메뉴 건너뛰기




Volumn 23, Issue 3, 2013, Pages 365-373

Technologies to keep an eye on: Alternative hosts for protein production in structural biology

Author keywords

[No Author keywords available]

Indexed keywords

MEMBRANE PROTEIN;

EID: 84879144027     PISSN: 0959440X     EISSN: 1879033X     Source Type: Journal    
DOI: 10.1016/j.sbi.2013.02.002     Document Type: Review
Times cited : (35)

References (61)
  • 7
    • 0034998070 scopus 로고    scopus 로고
    • High-rate 3-methylcatechol production in Pseudomonas putida strains by means of a novel expression system
    • Husken L.E., Beeftink R., de Bont J.A., Wery J. High-rate 3-methylcatechol production in Pseudomonas putida strains by means of a novel expression system. Appl Microbiol Biotechnol 2001, 55:571-577.
    • (2001) Appl Microbiol Biotechnol , vol.55 , pp. 571-577
    • Husken, L.E.1    Beeftink, R.2    de Bont, J.A.3    Wery, J.4
  • 10
    • 0025892985 scopus 로고
    • Inducible high-level expression of heterologous genes in Bacillus megaterium using the regulatory elements of the xylose-utilization operon
    • Rygus T., Hillen W. Inducible high-level expression of heterologous genes in Bacillus megaterium using the regulatory elements of the xylose-utilization operon. Appl Microbiol Biotechnol 1991, 35:594-599.
    • (1991) Appl Microbiol Biotechnol , vol.35 , pp. 594-599
    • Rygus, T.1    Hillen, W.2
  • 16
    • 75749100234 scopus 로고    scopus 로고
    • Adaptation of the highly productive T7 expression system to Streptomyces lividans
    • Lussier F.X., Denis F., Shareck F. Adaptation of the highly productive T7 expression system to Streptomyces lividans. Appl Environ Microbiol 2010, 76:967-970.
    • (2010) Appl Environ Microbiol , vol.76 , pp. 967-970
    • Lussier, F.X.1    Denis, F.2    Shareck, F.3
  • 17
    • 67649933582 scopus 로고    scopus 로고
    • Crystal structures of Mycobacterium tuberculosis KasA show mode of action within cell wall biosynthesis and its inhibition by thiolactomycin
    • Luckner S.R., Machutta C.A., Tonge P.J., Kisker C. Crystal structures of Mycobacterium tuberculosis KasA show mode of action within cell wall biosynthesis and its inhibition by thiolactomycin. Structure 2009, 17:1004-1013.
    • (2009) Structure , vol.17 , pp. 1004-1013
    • Luckner, S.R.1    Machutta, C.A.2    Tonge, P.J.3    Kisker, C.4
  • 18
    • 0344443250 scopus 로고    scopus 로고
    • Improved green fluorescent protein reporter gene-based microplate screening for antituberculosis compounds by utilizing an acetamidase promoter
    • Changsen C., Franzblau S.G., Palittapongarnpim P. Improved green fluorescent protein reporter gene-based microplate screening for antituberculosis compounds by utilizing an acetamidase promoter. Antimicrob Agents Chemother 2003, 47:3682-3687.
    • (2003) Antimicrob Agents Chemother , vol.47 , pp. 3682-3687
    • Changsen, C.1    Franzblau, S.G.2    Palittapongarnpim, P.3
  • 19
    • 0025303033 scopus 로고
    • An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium
    • Ni B.F., Chang M., Duschl A., Lanyi J., Needleman R. An efficient system for the synthesis of bacteriorhodopsin in Halobacterium halobium. Gene 1990, 90:169-172.
    • (1990) Gene , vol.90 , pp. 169-172
    • Ni, B.F.1    Chang, M.2    Duschl, A.3    Lanyi, J.4    Needleman, R.5
  • 21
    • 0027401509 scopus 로고
    • Homologous overexpression of a light-driven anion pump in an archaebacterium
    • Heymann J.A., Havelka W.A., Oesterhelt D. Homologous overexpression of a light-driven anion pump in an archaebacterium. Mol Microbiol 1993, 7:623-630.
    • (1993) Mol Microbiol , vol.7 , pp. 623-630
    • Heymann, J.A.1    Havelka, W.A.2    Oesterhelt, D.3
  • 22
    • 46249089993 scopus 로고    scopus 로고
    • Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins
    • Joh N.H., Min A., Faham S., Whitelegge J.P., Yang D., Woods V.L., Bowie J.U. Modest stabilization by most hydrogen-bonded side-chain interactions in membrane proteins. Nature 2008, 453:1266-1270.
    • (2008) Nature , vol.453 , pp. 1266-1270
    • Joh, N.H.1    Min, A.2    Faham, S.3    Whitelegge, J.P.4    Yang, D.5    Woods, V.L.6    Bowie, J.U.7
  • 23
    • 0024730742 scopus 로고
    • Transformation of the archaebacterium Halobacterium volcanii with genomic DNA
    • Cline S.W., Schalkwyk L.C., Doolittle W.F. Transformation of the archaebacterium Halobacterium volcanii with genomic DNA. J Bacteriol 1989, 171:4987-4991.
    • (1989) J Bacteriol , vol.171 , pp. 4987-4991
    • Cline, S.W.1    Schalkwyk, L.C.2    Doolittle, W.F.3
  • 24
    • 23044489637 scopus 로고    scopus 로고
    • G-protein-coupled receptor domain overexpression in Halobacterium salinarum: long-range transmembrane interactions in heptahelical membrane proteins
    • Jaakola V.P., Rehn M., Moeller M., Alexiev U., Goldman A., Turner G.J. G-protein-coupled receptor domain overexpression in Halobacterium salinarum: long-range transmembrane interactions in heptahelical membrane proteins. Proteins 2005, 60:412-423.
    • (2005) Proteins , vol.60 , pp. 412-423
    • Jaakola, V.P.1    Rehn, M.2    Moeller, M.3    Alexiev, U.4    Goldman, A.5    Turner, G.J.6
  • 26
    • 1842530397 scopus 로고    scopus 로고
    • Heterologous protein expression and secretion in the non-conventional yeast Yarrowia lipolytica: a review
    • Madzak C., Gaillardin C., Beckerich J.M. Heterologous protein expression and secretion in the non-conventional yeast Yarrowia lipolytica: a review. J Biotechnol 2004, 109:63-81.
    • (2004) J Biotechnol , vol.109 , pp. 63-81
    • Madzak, C.1    Gaillardin, C.2    Beckerich, J.M.3
  • 28
    • 17244363998 scopus 로고    scopus 로고
    • Heterologous protein production using the Pichia pastoris expression system
    • Macauley-Patrick S., Fazenda M.L., McNeil B., Harvey L.M. Heterologous protein production using the Pichia pastoris expression system. Yeast 2005, 22:249-270.
    • (2005) Yeast , vol.22 , pp. 249-270
    • Macauley-Patrick, S.1    Fazenda, M.L.2    McNeil, B.3    Harvey, L.M.4
  • 31
    • 27644574423 scopus 로고    scopus 로고
    • New yeast expression platforms based on methylotrophic Hansenula polymorpha and Pichia pastoris and on dimorphic Arxula adeninivorans and Yarrowia lipolyticainosa is exploited to recombinantly express the-a comparison
    • Gellissen G., Kunze G., Gaillardin C., Cregg J.M., Berardi E., Veenhuis M., van der Klei I. New yeast expression platforms based on methylotrophic Hansenula polymorpha and Pichia pastoris and on dimorphic Arxula adeninivorans and Yarrowia lipolyticainosa is exploited to recombinantly express the-a comparison. FEMS Yeast Res 2005, 5:1079-1096.
    • (2005) FEMS Yeast Res , vol.5 , pp. 1079-1096
    • Gellissen, G.1    Kunze, G.2    Gaillardin, C.3    Cregg, J.M.4    Berardi, E.5    Veenhuis, M.6    van der Klei, I.7
  • 32
    • 44449117421 scopus 로고    scopus 로고
    • Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors
    • Son S.Y., Ma J., Kondou Y., Yoshimura M., Yamashita E., Tsukihara T. Structure of human monoamine oxidase A at 2.2-A resolution: the control of opening the entry for substrates/inhibitors. Proc Natl Acad Sci U S A 2008, 105:5739-5744.
    • (2008) Proc Natl Acad Sci U S A , vol.105 , pp. 5739-5744
    • Son, S.Y.1    Ma, J.2    Kondou, Y.3    Yoshimura, M.4    Yamashita, E.5    Tsukihara, T.6
  • 34
    • 0032541478 scopus 로고    scopus 로고
    • A strong nitrogen source-regulated promoter for controlled expression of foreign genes in the yeast Pichia pastoris
    • Shen S., Sulter G., Jeffries T.W., Cregg J.M. A strong nitrogen source-regulated promoter for controlled expression of foreign genes in the yeast Pichia pastoris. Gene 1998, 216:93-102.
    • (1998) Gene , vol.216 , pp. 93-102
    • Shen, S.1    Sulter, G.2    Jeffries, T.W.3    Cregg, J.M.4
  • 35
    • 0031579445 scopus 로고    scopus 로고
    • Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter
    • Waterham H.R., Digan M.E., Koutz P.J., Lair S.V., Cregg J.M. Isolation of the Pichia pastoris glyceraldehyde-3-phosphate dehydrogenase gene and regulation and use of its promoter. Gene 1997, 186:37-44.
    • (1997) Gene , vol.186 , pp. 37-44
    • Waterham, H.R.1    Digan, M.E.2    Koutz, P.J.3    Lair, S.V.4    Cregg, J.M.5
  • 39
    • 0036678090 scopus 로고    scopus 로고
    • The crystal structure of human CD21: implications for Epstein-Barr virus and C3d binding
    • Prota A.E., Sage D.R., Stehle T., Fingeroth J.D. The crystal structure of human CD21: implications for Epstein-Barr virus and C3d binding. Proc Natl Acad Sci U S A 2002, 99:10641-10646.
    • (2002) Proc Natl Acad Sci U S A , vol.99 , pp. 10641-10646
    • Prota, A.E.1    Sage, D.R.2    Stehle, T.3    Fingeroth, J.D.4
  • 41
    • 77955557873 scopus 로고    scopus 로고
    • Expression and export: recombinant protein production systems for Aspergillus
    • Fleissner A., Dersch P. Expression and export: recombinant protein production systems for Aspergillus. Appl Microbiol Biotechnol 2010, 87:1255-1270.
    • (2010) Appl Microbiol Biotechnol , vol.87 , pp. 1255-1270
    • Fleissner, A.1    Dersch, P.2
  • 42
    • 57249097123 scopus 로고    scopus 로고
    • Developing Aspergillus as a host for heterologous expression
    • Lubertozzi D., Keasling J.D. Developing Aspergillus as a host for heterologous expression. Biotechnol Adv 2009, 27:53-75.
    • (2009) Biotechnol Adv , vol.27 , pp. 53-75
    • Lubertozzi, D.1    Keasling, J.D.2
  • 43
    • 56049127329 scopus 로고    scopus 로고
    • Characterization of the Aspergillus niger prtT, a unique regulator of extracellular protease encoding genes
    • Punt P.J., Schuren F.H., Lehmbeck J., Christensen T., Hjort C., van den Hondel C.A. Characterization of the Aspergillus niger prtT, a unique regulator of extracellular protease encoding genes. Fungal Genet Biol 2008, 45:1591-1599.
    • (2008) Fungal Genet Biol , vol.45 , pp. 1591-1599
    • Punt, P.J.1    Schuren, F.H.2    Lehmbeck, J.3    Christensen, T.4    Hjort, C.5    van den Hondel, C.A.6
  • 44
    • 58149359283 scopus 로고    scopus 로고
    • Agrobacterium-mediated transformation of the filamentous fungus Aspergillus awamori
    • Michielse C.B., Hooykaas P.J., van den Hondel C.A., Ram A.F. Agrobacterium-mediated transformation of the filamentous fungus Aspergillus awamori. Nat Protoc 2008, 3:1671-1678.
    • (2008) Nat Protoc , vol.3 , pp. 1671-1678
    • Michielse, C.B.1    Hooykaas, P.J.2    van den Hondel, C.A.3    Ram, A.F.4
  • 45
    • 59849087031 scopus 로고    scopus 로고
    • An enzyme cocktail for efficient protoplast formation in Aspergillus niger
    • de Bekker C., Wiebenga A., Aguilar G., Wosten H.A. An enzyme cocktail for efficient protoplast formation in Aspergillus niger. J Microbiol Methods 2009, 76:305-306.
    • (2009) J Microbiol Methods , vol.76 , pp. 305-306
    • de Bekker, C.1    Wiebenga, A.2    Aguilar, G.3    Wosten, H.A.4
  • 46
    • 0025601688 scopus 로고
    • Regulation of the glaA gene of Aspergillus niger
    • Fowler T., Berka R.M., Ward M. Regulation of the glaA gene of Aspergillus niger. Curr Genet 1990, 18:537-545.
    • (1990) Curr Genet , vol.18 , pp. 537-545
    • Fowler, T.1    Berka, R.M.2    Ward, M.3
  • 48
    • 13544263301 scopus 로고    scopus 로고
    • Metabolically independent and accurately adjustable Aspergillus sp. expression system
    • Pachlinger R., Mitterbauer R., Adam G., Strauss J. Metabolically independent and accurately adjustable Aspergillus sp. expression system. Appl Environ Microbiol 2005, 71:672-678.
    • (2005) Appl Environ Microbiol , vol.71 , pp. 672-678
    • Pachlinger, R.1    Mitterbauer, R.2    Adam, G.3    Strauss, J.4
  • 49
    • 77249093008 scopus 로고    scopus 로고
    • A novel expression system for intracellular production and purification of recombinant affinity-tagged proteins in Aspergillus niger
    • Roth A.H., Dersch P. A novel expression system for intracellular production and purification of recombinant affinity-tagged proteins in Aspergillus niger. Appl Microbiol Biotechnol 2010, 86:659-670.
    • (2010) Appl Microbiol Biotechnol , vol.86 , pp. 659-670
    • Roth, A.H.1    Dersch, P.2
  • 51
    • 31844452566 scopus 로고    scopus 로고
    • High expression of a synthetic gene encoding potato alpha-glucan phosphorylase in Aspergillus niger
    • Koda A., Bogaki T., Minetoki T., Hirotsune M. High expression of a synthetic gene encoding potato alpha-glucan phosphorylase in Aspergillus niger. J Biosci Bioeng 2005, 100:531-537.
    • (2005) J Biosci Bioeng , vol.100 , pp. 531-537
    • Koda, A.1    Bogaki, T.2    Minetoki, T.3    Hirotsune, M.4
  • 54
    • 0036081372 scopus 로고    scopus 로고
    • Genomic database resources for Dictyostelium discoideum
    • Kreppel L., Kimmel A.R. Genomic database resources for Dictyostelium discoideum. Nucleic Acids Res 2002, 30:84-86.
    • (2002) Nucleic Acids Res , vol.30 , pp. 84-86
    • Kreppel, L.1    Kimmel, A.R.2
  • 56
    • 0024297025 scopus 로고
    • Codon preference in Dictyostelium discoideum
    • Warrick H.M., Spudich J.A. Codon preference in Dictyostelium discoideum. Nucleic Acids Res 1988, 16:6617-6635.
    • (1988) Nucleic Acids Res , vol.16 , pp. 6617-6635
    • Warrick, H.M.1    Spudich, J.A.2
  • 58
    • 0028881911 scopus 로고
    • Recombinant glycoprotein production in the slime mould Dictyostelium discoideum
    • Williams K.L., Emslie K.R., Slade M.B. Recombinant glycoprotein production in the slime mould Dictyostelium discoideum. Curr Opin Biotechnol 1995, 6:538-542.
    • (1995) Curr Opin Biotechnol , vol.6 , pp. 538-542
    • Williams, K.L.1    Emslie, K.R.2    Slade, M.B.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.