메뉴 건너뛰기




Volumn 11, Issue , 2011, Pages

Increasing gene dosage greatly enhances recombinant expression of aquaporins in Pichia pastoris

Author keywords

Major Intrinsic Proteins; Pichia pastoris aquaporins; qPCR

Indexed keywords

AQUAPORINS; EUKARYOTIC MEMBRANE PROTEIN; EUKARYOTIC PROTEINS; EXPRESSION LEVELS; EXPRESSION SYSTEM; GENE DOSAGE; HETEROLOGOUS EXPRESSION; HIGH YIELD; INSECT CELLS; ISOFORMS; LOCALISATION; MAJOR INTRINSIC PROTEINS; MEMBRANE PROTEINS; NATURAL SOURCES; OVER-EXPRESSION; P. PASTORIS; PICHIA PASTORIS; POST-TRANSCRIPTIONAL; PROTEIN YIELD; QPCR; RECOMBINANT EXPRESSION; RECOMBINANT PROTEIN EXPRESSION; ROBUST METHODS; STRUCTURAL STUDIES; TRANSCRIPT LEVEL;

EID: 79955746703     PISSN: None     EISSN: 14726750     Source Type: Journal    
DOI: 10.1186/1472-6750-11-47     Document Type: Article
Times cited : (89)

References (49)
  • 1
    • 33745894174 scopus 로고    scopus 로고
    • Rationalizing membrane protein overexpression
    • 10.1016/j.tibtech.2006.06.008, 16820235
    • Wagner S, Bader ML, Drew D, de Gier JW. Rationalizing membrane protein overexpression. Trends Biotechnol 2006, 24(8):364-371. 10.1016/j.tibtech.2006.06.008, 16820235.
    • (2006) Trends Biotechnol , vol.24 , Issue.8 , pp. 364-371
    • Wagner, S.1    Bader, M.L.2    Drew, D.3    de Gier, J.W.4
  • 2
    • 44749088968 scopus 로고    scopus 로고
    • Large-scale production of functional membrane proteins
    • 10.1007/s00018-008-8067-5, 18408885
    • Junge F, Schneider B, Reckel S, Schwarz D, Dotsch V, Bernhard F. Large-scale production of functional membrane proteins. Cell Mol Life Sci 2008, 65(11):1729-1755. 10.1007/s00018-008-8067-5, 18408885.
    • (2008) Cell Mol Life Sci , vol.65 , Issue.11 , pp. 1729-1755
    • Junge, F.1    Schneider, B.2    Reckel, S.3    Schwarz, D.4    Dotsch, V.5    Bernhard, F.6
  • 3
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors: comparison of expression systems fron the standpoint of large-scale production and purification
    • 10.1007/s00018-003-3168-7, 14513829
    • Sarramegna V, Talmont F, Demange P, Milon A. Heterologous expression of G-protein-coupled receptors: comparison of expression systems fron the standpoint of large-scale production and purification. Cell Mol Life Sci 2003, 60(8):1529-1546. 10.1007/s00018-003-3168-7, 14513829.
    • (2003) Cell Mol Life Sci , vol.60 , Issue.8 , pp. 1529-1546
    • Sarramegna, V.1    Talmont, F.2    Demange, P.3    Milon, A.4
  • 4
    • 34548110776 scopus 로고    scopus 로고
    • Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes
    • 10.1016/j.jbiotec.2006.07.012, 16959350
    • Yin J, Li G, Ren X, Herrler G. Select what you need: a comparative evaluation of the advantages and limitations of frequently used expression systems for foreign genes. J Biotechnol 2007, 127(3):335-347. 10.1016/j.jbiotec.2006.07.012, 16959350.
    • (2007) J Biotechnol , vol.127 , Issue.3 , pp. 335-347
    • Yin, J.1    Li, G.2    Ren, X.3    Herrler, G.4
  • 5
    • 14744285206 scopus 로고    scopus 로고
    • Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production
    • 10.1002/jmr.687, 15565717
    • Daly R, Hearn MT. Expression of heterologous proteins in Pichia pastoris: a useful experimental tool in protein engineering and production. J Mol Recognit 2005, 18(2):119-138. 10.1002/jmr.687, 15565717.
    • (2005) J Mol Recognit , vol.18 , Issue.2 , pp. 119-138
    • Daly, R.1    Hearn, M.T.2
  • 6
    • 33746813576 scopus 로고    scopus 로고
    • Understanding recombinant expression of membrane proteins
    • 10.1016/j.copbio.2006.06.001, 16777403
    • Grisshammer R. Understanding recombinant expression of membrane proteins. Curr Opin Biotechnol 2006, 17(4):337-340. 10.1016/j.copbio.2006.06.001, 16777403.
    • (2006) Curr Opin Biotechnol , vol.17 , Issue.4 , pp. 337-340
    • Grisshammer, R.1
  • 8
    • 0033955337 scopus 로고    scopus 로고
    • Heterologous protein expression in the methylotrophic yeast Pichia pastoris
    • 10.1111/j.1574-6976.2000.tb00532.x, 10640598
    • Cereghino JL, Cregg JM. Heterologous protein expression in the methylotrophic yeast Pichia pastoris. FEMS Microbiol Rev 2000, 24(1):45-66. 10.1111/j.1574-6976.2000.tb00532.x, 10640598.
    • (2000) FEMS Microbiol Rev , vol.24 , Issue.1 , pp. 45-66
    • Cereghino, J.L.1    Cregg, J.M.2
  • 9
    • 0031587763 scopus 로고    scopus 로고
    • Expression and functional characterization of the mammalian intestinal peptide transporter PepT1 in the methylotropic yeast Pichia pastoris
    • 10.1006/bbrc.1997.6351, 9126331
    • Doring F, Theis S, Daniel H. Expression and functional characterization of the mammalian intestinal peptide transporter PepT1 in the methylotropic yeast Pichia pastoris. Biochem Biophys Res Commun 1997, 232(3):656-662. 10.1006/bbrc.1997.6351, 9126331.
    • (1997) Biochem Biophys Res Commun , vol.232 , Issue.3 , pp. 656-662
    • Doring, F.1    Theis, S.2    Daniel, H.3
  • 10
    • 0141457531 scopus 로고    scopus 로고
    • Structural characterisation of neuronal voltage-sensitive K+ channels heterologously expressed in Pichia pastoris
    • 10.1016/j.jmb.2003.07.009, 14516746
    • Parcej DN, Eckhardt-Strelau L. Structural characterisation of neuronal voltage-sensitive K+ channels heterologously expressed in Pichia pastoris. J Mol Biol 2003, 333(1):103-116. 10.1016/j.jmb.2003.07.009, 14516746.
    • (2003) J Mol Biol , vol.333 , Issue.1 , pp. 103-116
    • Parcej, D.N.1    Eckhardt-Strelau, L.2
  • 11
    • 23244456428 scopus 로고    scopus 로고
    • Crystal structure of a mammalian voltage-dependent Shaker family K+ channel
    • 10.1126/science.1116269, 16002581
    • Long SB, Campbell EB, Mackinnon R. Crystal structure of a mammalian voltage-dependent Shaker family K+ channel. Science 2005, 309(5736):897-903. 10.1126/science.1116269, 16002581.
    • (2005) Science , vol.309 , Issue.5736 , pp. 897-903
    • Long, S.B.1    Campbell, E.B.2    Mackinnon, R.3
  • 12
    • 0242664242 scopus 로고    scopus 로고
    • Expression of Na+,K+-ATPase in Pichia pastoris: analysis of wild type and D369N mutant proteins by Fe2+-catalyzed oxidative cleavage and molecular modeling
    • 10.1074/jbc.M308303200, 12949069
    • Strugatsky D, Gottschalk KE, Goldshleger R, Bibi E, Karlish SJ. Expression of Na+,K+-ATPase in Pichia pastoris: analysis of wild type and D369N mutant proteins by Fe2+-catalyzed oxidative cleavage and molecular modeling. J Biol Chem 2003, 278(46):46064-46073. 10.1074/jbc.M308303200, 12949069.
    • (2003) J Biol Chem , vol.278 , Issue.46 , pp. 46064-46073
    • Strugatsky, D.1    Gottschalk, K.E.2    Goldshleger, R.3    Bibi, E.4    Karlish, S.J.5
  • 13
    • 37349040730 scopus 로고    scopus 로고
    • Purification of the human alpha2 Isoform of Na,K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1
    • 10.1021/bi701812c, 18052210
    • Lifshitz Y, Petrovich E, Haviv H, Goldshleger R, Tal DM, Garty H, Karlish SJ. Purification of the human alpha2 Isoform of Na,K-ATPase expressed in Pichia pastoris. Stabilization by lipids and FXYD1. Biochemistry 2007, 46(51):14937-14950. 10.1021/bi701812c, 18052210.
    • (2007) Biochemistry , vol.46 , Issue.51 , pp. 14937-14950
    • Lifshitz, Y.1    Petrovich, E.2    Haviv, H.3    Goldshleger, R.4    Tal, D.M.5    Garty, H.6    Karlish, S.J.7
  • 14
    • 0030574052 scopus 로고    scopus 로고
    • Expression and pharmacological characterization of the human mu-opioid receptor in the methylotrophic yeast Pichia pastoris
    • 10.1016/0014-5793(96)00971-4, 8830656
    • Talmont F, Sidobre S, Demange P, Milon A, Emorine LJ. Expression and pharmacological characterization of the human mu-opioid receptor in the methylotrophic yeast Pichia pastoris. FEBS Lett 1996, 394(3):268-272. 10.1016/0014-5793(96)00971-4, 8830656.
    • (1996) FEBS Lett , vol.394 , Issue.3 , pp. 268-272
    • Talmont, F.1    Sidobre, S.2    Demange, P.3    Milon, A.4    Emorine, L.J.5
  • 15
    • 0032521005 scopus 로고    scopus 로고
    • Comparative biochemical and pharmacological characterization of the mouse 5HT5A 5-hydroxytryptamine receptor and the human beta2-adrenergic receptor produced in the methylotrophic yeast Pichia pastoris
    • 1219254, 9494078
    • Weiss HM, Haase W, Michel H, Reilander H. Comparative biochemical and pharmacological characterization of the mouse 5HT5A 5-hydroxytryptamine receptor and the human beta2-adrenergic receptor produced in the methylotrophic yeast Pichia pastoris. Biochem J 1998, 330(Pt 3):1137-1147. 1219254, 9494078.
    • (1998) Biochem J , vol.330 , Issue.PART 3 , pp. 1137-1147
    • Weiss, H.M.1    Haase, W.2    Michel, H.3    Reilander, H.4
  • 16
    • 77951122101 scopus 로고    scopus 로고
    • Expression, purification and characterization of leukotriene B(4) receptor, BLT1 in Pichia pastoris
    • 10.1016/j.pep.2010.02.013, 20188179
    • Hori T, Sato Y, Takahashi N, Takio K, Yokomizo T, Nakamura M, Shimizu T, Miyano M. Expression, purification and characterization of leukotriene B(4) receptor, BLT1 in Pichia pastoris. Protein Expr Purif 2010, 72(1):66-74. 10.1016/j.pep.2010.02.013, 20188179.
    • (2010) Protein Expr Purif , vol.72 , Issue.1 , pp. 66-74
    • Hori, T.1    Sato, Y.2    Takahashi, N.3    Takio, K.4    Yokomizo, T.5    Nakamura, M.6    Shimizu, T.7    Miyano, M.8
  • 17
    • 0037450545 scopus 로고    scopus 로고
    • Overexpression, purification, and functional characterization of ATP-binding cassette transporters in the yeast, Pichia pastoris
    • 10.1016/S0005-2736(02)00718-6, 12586381
    • Cai J, Gros P. Overexpression, purification, and functional characterization of ATP-binding cassette transporters in the yeast, Pichia pastoris. Biochim Biophys Acta 2003, 1610(1):63-76. 10.1016/S0005-2736(02)00718-6, 12586381.
    • (2003) Biochim Biophys Acta , vol.1610 , Issue.1 , pp. 63-76
    • Cai, J.1    Gros, P.2
  • 18
    • 75349092314 scopus 로고    scopus 로고
    • Purification and characterization of mammalian glucose transporters expressed in Pichia pastoris
    • 10.1016/j.pep.2009.10.011, 2823836, 19883765
    • Alisio A, Mueckler M. Purification and characterization of mammalian glucose transporters expressed in Pichia pastoris. Protein Expr Purif 2010, 70(1):81-87. 10.1016/j.pep.2009.10.011, 2823836, 19883765.
    • (2010) Protein Expr Purif , vol.70 , Issue.1 , pp. 81-87
    • Alisio, A.1    Mueckler, M.2
  • 19
    • 28244499592 scopus 로고    scopus 로고
    • High-yield functional expression of human sodium/d-glucose cotransporter1 in Pichia pastoris and characterization of ligand-induced conformational changes as studied by tryptophan fluorescence
    • 10.1021/bi051377q, 16300400
    • Tyagi NK, Goyal P, Kumar A, Pandey D, Siess W, Kinne RK. High-yield functional expression of human sodium/d-glucose cotransporter1 in Pichia pastoris and characterization of ligand-induced conformational changes as studied by tryptophan fluorescence. Biochemistry 2005, 44(47):15514-15524. 10.1021/bi051377q, 16300400.
    • (2005) Biochemistry , vol.44 , Issue.47 , pp. 15514-15524
    • Tyagi, N.K.1    Goyal, P.2    Kumar, A.3    Pandey, D.4    Siess, W.5    Kinne, R.K.6
  • 20
  • 22
    • 79959222792 scopus 로고    scopus 로고
    • EasySelect Pichia Expression Kit,version G
    • Invitrogen
    • Invitrogen EasySelect Pichia Expression Kit,version G. 2005, Invitrogen., http://tools.invitrogen.com/content/sfs/manuals/easyselect_man.pdf
    • (2005)
  • 23
    • 0032790856 scopus 로고    scopus 로고
    • High-yield secretion of recombinant gelatins by Pichia pastoris
    • 10.1002/(SICI)1097-0061(199908)15:11<1087::AID-YEA436>3.0.CO;2-F, 10455232
    • Werten MW, van den Bosch TJ, Wind RD, Mooibroek H, de Wolf FA. High-yield secretion of recombinant gelatins by Pichia pastoris. Yeast 1999, 15(11):1087-1096. 10.1002/(SICI)1097-0061(199908)15:11<1087::AID-YEA436>3.0.CO;2-F, 10455232.
    • (1999) Yeast , vol.15 , Issue.11 , pp. 1087-1096
    • Werten, M.W.1    van den Bosch, T.J.2    Wind, R.D.3    Mooibroek, H.4    de Wolf, F.A.5
  • 24
    • 0026138116 scopus 로고
    • High-level secretion of biologically active aprotinin from the yeast Pichia pastoris
    • 10.1007/BF01575883, 1370032
    • Vedvick T, Buckholz RG, Engel M, Urcan M, Kinney J, Provow S, Siegel RS, Thill GP. High-level secretion of biologically active aprotinin from the yeast Pichia pastoris. J Ind Microbiol 1991, 7(3):197-201. 10.1007/BF01575883, 1370032.
    • (1991) J Ind Microbiol , vol.7 , Issue.3 , pp. 197-201
    • Vedvick, T.1    Buckholz, R.G.2    Engel, M.3    Urcan, M.4    Kinney, J.5    Provow, S.6    Siegel, R.S.7    Thill, G.P.8
  • 25
    • 0030974549 scopus 로고    scopus 로고
    • Expression of trimeric CD40 ligand in Pichia pastoris: use of a rapid method to detect high-level expressing transformants
    • 10.1016/S0378-1119(96)00747-0, 9099880
    • McGrew JT, Leiske D, Dell B, Klinke R, Krasts D, Wee SF, Abbott N, Armitage R, Harrington K. Expression of trimeric CD40 ligand in Pichia pastoris: use of a rapid method to detect high-level expressing transformants. Gene 1997, 187(2):193-200. 10.1016/S0378-1119(96)00747-0, 9099880.
    • (1997) Gene , vol.187 , Issue.2 , pp. 193-200
    • McGrew, J.T.1    Leiske, D.2    Dell, B.3    Klinke, R.4    Krasts, D.5    Wee, S.F.6    Abbott, N.7    Armitage, R.8    Harrington, K.9
  • 26
    • 0031604266 scopus 로고    scopus 로고
    • Secretion of recombinant human insulin-like growth factor I (IGF-I)
    • Brierley RA. Secretion of recombinant human insulin-like growth factor I (IGF-I). Methods Mol Biol 1998, 103:149-177.
    • (1998) Methods Mol Biol , vol.103 , pp. 149-177
    • Brierley, R.A.1
  • 27
    • 0034963608 scopus 로고    scopus 로고
    • Effect of copy number on the expression levels of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris
    • 10.1006/prep.2000.1335, 11162389
    • Vassileva A, Chugh DA, Swaminathan S, Khanna N. Effect of copy number on the expression levels of hepatitis B surface antigen in the methylotrophic yeast Pichia pastoris. Protein Expr Purif 2001, 21(1):71-80. 10.1006/prep.2000.1335, 11162389.
    • (2001) Protein Expr Purif , vol.21 , Issue.1 , pp. 71-80
    • Vassileva, A.1    Chugh, D.A.2    Swaminathan, S.3    Khanna, N.4
  • 28
    • 14744271884 scopus 로고
    • High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene
    • Clare JJ, Rayment FB, Ballantine SP, Sreekrishna K, Romanos MA. High-level expression of tetanus toxin fragment C in Pichia pastoris strains containing multiple tandem integrations of the gene. Biotechnology (N Y) 1991, 9(5):455-460.
    • (1991) Biotechnology (N Y) , vol.9 , Issue.5 , pp. 455-460
    • Clare, J.J.1    Rayment, F.B.2    Ballantine, S.P.3    Sreekrishna, K.4    Romanos, M.A.5
  • 29
    • 10644247772 scopus 로고    scopus 로고
    • Improved secretory production of glucoamylase in Pichia pastoris by combination of genetic manipulations
    • 10.1016/j.bbrc.2004.11.112, 15607743
    • Liu SH, Chou WI, Sheu CC, Chang MD. Improved secretory production of glucoamylase in Pichia pastoris by combination of genetic manipulations. Biochem Biophys Res Commun 2005, 326(4):817-824. 10.1016/j.bbrc.2004.11.112, 15607743.
    • (2005) Biochem Biophys Res Commun , vol.326 , Issue.4 , pp. 817-824
    • Liu, S.H.1    Chou, W.I.2    Sheu, C.C.3    Chang, M.D.4
  • 30
  • 31
    • 0026094226 scopus 로고
    • Production of mouse epidermal growth factor in yeast: high-level secretion using Pichia pastoris strains containing multiple gene copies
    • 10.1016/0378-1119(91)90152-2, 1937016
    • Clare JJ, Romanos MA, Rayment FB, Rowedder JE, Smith MA, Payne MM, Sreekrishna K, Henwood CA. Production of mouse epidermal growth factor in yeast: high-level secretion using Pichia pastoris strains containing multiple gene copies. Gene 1991, 105(2):205-212. 10.1016/0378-1119(91)90152-2, 1937016.
    • (1991) Gene , vol.105 , Issue.2 , pp. 205-212
    • Clare, J.J.1    Romanos, M.A.2    Rayment, F.B.3    Rowedder, J.E.4    Smith, M.A.5    Payne, M.M.6    Sreekrishna, K.7    Henwood, C.A.8
  • 32
    • 68849130616 scopus 로고    scopus 로고
    • Efficient generation of multi-copy strains for optimizing secretory expression of porcine insulin precursor in yeast Pichia pastoris
    • 10.1111/j.1365-2672.2009.04279.x, 19486418
    • Zhu T, Guo M, Tang Z, Zhang M, Zhuang Y, Chu J, Zhang S. Efficient generation of multi-copy strains for optimizing secretory expression of porcine insulin precursor in yeast Pichia pastoris. J Appl Microbiol 2009, 107(3):954-963. 10.1111/j.1365-2672.2009.04279.x, 19486418.
    • (2009) J Appl Microbiol , vol.107 , Issue.3 , pp. 954-963
    • Zhu, T.1    Guo, M.2    Tang, Z.3    Zhang, M.4    Zhuang, Y.5    Chu, J.6    Zhang, S.7
  • 33
    • 0036514182 scopus 로고    scopus 로고
    • Optimizing functional versus total expression of the human mu-opioid receptor in Pichia pastoris
    • 10.1006/prep.2001.1564, 11858715
    • Sarramegna V, Demange P, Milon A, Talmont F. Optimizing functional versus total expression of the human mu-opioid receptor in Pichia pastoris. Protein Expr Purif 2002, 24(2):212-220. 10.1006/prep.2001.1564, 11858715.
    • (2002) Protein Expr Purif , vol.24 , Issue.2 , pp. 212-220
    • Sarramegna, V.1    Demange, P.2    Milon, A.3    Talmont, F.4
  • 35
    • 0037468462 scopus 로고    scopus 로고
    • Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris
    • 10.1016/S0014-5793(03)00082-6, 12606033
    • Karlsson M, Fotiadis D, Sjovall S, Johansson I, Hedfalk K, Engel A, Kjellbom P. Reconstitution of water channel function of an aquaporin overexpressed and purified from Pichia pastoris. FEBS Lett 2003, 537(1-3):68-72. 10.1016/S0014-5793(03)00082-6, 12606033.
    • (2003) FEBS Lett , 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
  • 37
    • 27644442731 scopus 로고    scopus 로고
    • Phosphorylation of aquaporin PvTIP3;1 defined by mass spectrometry and molecular modeling
    • 10.1021/bi050565d, 16262244
    • Daniels MJ, Yeager M. Phosphorylation of aquaporin PvTIP3;1 defined by mass spectrometry and molecular modeling. Biochemistry 2005, 44(44):14443-14454. 10.1021/bi050565d, 16262244.
    • (2005) Biochemistry , vol.44 , Issue.44 , pp. 14443-14454
    • Daniels, M.J.1    Yeager, M.2
  • 38
    • 40849133922 scopus 로고    scopus 로고
    • Production, characterization and crystallization of the Plasmodium falciparum aquaporin
    • 10.1016/j.pep.2008.01.004, 18295508
    • Hedfalk K, Pettersson N, Oberg F, Hohmann S, Gordon E. Production, characterization and crystallization of the Plasmodium falciparum aquaporin. Protein Expr Purif 2008, 59(1):69-78. 10.1016/j.pep.2008.01.004, 18295508.
    • (2008) Protein Expr Purif , vol.59 , Issue.1 , pp. 69-78
    • Hedfalk, K.1    Pettersson, N.2    Oberg, F.3    Hohmann, S.4    Gordon, E.5
  • 39
    • 4444221676 scopus 로고    scopus 로고
    • From structure to disease: the evolving tale of aquaporin biology
    • 10.1038/nrm1469, 15340377
    • King LS, Kozono D, Agre P. From structure to disease: the evolving tale of aquaporin biology. Nat Rev Mol Cell Biol 2004, 5(9):687-698. 10.1038/nrm1469, 15340377.
    • (2004) Nat Rev Mol Cell Biol , vol.5 , Issue.9 , pp. 687-698
    • King, L.S.1    Kozono, D.2    Agre, P.3
  • 40
    • 65649092165 scopus 로고    scopus 로고
    • Aquaporins are multifunctional water and solute transporters highly divergent in living organisms
    • 10.1016/j.bbamem.2009.03.009, 19327343
    • Gomes D, Agasse A, Thiebaud P, Delrot S, Geros H, Chaumont F. Aquaporins are multifunctional water and solute transporters highly divergent in living organisms. Biochim Biophys Acta 2009, 1788(6):1213-1228. 10.1016/j.bbamem.2009.03.009, 19327343.
    • (2009) Biochim Biophys Acta , vol.1788 , Issue.6 , pp. 1213-1228
    • Gomes, D.1    Agasse, A.2    Thiebaud, P.3    Delrot, S.4    Geros, H.5    Chaumont, F.6
  • 43
    • 49749139770 scopus 로고    scopus 로고
    • Posttransformational vector amplification in the yeast Pichia pastoris
    • 10.1111/j.1567-1364.2008.00410.x, 18637138
    • Sunga AJ, Tolstorukov I, Cregg JM. Posttransformational vector amplification in the yeast Pichia pastoris. FEMS Yeast Res 2008, 8(6):870-876. 10.1111/j.1567-1364.2008.00410.x, 18637138.
    • (2008) FEMS Yeast Res , vol.8 , Issue.6 , pp. 870-876
    • Sunga, A.J.1    Tolstorukov, I.2    Cregg, J.M.3
  • 44
    • 34249001008 scopus 로고    scopus 로고
    • High-level expression of human tumour suppressor P53 in the methylotrophic yeast: Pichia pastoris
    • 10.1016/j.pep.2007.03.015, 17482479
    • Abdelmoula-Souissi S, Rekik L, Gargouri A, Mokdad-Gargouri R. High-level expression of human tumour suppressor P53 in the methylotrophic yeast: Pichia pastoris. Protein Expr Purif 2007, 54(2):283-288. 10.1016/j.pep.2007.03.015, 17482479.
    • (2007) Protein Expr Purif , vol.54 , Issue.2 , pp. 283-288
    • Abdelmoula-Souissi, S.1    Rekik, L.2    Gargouri, A.3    Mokdad-Gargouri, R.4
  • 45
    • 43749115583 scopus 로고    scopus 로고
    • ER membrane aquaporins in plants
    • 10.1007/s00424-007-0363-7, 17924135
    • Maeshima M, Ishikawa F. ER membrane aquaporins in plants. Pflugers Arch 2008, 456(4):709-716. 10.1007/s00424-007-0363-7, 17924135.
    • (2008) Pflugers Arch , vol.456 , Issue.4 , pp. 709-716
    • Maeshima, M.1    Ishikawa, F.2
  • 46
    • 0035910555 scopus 로고    scopus 로고
    • Structural characterization of two aquaporins isolated from native spinach leaf plasma membranes
    • 10.1074/jbc.M009383200, 11050104
    • Fotiadis D, Jeno P, Mini T, Wirtz S, Muller SA, Fraysse L, Kjellbom P, Engel A. Structural characterization of two aquaporins isolated from native spinach leaf plasma membranes. J Biol Chem 2001, 276(3):1707-1714. 10.1074/jbc.M009383200, 11050104.
    • (2001) J Biol Chem , vol.276 , Issue.3 , pp. 1707-1714
    • Fotiadis, D.1    Jeno, P.2    Mini, T.3    Wirtz, S.4    Muller, S.A.5    Fraysse, L.6    Kjellbom, P.7    Engel, A.8
  • 48
    • 0033990048 scopus 로고    scopus 로고
    • Primer3 on the www for general users and for biologist programmers
    • Rozen S, Skaletsky H. Primer3 on the www for general users and for biologist programmers. Methods Mol Biol 2000, 132:365-386.
    • (2000) Methods Mol Biol , vol.132 , pp. 365-386
    • Rozen, S.1    Skaletsky, H.2
  • 49
    • 17344392308 scopus 로고    scopus 로고
    • A new mathematical model for relative quantification in real-time RT-PCR
    • 10.1093/nar/29.9.e45, 55695, 11328886
    • Pfaffl MW. A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res 2001, 29(9):e45. 10.1093/nar/29.9.e45, 55695, 11328886.
    • (2001) Nucleic Acids Res , vol.29 , Issue.9
    • Pfaffl, M.W.1


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.