) Inositol induces a profound alteration in the pattern and rate of synthesis and turnover of membrane lipids in Saccharomyces cerevisiae. J Biol Chem 281:22773-22785. doi:10.1074/jbc.M603548200
    • (2006) J Biol Chem , vol.281 , pp. 22773-22785
    • Gaspar, M.L.1    Aregullin, M.A.2    Jesch, S.A.3    Henry, S.A.4
  • 107
    • 84883531464 scopus 로고    scopus 로고
    • Functional genomics indicates yeast requires Golgi/ER transport, chromatin remodeling, and DNA repair for low dose DMSO tolerance
    • doi:10.3389/fgene.2013.00154
    • Gaytán BD, Loguinov AV, De La Rosa VY, Lerot J-M, Vulpe CD (2013) Functional genomics indicates yeast requires Golgi/ER transport, chromatin remodeling, and DNA repair for low dose DMSO tolerance. Front Genet 4:154. doi:10.3389/fgene.2013.00154
    • (2013) Front Genet , vol.4 , pp. 154
    • Gaytán, B.D.1    Loguinov, A.V.2    De La Rosa, V.Y.3    Lerot, J.-M.4    Vulpe, C.D.5
  • 108
    • 84868633712 scopus 로고    scopus 로고
    • Production of human cytochrome P450 2D6 drug metabolites with recombinant microbes - A comparative study
    • doi:10.1002/biot.201200187
    • Geier M, Braun A, Emmerstorfer A, Pichler H, Glieder A (2012) Production of human cytochrome P450 2D6 drug metabolites with recombinant microbes - a comparative study. Biotechnol J 7:1346-1358. doi:10.1002/biot.201200187
    • (2012) Biotechnol J , vol.7 , pp. 1346-1358
    • Geier, M.1    Braun, A.2    Emmerstorfer, A.3    Pichler, H.4    Glieder, A.5
  • 109
    • 27644574423 scopus 로고    scopus 로고
    • New yeast expression platforms based on methylotrophic Hansenula polymorpha and Pichia pastoris and on dimorphic Arxula adeninivorans and Yarrowia lipolytica - A comparison
    • DOI 10.1016/j.femsyr.2005.06.004, PII S1567135605001169
    • Gellissen G, Kunze G, Gaillardin C, Cregg JM, Berardi E, Veenhuis M, van der Klei I (2005a) New yeast expression platforms based on methylotrophic Hansenula polymorpha and Pichia pastoris and on dimorphic Arxula adeninivorans and Yarrowia lipolytica - a comparison. FEMS Yeast Res 5:1079-1096. doi:10.1016/j.femsyr.2005.06.004 (Pubitemid 41564061)
    • (2005) FEMS Yeast Research , vol.5 , Issue.11 , pp. 1079-1096
    • Gellissen, G.1    Kunze, G.2    Gaillardin, C.3    Cregg, J.M.4    Berardi, E.5    Veenhuis, M.6    Van Der, K.I.7
  • 112
    • 84862626383 scopus 로고    scopus 로고
    • Biosynthesis and purification of human beta2-adrenergic receptor expressed in methylotrophic yeast Pichia pastoris
    • doi:10.1134/S0026893312020057
    • Gerasimov AS, Zeǐnalov OA, Él'darov MA, Shul'ga AA (2012) Biosynthesis and purification of human beta2-adrenergic receptor expressed in methylotrophic yeast Pichia pastoris. Mol Biol (Mosk) 46:308-316. doi:10.1134/S0026893312020057
    • (2012) Mol Biol (Mosk) , vol.46 , pp. 308-316
    • Gerasimov, A.S.1    Zeǐnalov, O.A.2    Él'darov, M.A.3    Shul'ga, A.A.4
  • 114
    • 84877343772 scopus 로고    scopus 로고
    • Pichia pastoris: A recombinant microfactory for antibodies and human membrane proteins
    • doi:10.4014/jmb.1210.10063
    • Gonçalves AM, Pedro AQ, Maia C, Sousa F, Queiroz JA, Passarinha LA (2013) Pichia pastoris: a recombinant microfactory for antibodies and human membrane proteins. J Microbiol Biotechnol 23:587-601. doi:10.4014/jmb.1210.10063
    • (2013) J Microbiol Biotechnol , vol.23 , pp. 587-601
    • Gonçalves, A.M.1    Pedro, A.Q.2    Maia, C.3    Sousa, F.4    Queiroz, J.A.5    Passarinha, L.A.6
  • 115
    • 0141794536 scopus 로고    scopus 로고
    • A novel yeast expression system for the overproduction of quality-controlled membrane proteins
    • DOI 10.1016/S0014-5793(03)00952-9
    • Griffith DA, Delipala C, Leadsham J, Jarvis SM, Oesterhelt D (2003) A novel yeast expression system for the overproduction of quality-controlled membrane proteins. FEBS Lett 553:45-50. doi:10.1016/S0014-5793(03)00952-9 (Pubitemid 37206322)
    • (2003) FEBS Letters , vol.553 , Issue.1-2 , pp. 45-50
    • Griffith, D.A.1    Delipala, C.2    Leadsham, J.3    Jarvis, S.M.4    Oesterhelt, D.5
  • 116
    • 33749546643 scopus 로고    scopus 로고
    • + channel Kir2.1
    • DOI 10.1074/jbc.M602439200
    • Grishin A, Li H, Levitan ES, Zaks-Makhina E (2006) Identification of gamma-aminobutyric acid receptor-interacting factor 1 (TRAK2) as a trafficking factor for the K+ channel Kir2.1. J Biol Chem 281:30104-30111. doi:10.1074/jbc.M602439200 (Pubitemid 44537018)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.40 , pp. 30104-30111
    • Grishin, A.1    Li, H.2    Levitan, E.S.3    Zaks-Makhina, E.4
  • 117
    • 33746813576 scopus 로고    scopus 로고
    • Understanding recombinant expression of membrane proteins
    • doi:10.1016/j.copbio.2006.06.001
    • Grisshammer R (2006) Understanding recombinant expression of membrane proteins. Curr Opin Biotechnol 17:337-340. doi:10.1016/j.copbio.2006.06.001
    • (2006) Curr Opin Biotechnol , vol.17 , pp. 337-340
    • Grisshammer, R.1
  • 118
    • 0029142564 scopus 로고
    • Overexpression of integral membrane proteins for structural studies
    • doi:10.1017/S0033583500003504
    • Grisshammer R, Tate CG (1995) Overexpression of integral membrane proteins for structural studies. Q Rev Biophys 28:315-422. doi:10.1017/ S0033583500003504
    • (1995) Q Rev Biophys , vol.28 , pp. 315-422
    • Grisshammer, R.1    Tate, C.G.2
  • 119
    • 1542376711 scopus 로고    scopus 로고
    • Production of the human D2S receptor in the methylotrophic yeast P. pastoris
    • doi:10.1080/10606820490279466
    • Grünewald S, Haase W, Molsberger E, Michel H, Reiländer H (2004) Production of the human D2S receptor in the methylotrophic yeast P. pastoris. Receptors Channels 10:37-50. doi:10.1080/10606820490279466
    • (2004) Receptors Channels , vol.10 , pp. 37-50
    • Grünewald, S.1    Haase, W.2    Molsberger, E.3    Michel, H.4    Reiländer, H.5
  • 120
    • 0038507099 scopus 로고    scopus 로고
    • Liver-specific deletion of the NADPH-cytochrome P450 reductase gene. Impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase
    • DOI 10.1074/jbc.M303125200
    • Gu J, Weng Y, Zhang Q-Y, Cui H, Behr M, Wu L, Yang W, Zhang L, Ding X (2003) Liver-specific deletion of the NADPH-cytochrome P450 reductase gene: impact on plasma cholesterol homeostasis and the function and regulation of microsomal cytochrome P450 and heme oxygenase. J Biol Chem 278:25895-25901. doi:10.1074/jbc.M303125200 (Pubitemid 36835351)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.28 , pp. 25895-25901
    • Gu, J.1    Weng, Y.2    Zhang, Q.-Y.3    Cui, H.4    Behr, M.5    Wu, L.6    Yang, W.7    Zhang, L.8    Ding, X.9
  • 121
    • 84887934896 scopus 로고    scopus 로고
    • Characterization of AMT-mediated high-affinity ammonium uptake in roots of maize (Zea mays L.)
    • doi:10.1093/pcp/pct099
    • Gu R, Duan F, An X, Zhang F, von Wirén N, Yuan L (2013) Characterization of AMT-mediated high-affinity ammonium uptake in roots of maize (Zea mays L.). Plant Cell Physiol 54:1515-1524. doi:10.1093/pcp/pct099
    • (2013) Plant Cell Physiol , vol.54 , pp. 1515-1524
    • Gu, R.1    Duan, F.2    An, X.3    Zhang, F.4    Von Wirén, N.5    Yuan, L.6
  • 122
    • 77954040576 scopus 로고    scopus 로고
    • The HAC1 gene from Pichia pastoris: Characterization and effect of its overexpression on the production of secreted, surface displayed and membrane proteins
    • doi:10.1186/1475-2859-9-49
    • Guerfal M, Ryckaert S, Jacobs PP, Ameloot P, Van Craenenbroeck K, Derycke R, Callewaert N (2010) The HAC1 gene from Pichia pastoris: characterization and effect of its overexpression on the production of secreted, surface displayed and membrane proteins. Microb Cell Factories 9:49. doi:10.1186/1475-2859-9-49
    • (2010) Microb Cell Factories , vol.9 , pp. 49
    • Guerfal, M.1    Ryckaert, S.2    Jacobs, P.P.3    Ameloot, P.4    Van Craenenbroeck, K.5    Derycke, R.6    Callewaert, N.7
  • 123
    • 84889799543 scopus 로고    scopus 로고
    • Enhanced membrane protein expression by engineering increased intracellular membrane production
    • doi:10.1186/1475-2859-12-122
    • Guerfal M, Claes K, Knittelfelder O, De Rycke R, Kohlwein SD, Callewaert N (2013) Enhanced membrane protein expression by engineering increased intracellular membrane production. Microb Cell Factories 12:122. doi:10.1186/1475-2859-12-122
    • (2013) Microb Cell Factories , vol.12 , pp. 122
    • Guerfal, M.1    Claes, K.2    Knittelfelder, O.3    De Rycke, R.4    Kohlwein, S.D.5    Callewaert, N.6
  • 124
    • 37349007629 scopus 로고    scopus 로고
    • Coexpression of redox partners increases the hydrocortisone (cortisol) production efficiency in CYP11B1 expressing fission yeast Schizosaccharomyces pombe
    • DOI 10.1016/j.jbiotec.2007.06.022, PII S0168165607009625
    • Hakki T, Zearo S, Drǎgan C-A, Bureik M, Bernhardt R (2008) Coexpression of redox partners increases the hydrocortisone (cortisol) production efficiency in CYP11B1 expressing fission yeast Schizosaccharomyces pombe. J Biotechnol 133:351-359. doi:10.1016/j.jbiotec.2007.06.022 (Pubitemid 350299594)
    • (2008) Journal of Biotechnology , vol.133 , Issue.3 , pp. 351-359
    • Hakki, T.1    Zearo, S.2    Dragan, C.-A.3    Bureik, M.4    Bernhardt, R.5
  • 125
    • 84872672644 scopus 로고    scopus 로고
    • Tunable nano-oleosomes derived from engineered Yarrowia lipolytica
    • doi:10.1002/bit.24761
    • Han Z, Madzak C, Su WW (2013) Tunable nano-oleosomes derived from engineered Yarrowia lipolytica. Biotechnol Bioeng 110:702-710. doi:10.1002/bit.24761
    • (2013) Biotechnol Bioeng , vol.110 , pp. 702-710
    • Han, Z.1    Madzak, C.2    Su, W.W.3
  • 129
    • 84875987246 scopus 로고    scopus 로고
    • Neutral phospholipids stimulate Na, K-ATPase activity: A specific lipidprotein interaction
    • doi:10.1074/jbc.M112.446997
    • Haviv H, Habeck M, Kanai R, Toyoshima C, Karlish SJD (2013) Neutral phospholipids stimulate Na, K-ATPase activity: a specific lipidprotein
    • (2013) J Biol Chem , vol.288 , pp. 10073-10081
    • Haviv, H.1    Habeck, M.2    Kanai, R.3    Toyoshima, C.4    Karlish, S.J.D.5
  • 130
    • 35748948975 scopus 로고    scopus 로고
    • In and out of the ER: Protein folding, quality control, degradation, and related human diseases
    • DOI 10.1152/physrev.00050.2006
    • Hebert DN, Molinari M (2007) In and out of the ER: protein folding, quality control, degradation, and related human diseases. Physiol Rev 87:1377-1408. doi:10.1152/physrev.00050.2006 (Pubitemid 350041473)
    • (2007) Physiological Reviews , vol.87 , Issue.4 , pp. 1377-1408
    • Hebert, D.N.1    Molinari, M.2
  • 132
    • 84887530043 scopus 로고    scopus 로고
    • Further advances in the production of membrane proteins in Pichia pastoris
    • doi:10.4161/bioe.23886
    • Hedfalk K (2013) Further advances in the production of membrane proteins in Pichia pastoris. Bioengineered 4:363-367. doi:10.4161/bioe.23886
    • (2013) Bioengineered , vol.4 , pp. 363-367
    • Hedfalk, K.1
  • 133
    • 0037790603 scopus 로고    scopus 로고
    • Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase
    • DOI 10.1074/jbc.M212087200
    • Henderson CJ, Otto DME, Carrie D, Magnuson MA, McLaren AW, Rosewell I, Wolf CR (2003) Inactivation of the hepatic cytochrome P450 system by conditional deletion of hepatic cytochrome P450 reductase. J Biol Chem 278:13480-13486. doi:10.1074/jbc.M212087200 (Pubitemid 36800122)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.15 , pp. 13480-13486
    • Henderson, C.J.1    Otto, D.M.E.2    Carrie, D.3    Magnuson, M.A.4    McLaren, A.W.5    Rosewell, I.6    Wolf, C.R.7
  • 134
    • 20444369212 scopus 로고    scopus 로고
    • Molecular cloning and characterization of genes encoding two microsomal oleate desaturases (FAD2) from olive
    • doi: 10.1016/j.phytochem.2005.04.004
    • Hernández ML, Mancha M, Martínez-Rivas JM (2005) Molecular cloning and characterization of genes encoding two microsomal oleate desaturases (FAD2) from olive. Phytochemistry 66:1417-1426. doi: 10.1016/j.phytochem.2005. 04.004
    • (2005) Phytochemistry , vol.66 , pp. 1417-1426
    • Hernández, M.L.1    Mancha, M.2    Martínez-Rivas, J.M.3
  • 135
    • 67649756756 scopus 로고    scopus 로고
    • + antiporter AtNHX1 conferring increased salt tolerance in yeast: The endosome/prevacuolar compartment is a target for salt toxicity
    • doi:10.1074/jbc.M806203200
    • + antiporter AtNHX1 conferring increased salt tolerance in yeast: the endosome/prevacuolar compartment is a target for salt toxicity. J Biol Chem 284:14276-14285. doi:10.1074/jbc.M806203200
    • (2009) J Biol Chem , vol.284 , pp. 14276-14285
    • Hernández, A.1    Jiang, X.2    Cubero, B.3    Nieto, P.M.4    Bressan, R.A.5    Hasegawa, P.M.6    Pardo, J.M.7
  • 137
    • 84881096190 scopus 로고    scopus 로고
    • Generation of functional antibodies for mammalian membrane protein crystallography
    • doi:10.1016/j.sbi.2013.04.007
    • Hino T, Iwata S, Murata T (2013) Generation of functional antibodies for mammalian membrane protein crystallography. Curr Opin Struct Biol 23:563-568. doi:10.1016/j.sbi.2013.04.007
    • (2013) Curr Opin Struct Biol , vol.23 , pp. 563-568
    • Hino, T.1    Iwata, S.2    Murata, T.3
  • 138
    • 84885955436 scopus 로고    scopus 로고
    • A novel cholesterol-producing Pichia pastoris strain is an ideal host for functional expression of human Na, K-ATPase α3β1 isoform
    • doi:10.1007/s00253-013-5156-7
    • Hirz M, Richter G, Leitner E, Wriessnegger T, Pichler H (2013) A novel cholesterol-producing Pichia pastoris strain is an ideal host for functional expression of human Na, K-ATPase α3β1 isoform. Appl Microbiol Biotechnol 97:9465-9478. doi:10.1007/s00253-013-5156-7
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 9465-9478
    • Hirz, M.1    Richter, G.2    Leitner, E.3    Wriessnegger, T.4    Pichler, H.5
  • 140
    • 68449104172 scopus 로고    scopus 로고
    • Developing a scalable model of recombinant protein yield from Pichia pastoris: The influence of culture conditions, biomass and induction regime
    • doi:10.1186/1475-2859-8-35
    • Holmes WJ, Darby RA, Wilks MD, Smith R, Bill RM (2009) Developing a scalable model of recombinant protein yield from Pichia pastoris: the influence of culture conditions, biomass and induction regime. Microb Cell Factories 8:35. doi:10.1186/1475-2859-8-35
    • (2009) Microb Cell Factories , vol.8 , pp. 35
    • Holmes, W.J.1    Darby, R.A.2    Wilks, M.D.3    Smith, R.4    Bill, R.M.5
  • 142
    • 84870655957 scopus 로고    scopus 로고
    • Crystal structure of the calcium release-activated calcium channel Orai
    • doi:10.1126/science.1228757
    • Hou X, Pedi L, Diver MM, Long SB (2012) Crystal structure of the calcium release-activated calcium channel Orai. Science 338:1308-1313. doi:10.1126/science.1228757
    • (2012) Science , vol.338 , pp. 1308-1313
    • Hou, X.1    Pedi, L.2    Diver, M.M.3    Long, S.B.4
  • 144
    • 27844436560 scopus 로고    scopus 로고
    • Specific protein-lipid interactions in membrane proteins
    • doi:10.1042/BST20050938
    • Hunte C (2005) Specific protein-lipid interactions in membrane proteins. Biochem Soc Trans 33:938-942. doi:10.1042/BST20050938
    • (2005) Biochem Soc Trans , vol.33 , pp. 938-942
    • Hunte, C.1
  • 145
    • 79952572657 scopus 로고    scopus 로고
    • Modification of yeast characteristics by soy peptides: Cultivation with soy peptides represses the formation of lipid bodies
    • doi:10.1007/s00253-010-3001-9
    • Ikeda K, Kitagawa S, Tada T, Iefuji H, Inoue Y, Izawa S (2011) Modification of yeast characteristics by soy peptides: cultivation with soy peptides represses the formation of lipid bodies. Appl Microbiol Biotechnol 89:1971-1977. doi:10.1007/s00253-010-3001-9
    • (2011) Appl Microbiol Biotechnol , vol.89 , pp. 1971-1977
    • Ikeda, K.1    Kitagawa, S.2    Tada, T.3    Iefuji, H.4    Inoue, Y.5    Izawa, S.6
  • 146
    • 28544442229 scopus 로고    scopus 로고
    • OsZIP4, a novel zinc-regulated zinc transporter in rice
    • DOI 10.1093/jxb/eri317, The Multi-Country Evaluation of Integrated Management of Childhood Illness (IMCI) Effectiveness, Cost and Impact
    • Ishimaru Y, Suzuki M, Kobayashi T, Takahashi M, Nakanishi H, Mori S, Nishizawa NK (2005) OsZIP4, a novel zinc-regulated zinc transporter in rice. J Exp Bot 56:3207-3214. doi:10.1093/jxb/eri317 (Pubitemid 41746670)
    • (2005) Journal of Experimental Botany , vol.56 , Issue.422 , pp. 3207-3214
    • Ishimaru, Y.1    Suzuki, M.2    Kobayashi, T.3    Takahashi, M.4    Nakanishi, H.5    Mori, S.6    Nishizawa, N.K.7
  • 147
    • 33748288240 scopus 로고    scopus 로고
    • Functional analysis of skunk cabbage SfUCPB, a unique uncoupling protein lacking the fifth transmembrane domain, in yeast cells
    • DOI 10.1016/j.bbrc.2006.08.058, PII S0006291X06018560
    • Ito K, Matsukawa K, Kato Y (2006) Functional analysis of skunk cabbage SfUCPB, a unique uncoupling protein lacking the fifth transmembrane domain, in yeast cells. Biochem Biophys Res Commun 349:383-390. doi:10.1016/j.bbrc.2006.08. 058 (Pubitemid 44331803)
    • (2006) Biochemical and Biophysical Research Communications , vol.349 , Issue.1 , pp. 383-390
    • Ito, K.1    Matsukawa, K.2    Kato, Y.3
  • 148
    • 84859074173 scopus 로고    scopus 로고
    • Soy peptides enhance heterologous membrane protein productivity during the exponential growth phase of Saccharomyces cerevisiae
    • doi:10.1271/bbb.110965
    • Ito K, Hikida A, Kitagawa S, Misaka T, Abe K, Kawarasaki Y (2012) Soy peptides enhance heterologous membrane protein productivity during the exponential growth phase of Saccharomyces cerevisiae. Biosci Biotechnol Biochem 76:628-631. doi:10.1271/bbb.110965
    • (2012) Biosci Biotechnol Biochem , vol.76 , pp. 628-631
    • Ito, K.1    Hikida, A.2    Kitagawa, S.3    Misaka, T.4    Abe, K.5    Kawarasaki, Y.6
  • 150
    • 84888101258 scopus 로고    scopus 로고
    • Expression of oleosin and perilipins in yeast promotes formation of lipid droplets from the endoplasmic reticulum
    • doi:10.1242/jcs.131896
    • Jacquier N, Mishra S, Choudhary V, Schneiter R (2013) Expression of oleosin and perilipins in yeast promotes formation of lipid droplets from the endoplasmic reticulum. J Cell Sci 126:5198-5209. doi:10.1242/jcs.131896
    • (2013) J Cell Sci , vol.126 , pp. 5198-5209
    • Jacquier, N.1    Mishra, S.2    Choudhary, V.3    Schneiter, R.4
  • 151
    • 0037430841 scopus 로고    scopus 로고
    • Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes
    • DOI 10.1016/S0168-1656(03)00003-8
    • Jahic M, Gustavsson M, Jansen A-K, Martinelle M, Enfors S-O (2003a) Analysis and control of proteolysis of a fusion protein in Pichia pastoris fed-batch processes. J Biotechnol 102:45-53. doi:10.1016/S0168-1656(03)00003-8 (Pubitemid 36369202)
    • (2003) Journal of Biotechnology , vol.102 , Issue.1 , pp. 45-53
    • Jahic, M.1    Gustavsson, M.2    Jansen, A.-K.3    Martinelle, M.4    Enfors, S.-O.5
  • 152
    • 2942627936 scopus 로고    scopus 로고
    • Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures
    • doi:10.1186/1475-2859-2-6
    • Jahic M, Wallberg F, Bollok M, Garcia P, Enfors S-O (2003b) Temperature limited fed-batch technique for control of proteolysis in Pichia pastoris bioreactor cultures. Microb Cell Factories 2:6. doi:10.1186/1475-2859-2-6
    • (2003) Microb Cell Factories , vol.2 , pp. 6
    • Jahic, M.1    Wallberg, F.2    Bollok, M.3    Garcia, P.4    Enfors, S.-O.5
  • 153
    • 84901736406 scopus 로고    scopus 로고
    • Single cell synchrotron FT-IR microspectroscopy reveals a link between neutral lipid and storage carbohydrate fluxes in S. cerevisiae
    • Jamme F, Vindigni J-D, Méchin V, Cherifi T, Chardot T, Froissard M (2013) Single cell synchrotron FT-IR microspectroscopy reveals a link between neutral lipid and storage carbohydrate fluxes in S. cerevisiae. PLoS One 8:e74421
    • (2013) PLoS One , vol.8
    • Jamme, F.1    Vindigni, J.-D.2    Méchin, V.3    Cherifi, T.4    Chardot, T.5    Froissard, M.6
  • 156
    • 33744491058 scopus 로고    scopus 로고
    • Expression in yeast and purification of a membrane protein, SERCA1a, using a biotinylated acceptor domain
    • DOI 10.1016/j.pep.2006.03.001, PII S1046592806000751
    • Jidenko M, Lenoir G, Fuentes JM, leMaire M, Jaxel C (2006) Expression in yeast and purification of a membrane protein, SERCA1a, using a biotinylated acceptor domain. Protein Expr Purif 48:32-42. doi:10.1016/j.pep.2006.03.001 (Pubitemid 43796217)
    • (2006) Protein Expression and Purification , vol.48 , Issue.1 , pp. 32-42
    • Jidenko, M.1    Lenoir, G.2    Fuentes, J.M.3    Maire, M.L.4    Jaxel, C.5
  • 157
    • 84867883248 scopus 로고    scopus 로고
    • Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans
    • doi:10.1038/nature11448
    • Jin MS, Oldham ML, Zhang Q, Chen J (2012) Crystal structure of the multidrug transporter P-glycoprotein from Caenorhabditis elegans. Nature 490:566-569. doi:10.1038/nature11448
    • (2012) Nature , vol.490 , pp. 566-569
    • Jin, M.S.1    Oldham, M.L.2    Zhang, Q.3    Chen, J.4
  • 159
  • 161
    • 0037468462 scopus 로고    scopus 로고
    • Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris
    • DOI 10.1016/S0014-5793(03)00082-6
    • Karlsson M, Fotiadis D, Sjvall S, Johansson I, Hedfalk K, Engel A, Kjellbom P (2003) Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris. FEBS Lett 537:68-72. doi:10.1016/S0014-5793(03)00082-6 (Pubitemid 36246678)
    • (2003) FEBS Letters , vol.537 , Issue.1-3 , pp. 68-72
    • Karlsson, M.1    Fotiadis, D.2    Sjovall, S.3    Johansson, I.4    Hedfalk, K.5    Engel, A.6    Kjellbom, P.7
  • 162
    • 33646011258 scopus 로고    scopus 로고
    • Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins
    • doi:10.1016/j.str.2006.01.013
    • Kawate T, Gouaux E (2006) Fluorescence-detection size-exclusion chromatography for precrystallization screening of integral membrane proteins. Structure 14:673-681. doi:10.1016/j.str.2006.01.013
    • (2006) Structure , vol.14 , pp. 673-681
    • Kawate, T.1    Gouaux, E.2
  • 163
    • 84864366272 scopus 로고    scopus 로고
    • The structure and catalytic cycle of a sodium-pumping pyrophosphatase
    • doi:10.1126/science.1222505
    • Kellosalo J, Kajander T, Kogan K, Pokharel K, Goldman A (2012) The structure and catalytic cycle of a sodium-pumping pyrophosphatase. Science 337:473-476. doi:10.1126/science.1222505
    • (2012) Science , vol.337 , pp. 473-476
    • Kellosalo, J.1    Kajander, T.2    Kogan, K.3    Pokharel, K.4    Goldman, A.5
  • 164
    • 48249132926 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells
    • doi:10.1146/annurev.biophys.37.032807.125842
    • Kerppola TK (2008) Bimolecular fluorescence complementation (BiFC) analysis as a probe of protein interactions in living cells. Annu Rev Biophys 37:465-487. doi:10.1146/annurev.biophys.37.032807.125842
    • (2008) Annu Rev Biophys , vol.37 , pp. 465-487
    • Kerppola, T.K.1
  • 165
    • 1542285491 scopus 로고    scopus 로고
    • Characterization of N-linked oligosaccharides assembled on secretory recombinant glucose oxidase and cell wall mannoproteins from the methylotrophic yeast Hansenula polymorpha
    • DOI 10.1093/glycob/cwh030
    • Kim MW, Rhee SK, Kim J-Y, Shimma Y, Chiba Y, Jigami Y, Kang HA (2004) Characterization of N-linked oligosaccharides assembled on secretory recombinant glucose oxidase and cell wall mannoproteins from the methylotrophic yeast Hansenula polymorpha. Glycobiology 14:243-251. doi:10.1093/glycob/cwh030 (Pubitemid 38324940)
    • (2004) Glycobiology , vol.14 , Issue.3 , pp. 243-251
    • Kim, M.W.1    Rhee, S.K.2    Kim, J.-Y.3    Shimma, Y.-I.4    Chiba, Y.5    Jigami, Y.6    Kang, H.A.7
  • 166
    • 33646575970 scopus 로고    scopus 로고
    • Functional characterization of the Hansenula polymorpha HOC1, OCH1, and OCR1 genes as members of the yeast OCH1 mannosyltransferase family involved in protein glycosylation
    • DOI 10.1074/jbc.M508507200
    • Kim MW, Kim EJ, Kim J-Y, Park J-S, Oh D-B, Shimma Y, Chiba Y, Jigami Y, Rhee SK, Kang HA (2006) Functional characterization of the Hansenula polymorpha HOC1, OCH1, and OCR1 genes as members of the yeast OCH1 mannosyltransferase family involved in protein glycosylation. J Biol Chem 281:6261-6272. doi:10.1074/jbc.M508507200 (Pubitemid 43847557)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.10 , pp. 6261-6272
    • Moo, W.K.1    Eun, J.2    Kim, J.-Y.3    Park, J.-S.4    Oh, D.-B.5    Shimma, Y.-I.6    Chiba, Y.7    Jigami, Y.8    Sang, K.R.9    Hyun, A.K.10
  • 167
    • 0025153120 scopus 로고
    • 2-adrenergic receptor and G(s) alpha subunit
    • King K, Dohlman HG, Thorner J, Caron MG, Lefkowitz RJ (1990) Control of yeast mating signal transduction by a mammalian beta 2-adrenergic receptor and Gs alpha subunit. Science 250:121-123. doi:10.1126/science.2171146 (Pubitemid 20374972)
    • (1990) Science , vol.250 , Issue.4977 , pp. 121-123
    • King, K.1    Dohlman, H.G.2    Thorner, J.3    Caron, M.G.4    Lefkowitz, R.J.5
  • 168
    • 4444221676 scopus 로고    scopus 로고
    • From structure to disease: The evolving tale of aquaporin biology
    • DOI 10.1038/nrm1469
    • King LS, Kozono D, Agre P (2004) From structure to disease: the evolving tale of aquaporin biology. Nat Rev Mol Cell Biol 5:687-698. doi:10.1038/nrm1469 (Pubitemid 39208179)
    • (2004) Nature Reviews Molecular Cell Biology , vol.5 , Issue.9 , pp. 687-698
    • King, L.S.1    Kozono, D.2    Agre, P.3
  • 169
    • 70350460026 scopus 로고    scopus 로고
    • Crystal structure of native RPE65, the retinoid isomerase of the visual cycle
    • doi:10.1073/pnas.0906600106
    • Kiser PD, Golczak M, Lodowski DT, Chance MR, Palczewski K (2009) Crystal structure of native RPE65, the retinoid isomerase of the visual cycle. Proc Natl Acad Sci U S A 106:17325-17330. doi:10.1073/pnas.0906600106
    • (2009) Proc Natl Acad Sci U S A , vol.106 , pp. 17325-17330
    • Kiser, P.D.1    Golczak, M.2    Lodowski, D.T.3    Chance, M.R.4    Palczewski, K.5
  • 170
    • 84855984250 scopus 로고    scopus 로고
    • GPCR production in a novel yeast strain that makes cholesterol-like sterols
    • doi:10.1016/j.ymeth.2011.09.023
    • Kitson SM, Mullen W, Cogdell RJ, Bill RM, Fraser NJ (2011) GPCR production in a novel yeast strain that makes cholesterol-like sterols. Methods 55:287-292. doi:10.1016/j.ymeth.2011.09.023
    • (2011) Methods , vol.55 , pp. 287-292
    • Kitson, S.M.1    Mullen, W.2    Cogdell, R.J.3    Bill, R.M.4    Fraser, N.J.5
  • 172
    • 0036137786 scopus 로고    scopus 로고
    • Uncoupling proteins-how do they work and how are they regulated
    • doi:10.1080/15216540152845975
    • Klingenberg M (2001) Uncoupling proteins-how do they work and how are they regulated. IUBMB Life 52:175-179. doi:10.1080/15216540152845975
    • (2001) IUBMB Life , vol.52 , pp. 175-179
    • Klingenberg, M.1
  • 174
    • 31144455913 scopus 로고    scopus 로고
    • New phenotypes of functional expression of the mKir2.1 channel in potassium efflux-deficient Saccharomyces cerevisiae strains
    • DOI 10.1002/yea.1333
    • Kolacna L, Zimmermannova O, Hasenbrink G, Schwarzer S, Ludwig J, Lichtenberg-Fraté H, Sychrova H (2005) New phenotypes of functional expression of the mKir2.1 channel in potassium effluxdeficient Saccharomyces cerevisiae strains. Yeast 22:1315-1323. doi:10.1002/yea.1333 (Pubitemid 43125503)
    • (2005) Yeast , vol.22 , Issue.16 , pp. 1315-1323
    • Kolacna, L.1    Zimmermannova, O.2    Hasenbrink, G.3    Schwarzer, S.4    Ludwig, J.5    Lichtenberg-Frate, H.6    Sychrova, H.7
  • 175
    • 0033137141 scopus 로고    scopus 로고
    • The IRT1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range
    • Korshunova YO, Eide D, Clark WG, Guerinot ML, Pakrasi HB (1999) The IRT1 protein from Arabidopsis thaliana is a metal transporter with a broad substrate range. Plant Mol Biol 40:37-44
    • (1999) Plant Mol Biol , vol.40 , pp. 37-44
    • Korshunova, Y.O.1    Eide, D.2    Clark, W.G.3    Guerinot, M.L.4    Pakrasi, H.B.5
  • 176
    • 84893742390 scopus 로고    scopus 로고
    • Human papillomavirus E5 oncoproteins bind the A4 endoplasmic reticulum protein to regulate proliferative ability upon differentiation
    • doi:10.1016/j.virol.2014.01.013
    • Kotnik Halavaty K, Regan J, Mehta K, Laimins L (2014) Human papillomavirus E5 oncoproteins bind the A4 endoplasmic reticulum protein to regulate proliferative ability upon differentiation. Virology 452-453:223-230. doi:10.1016/j.virol.2014.01.013
    • (2014) Virology , vol.452-453 , pp. 223-230
    • Kotnik Halavaty, K.1    Regan, J.2    Mehta, K.3    Laimins, L.4
  • 178
    • 84872552572 scopus 로고    scopus 로고
    • Expression of GPCRs in Pichia pastoris for structural studies
    • doi:10.1016/B978-0-12-391861-1.00001-0
    • Krettler C, Reinhart C, Bevans CG (2013) Expression of GPCRs in Pichia pastoris for structural studies. Methods Enzymol 520:1-29. doi:10.1016/B978-0- 12-391861-1.00001-0
    • (2013) Methods Enzymol , vol.520 , pp. 1-29
    • Krettler, C.1    Reinhart, C.2    Bevans, C.G.3
  • 179
    • 0035910270 scopus 로고    scopus 로고
    • Predicting transmembrane protein topology with a hidden Markov model: Application to complete genomes
    • DOI 10.1006/jmbi.2000.4315
    • Krogh A, Larsson B, von Heijne G, Sonnhammer EL (2001) Predicting transmembrane protein topology with a hidden Markov model: application to complete genomes. J Mol Biol 305:567-580. doi:10.1006/jmbi.2000.4315 (Pubitemid 33032862)
    • (2001) Journal of Molecular Biology , vol.305 , Issue.3 , pp. 567-580
    • Krogh, A.1    Larsson, B.2    Von Heijne, G.3    Sonnhammer, E.L.L.4
  • 180
    • 0029052099 scopus 로고
    • High yield expression of functionally active human liver CYP2D6 in yeast cells
    • Krynetski EY, Drutsa VL, Kovaleva IE, Luzikov VN (1995) High yield expression of functionally active human liver CYP2D6 in yeast cells. Pharmacogenetics 5:103-109
    • (1995) Pharmacogenetics , vol.5 , pp. 103-109
    • Krynetski, E.Y.1    Drutsa, V.L.2    Kovaleva, I.E.3    Luzikov, V.N.4
  • 181
    • 0037241864 scopus 로고    scopus 로고
    • Modified yeast cells to investigate the coupling of G protein-coupled receptors to specific G proteins
    • DOI 10.1046/j.1365-2958.2003.03336.x
    • Ladds G, Davis K, Hillhouse EW, Davey J (2003) Modified yeast cells to investigate the coupling of G protein-coupled receptors to specific G proteins. Mol Microbiol 47:781-792. doi:10.1046/j.1365-2958.2003.03336.x (Pubitemid 36114985)
    • (2003) Molecular Microbiology , vol.47 , Issue.3 , pp. 781-792
    • Ladds, G.1    Davis, K.2    Hillhouse, E.W.3    Davey, J.4
  • 182
    • 20644449483 scopus 로고    scopus 로고
    • Functional analysis of heterologous GPCR signalling pathways in yeast
    • DOI 10.1016/j.tibtech.2005.05.007, PII S0167779905001356
    • Ladds G, Goddard A, Davey J (2005) Functional analysis of heterologous GPCR signalling pathways in yeast. Trends Biotechnol 23:367-373. doi:10.1016/j.tibtech.2005.05.007 (Pubitemid 40835767)
    • (2005) Trends in Biotechnology , vol.23 , Issue.7 , pp. 367-373
    • Ladds, G.1    Goddard, A.2    Davey, J.3
  • 184
    • 7044241302 scopus 로고    scopus 로고
    • How lipids affect the activities of integral membrane proteins
    • doi:10.1016/j.bbamem.2004.05.012
    • Lee AG (2004) How lipids affect the activities of integral membrane proteins. Biochim Biophys Acta 1666:62-87. doi:10.1016/j.bbamem.2004.05.012
    • (2004) Biochim Biophys Acta , vol.1666 , pp. 62-87
    • Lee, A.G.1
  • 185
    • 77958155470 scopus 로고    scopus 로고
    • Comparative functional genomics of stress responses in yeasts
    • doi:10.1089/omi.2010.0029
    • Lelandais G, Devaux F (2010) Comparative functional genomics of stress responses in yeasts. OMICS 14:501-515. doi:10.1089/omi.2010.0029
    • (2010) OMICS , vol.14 , pp. 501-515
    • Lelandais, G.1    Devaux, F.2
  • 186
    • 84879311801 scopus 로고    scopus 로고
    • Stabilizing the heterologously expressed uric acid-xanthine transporter UapA from the lower eukaryote Aspergillus nidulans
    • doi:10.3109/09687688.2012.690572
    • Leung J, Cameron AD, Diallinas G, Byrne B (2013) Stabilizing the heterologously expressed uric acid-xanthine transporter UapA from the lower eukaryote Aspergillus nidulans. Mol Membr Biol 30:32-42. doi:10.3109/09687688. 2012.690572
    • (2013) Mol Membr Biol , vol.30 , pp. 32-42
    • Leung, J.1    Cameron, A.D.2    Diallinas, G.3    Byrne, B.4
  • 187
    • 0035996741 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase A in Pichia pastoris: Comparison with the enzyme expressed in Saccharomyces cerevisiae
    • DOI 10.1006/prep.2001.1546
    • Li M, Hubálek F, Newton-Vinson P, Edmondson DE (2002) High-level expression of human liver monoamine oxidase A in Pichia pastoris: comparison with the enzyme expressed in Saccharomyces cerevisiae. Protein Expr Purif 24:152-162. doi:10.1006/prep.2001.1546 (Pubitemid 34805422)
    • (2002) Protein Expression and Purification , vol.24 , Issue.1 , pp. 152-162
    • Li, M.1    Hubalek, F.2    Newton-Vinson, P.3    Edmondson, D.E.4
  • 188
    • 35348920624 scopus 로고    scopus 로고
    • Molecular cloning and characterization of a novel microsomal oleate desaturase gene from soybean
    • DOI 10.1016/j.jplph.2006.08.007, PII S0176161706002434
    • Li L, Wang X, Gai J, Yu D (2007) Molecular cloning and characterization of a novel microsomal oleate desaturase gene from soybean. J Plant Physiol 164:1516-1526. doi:10.1016/j.jplph.2006.08.007 (Pubitemid 47576477)
    • (2007) Journal of Plant Physiology , vol.164 , Issue.11 , pp. 1516-1526
    • Li, L.1    Wang, X.2    Gai, J.3    Yu, D.4
  • 190
    • 84900449189 scopus 로고    scopus 로고
    • Refined structures of mouse P-glycoprotein
    • doi:10.1002/pro.2387
    • Li J, Jaimes KF, Aller SG (2014) Refined structures of mouse P-glycoprotein. Protein Sci 23:34-46. doi:10.1002/pro.2387
    • (2014) Protein Sci , vol.23 , pp. 34-46
    • Li, J.1    Jaimes, K.F.2    Aller, S.G.3
  • 191
    • 84856001167 scopus 로고    scopus 로고
    • Crystallization chaperone strategies for membrane proteins
    • doi:10.1016/j.ymeth.2011.08.004
    • Lieberman RL, Culver JA, Entzminger KC, Pai JC, Maynard JA (2011) Crystallization chaperone strategies for membrane proteins. Methods 55:293-302. doi:10.1016/j.ymeth.2011.08.004
    • (2011) Methods , vol.55 , pp. 293-302
    • Lieberman, R.L.1    Culver, J.A.2    Entzminger, K.C.3    Pai, J.C.4    Maynard, J.A.5
  • 193
    • 14844321947 scopus 로고    scopus 로고
    • 561 expressed in insect and yeast cell systems
    • DOI 10.1016/j.pep.2004.12.027
    • Liu W, Kamensky Y, Kakkar R, Foley E, Kulmacz RJ, Palmer G (2005) Purification and characterization of bovine adrenal cytochrome b561 expressed in insect and yeast cell systems. Protein Expr Purif 40:429-439. doi:10.1016/j.pep.2004.12.027 (Pubitemid 40335928)
    • (2005) Protein Expression and Purification , vol.40 , Issue.2 , pp. 429-439
    • Liu, W.1    Kamensky, Y.2    Kakkar, R.3    Foley, E.4    Kulmacz, R.J.5    Palmer, G.6
  • 195
    • 23244441222 scopus 로고    scopus 로고
    • Voltage sensor of Kv1.2: Structural basis of electromechanical coupling
    • DOI 10.1126/science.1116270
    • Long SB, Campbell EB, Mackinnon R (2005a) Voltage sensor of Kv1.2: structural basis of electromechanical coupling. Science 309:903-908. doi:10.1126/science.1116270 (Pubitemid 41099920)
    • (2005) Science , vol.309 , Issue.5736 , pp. 903-908
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 196
    • 23244456428 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1126/science.1116269
    • Long SB, Campbell EB, Mackinnon R (2005b) Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 309:897-903. doi:10.1126/science.1116269 (Pubitemid 41099919)
    • (2005) Science , vol.309 , Issue.5736 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    MacKinnon, R.3
  • 197
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • doi:10.1038/nature06265
    • + channel in a lipid membrane-like environment. Nature 450:376-382. doi:10.1038/nature06265
    • (2007) Nature , vol.450 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 199
    • 1842474296 scopus 로고    scopus 로고
    • Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors
    • DOI 10.1016/j.jmb.2004.02.032, PII S0022283604001998
    • Ma J, Yoshimura M, Yamashita E, Nakagawa A, Ito A, Tsukihara T (2004) Structure of rat monoamine oxidase A and its specific recognitions for substrates and inhibitors. J Mol Biol 338:103-114. doi:10.1016/j.jmb.2004.02.032 (Pubitemid 38429789)
    • (2004) Journal of Molecular Biology , vol.338 , Issue.1 , pp. 103-114
    • Ma, J.1    Yoshimura, M.2    Yamashita, E.3    Nakagawa, A.4    Ito, A.5    Tsukihara, T.6
  • 200
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • DOI 10.1002/yea.1208
    • Macauley-Patrick S, Fazenda ML, McNeil B, Harvey LM (2005) Heterologous protein production using the Pichia pastoris expression system. Yeast 22:249-270. doi:10.1002/yea.1208 (Pubitemid 40528349)
    • (2005) Yeast , vol.22 , Issue.4 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 202
    • 33845755468 scopus 로고    scopus 로고
    • Arabidopsis thaliana CHX17 gene complements the kha1 deletion phenotypes in Saccharomyces cerevisiae
    • DOI 10.1002/yea.1424
    • Maresova L, Sychrova H (2006) Arabidopsis thaliana CHX17 gene complements the kha1 deletion phenotypes in Saccharomyces cerevisiae. Yeast 23:1167-1171. doi:10.1002/yea.1424 (Pubitemid 46002047)
    • (2006) Yeast , vol.23 , Issue.16 , pp. 1167-1171
    • Maresova, L.1    Sychrova, H.2
  • 203
    • 80051785290 scopus 로고    scopus 로고
    • Evidence that prokineticin receptor 2 exists as a dimer in vivo
    • doi:10.1007/s00018-010-0601-6
    • Marsango S, Bonaccorsi di Patti MC, Barra D, Miele R (2011) Evidence that prokineticin receptor 2 exists as a dimer in vivo. Cell Mol Life Sci 68:2919-2929. doi:10.1007/s00018-010-0601-6
    • (2011) Cell Mol Life Sci , vol.68 , pp. 2919-2929
    • Marsango, S.1    Bonaccorsi Di Patti, M.C.2    Barra, D.3    Miele, R.4
  • 205
    • 84871197528 scopus 로고    scopus 로고
    • Functional fusions of T4 lysozyme in the third intracellular loop of a G protein-coupled receptor identified by a random screening approach in yeast
    • doi:10.1093/protein/gzs070
    • Mathew E, Ding F-X, Naider F, Dumont ME (2013) Functional fusions of T4 lysozyme in the third intracellular loop of a G protein-coupled receptor identified by a random screening approach in yeast. Protein Eng Des Sel 26:59-71. doi:10.1093/protein/gzs070
    • (2013) Protein Eng des Sel , vol.26 , pp. 59-71
    • Mathew, E.1    Ding, F.-X.2    Naider, F.3    Dumont, M.E.4
  • 206
    • 4544253524 scopus 로고    scopus 로고
    • Stress in recombinant protein producing yeasts
    • DOI 10.1016/j.jbiotec.2004.04.035, PII S0168165604003104
    • Mattanovich D, Gasser B, Hohenblum H, Sauer M (2004) Stress in recombinant protein producing yeasts. J Biotechnol 113:121-135. doi:10.1016/j.jbiotec.2004.04.035 (Pubitemid 39237075)
    • (2004) Journal of Biotechnology , vol.113 , Issue.1-3 , pp. 121-135
    • Mattanovich, D.1    Gasser, B.2    Hohenblum, H.3    Sauer, M.4
  • 208
    • 0030828058 scopus 로고    scopus 로고
    • Inducible membranes in yeast: Relation to the unfolded-protein-response pathway
    • doi:10.1002/(SICI)1097-0061(199710) 13:13〈1211::AID-YEA168〉3.0. CO;2-8
    • Menzel R, Vogel F, Kärgel E, Schunck WH (1997) Inducible membranes in yeast: relation to the unfolded-protein-response pathway. Yeast 13:1211-1229. doi:10.1002/(SICI)1097-0061(199710) 13:13〈1211::AID-YEA168〉3.0.CO;2-8
    • (1997) Yeast , vol.13 , pp. 1211-1229
    • Menzel, R.1    Vogel, F.2    Kärgel, E.3    Schunck, W.H.4
  • 210
    • 36148942092 scopus 로고    scopus 로고
    • Breaking the bottleneck: Eukaryotic membrane protein expression for high-resolution structural studies
    • DOI 10.1016/j.jsb.2007.07.001, PII S1047847707001505, Electron Crystallography of Membrane Proteins
    • Midgett CR, Madden DR (2007) Breaking the bottleneck: eukaryotic membrane protein expression for high-resolution structural studies. J Struct Biol 160:265-274. doi:10.1016/j.jsb.2007.07.001 (Pubitemid 350103823)
    • (2007) Journal of Structural Biology , vol.160 , Issue.3 , pp. 265-274
    • Midgett, C.R.1    Madden, D.R.2
  • 211
    • 84856297467 scopus 로고    scopus 로고
    • Crystal structure of the human two-pore domain potassium channel K2P1
    • doi:10. 1126/science.1213274
    • Miller AN, Long SB (2012) Crystal structure of the human two-pore domain potassium channel K2P1. Science 335:432-436. doi:10. 1126/science.1213274
    • (2012) Science , vol.335 , pp. 432-436
    • Miller, A.N.1    Long, S.B.2
  • 212
    • 80054701691 scopus 로고    scopus 로고
    • 1-adrenoceptor
    • doi:10.1016/j.jmb.2011.08.057
    • 1-adrenoceptor. J Mol Biol 413:628-638. doi:10.1016/j.jmb.2011. 08.057
    • (2011) J Mol Biol , vol.413 , pp. 628-638
    • Miller, J.L.1    Tate, C.G.2
  • 213
    • 12544250956 scopus 로고    scopus 로고
    • Functional expression of olfactory receptors in yeast and development of a bioassay for odorant screening
    • doi:10.1111/j.1742-4658.2004.04494.x
    • Minic J, Persuy M-A, Godel E, Aioun J, Connerton I, Salesse R, Pajot-Augy E (2005a) Functional expression of olfactory receptors in yeast and development of a bioassay for odorant screening. FEBS J 272:524-537. doi:10.1111/j.1742- 4658.2004.04494.x
    • (2005) FEBS J , vol.272 , pp. 524-537
    • Minic, J.1    Persuy, M.-A.2    Godel, E.3    Aioun, J.4    Connerton, I.5    Salesse, R.6    Pajot-Augy, E.7
  • 214
    • 15944366921 scopus 로고    scopus 로고
    • Yeast systems as a screening tool for pharmacological assessment of G protein coupled receptors
    • DOI 10.2174/0929867053507261
    • Minic J, Sautel M, Salesse R, Pajot-Augy E (2005b) Yeast system as a screening tool for pharmacological assessment of G protein coupled receptors. Curr Med Chem 12:961-969. doi:10.2174/0929867053507261 (Pubitemid 40443850)
    • (2005) Current Medicinal Chemistry , vol.12 , Issue.8 , pp. 961-969
    • Minic, J.1    Sautel, M.2    Salesse, R.3    Pajot-Augy, E.4
  • 215
    • 0026628290 scopus 로고
    • A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins
    • Mori K, Sant A, Kohno K, Normington K, Gething MJ, Sambrook JF (1992) A 22 bp cis-acting element is necessary and sufficient for the induction of the yeast KAR2 (BiP) gene by unfolded proteins. EMBO J 11:2583-2593
    • (1992) EMBO J , vol.11 , pp. 2583-2593
    • Mori, K.1    Sant, A.2    Kohno, K.3    Normington, K.4    Gething, M.J.5    Sambrook, J.F.6
  • 216
    • 84885915525 scopus 로고    scopus 로고
    • Effect of sterol composition on the activity of the yeast G-protein-coupled receptor Ste2
    • doi:10.1007/s00253-012-4470-9
    • Morioka S, Shigemori T, Hara K, Morisaka H, Kuroda K, Ueda M (2013) Effect of sterol composition on the activity of the yeast G-protein-coupled receptor Ste2. Appl Microbiol Biotechnol 97:4013-4020. doi:10.1007/s00253-012- 4470-9
    • (2013) Appl Microbiol Biotechnol , vol.97 , pp. 4013-4020
    • Morioka, S.1    Shigemori, T.2    Hara, K.3    Morisaka, H.4    Kuroda, K.5    Ueda, M.6
  • 219
    • 0042357176 scopus 로고    scopus 로고
    • Dimethyl sulfoxide exposure facilitates phospholipid biosynthesis and cellular membrane proliferation in yeast cells
    • DOI 10.1074/jbc.M300450200
    • Murata Y, Watanabe T, Sato M, Momose Y, Nakahara T, Oka S, Iwahashi H (2003) Dimethyl sulfoxide exposure facilitates phospholipid biosynthesis and cellular membrane proliferation in yeast cells. J Biol Chem 278:33185-33193. doi:10.1074/jbc.M300450200 (Pubitemid 37055766)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.35 , pp. 33185-33193
    • Murata, Y.1    Watanabe, T.2    Sato, M.3    Momose, Y.4    Nakahara, T.5    Oka, S.-I.6    Iwahashi, H.7
  • 221
    • 84879181564 scopus 로고    scopus 로고
    • Bimolecular fluorescence complementation and interaction of various Arabidopsis major intrinsic proteins expressed in yeast
    • doi:10.1111/ppl.12000
    • Murozuka E, Hanisch S, Pomorski TG, Jahn TP, Schjoerring JK (2013) Bimolecular fluorescence complementation and interaction of various Arabidopsis major intrinsic proteins expressed in yeast. Physiol Plant 148:422-431. doi:10.1111/ppl.12000
    • (2013) Physiol Plant , vol.148 , pp. 422-431
    • Murozuka, E.1    Hanisch, S.2    Pomorski, T.G.3    Jahn, T.P.4    Schjoerring, J.K.5
  • 222
    • 84879272201 scopus 로고    scopus 로고
    • Rapid, facile detection of heterodimer partners for target human G-protein-coupled receptors using a modified split-ubiquitin membrane yeast two-hybrid system
    • doi:10.1371/journal.pone.0066793
    • Nakamura Y, Ishii J, Kondo A (2013) Rapid, facile detection of heterodimer partners for target human G-protein-coupled receptors using a modified split-ubiquitin membrane yeast two-hybrid system. PLoS One 8:e66793. doi:10.1371/journal.pone.0066793
    • (2013) PLoS One , vol.8
    • Nakamura, Y.1    Ishii, J.2    Kondo, A.3
  • 223
    • 83755181547 scopus 로고    scopus 로고
    • The thiazide-sensitive NaCl cotransporter is targeted for chaperone-dependent endoplasmic reticulum-associated degradation
    • doi:10.1074/jbc.M111.288928
    • Needham PG, Mikoluk K, Dhakarwal P, Khadem S, Snyder AC, Subramanya AR, Brodsky JL (2011) The thiazide-sensitive NaCl cotransporter is targeted for chaperone-dependent endoplasmic reticulum-associated degradation. J Biol Chem 286:43611-43621. doi:10.1074/jbc.M111.288928
    • (2011) J Biol Chem , vol.286 , pp. 43611-43621
    • Needham, P.G.1    Mikoluk, K.2    Dhakarwal, P.3    Khadem, S.4    Snyder, A.C.5    Subramanya, A.R.6    Brodsky, J.L.7
  • 224
    • 84899419571 scopus 로고    scopus 로고
    • Uncoupling of ionic currents from substrate transport in the plant ammonium transporter AtAMT1;2
    • doi:10.1074/jbc.C114.552802
    • Neuhäuser B, Ludewig U (2014) Uncoupling of ionic currents from substrate transport in the plant ammonium transporter AtAMT1;2. J Biol Chem 289:11650-11655. doi:10.1074/jbc.C114.552802
    • (2014) J Biol Chem , vol.289 , pp. 11650-11655
    • Neuhäuser, B.1    Ludewig, U.2
  • 226
  • 227
    • 0033773601 scopus 로고    scopus 로고
    • High-level expression of human liver monoamine oxidase B in Pichia pastoris
    • doi:10.1006/prep.2000.1309
    • Newton-Vinson P, Hubalek F, Edmondson DE (2000) High-level expression of human liver monoamine oxidase B in Pichia pastoris. Protein Expr Purif 20:334-345. doi:10.1006/prep.2000.1309
    • (2000) Protein Expr Purif , vol.20 , pp. 334-345
    • Newton-Vinson, P.1    Hubalek, F.2    Edmondson, D.E.3
  • 228
    • 84867632249 scopus 로고    scopus 로고
    • Yarrowia lipolytica
    • doi:10.1002/yea.2921
    • Nicaud J-M (2012) Yarrowia lipolytica. Yeast 29:409-418. doi:10.1002/yea.2921
    • (2012) Yeast , vol.29 , pp. 409-418
    • Nicaud, J.-M.1
  • 229
    • 33645415883 scopus 로고    scopus 로고
    • Exceptional total and functional yields of the human adenosine (A2a) receptor expressed in the yeast Saccharomyces cerevisiae
    • doi:10.1016/j.pep.2005.09.020
    • Niebauer RT, Robinson AS (2006) Exceptional total and functional yields of the human adenosine (A2a) receptor expressed in the yeast Saccharomyces cerevisiae. Protein Expr Purif 46:204-211. doi:10.1016/j.pep.2005.09.020
    • (2006) Protein Expr Purif , vol.46 , pp. 204-211
    • Niebauer, R.T.1    Robinson, A.S.2
  • 230
    • 84894488420 scopus 로고    scopus 로고
    • Crystal structures of leukotriene C4 synthase in complex with product analogs: Implications for the enzyme mechanism
    • doi:10.1074/jbc.M113. 534628
    • Niegowski D, Kleinschmidt T, Olsson U, Ahmad S, Rinaldo-Matthis A, Haeggström JZ (2014) Crystal structures of leukotriene C4 synthase in complex with product analogs: implications for the enzyme mechanism. J Biol Chem 289:5199-5207. doi:10.1074/jbc.M113. 534628
    • (2014) J Biol Chem , vol.289 , pp. 5199-5207
    • Niegowski, D.1    Kleinschmidt, T.2    Olsson, U.3    Ahmad, S.4    Rinaldo-Matthis, A.5    Haeggström, J.Z.6
  • 231
    • 79955746703 scopus 로고    scopus 로고
    • Increasing gene dosage greatly enhances recombinant expression of aquaporins in Pichia pastoris
    • doi:10.1186/1472-6750-11-47
    • Nordén K, Agemark M, Danielson JÅH, Alexandersson E, Kjellbom P, Johanson U (2011) Increasing gene dosage greatly enhances recombinant expression of aquaporins in Pichia pastoris. BMC Biotechnol 11:47. doi:10.1186/1472-6750-11-47
    • (2011) BMC Biotechnol , vol.11 , pp. 47
    • Nordén, K.1    Agemark, M.2    Danielson, J.3    Alexandersson, E.4    Kjellbom, P.5    Johanson, U.6
  • 232
    • 2542510763 scopus 로고    scopus 로고
    • The use of Yarrowia lipolytica for the expression of human cytochrome P450 CYP1A1
    • DOI 10.1002/yea.1127
    • Nthangeni MB, Urban P, Pompon D, Smit MS, Nicaud J-M (2004) The use of Yarrowia lipolytica for the expression of human cytochrome P450 CYP1A1. Yeast 21:583-592. doi:10.1002/yea.1127 (Pubitemid 38702115)
    • (2004) Yeast , vol.21 , Issue.7 , pp. 583-592
    • Nthangeni, M.B.1    Urban, P.2    Pompon, D.3    Smit, M.S.4    Nicaud, J.-M.5
  • 236
    • 70350509579 scopus 로고    scopus 로고
    • Progress toward heterologous expression of active G-protein-coupled receptors in Saccharomyces cerevisiae: Linking cellular stress response with translocation and trafficking
    • doi:10.1002/pro.246
    • O'Malley MA, Mancini JD, Young CL, McCusker EC, Raden D, Robinson AS (2009) Progress toward heterologous expression of active G-protein-coupled receptors in Saccharomyces cerevisiae: linking cellular stress response with translocation and trafficking. Protein Sci 18:2356-2370. doi:10.1002/pro.246
    • (2009) Protein Sci , vol.18 , pp. 2356-2370
    • O'Malley, M.A.1    Mancini, J.D.2    Young, C.L.3    McCusker, E.C.4    Raden, D.5    Robinson, A.S.6
  • 237
    • 84878928639 scopus 로고    scopus 로고
    • Recombinant production of the human aquaporins in the yeast Pichia pastoris
    • (invited review). doi:10.3109/09687688.2012.665503
    • Oberg F, Hedfalk K (2013) Recombinant production of the human aquaporins in the yeast Pichia pastoris (invited review). Mol Membr Biol 30:15-31. doi:10.3109/09687688.2012.665503
    • (2013) Mol Membr Biol , vol.30 , pp. 15-31
    • Oberg, F.1    Hedfalk, K.2
  • 238
    • 67650287112 scopus 로고    scopus 로고
    • Insight into factors directing high production of eukaryotic membrane proteins; production of 13 human AQPs in Pichia pastoris
    • doi:10.1080/09687680902862085
    • Oberg F, Ekvall M, Nyblom M, Backmark A, Neutze R, Hedfalk K (2009) Insight into factors directing high production of eukaryotic membrane proteins; production of 13 human AQPs in Pichia pastoris. Mol Membr Biol 26:215-227. doi:10.1080/09687680902862085
    • (2009) Mol Membr Biol , vol.26 , pp. 215-227
    • Oberg, F.1    Ekvall, M.2    Nyblom, M.3    Backmark, A.4    Neutze, R.5    Hedfalk, K.6
  • 239
    • 80052008858 scopus 로고    scopus 로고
    • Improving recombinant eukaryotic membrane protein yields in Pichia pastoris: The importance of codon optimization and clone selection
    • doi:10.3109/09687688.2011.602219
    • Öberg F, Sjöhamn J, Conner MT, Bill RM, Hedfalk K (2011) Improving recombinant eukaryotic membrane protein yields in Pichia pastoris: the importance of codon optimization and clone selection. Mol Membr Biol 28:398-411. doi:10.3109/09687688.2011.602219
    • (2011) Mol Membr Biol , vol.28 , pp. 398-411
    • Öberg, F.1    Sjöhamn, J.2    Conner, M.T.3    Bill, R.M.4    Hedfalk, K.5
  • 241
    • 0029328579 scopus 로고
    • Lipid biosynthesis
    • doi:10.1105/tpc.7.7.957
    • Ohlrogge J, Browse J (1995) Lipid biosynthesis. Plant Cell 7:957-970. doi:10.1105/tpc.7.7.957
    • (1995) Plant Cell , vol.7 , pp. 957-970
    • Ohlrogge, J.1    Browse, J.2
  • 242
    • 77249084638 scopus 로고    scopus 로고
    • Structural diversity of cytochrome P450 enzyme system
    • doi:10.1093/jb/mvq001
    • Omura T (2010) Structural diversity of cytochrome P450 enzyme system. J Biochem 147:297-306. doi:10.1093/jb/mvq001
    • (2010) J Biochem , vol.147 , pp. 297-306
    • Omura, T.1
  • 243
    • 0037450544 scopus 로고    scopus 로고
    • Specific lipid requirements of membrane proteins - A putative bottleneck in heterologous expression
    • DOI 10.1016/S0005-2736(02)00708-3
    • Opekarová M, Tanner W (2003) Specific lipid requirements of membrane proteins - a putative bottleneck in heterologous expression. Biochim Biophys Acta 1610:11-22. doi:10.1016/S0005-2736(02)00708-3 (Pubitemid 36173992)
    • (2003) Biochimica et Biophysica Acta - Biomembranes , vol.1610 , Issue.1 , pp. 11-22
    • Opekarova, M.1    Tanner, W.2
  • 246
    • 84855681112 scopus 로고    scopus 로고
    • The phytochelatin transporters AtABCC1 and AtABCC2 mediate tolerance to cadmium and mercury
    • doi:10.1111/j.1365-313X.2011.04789.x
    • Park J, Song W-Y, Ko D, Eom Y, Hansen TH, Schiller M, Lee TG, Martinoia E, Lee Y (2012) The phytochelatin transporters AtABCC1 and AtABCC2 mediate tolerance to cadmium and mercury. Plant J 69:278-288. doi:10.1111/j.1365-313X. 2011.04789.x
    • (2012) Plant J , vol.69 , pp. 278-288
    • Park, J.1    Song, W.-Y.2    Ko, D.3    Eom, Y.4    Hansen, T.H.5    Schiller, M.6    Lee, T.G.7    Martinoia, E.8    Lee, Y.9
  • 247
    • 84895877254 scopus 로고    scopus 로고
    • Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1
    • doi:10.1038/nature13116
    • Parker JL, Newstead S (2014) Molecular basis of nitrate uptake by the plant nitrate transporter NRT1.1. Nature 507:68-72. doi:10.1038/nature13116
    • (2014) Nature , vol.507 , pp. 68-72
    • Parker, J.L.1    Newstead, S.2
  • 248
    • 84855834314 scopus 로고    scopus 로고
    • Oleosin is bifunctional enzyme that has both monoacylglycerol acyltransferase and phospholipase activities
    • doi:10.1074/jbc.M111.309955
    • Parthibane V, Rajakumari S, Venkateshwari V, Iyappan R, Rajasekharan R (2012) Oleosin is bifunctional enzyme that has both monoacylglycerol acyltransferase and phospholipase activities. J Biol Chem 287:1946-1954. doi:10.1074/jbc.M111.309955
    • (2012) J Biol Chem , vol.287 , pp. 1946-1954
    • Parthibane, V.1    Rajakumari, S.2    Venkateshwari, V.3    Iyappan, R.4    Rajasekharan, R.5
  • 249
    • 0035370949 scopus 로고    scopus 로고
    • Intracellular signaling from the endoplasmic reticulum to the nucleus: The unfolded protein response in yeast and mammals
    • doi:10.1016/S0955-0674(00)00219-2
    • Patil C, Walter P (2001) Intracellular signaling from the endoplasmic reticulum to the nucleus: the unfolded protein response in yeast and mammals. Curr Opin Cell Biol 13:349-355. doi:10.1016/S0955-0674(00)00219-2
    • (2001) Curr Opin Cell Biol , vol.13 , pp. 349-355
    • Patil, C.1    Walter, P.2
  • 250
    • 0031543433 scopus 로고    scopus 로고
    • G-protein-coupled receptors in high-throughput screening assays for drug discovery
    • doi:10.1016/S0167-7799(97)01119-0
    • Pausch MH (1997) G-protein-coupled receptors in high-throughput screening assays for drug discovery. Trends Biotechnol 15:487-494. doi:10.1016/S0167- 7799(97)01119-0
    • (1997) Trends Biotechnol , vol.15 , pp. 487-494
    • Pausch, M.H.1
  • 251
    • 55549099272 scopus 로고    scopus 로고
    • Manganese efficiency in barley: Identification and characterization of the metal ion transporter HvIRT1
    • doi:10.1104/pp. 108.118851
    • Pedas P, Ytting CK, Fuglsang AT, Jahn TP, Schjoerring JK, Husted S (2008) Manganese efficiency in barley: identification and characterization of the metal ion transporter HvIRT1. Plant Physiol 148:455-466. doi:10.1104/pp. 108.118851
    • (2008) Plant Physiol , vol.148 , pp. 455-466
    • Pedas, P.1    Ytting, C.K.2    Fuglsang, A.T.3    Jahn, T.P.4    Schjoerring, J.K.5    Husted, S.6
  • 252
    • 63649098494 scopus 로고    scopus 로고
    • Identification and characterization of zinc-starvation-induced ZIP transporters from barley roots
    • doi:10.1016/j.plaphy.2009.01.006
    • Pedas P, Schjoerring JK, Husted S (2009) Identification and characterization of zinc-starvation-induced ZIP transporters from barley roots. Plant Physiol Biochem 47:377-383. doi:10.1016/j.plaphy.2009.01.006
    • (2009) Plant Physiol Biochem , vol.47 , pp. 377-383
    • Pedas, P.1    Schjoerring, J.K.2    Husted, S.3
  • 253
    • 0030027897 scopus 로고    scopus 로고
    • Expression in high yield of pig alpha1β1 Na,K-ATPase and inactive mutants D369N and D807N in Saccharomyces cerevisiae
    • DOI 10.1074/jbc.271.5.2514
    • Pedersen PA, Rasmussen JH, Jøorgensen PL (1996) Expression in high yield of pig α1β1 Na, K-ATPase and inactive mutants D369N and D807N in Saccharomyces cerevisiae. J Biol Chem 271:2514-2522 (Pubitemid 26047857)
    • (1996) Journal of Biological Chemistry , vol.271 , Issue.5 , pp. 2514-2522
    • Pedersen, P.A.1    Rasmussen, J.H.2    Jorgensen, P.L.3
  • 255
    • 79959716999 scopus 로고    scopus 로고
    • A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast
    • doi:10.1042/BJ20110447
    • Pérez-Castiñeira JR, Hernández A, Drake R, Serrano A (2011) A plant proton-pumping inorganic pyrophosphatase functionally complements the vacuolar ATPase transport activity and confers bafilomycin resistance in yeast. Biochem J 437:269-278. doi:10.1042/BJ20110447
    • (2011) Biochem J , vol.437 , pp. 269-278
    • Pérez-Castiñeira, J.R.1    Hernández, A.2    Drake, R.3    Serrano, A.4
  • 256
    • 0037007201 scopus 로고    scopus 로고
    • Ligands act as pharmacological chaperones and increase the efficiency of δ opioid receptor maturation
    • DOI 10.1093/emboj/21.7.1628
    • Petäjä-Repo UE, Hogue M, Bhalla S, Laperrière A, Morello J-P, Bouvier M (2002) Ligands act as pharmacological chaperones and increase the efficiency of δ-opioid receptor maturation. EMBO J 21:1628-1637. doi:10.1093/emboj/21.7.1628 (Pubitemid 34614619)
    • (2002) EMBO Journal , vol.21 , Issue.7 , pp. 1628-1637
    • Petaja-Repo, U.E.1    Hogue, M.2    Bhalla, S.3    Laperriere, A.4    Morello, J.-P.5    Bouvier, M.6
  • 257
    • 58249126709 scopus 로고    scopus 로고
    • Use of fission yeast heterologously expressing human cytochrome P450 2B6 in biotechnological synthesis of the designer drug metabolite N-(1-phenylcyclohexyl)-2-hydroxyethanamine
    • doi:10.1016/j.forsciint.2008.12.001
    • Peters FT, Dragan C-A, Schwaninger AE, Sauer C, Zapp J, Bureik M, Maurer HH (2009) Use of fission yeast heterologously expressing human cytochrome P450 2B6 in biotechnological synthesis of the designer drug metabolite N-(1-phenylcyclohexyl)-2-hydroxyethanamine. Forensic Sci Int 184:69-73. doi:10.1016/j.forsciint.2008.12.001
    • (2009) Forensic Sci Int , vol.184 , pp. 69-73
    • Peters, F.T.1    Dragan, C.-A.2    Schwaninger, A.E.3    Sauer, C.4    Zapp, J.5    Bureik, M.6    Maurer, H.H.7
  • 258
    • 84879508959 scopus 로고    scopus 로고
    • MOR is not enough: Identification of novel mu-opioid receptor interacting proteins using traditional and modified membrane yeast two-hybrid screens
    • doi:10.1371/journal.pone.0067608
    • Petko J, Justice-Bitner S, Jin J, Wong V, Kittanakom S, Ferraro TN, Stagljar I, Levenson R (2013) MOR is not enough: identification of novel mu-opioid receptor interacting proteins using traditional and modified membrane yeast two-hybrid screens. PLoS One 8:e67608. doi:10.1371/journal.pone.0067608
    • (2013) PLoS One , vol.8
    • Petko, J.1    Justice-Bitner, S.2    Jin, J.3    Wong, V.4    Kittanakom, S.5    Ferraro, T.N.6    Stagljar, I.7    Levenson, R.8
  • 259
    • 79958781958 scopus 로고    scopus 로고
    • Using yeast as a model to study membrane proteins
    • doi:10.1097/MNH.0b013e3283478611
    • Petschnigg J, Moe OW, Stagljar I (2011) Using yeast as a model to study membrane proteins. Curr Opin Nephrol Hypertens 20:425-432. doi:10.1097/MNH. 0b013e3283478611
    • (2011) Curr Opin Nephrol Hypertens , vol.20 , pp. 425-432
    • Petschnigg, J.1    Moe, O.W.2    Stagljar, I.3
  • 260
    • 84892614588 scopus 로고    scopus 로고
    • Inter-subunit interactions between glutamate-like receptors in Arabidopsis
    • doi:10.4161/psb.27034
    • Price M, Okumoto S (2013) Inter-subunit interactions between glutamate-like receptors in Arabidopsis. Plant Signal Behav 8:e27034. doi:10.4161/psb.27034
    • (2013) Plant Signal Behav , vol.8
    • Price, M.1    Okumoto, S.2
  • 261
    • 0041700130 scopus 로고    scopus 로고
    • Intracellular transport of a heterologous membrane protein, the human transferrin receptor, in Saccharomyces cerevisiae
    • Prinz B, Stahl U, Lang C (2003) Intracellular transport of a heterologous membrane protein, the human transferrin receptor, in Saccharomyces cerevisiae. Int Microbiol 6:49-55. doi:10.1007/s10123-003-0100-9 (Pubitemid 37222525)
    • (2003) International Microbiology , vol.6 , Issue.1 , pp. 49-55
    • Prinz, B.1    Stahl, U.2    Lang, C.3
  • 263
    • 79957809202 scopus 로고    scopus 로고
    • Advances in the production of membrane proteins in Pichia pastoris
    • doi:10.1002/biot.201100146
    • Ramón A, Marín M (2011) Advances in the production of membrane proteins in Pichia pastoris. Biotechnol J 6:700-706. doi:10.1002/biot.201100146
    • (2011) Biotechnol J , vol.6 , pp. 700-706
    • Ramón, A.1    Marín, M.2
  • 267
    • 0036710840 scopus 로고    scopus 로고
    • Mammalian peptide transporters as targets for drug delivery
    • DOI 10.1016/S0165-6147(02)02072-2, PII S0165614702020722
    • Rubio-Aliaga I, Daniel H (2002) Mammalian peptide transporters as targets for drug delivery. Trends Pharmacol Sci 23:434-440. doi: 10.1016/S0165-6147(02) 02072-2 (Pubitemid 35247773)
    • (2002) Trends in Pharmacological Sciences , vol.23 , Issue.9 , pp. 434-440
    • Rubio-Aliaga, I.1    Daniel, H.2
  • 268
    • 0028174726 scopus 로고
    • Expression of the human D2S dopamine receptor in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe: A comparative study
    • Sander P, Grünewald S, Reiländer H, Michel H (1994) Expression of the human D2S dopamine receptor in the yeasts Saccharomyces cerevisiae and Schizosaccharomyces pombe: a comparative study. FEBS Lett 344:41-46
    • (1994) FEBS Lett , vol.344 , pp. 41-46
    • Sander, P.1    Grünewald, S.2    Reiländer, H.3    Michel, H.4
  • 269
    • 84884780109 scopus 로고    scopus 로고
    • Deciphering activation of olfactory receptors using heterologous expression in Saccharomyces cerevisiae and bioluminescence resonance energy transfer
    • doi:10.1007/978-1-62703-377-0-11
    • Sanz G, Pajot-Augy E (2013) Deciphering activation of olfactory receptors using heterologous expression in Saccharomyces cerevisiae and bioluminescence resonance energy transfer. Methods Mol Biol 1003:149-160. doi:10.1007/978-1- 62703-377-0-11
    • (2013) Methods Mol Biol , vol.1003 , pp. 149-160
    • Sanz, G.1    Pajot-Augy, E.2
  • 270
    • 0035943688 scopus 로고    scopus 로고
    • Water and ion permeation of aquaporin-1 in planar lipid bilayers. Major differences in structural determinants and stoichiometry
    • doi:10.1074/jbc.M104267200
    • Saparov SM, Kozono D, Rothe U, Agre P, Pohl P (2001) Water and ion permeation of aquaporin-1 in planar lipid bilayers. Major differences in structural determinants and stoichiometry. J Biol Chem 276:31515-31520. doi:10.1074/jbc.M104267200
    • (2001) J Biol Chem , vol.276 , pp. 31515-31520
    • Saparov, S.M.1    Kozono, D.2    Rothe, U.3    Agre, P.4    Pohl, P.5
  • 271
    • 0036514182 scopus 로고    scopus 로고
    • Optimizing functional versus total expression of the human mu-opioid receptor in Pichia pastoris
    • DOI 10.1006/prep.2001.1564
    • Sarramegna V, Demange P, Milon A, Talmont F (2002) Optimizing functional versus total expression of the human mu-opioid receptor in Pichia pastoris. Protein Expr Purif 24:212-220. doi:10.1006/prep.2001.1564 (Pubitemid 40047437)
    • (2002) Protein Expression and Purification , vol.24 , Issue.2 , pp. 212-220
    • Sarramegna, V.1    Demange, P.2    Milon, A.3    Talmont, F.4
  • 272
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors: Comparison of expression systems from the standpoint of large-scale production and purification
    • DOI 10.1007/s00018-003-3168-7
    • Sarramegna V, Talmont F, Demange P, Milon A (2003) Heterologous expression of G-protein-coupled receptors: comparison of expression systems from the standpoint of large-scale production and purification. Cell Mol Life Sci 60:1529-1546. doi:10.1007/s00018-003-3168-7 (Pubitemid 37041353)
    • (2003) Cellular and Molecular Life Sciences , vol.60 , Issue.8 , pp. 1529-1546
    • Sarramegna, V.1    Talmont, F.2    Demange, P.3    Milon, A.4
  • 273
    • 84885061797 scopus 로고    scopus 로고
    • Saccharomyces cerevisiae-based platform for rapid production and evaluation of eukaryotic nutrient transporters and transceptors for biochemical studies and crystallography
    • doi:10.1371/journal.pone.0076851
    • Scharff-Poulsen P, Pedersen PA (2013) Saccharomyces cerevisiae-based platform for rapid production and evaluation of eukaryotic nutrient transporters and transceptors for biochemical studies and crystallography. PLoS One 8:e76851. doi:10.1371/journal.pone.0076851
    • (2013) PLoS One , vol.8
    • Scharff-Poulsen, P.1    Pedersen, P.A.2
  • 274
    • 0042530487 scopus 로고    scopus 로고
    • 3 receptor and greatly impair receptor/G protein coupling
    • DOI 10.1074/jbc.M304991200
    • Schmidt C, Li B, Bloodworth L, Erlenbacher I, Zeng FY, Wess J (2003) Random mutagenesis of the M3 muscarinic acetylcholine receptor expressed in yeast. Identification of point mutations that 'silence' a constitutively active mutant M3 receptor and greatly impair receptor/G protein coupling. J Biol Chem 278:30248-30260. doi:10.1074/jbc.M304991200 (Pubitemid 36962419)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.32 , pp. 30248-30260
    • Schmidt, C.1    Li, B.2    Bloodworth, L.3    Erlenbach, I.4    Zeng, F.-Y.5    Wess, J.6
  • 275
    • 1842587801 scopus 로고    scopus 로고
    • Applied biocatalysis for the synthesis of natural flavour compounds - Current industrial processes and future prospects
    • DOI 10.1023/B:BILE.0000019576.80594.0e
    • Schrader J, Etschmann MMW, Sell D, Hilmer JM, Rabenhorst J (2004) Applied biocatalysis for the synthesis of natural flavour compounds - current industrial processes and future prospects. Biotechnol Lett 26:463-472. doi:10.1023/B:BILE.0000019576.80594.0e (Pubitemid 38448414)
    • (2004) Biotechnology Letters , vol.26 , Issue.6 , pp. 463-472
    • Schrader, J.1    Etschmann, M.M.W.2    Sell, D.3    Hilmer, J.-M.4    Rabenhorst, J.5
  • 276
    • 42549168016 scopus 로고    scopus 로고
    • Functional expression of the voltage-gated neuronal mammalian potassium channel rat ether à go-go1 in yeast
    • DOI 10.1111/j.1567-1364.2007.00351.x
    • Schwarzer S, Kolacna L, Lichtenberg-Fraté H, Sychrova H, Ludwig J (2008) Functional expression of the voltage-gated neuronal mammalian potassium channel rat ether à go-go1 in yeast. FEMS Yeast Res 8:405-413. doi:10.1111/j.1567-1364.2007.00351.x (Pubitemid 351579651)
    • (2008) FEMS Yeast Research , vol.8 , Issue.3 , pp. 405-413
    • Schwarzer, S.1    Kolacna, L.2    Lichtenberg-Frate, H.3    Sychrova, H.4    Ludwig, J.5
  • 277
    • 0028900487 scopus 로고
    • Golgi localization in yeast is mediated by the membrane anchor region of rat liver sialyltransferase
    • doi:10.1074/jbc.270.10.5483
    • Schwientek T, Lorenz C, Ernst JF (1995) Golgi localization in yeast is mediated by the membrane anchor region of rat liver sialyltransferase. J Biol Chem 270:5483-5489. doi:10.1074/jbc.270.10.5483
    • (1995) J Biol Chem , vol.270 , pp. 5483-5489
    • Schwientek, T.1    Lorenz, C.2    Ernst, J.F.3
  • 279
    • 70350749580 scopus 로고    scopus 로고
    • Transferability of thermostabilizing mutations between β-adrenergic receptors
    • doi:10.3109/09687680903208239
    • Serrano-Vega MJ, Tate CG (2009) Transferability of thermostabilizing mutations between β-adrenergic receptors. Mol Membr Biol 26:385-396. doi:10.3109/09687680903208239
    • (2009) Mol Membr Biol , vol.26 , pp. 385-396
    • Serrano-Vega, M.J.1    Tate, C.G.2
  • 282
    • 33747714615 scopus 로고    scopus 로고
    • Heterologous expression of the benzoate para-hydroxylase encoding gene (CYP53B1) from Rhodotorula minuta by Yarrowia lipolytica
    • DOI 10.1007/s00253-005-0264-7
    • Shiningavamwe A, Obiero G, Albertyn J, Nicaud J-M, Smit M (2006) Heterologous expression of the benzoate para-hydroxylase encoding gene (CYP53B1) from Rhodotorula minuta by Yarrowia lipolytica. Appl Microbiol Biotechnol 72:323-329. doi:10.1007/s00253-005-0264-7 (Pubitemid 44273055)
    • (2006) Applied Microbiology and Biotechnology , vol.72 , Issue.2 , pp. 323-329
    • Shiningavamwe, A.1    Obiero, G.2    Albertyn, J.3    Nicaud, J.-M.4    Smit, M.5
  • 283
    • 66249147196 scopus 로고    scopus 로고
    • Crystal structure of the sodium-potassiumpump at 2.4 Å resolution
    • doi:10.1038/nature07939
    • Shinoda T, Ogawa H, Cornelius F, Toyoshima C (2009) Crystal structure of the sodium-potassiumpump at 2.4 Å resolution. Nature 459:446-450. doi:10.1038/nature07939
    • (2009) Nature , vol.459 , pp. 446-450
    • Shinoda, T.1    Ogawa, H.2    Cornelius, F.3    Toyoshima, C.4
  • 284
    • 84855989800 scopus 로고    scopus 로고
    • Production of the stable human histamine H1 receptor in Pichia pastoris for structural determination
    • doi:10.1016/j.ymeth. 2011.08.015
    • Shiroishi M, Kobayashi T, Ogasawara S, Tsujimoto H, Ikeda-Suno C, Iwata S, Shimamura T (2011) Production of the stable human histamine H1 receptor in Pichia pastoris for structural determination. Methods 55:281-286. doi:10.1016/j.ymeth. 2011.08.015
    • (2011) Methods , vol.55 , pp. 281-286
    • Shiroishi, M.1    Kobayashi, T.2    Ogasawara, S.3    Tsujimoto, H.4    Ikeda-Suno, C.5    Iwata, S.6    Shimamura, T.7
  • 286
    • 34147097998 scopus 로고    scopus 로고
    • Heterologous expression and comparative characterization of the human neuromedin U subtype II receptor using the methylotrophic yeast Pichia pastoris and mammalian cells
    • DOI 10.1016/j.biocel.2007.01.016, PII S1357272507000349
    • Shukla AK, Haase W, Reinhart C, Michel H (2007a) Heterologous expression and comparative characterization of the human neuromedin U subtype II receptor using the methylotrophic yeast Pichia pastoris and mammalian cells. Int J Biochem Cell Biol 39:931-942. doi:10.1016/j.biocel.2007.01.016 (Pubitemid 46575324)
    • (2007) International Journal of Biochemistry and Cell Biology , vol.39 , Issue.5 , pp. 931-942
    • Shukla, A.K.1    Haase, W.2    Reinhart, C.3    Michel, H.4
  • 287
    • 34547878682 scopus 로고    scopus 로고
    • 2 receptor using the methylotrophic yeast Pichia pastoris
    • DOI 10.1016/j.pep.2007.02.021, PII S1046592807000563
    • Shukla AK, Haase W, Reinhart C, Michel H (2007b) Heterologous expression and characterization of the recombinant bradykinin B2 receptor using the methylotrophic yeast Pichia pastoris. Protein Expr Purif 55:1-8. doi:10.1016/j.pep.2007.02.021 (Pubitemid 47259681)
    • (2007) Protein Expression and Purification , vol.55 , Issue.1 , pp. 1-8
    • Shukla, A.K.1    Haase, W.2    Reinhart, C.3    Michel, H.4
  • 290
    • 84859808193 scopus 로고    scopus 로고
    • Screening for high-yielding Pichia pastoris clones: The production of G protein-coupled receptors as a case study
    • doi:10.1007/978-1-61779-770-5-7
    • Singh S, Gras A, Fiez-Vandal C, Martinez M, Wagner R, Byrne B (2012a) Screening for high-yielding Pichia pastoris clones: the production of G protein-coupled receptors as a case study. Methods Mol Biol 866:65-73. doi:10.1007/978-1-61779-770-5-7
    • (2012) Methods Mol Biol , vol.866 , pp. 65-73
    • Singh, S.1    Gras, A.2    Fiez-Vandal, C.3    Martinez, M.4    Wagner, R.5    Byrne, B.6
  • 291
    • 84859879097 scopus 로고    scopus 로고
    • Large-scale production of membrane proteins in Pichia pastoris: The production of G protein-coupled receptors as a case study
    • doi:10.1007/978-1-61779-770-5-17
    • Singh S, Gras A, Fiez-Vandal C, Martinez M, Wagner R, Byrne B (2012b) Large-scale production of membrane proteins in Pichia pastoris: the production of G protein-coupled receptors as a case study. Methods Mol Biol 866:197-207. doi:10.1007/978-1-61779-770-5-17
    • (2012) Methods Mol Biol , vol.866 , pp. 197-207
    • Singh, S.1    Gras, A.2    Fiez-Vandal, C.3    Martinez, M.4    Wagner, R.5    Byrne, B.6
  • 292
    • 0034577919 scopus 로고    scopus 로고
    • Where does fission yeast sit on the tree of life?
    • doi: 10.1186/gb-2000-1-2-reviews1011
    • Sipiczki M (2000) Where does fission yeast sit on the tree of life? Genome Biol 1:REVIEWS1011. doi: 10.1186/gb-2000-1-2-reviews1011
    • (2000) Genome Biol , vol.1
    • Sipiczki, M.1
  • 295
    • 77953133721 scopus 로고    scopus 로고
    • Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins
    • doi:10.1016/j.febslet.2010.04.015
    • Sonoda Y, Cameron A, Newstead S, Omote H, Moriyama Y, Kasahara M, Iwata S, Drew D (2010) Tricks of the trade used to accelerate high-resolution structure determination of membrane proteins. FEBS Lett 584:2539-2547. doi:10.1016/j.febslet.2010.04.015
    • (2010) FEBS Lett , vol.584 , pp. 2539-2547
    • Sonoda, Y.1    Cameron, A.2    Newstead, S.3    Omote, H.4    Moriyama, Y.5    Kasahara, M.6    Iwata, S.7    Drew, D.8
  • 297
    • 80052033032 scopus 로고    scopus 로고
    • A stable yeast strain efficiently producing cholesterol instead of ergosterol is functional for tryptophan uptake, but not weak organic acid resistance
    • doi:10.1016/j.ymben.2011.06.006
    • Souza CM, Schwabe TME, Pichler H, Ploier B, Leitner E, Guan XL, Wenk MR, Riezman I, Riezman H (2011) A stable yeast strain efficiently producing cholesterol instead of ergosterol is functional for tryptophan uptake, but not weak organic acid resistance. Metab Eng 13:555-569. doi:10.1016/j.ymben.2011.06. 006
    • (2011) Metab Eng , vol.13 , pp. 555-569
    • Souza, C.M.1    Schwabe, T.M.E.2    Pichler, H.3    Ploier, B.4    Leitner, E.5    Guan, X.L.6    Wenk, M.R.7    Riezman, I.8    Riezman, H.9
  • 301
    • 77954948432 scopus 로고    scopus 로고
    • Prediction of functionally selective allosteric interactions at an M3 muscarinic acetylcholine receptor mutant using Saccharomyces cerevisiae
    • doi:10.1124/mol.110.064253
    • Stewart GD, Sexton PM, Christopoulos A (2010) Prediction of functionally selective allosteric interactions at an M3 muscarinic acetylcholine receptor mutant using Saccharomyces cerevisiae. Mol Pharmacol 78:205-214. doi:10.1124/mol.110.064253
    • (2010) Mol Pharmacol , vol.78 , pp. 205-214
    • Stewart, G.D.1    Sexton, P.M.2    Christopoulos, A.3
  • 302
    • 80052083563 scopus 로고    scopus 로고
    • Nanobody stabilization of G protein-coupled receptor conformational states
    • doi:10.1016/j.sbi.2011.06.011
    • Steyaert J, Kobilka BK (2011) Nanobody stabilization of G protein-coupled receptor conformational states. Curr Opin Struct Biol 21:567-572. doi:10.1016/j.sbi.2011.06.011
    • (2011) Curr Opin Struct Biol , vol.21 , pp. 567-572
    • Steyaert, J.1    Kobilka, B.K.2
  • 303
    • 79957845495 scopus 로고    scopus 로고
    • Heterologous overexpression and mutagenesis of the human bile salt export pump (ABCB11) using DREAM (Directed REcombination-Assisted Mutagenesis)
    • doi:10.1371/journal.pone.0020562
    • Stindt J, Ellinger P, Stross C, Keitel V, Häussinger D, Smits SHJ, Kubitz R, Schmitt L (2011) Heterologous overexpression and mutagenesis of the human bile salt export pump (ABCB11) using DREAM (Directed REcombination- Assisted Mutagenesis). PLoS One 6:e20562. doi:10.1371/journal.pone.0020562
    • (2011) PLoS One , vol.6
    • Stindt, J.1    Ellinger, P.2    Stross, C.3    Keitel, V.4    Häussinger, D.5    Smits, S.H.J.6    Kubitz, R.7    Schmitt, L.8
  • 305
    • 0035875366 scopus 로고    scopus 로고
    • A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast
    • DOI 10.1042/0264-6021:3560779
    • Stuart JA, Harper JA, Brindle KM, Jekabsons MB, Brand MD (2001) A mitochondrial uncoupling artifact can be caused by expression of uncoupling protein 1 in yeast. Biochem J 356:779-789. doi:10.1042/0264-6021:3560779 (Pubitemid 32588449)
    • (2001) Biochemical Journal , vol.356 , Issue.3 , pp. 779-789
    • Stuart, J.A.1    Harper, J.A.2    Brindle, K.M.3    Jekabsons, M.B.4    Brand, M.D.5
  • 306
    • 34547471030 scopus 로고    scopus 로고
    • Ligand screening system using fusion proteins of G protein-coupled receptors with G protein alpha subunits
    • DOI 10.1016/j.neuint.2007.06.006, PII S0197018607001428
    • Suga H, Haga T (2007) Ligand screening system using fusion proteins of G protein-coupled receptors with G protein alpha subunits. Neurochem Int 51:140-164. doi:10.1016/j.neuint.2007.06.006 (Pubitemid 47176709)
    • (2007) Neurochemistry International , vol.51 , Issue.2-4 SPEC. ISS. , pp. 140-164
    • Suga, H.1    Haga, T.2
  • 307
    • 84874896510 scopus 로고    scopus 로고
    • DTome: A web-based tool for drugtarget interactome construction
    • doi:10.1186/1471-2105-13-S9-S7
    • Sun J, Wu Y, Xu H, Zhao Z (2012) DTome: a web-based tool for drugtarget interactome construction. BMC Bioinforma 13(Suppl 9):S7. doi:10.1186/1471-2105- 13-S9-S7
    • (2012) BMC Bioinforma , vol.13 , Issue.SUPPL. 9
    • Sun, J.1    Wu, Y.2    Xu, H.3    Zhao, Z.4
  • 309
  • 310
    • 0032908634 scopus 로고    scopus 로고
    • Null mutation in IRE1 gene inhibits overproduction of microsomal cytochrome P450Alk1 (CYP 52A3) and proliferation of the endoplasmic reticulum in Saccharomyces cerevisiae
    • Takewaka T, Zimmer T, Hirata A, Ohta A, Takagi M (1999) Null mutation in IRE1 gene inhibits overproduction of microsomal cytochrome P450Alk1 (CYP52A3) and proliferation of the endoplasmic reticulum in Saccharomyces cerevisiae. J Biochem 125:507-514 (Pubitemid 29164223)
    • (1999) Journal of Biochemistry , vol.125 , Issue.3 , pp. 507-514
    • Takewaka, T.1    Zimmer, T.2    Hirata, A.3    Ohta, A.4    Takagi, M.5
  • 312
    • 72949091450 scopus 로고    scopus 로고
    • + channel Kir2.2 at 3.1 A resolution
    • doi:10.1126/science.1180310
    • + channel Kir2.2 at 3.1 A resolution. Science 326:1668-1674. doi:10.1126/science.1180310
    • (2009) Science , vol.326 , pp. 1668-1674
    • Tao, X.1    Avalos, J.L.2    Chen, J.3    MacKinnon, R.4
  • 313
    • 77950488909 scopus 로고    scopus 로고
    • A gating charge transfer center in voltage sensors
    • doi:10.1126/science.1185954
    • Tao X, Lee A, Limapichat W, Dougherty DA, MacKinnon R (2010) A gating charge transfer center in voltage sensors. Science 328:67-73. doi:10.1126/science.1185954
    • (2010) Science , vol.328 , pp. 67-73
    • Tao, X.1    Lee, A.2    Limapichat, W.3    Dougherty, D.A.4    MacKinnon, R.5
  • 314
    • 84892335136 scopus 로고    scopus 로고
    • Applications of the non-conventional yeast Yarrowia lipolytica
    • doi:10.1007/978-1-4020-8292-4
    • Thevenieau F, Nicaud J-M, Gaillardin C (2009) Applications of the non-conventional yeast Yarrowia lipolytica. Yeast Biotechnol Divers Appl. doi:10.1007/978-1-4020-8292-4
    • (2009) Yeast Biotechnol Divers Appl
    • Thevenieau, F.1    Nicaud, J.-M.2    Gaillardin, C.3
  • 318
    • 84896329131 scopus 로고    scopus 로고
    • Expression, purification and structural properties of ABC transporter ABCA4 and its individual domains
    • doi:10.1016/j.pep.2014.02.010
    • Tsybovsky Y, Palczewski K (2014) Expression, purification and structural properties of ABC transporter ABCA4 and its individual domains. Protein Expr Purif 97:50-60. doi:10.1016/j.pep.2014.02.010
    • (2014) Protein Expr Purif , vol.97 , pp. 50-60
    • Tsybovsky, Y.1    Palczewski, K.2
  • 320
    • 0034213195 scopus 로고    scopus 로고
    • The methylotrophic yeast Hansenula polymorpha: A versatile cell factory
    • DOI 10.1016/S0141-0229(00)00173-3, PII S0141022900001733
    • Van Dijk R, Faber KN, Kiel JAKW, Veenhuis M, van der Klei I (2000) The methylotrophic yeast Hansenula polymorpha: a versatile cell factory. Enzyme Microb Technol 26:793-800. doi:10.1016/S0141-0229(00)00173-3 (Pubitemid 30345548)
    • (2000) Enzyme and Microbial Technology , vol.26 , Issue.9-10 , pp. 793-800
    • Van Dijk, R.1    Faber, K.N.2    Kiel, J.A.K.W.3    Veenhuis, M.4    Van Der, K.I.5
  • 321
    • 1542329068 scopus 로고    scopus 로고
    • Production of lipid compounds in the yeast Saccharomyces cerevisiae
    • DOI 10.1007/s00253-003-1456-7
    • Veen M, Lang C (2004) Production of lipid compounds in the yeast Saccharomyces cerevisiae. Appl Microbiol Biotechnol 63:635-646. doi:10.1007/s00253-003-1456-7 (Pubitemid 38316689)
    • (2004) Applied Microbiology and Biotechnology , vol.63 , Issue.6 , pp. 635-646
    • Veen, M.1    Lang, C.2
  • 322
    • 67349240827 scopus 로고    scopus 로고
    • Effect of the ferredoxin electron donor on sunflower (Helianthus annuus) desaturases
    • doi:10.1016/j.plaphy.2009.03.005
    • Venegas-Calerón M, Youssar L, Salas JJ, Garcés R, Martínez-Force E (2009) Effect of the ferredoxin electron donor on sunflower (Helianthus annuus) desaturases. Plant Physiol Biochem 47:657-662. doi:10.1016/j.plaphy.2009.03.005
    • (2009) Plant Physiol Biochem , vol.47 , pp. 657-662
    • Venegas-Calerón, M.1    Youssar, L.2    Salas, J.J.3    Garcés, R.4    Martínez-Force, E.5
  • 323
    • 84855932788 scopus 로고    scopus 로고
    • Aquaporins in clinical medicine
    • doi:10.1146/annurev-med-043010-193843
    • Verkman AS (2012) Aquaporins in clinical medicine. Annu Rev Med 63:303-316. doi:10.1146/annurev-med-043010-193843
    • (2012) Annu Rev Med , vol.63 , pp. 303-316
    • Verkman, A.S.1
  • 324
    • 0034965318 scopus 로고    scopus 로고
    • Arabidopsis IRT2 gene encodes a root-periphery iron transporter
    • DOI 10.1046/j.1365-313X.2001.01018.x
    • Vert G, Briat J-F, Curie C (2001) Arabidopsis IRT2 gene encodes a rootperiphery iron transporter. Plant J 26:181-189. doi:10.1046/j.1365-313x. 2001.01018.x (Pubitemid 32532725)
    • (2001) Plant Journal , vol.26 , Issue.2 , pp. 181-189
    • Vert, G.1    Briat, J.-F.2    Curie, C.3
  • 327
    • 84872073078 scopus 로고    scopus 로고
    • Practical aspects in expression and purification of membrane proteins for structural analysis
    • doi:10.1007/978-1-62703-176-9-2
    • Vinothkumar KR, Edwards PC, Standfuss J (2013) Practical aspects in expression and purification of membrane proteins for structural analysis. Methods Mol Biol 955:17-30. doi:10.1007/978-1-62703-176-9-2
    • (2013) Methods Mol Biol , vol.955 , pp. 17-30
    • Vinothkumar, K.R.1    Edwards, P.C.2    Standfuss, J.3
  • 328
    • 79955460451 scopus 로고    scopus 로고
    • Relationship between homooligomerization of amammalian olfactory receptor and its activation state demonstrated by bioluminescence resonance energy transfer
    • doi:10.1074/jbc.M110.184580
    • Wade F, Espagne A, Persuy M-A, Vidic J, Monnerie R, Merola F, Pajot-Augy E, Sanz G (2011) Relationship between homooligomerization of amammalian olfactory receptor and its activation state demonstrated by bioluminescence resonance energy transfer. J Biol Chem 286:15252-15259. doi:10.1074/jbc.M110. 184580
    • (2011) J Biol Chem , vol.286 , pp. 15252-15259
    • Wade, F.1    Espagne, A.2    Persuy, M.-A.3    Vidic, J.4    Monnerie, R.5    Merola, F.6    Pajot-Augy, E.7    Sanz, G.8
  • 329
    • 33745894174 scopus 로고    scopus 로고
    • Rationalizing membrane protein overexpression
    • DOI 10.1016/j.tibtech.2006.06.008, PII S0167779906001569
    • Wagner S, Bader ML, Drew D, de Gier J-W (2006) Rationalizing membrane protein overexpression. Trends Biotechnol 24:364-371. doi:10.1016/j.tibtech. 2006.06.008 (Pubitemid 44041706)
    • (2006) Trends in Biotechnology , vol.24 , Issue.8 , pp. 364-371
    • Wagner, S.1    Bader, M.L.2    Drew, D.3    De Gier, J.-W.4
  • 330
    • 82255173966 scopus 로고    scopus 로고
    • The unfolded protein response: From stress pathway to homeostatic regulation
    • doi:10.1126/science.1209038
    • Walter P, Ron D (2011) The unfolded protein response: from stress pathway to homeostatic regulation. Science 334:1081-1086. doi:10.1126/science.1209038
    • (2011) Science , vol.334 , pp. 1081-1086
    • Walter, P.1    Ron, D.2
  • 331
    • 76749104256 scopus 로고    scopus 로고
    • High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: Comparison with human MAO A
    • doi:10.1016/j.pep.2009.10.013
    • Wang J, Edmondson DE (2010) High-level expression and purification of rat monoamine oxidase A (MAO A) in Pichia pastoris: comparison with human MAO A. Protein Expr Purif 70:211-217. doi:10.1016/j.pep.2009.10.013
    • (2010) Protein Expr Purif , vol.70 , pp. 211-217
    • Wang, J.1    Edmondson, D.E.2
  • 332
    • 0029560973 scopus 로고
    • Expression of functional mouse 5-HT(5A) serotonin receptor in the myelotrophic yeast Pichia pastoris: Pharmacological characterization and localization
    • DOI 10.1016/0014-5793(95)01389-X
    • Weiss HM, Haase W, Michel H, Reiländer H (1995) Expression of functional mouse 5-HT5A serotonin receptor in the methylotrophic yeast Pichia pastoris: pharmacological characterization and localization. FEBS Lett 377:451-456. doi:10.1016/0014-5793(95)01389-X (Pubitemid 26027162)
    • (1995) FEBS Letters , vol.377 , Issue.3 , pp. 451-456
    • Weiss, H.M.1    Haase, W.2    Michel, H.3    Reilander, H.4
  • 333
    • 0032521005 scopus 로고    scopus 로고
    • Comparative biochemical and pharmacological characterization of the mouse 5HT5A 5-hydroxytryptamine receptor and the human β2-adrenergic receptor produced in the methylotrophic yeast Pichia pastoris
    • Weiss HM, Haase W, Michel H, Reiländer H (1998) Comparative biochemical and pharmacological characterization of the mouse 5HT5A 5-hydroxytryptamine receptor and the human β2-adrenergic receptor produced in the methylotrophic yeast Pichia pastoris. Biochem J 330:1137-1147
    • (1998) Biochem J , vol.330 , pp. 1137-1147
    • Weiss, H.M.1    Haase, W.2    Michel, H.3    Reiländer, H.4
  • 334
    • 0025552746 scopus 로고
    • Catalytically active monoamine oxidase type A from human liver expressed in Saccharomyces cerevisiae contains covalent FAD
    • doi:10.1016/S0006-291X(05)80914-3
    • Weyler W, Titlow CC, Salach JI (1990) Catalytically active monoamine oxidase type A from human liver expressed in Saccharomyces cerevisiae contains covalent FAD. Biochem Biophys Res Commun 173:1205-1211. doi:10.1016/S0006- 291X(05)80914-3
    • (1990) Biochem Biophys Res Commun , vol.173 , pp. 1205-1211
    • Weyler, W.1    Titlow, C.C.2    Salach, J.I.3
  • 335
    • 33845629883 scopus 로고    scopus 로고
    • Characteristics Affecting Expression and Solubilization of Yeast Membrane Proteins
    • DOI 10.1016/j.jmb.2006.10.004, PII S0022283606013428
    • White MA, Clark KM, Grayhack EJ, Dumont ME (2007) Characteristics affecting expression and solubilization of yeast membrane proteins. J Mol Biol 365:621-636. doi:10.1016/j.jmb.2006.10.004 (Pubitemid 44960350)
    • (2007) Journal of Molecular Biology , vol.365 , Issue.3 , pp. 621-636
    • White, M.A.1    Clark, K.M.2    Grayhack, E.J.3    Dumont, M.E.4
  • 336
    • 80053485088 scopus 로고    scopus 로고
    • 2, and sodium
    • doi:10.1016/j.cell.2011.07.046
    • 2, and sodium. Cell 147:199-208. doi:10.1016/j.cell.2011.07.046
    • (2011) Cell , vol.147 , pp. 199-208
    • Whorton, M.R.1    MacKinnon, R.2
  • 337
    • 84878996278 scopus 로고    scopus 로고
    • X-ray structure of the mammalian GIRK2-βγ G-protein complex
    • doi:10.1038/nature12241
    • Whorton MR, MacKinnon R (2013) X-ray structure of the mammalian GIRK2-βγ G-protein complex. Nature 498:190-197. doi:10.1038/ nature12241
    • (2013) Nature , vol.498 , pp. 190-197
    • Whorton, M.R.1    MacKinnon, R.2
  • 338
    • 0027732208 scopus 로고
    • Overexpression of the ER-membrane protein P-450 CYP52A3 mimics sec mutant characteristics in Saccharomyces cerevisiae
    • DOI 10.1016/0005-2736(93)90415-V
    • Wiedmann B, Silver P, Schunck WH, Wiedmann M (1993) Overexpression of the ER-membrane protein P-450 CYP52A3 mimics sec mutant characteristics in Saccharomyces cerevisiae. Biochim Biophys Acta 1153:267-276. doi:10.1016/0005-2736(93)90415-V (Pubitemid 24028298)
    • (1993) Biochimica et Biophysica Acta - Biomembranes , vol.1153 , Issue.2 , pp. 267-276
    • Wiedmann, B.1    Silver, P.2    Schunck, W.-H.3    Wiedmann, M.4
  • 340
    • 84877036789 scopus 로고    scopus 로고
    • Yeast metabolic engineering - Targeting sterol metabolism and terpenoid formation
    • doi:10.1016/j.plipres.2013.03.001
    • Wriessnegger T, Pichler H (2013) Yeast metabolic engineering - targeting sterol metabolism and terpenoid formation. Prog Lipid Res 52:277-293. doi:10.1016/j.plipres.2013.03.001
    • (2013) Prog Lipid Res , vol.52 , pp. 277-293
    • Wriessnegger, T.1    Pichler, H.2
  • 342
    • 0023788653 scopus 로고
    • Increased amounts of HMG-CoA reductase induce "karmellae": A proliferation of stacked membrane pairs surrounding the yeast nucleus
    • doi:10.1083/jcb.107.1.101
    • Wright R, Basson M, D'Ari L, Rine J (1988) Increased amounts of HMG-CoA reductase induce "karmellae": a proliferation of stacked membrane pairs surrounding the yeast nucleus. J Cell Biol 107:101-114. doi:10.1083/jcb.107.1.101
    • (1988) J Cell Biol , vol.107 , pp. 101-114
    • Wright, R.1    Basson, M.2    D'Ari, L.3    Rine, J.4
  • 344
    • 56449121491 scopus 로고    scopus 로고
    • The iron-regulated transporter, MbNRAMP1, isolated from Malus baccata is involved in Fe, Mn and Cd trafficking
    • doi:10.1093/aob/mcn178
    • Xiao H, Yin L, Xu X, Li T, Han Z (2008) The iron-regulated transporter, MbNRAMP1, isolated from Malus baccata is involved in Fe, Mn and Cd trafficking. Ann Bot 102:881-889. doi:10.1093/aob/mcn178
    • (2008) Ann Bot , vol.102 , pp. 881-889
    • Xiao, H.1    Yin, L.2    Xu, X.3    Li, T.4    Han, Z.5
  • 346
    • 0035049090 scopus 로고    scopus 로고
    • Yeast screen for constitutively active mutant G protein-activated potassium channels
    • DOI 10.1016/S0896-6273(01)00241-0
    • Yi BA, Lin Y-F, Jan YN, Jan LY (2001) Yeast screen for constitutively active mutant G protein-activated potassium channels. Neuron 29:657-667. doi:10.1016/S0896-6273(01)00241-0 (Pubitemid 32323939)
    • (2001) Neuron , vol.29 , Issue.3 , pp. 657-667
    • Yi, B.A.1    Lin, Y.-F.2    Jan, Y.N.3    Jan, L.Y.4
  • 347
    • 84872654805 scopus 로고    scopus 로고
    • +-PPase-expressing transgenic Escherichia coli and Saccharomyces cerevisiae: A potentially useful mechanism for the development of stress-tolerant organisms
    • doi:10.1007/s13353-012-0117-x
    • +-PPase-expressing transgenic Escherichia coli and Saccharomyces cerevisiae: a potentially useful mechanism for the development of stress-tolerant organisms. J Appl Genet 54:129-133. doi:10.1007/s13353-012-0117- x
    • (2013) J Appl Genet , vol.54 , pp. 129-133
    • Yoon, H.-S.1    Kim, S.-Y.2    Kim, I.-S.3
  • 348
    • 0028673929 scopus 로고
    • Dimethyl sulphoxide: A review of its applications in cell biology
    • doi:10.1007/BF01199051
    • Yu ZW, Quinn PJ (1994) Dimethyl sulphoxide: a review of its applications in cell biology. Biosci Rep 14:259-281. doi:10.1007/BF01199051
    • (1994) Biosci Rep , vol.14 , pp. 259-281
    • Yu, Z.W.1    Quinn, P.J.2
  • 351
    • 34548393181 scopus 로고    scopus 로고
    • Biochemical and mass spectrometric characterization of the human CB2 cannabinoid receptor expressed in Pichia pastoris-Importance of correct processing of the N-terminus
    • DOI 10.1016/j.pep.2007.03.018, PII S1046592807000769
    • Zhang R, Kim T-K, Qiao Z-H, Cai J, Pierce WM, Song Z-H (2007) Biochemical and mass spectrometric characterization of the human CB2 cannabinoid receptor expressed in Pichia pastoris - importance of correct processing of the N-terminus. Protein Expr Purif 55:225-235. doi:10.1016/j.pep.2007.03.018 (Pubitemid 47369645)
    • (2007) Protein Expression and Purification , vol.55 , Issue.2 , pp. 225-235
    • Zhang, R.1    Kim, T.-K.2    Qiao, Z.-H.3    Cai, J.4    Pierce Jr., W.M.5    Song, Z.-H.6
  • 352
    • 84873747401 scopus 로고    scopus 로고
    • The transcriptional control machinery as well as the cell wall integrity and its regulation are involved in the detoxification of the organic solvent dimethyl sulfoxide in Saccharomyces cerevisiae
    • doi:10.1111/1567-1364.12022
    • Zhang L, Liu N, Ma X, Jiang L (2013a) The transcriptional control machinery as well as the cell wall integrity and its regulation are involved in the detoxification of the organic solvent dimethyl sulfoxide in Saccharomyces cerevisiae. FEMS Yeast Res 13:200-218. doi:10.1111/1567-1364.12022
    • (2013) FEMS Yeast Res , vol.13 , pp. 200-218
    • Zhang, L.1    Liu, N.2    Ma, X.3    Jiang, L.4
  • 353
    • 84878354682 scopus 로고    scopus 로고
    • Heterologous functional analysis of the Malus xiaojinensis MxIRT1 gene and the His-box motif by expression in yeast
    • doi:10.1007/s11033-012-2193-8
    • Zhang X-N, Han Z-H, Yin L-L, Kong J, Xu X-F, Zhang X-Z, Wang Y (2013b) Heterologous functional analysis of the Malus xiaojinensis MxIRT1 gene and the His-box motif by expression in yeast. Mol Biol Rep 40:1499-1504. doi:10.1007/s11033-012-2193-8
    • (2013) Mol Biol Rep , vol.40 , pp. 1499-1504
    • Zhang, X.-N.1    Han, Z.-H.2    Yin, L.-L.3    Kong, J.4    Xu, X.-F.5    Zhang, X.-Z.6    Wang, Y.7
  • 354
    • 84864778329 scopus 로고    scopus 로고
    • A simple guide to biochemical approaches for analyzing protein-lipid interactions
    • doi:10.1091/mbc.E11-07-0645
    • Zhao H, Lappalainen P (2012) A simple guide to biochemical approaches for analyzing protein-lipid interactions. Mol Biol Cell 23:2823-2830. doi:10.1091/mbc.E11-07-0645
    • (2012) Mol Biol Cell , vol.23 , pp. 2823-2830
    • Zhao, H.1    Lappalainen, P.2
  • 355
    • 0029048526 scopus 로고
    • Schizosaccharomyces pombe: A model for molecular studies of eukaryotic genes
    • Zhao Y, Lieberman HB (1995) Schizosaccharomyces pombe: a model for molecular studies of eukaryotic genes. DNA Cell Biol 14:359-371
    • (1995) DNA Cell Biol , vol.14 , pp. 359-371
    • Zhao, Y.1    Lieberman, H.B.2
  • 357
    • 84867131783 scopus 로고    scopus 로고
    • N-terminal T4 lysozyme fusion facilitates crystallization of a G protein coupled receptor
    • doi:10.1371/journal.pone.0046039
    • Zou Y, Weis WI, Kobilka BK (2012) N-terminal T4 lysozyme fusion facilitates crystallization of a G protein coupled receptor. PLoS One 7:e46039. doi:10.1371/journal.pone.0046039
    • (2012) PLoS One , vol.7
    • Zou, Y.1    Weis, W.I.2    Kobilka, B.K.3


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