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Volumn 3, Issue 4, 2010, Pages 403-411

Revolutionizing membrane protein overexpression in bacteria

Author keywords

[No Author keywords available]

Indexed keywords

BACTERIAL PROTEIN; MEMBRANE PROTEIN;

EID: 77954164253     PISSN: 17517907     EISSN: 17517915     Source Type: Journal    
DOI: 10.1111/j.1751-7915.2009.00148.x     Document Type: Short Survey
Times cited : (54)

References (68)
  • 1
    • 0014371028 scopus 로고
    • The nature of mutants in the lac promoter region
    • Arditti, R.R., Scaife, J.G., and Beckwith, J.R. (1968) The nature of mutants in the lac promoter region. J Mol Biol 38: 421-426.
    • (1968) J Mol Biol , vol.38 , pp. 421-426
    • Arditti, R.R.1    Scaife, J.G.2    Beckwith, J.R.3
  • 2
    • 0037450548 scopus 로고    scopus 로고
    • The expression of outer membrane proteins for crystallization
    • DOI 10.1016/S0005-2736(02)00711-3
    • Bannwarth, M., and Schulz, G.E. (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
  • 4
    • 57049180835 scopus 로고    scopus 로고
    • Cell-free co-expression of functional membrane proteins and apolipoprotein, forming soluble nanolipoprotein particles
    • Cappuccio, J.A., Blanchette, C.D., Sulchek, T.A., Arroyo, E.S., Kralj, J.M., Hinz, A.K., et al. (2008) Cell-free co-expression of functional membrane proteins and apolipoprotein, forming soluble nanolipoprotein particles. Mol Cell Proteomics 7: 2246-2253.
    • (2008) Mol Cell Proteomics , vol.7 , pp. 2246-2253
    • Cappuccio, J.A.1    Blanchette, C.D.2    Sulchek, T.A.3    Arroyo, E.S.4    Kralj, J.M.5    Hinz, A.K.6
  • 5
    • 0346935999 scopus 로고    scopus 로고
    • DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli
    • DOI 10.1016/S1046-5928(03)00233-X
    • Chen, Y., Song, J., Sui, S.F., and Wang, D.N. (2003) DnaK and DnaJ facilitated the folding process and reduced inclusion body formation of magnesium transporter CorA overexpressed in Escherichia coli. Protein Expr Purif 32: 221-231. (Pubitemid 38039013)
    • (2003) Protein Expression and Purification , vol.32 , Issue.2 , pp. 221-231
    • Chen, Y.1    Song, J.2    Sui, S.-F.3    Wang, D.-N.4
  • 8
    • 19744376674 scopus 로고    scopus 로고
    • Biochemistry: Global topology analysis of the Escherichia coli inner membrane proteome
    • DOI 10.1126/science.1109730
    • Daley, D.O., Rapp, M., Granseth, E., Melen, K., Drew, D., and von Heijne, G. (2005) Global topology analysis of the Escherichia coli inner membrane proteome. Science 308: 1321-1323. (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
  • 9
    • 0035955445 scopus 로고    scopus 로고
    • Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli
    • DOI 10.1016/S0014-5793(01)02980-5, PII S0014579301029805
    • Drew, D.E., von Heijne, G., Nordlund, P., and de Gier, J.W.L. (2001) Green fluorescent protein as an indicator to monitor membrane protein overexpression in Escherichia coli. FEBS Lett 507: 220-224. (Pubitemid 33001546)
    • (2001) FEBS Letters , vol.507 , Issue.2 , pp. 220-224
    • Drew, D.E.1    Von Heijne, G.2    Nordlund, P.3    De Gier, J.-W.L.4
  • 11
    • 33645454462 scopus 로고    scopus 로고
    • Optimization of membrane protein overexpression and purification using GFP fusions
    • Drew, D., Lerch, M., Kunji, E., Slotboom, D.J., and de Gier, J.W. (2006) Optimization of membrane protein overexpression and purification using GFP fusions. Nat Methods 3: 303-313.
    • (2006) Nat Methods , vol.3 , pp. 303-313
    • Drew, D.1    Lerch, M.2    Kunji, E.3    Slotboom, D.J.4    De Gier, J.W.5
  • 12
    • 68349160816 scopus 로고    scopus 로고
    • Bacterial expression of a eukaryotic membrane protein in fusion to various Mistic orthologs
    • Dvir, H., and Choe, S. (2009) Bacterial expression of a eukaryotic membrane protein in fusion to various Mistic orthologs. Protein Exp Purif 68: 28-33.
    • (2009) Protein Exp Purif , vol.68 , pp. 28-33
    • Dvir, H.1    Choe, S.2
  • 13
    • 38149060175 scopus 로고    scopus 로고
    • Lactococcus lactis as expression host for the biosynthetic incorporation of tryptophan analogues into recombinant proteins
    • El Khattabi, M., van Roosmalen, M.L., Jager, D., Metselaar, H., Permentier, H., Leenhouts, K., and Broos, J. (2008) Lactococcus lactis as expression host for the biosynthetic incorporation of tryptophan analogues into recombinant proteins. Biochem J 409: 193-198.
    • (2008) Biochem J , vol.409 , pp. 193-198
    • El Khattabi, M.1    Van Roosmalen, M.L.2    Jager, D.3    Metselaar, H.4    Permentier, H.5    Leenhouts, K.6    Broos, J.7
  • 14
    • 66149100100 scopus 로고    scopus 로고
    • Independent gene duplications of the YidC/Oxa/Alb3 family enabled a specialized cotranslational function
    • Funes, S., Hasona, A., Bauerschmitt, H., Grubbauer, C., Kauff, F., Collins, R., et al. (2009) Independent gene duplications of the YidC/Oxa/Alb3 family enabled a specialized cotranslational function. Proc Natl Acad Sci USA 106: 6656-6661.
    • (2009) Proc Natl Acad Sci USA , vol.106 , pp. 6656-6661
    • Funes, S.1    Hasona, A.2    Bauerschmitt, H.3    Grubbauer, C.4    Kauff, F.5    Collins, R.6
  • 15
    • 33646002978 scopus 로고    scopus 로고
    • Toxic protein expression in Escherichia coli using a rhamnose-based tightly regulated and tunable promoter system
    • Giacalone, M.J., Gentile, A.M., Lovitt, B.T., Berkley, N.L., Gunderson, C.W., and Surber, M.W. (2006) Toxic protein expression in Escherichia coli using a rhamnose-based tightly regulated and tunable promoter system. Biotechniques 40: 355-364.
    • (2006) Biotechniques , vol.40 , pp. 355-364
    • Giacalone, M.J.1    Gentile, A.M.2    Lovitt, B.T.3    Berkley, N.L.4    Gunderson, C.W.5    Surber, M.W.6
  • 16
    • 33748483846 scopus 로고    scopus 로고
    • Humanization of yeast to produce complex terminally sialylated glycoproteins
    • Hamilton, S.R., Davidson, R.C., Sethuraman, N., Nett, J.H., Jiang, Y., Rios, S., et al. (2006) Humanization of yeast to produce complex terminally sialylated glycoproteins. Science 313: 1441-1443.
    • (2006) Science , vol.313 , pp. 1441-1443
    • Hamilton, S.R.1    Davidson, R.C.2    Sethuraman, N.3    Nett, J.H.4    Jiang, Y.5    Rios, S.6
  • 18
    • 0033342531 scopus 로고    scopus 로고
    • Recent advances in the understanding of membrane protein assembly and structure
    • von Heijne, G. (1999) Recent advances in the understanding of membrane protein assembly and structure. Q Rev Biophys 32: 285-307.
    • (1999) Q Rev Biophys , vol.32 , pp. 285-307
    • Von Heijne, G.1
  • 19
    • 3943059566 scopus 로고    scopus 로고
    • Roles of N-linked glycans in the endoplasmic reticulum
    • DOI 10.1146/annurev.biochem.73.011303.073752
    • Helenius, A., and Aebi, M. (2004) Roles of N-linked glycans in the endoplasmic reticulum. Annu Rev Biochem 73: 1019-1049. (Pubitemid 39050393)
    • (2004) Annual Review of Biochemistry , vol.73 , pp. 1019-1049
    • Helenius, A.1    Aebi, M.2
  • 20
    • 0026544038 scopus 로고
    • Bacteriophage T7 RNA polymerase travels far ahead of ribosomes in vivo
    • Iost, I., Guillerez, J., and Dreyfus, M. (1992) Bacteriophage T7 RNA polymerase travels far ahead of ribosomes in vivo. J Bacteriol 174: 619-622.
    • (1992) J Bacteriol , vol.174 , pp. 619-622
    • Iost, I.1    Guillerez, J.2    Dreyfus, M.3
  • 21
    • 15744391469 scopus 로고    scopus 로고
    • Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors
    • DOI 10.1016/j.pep.2005.01.013
    • Ishihara, G., Goto, M., Saeki, M., Ito, K., Hori, T., Kigawa, T., et al. (2005) Expression of G protein coupled receptors in a cell-free translational system using detergents and thioredoxin-fusion vectors. Protein Expr Purif 41: 27-37. (Pubitemid 40406360)
    • (2005) Protein Expression and Purification , vol.41 , Issue.1 , pp. 27-37
    • Ishihara, G.1    Goto, M.2    Saeki, M.3    Ito, K.4    Hori, T.5    Kigawa, T.6    Shirouzu, M.7    Yokoyama, S.8
  • 22
    • 53049104570 scopus 로고    scopus 로고
    • Insertion of membrane proteins into discoidal membranes using a cell-free protein expression approach
    • Katzen, F., Fletcher, J.E., Yang, J.P., Kang, D., Peterson, T.C., Cappuccio, J.A., et al. (2008) Insertion of membrane proteins into discoidal membranes using a cell-free protein expression approach. J Proteome Res 7: 3535-3542.
    • (2008) J Proteome Res , vol.7 , pp. 3535-3542
    • Katzen, F.1    Fletcher, J.E.2    Yang, J.P.3    Kang, D.4    Peterson, T.C.5    Cappuccio, J.A.6
  • 23
    • 41049115757 scopus 로고    scopus 로고
    • Application of Mistic to improving the expression and membrane integration of histidine kinase receptors from Escherichia coli
    • Kefala, G., Kwiatkowski, W., Esquivies, L., Maslennikov, I., and Choe, S. (2007) Application of Mistic to improving the expression and membrane integration of histidine kinase receptors from Escherichia coli. J Struct Funct Genomics 8: 167-172.
    • (2007) J Struct Funct Genomics , vol.8 , pp. 167-172
    • Kefala, G.1    Kwiatkowski, W.2    Esquivies, L.3    Maslennikov, I.4    Choe, S.5
  • 25
    • 28244458078 scopus 로고    scopus 로고
    • Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system
    • DOI 10.1111/j.1742-4658.2005.05002.x
    • Klammt, C., Schwarz, D., Fendler, K., Haase, W., Dotsch, V., and Bernhard, F. (2005) Evaluation of detergents for the soluble expression of alpha-helical and beta-barrel-type integral membrane proteins by a preparative scale individual cell-free expression system. FEBS J 272: 6024-6038. (Pubitemid 41713694)
    • (2005) FEBS Journal , vol.272 , Issue.23 , pp. 6024-6038
    • Klammt, C.1    Schwarz, D.2    Fendler, K.3    Haase, W.4    Dotsch, V.5    Bernhard, F.6
  • 26
    • 62149096127 scopus 로고    scopus 로고
    • Use of folding modulators to improve heterologous protein production in Escherichia coli
    • Kolaj, O., Spada, S., Robin, S., and Wall, J.G. (2009) Use of folding modulators to improve heterologous protein production in Escherichia coli. Microb Cell Fact 8: 9.
    • (2009) Microb Cell Fact , vol.8 , pp. 9
    • Kolaj, O.1    Spada, S.2    Robin, S.3    Wall, J.G.4
  • 27
    • 11144234979 scopus 로고    scopus 로고
    • Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli
    • DOI 10.1110/ps.041022305
    • Korepanova, A., Gao, F.P., Hua, Y., Qin, H., Nakamoto, R.K., and Cross, T.A. (2005) Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli. Protein Sci 14: 148-158. (Pubitemid 40054126)
    • (2005) Protein Science , vol.14 , Issue.1 , pp. 148-158
    • Korepanova, A.1    Gao, F.P.2    Hua, Y.3    Qin, H.4    Nakamoto, R.K.5    Cross, T.A.6
  • 28
    • 0030888910 scopus 로고    scopus 로고
    • Controlled overproduction of proteins by lactic acid bacteria
    • DOI 10.1016/S0167-7799(97)01029-9, PII S0167779997010299
    • Kuipers, O.P., de Ruyter, P.G., Kleerebezem, M., and de Vos, W.M. (1997) Controlled overproduction of proteins by lactic acid bacteria. Trends Biotechnol 15: 135-140. (Pubitemid 27181696)
    • (1997) Trends in Biotechnology , vol.15 , Issue.4 , pp. 135-140
    • Kuipers, O.P.1    De Ruyter, P.G.G.A.2    Kleerebezem, M.3    De Vos, W.M.4
  • 29
    • 0037450575 scopus 로고    scopus 로고
    • Lactococcus lactis as host for overproduction of functional membrane proteins
    • Kunji, E.R., Slotboom, D.J., and Poolman, B. (2003) Lactococcus lactis as host for overproduction of functional membrane proteins. Biochim Biophys Acta 1610: 97-108.
    • (2003) Biochim Biophys Acta , vol.1610 , pp. 97-108
    • Kunji, E.R.1    Slotboom, D.J.2    Poolman, B.3
  • 30
    • 25844445376 scopus 로고    scopus 로고
    • Eukaryotic membrane protein overproduction in Lactococcus lactis
    • DOI 10.1016/j.copbio.2005.08.006, PII S0958166905001333, Tissue and Cell Engineering/Biochemical Engineering
    • Kunji, E.R., Chan, K.W., Slotboom, D.J., Floyd, S., O'Connor, R., and Monne, M. (2005) Eukaryotic membrane protein overproduction in Lactococcus lactis. Curr Opin Biotechnol 16: 546-551. (Pubitemid 41393836)
    • (2005) Current Opinion in Biotechnology , vol.16 , Issue.5 , pp. 546-551
    • Kunji, E.R.S.1    Ka, W.C.2    Slotboom, D.J.3    Floyd, S.4    O'Connor, R.5    Monne, M.6
  • 31
    • 52949105367 scopus 로고    scopus 로고
    • Efficient production of membrane-integrated and detergent-soluble G protein-coupled receptors in Escherichia coli
    • Link, A.J., Skretas, G., Strauch, E.M., Chari, N.S., and Georgiou, G. (2008) Efficient production of membrane-integrated and detergent-soluble G protein-coupled receptors in Escherichia coli. Protein Sci 17: 1857-1863.
    • (2008) Protein Sci , vol.17 , pp. 1857-1863
    • Link, A.J.1    Skretas, G.2    Strauch, E.M.3    Chari, N.S.4    Georgiou, G.5
  • 32
    • 0035854694 scopus 로고    scopus 로고
    • YidC/Oxa1p/A1b3: Evolutionarily conserved mediators of membrane protein assembly
    • PII S0014579301026163
    • Luirink, J., Samuelsson, T., and de Gier, J.W. (2001) YidC/Oxa1p/Alb3: evolutionarily conserved mediators of membrane protein assembly. FEBS Lett 501: 1-5. (Pubitemid 33712477)
    • (2001) FEBS Letters , vol.501 , Issue.1-3 , pp. 1-5
    • Luirink, J.1    Samuelsson, T.2    De Gier, J.-W.3
  • 33
    • 27144463438 scopus 로고    scopus 로고
    • Biogenesis of inner membrane proteins in Escherichia coli
    • DOI 10.1146/annurev.micro.59.030804.121246
    • Luirink, J., von Heijne, G., Houben, E., and de Gier, J.W. (2005) Biogenesis of inner membrane proteins in Escherichia coli. Annu Rev Microbiol 59: 329-355. (Pubitemid 41507435)
    • (2005) Annual Review of Microbiology , vol.59 , pp. 329-355
    • Luirink, J.1    Von Heijne, G.2    Houben, E.3    De Gier, J.-W.4
  • 34
    • 34247893770 scopus 로고    scopus 로고
    • Structural genomics and drug discovery
    • Lundstrom, K. (2007) Structural genomics and drug discovery. J Cell Mol Med 11: 224-238.
    • (2007) J Cell Mol Med , vol.11 , pp. 224-238
    • Lundstrom, K.1
  • 36
    • 49449114407 scopus 로고    scopus 로고
    • Co-evolving stability and conformational homogeneity of the human adenosine A2a receptor
    • Magnani, F., Shibata, Y., Serrano-Vega, M.J., and Tate, C.G. (2008) Co-evolving stability and conformational homogeneity of the human adenosine A2a receptor. Proc Natl Acad Sci USA 105: 10744-10749.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 10744-10749
    • Magnani, F.1    Shibata, Y.2    Serrano-Vega, M.J.3    Tate, C.G.4
  • 37
    • 41649116084 scopus 로고    scopus 로고
    • Engineering membrane protein overproduction in Escherichia coli
    • DOI 10.1110/ps.073242508
    • Martinez Molina, D., Cornvik, T., Eshaghi, S., Haeggstrom, J.Z., Nordlund, P., and Sabet, M.I. (2008) Engineering membrane protein overproduction in Escherichia coli. Protein Sci 17: 673-680. (Pubitemid 351480861)
    • (2008) Protein Science , vol.17 , Issue.4 , pp. 673-680
    • Molina, D.M.1    Cornvik, T.2    Eshaghi, S.3    Haeggstrom, J.Z.4    Nordlund, P.5    Sabet, M.I.6
  • 38
    • 59949092470 scopus 로고    scopus 로고
    • Genetic selection system for improving recombinant membrane protein expression in E. coli
    • Massey-Gendel, E., Zhao, A., Boulting, G., Kim, H.Y., Balamotis, M.A., Seligman, L.M., et al. (2009) Genetic selection system for improving recombinant membrane protein expression in E. coli. Protein Sci 18: 372-383.
    • (2009) Protein Sci , vol.18 , pp. 372-383
    • Massey-Gendel, E.1    Zhao, A.2    Boulting, G.3    Kim, H.Y.4    Balamotis, M.A.5    Seligman, L.M.6
  • 39
    • 0030593468 scopus 로고    scopus 로고
    • Over-production of proteins in Escherichia coli: Mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels
    • DOI 10.1006/jmbi.1996.0399
    • Miroux, B., and Walker, J.E. (1996) Over-production of proteins in Escherichia coli: mutant hosts that allow synthesis of some membrane proteins and globular proteins at high levels. J Mol Biol 260: 289-298. (Pubitemid 26254109)
    • (1996) Journal of Molecular Biology , vol.260 , Issue.3 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 40
    • 28844468525 scopus 로고    scopus 로고
    • Functional expression of eukaryotic membrane proteins in Lactococcus lactis
    • DOI 10.1110/ps.051689905
    • Monne, M., Chan, K.W., Slotboom, D.J., and Kunji, E.R. (2005a) Functional expression of eukaryotic membrane proteins in Lactococcus lactis. Protein Sci 14: 3048-3056. (Pubitemid 41770145)
    • (2005) Protein Science , vol.14 , Issue.12 , pp. 3048-3056
    • Monne, M.1    Ka, W.C.2    Slotboom, D.-J.3    Kunji, E.R.S.4
  • 41
    • 11444249293 scopus 로고    scopus 로고
    • Competition between neighboring topogenic signals during membrane protein insertion into the ER
    • DOI 10.1111/j.1432-1033.2004.04394.x
    • Monne, M., Hessa, T., Thissen, L., and von Heijne, G. (2005b) Competition between neighboring topogenic signals during membrane protein insertion into the ER. FEBS J 272: 28-36. (Pubitemid 40083064)
    • (2005) FEBS Journal , vol.272 , Issue.1 , pp. 28-36
    • Monne, M.1    Hessa, T.2    Thissen, L.3    Von Heijne, G.4
  • 42
    • 33947396752 scopus 로고    scopus 로고
    • The mimivirus genome encodes a mitochondrial carrier that transports dATP and dTTP
    • DOI 10.1128/JVI.02386-06
    • Monne, M., Robinson, A.J., Boes, C., Harbour, M.E., Fearnley, I.M., and Kunji, E.R. (2007) The mimivirus genome encodes a mitochondrial carrier that transports dATP and dTTP. J Virol 81: 3181-3186. (Pubitemid 46456627)
    • (2007) Journal of Virology , vol.81 , Issue.7 , pp. 3181-3186
    • Monne, M.1    Robinson, A.J.2    Boes, C.3    Harbour, M.E.4    Fearnley, I.M.5    Kunji, E.R.S.6
  • 43
    • 34147158906 scopus 로고    scopus 로고
    • Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis
    • DOI 10.1042/BJ20061473
    • Park, K.H., Berrier, C., Lebaupain, F., Pucci, B., Popot, J.L., Ghazi, A., and Zito, F. (2007) Fluorinated and hemifluorinated surfactants as alternatives to detergents for membrane protein cell-free synthesis. Biochem J 403: 183-187. (Pubitemid 46569880)
    • (2007) Biochemical Journal , vol.403 , Issue.1 , pp. 183-187
    • Park, K.-H.1    Berrier, C.2    Lebaupain, F.3    Pucci, B.4    Popot, J.-L.5    Ghazi, A.6    Zito, F.7
  • 44
    • 66249083118 scopus 로고    scopus 로고
    • Emerging roles for lipids in shaping membrane-protein function
    • Phillips, R., Ursell, T., Wiggins, P., and Sens, P. (2009) Emerging roles for lipids in shaping membrane-protein function. Nature 459: 379-385.
    • (2009) Nature , vol.459 , pp. 379-385
    • Phillips, R.1    Ursell, T.2    Wiggins, P.3    Sens, P.4
  • 45
    • 56249140425 scopus 로고    scopus 로고
    • Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL
    • Powl, A.M., East, J.M., and Lee, A.G. (2008) Importance of direct interactions with lipids for the function of the mechanosensitive channel MscL. Biochemistry 47: 12175-12184.
    • (2008) Biochemistry , vol.47 , pp. 12175-12184
    • Powl, A.M.1    East, J.M.2    Lee, A.G.3
  • 48
    • 14544292475 scopus 로고    scopus 로고
    • NMR structure of mistic, a membrane-integrating protein for membrane protein expression
    • DOI 10.1126/science.1106392
    • Roosild, T.P., Greenwald, J., Vega, M., Castronovo, S., Riek, R., and Choe, S. (2005) NMR structure of Mistic, a membrane-integrating protein for membrane protein expression. Science 307: 1317-1321. (Pubitemid 40299982)
    • (2005) Science , vol.307 , Issue.5713 , pp. 1317-1321
    • Roosild, T.P.1    Greenwald, J.2    Vega, M.3    Castronovo, S.4    Riek, R.5    Choe, S.6
  • 49
    • 54449087770 scopus 로고    scopus 로고
    • Directed evolution of a G protein-coupled receptor for expression, stability, and binding selectivity
    • Sarkar, C.A., Dodevski, I., Kenig, M., Dudli, S., Mohr, A., Hermans, E., and Pluckthun, A. (2008) Directed evolution of a G protein-coupled receptor for expression, stability, and binding selectivity. Proc Natl Acad Sci USA 105: 14808-14813.
    • (2008) Proc Natl Acad Sci USA , vol.105 , pp. 14808-14813
    • Sarkar, C.A.1    Dodevski, I.2    Kenig, M.3    Dudli, S.4    Mohr, A.5    Hermans, E.6    Pluckthun, A.7
  • 50
    • 34247566971 scopus 로고    scopus 로고
    • Cell-free complements in vivo expression of the E. coli membrane proteome
    • DOI 10.1110/ps.062696307
    • Savage, D.F., Anderson, C.L., Robles-Colmenares, Y., Newby, Z.E., and Stroud, R.M. (2007) Cell-free complements in vivo expression of the E. coli membrane proteome. Protein Sci 16: 966-976. (Pubitemid 46683201)
    • (2007) Protein Science , vol.16 , Issue.5 , pp. 966-976
    • Savage, D.F.1    Anderson, C.L.2    Robles-Colmenares, Y.3    Newby, Z.E.4    Stroud, R.M.5
  • 51
    • 55749110716 scopus 로고    scopus 로고
    • Production of membrane proteins using cell-free expression systems
    • Schwarz, D., Dotsch, V., and Bernhard, F. (2008) Production of membrane proteins using cell-free expression systems. Proteomics 8: 3933-3946.
    • (2008) Proteomics , vol.8 , pp. 3933-3946
    • Schwarz, D.1    Dotsch, V.2    Bernhard, F.3
  • 54
    • 58249084813 scopus 로고    scopus 로고
    • Genetic analysis of G protein-coupled receptor expression in Escherichia coli: Inhibitory role of DnaJ on the membrane integration of the human central cannabinoid receptor
    • Skretas, G., and Georgiou, G. (2009) Genetic analysis of G protein-coupled receptor expression in Escherichia coli: inhibitory role of DnaJ on the membrane integration of the human central cannabinoid receptor. Biotechnol Bioeng 102: 357-367.
    • (2009) Biotechnol Bioeng , vol.102 , pp. 357-367
    • Skretas, G.1    Georgiou, G.2
  • 56
    • 33748129976 scopus 로고    scopus 로고
    • Comparative analysis and 'expression space' coverage of the production of prokaryotic membrane proteins for structural genomics
    • DOI 10.1110/ps.062312706
    • Surade, S., Klein, M., Stolt-Bergner, P.C., Muenke, C., Roy, A., and Michel, H. (2006) Comparative analysis and 'expression space' coverage of the production of prokaryotic membrane proteins for structural genomics. Protein Sci 15: 2178-2189. (Pubitemid 44316020)
    • (2006) Protein Science , vol.15 , Issue.9 , pp. 2178-2189
    • Surade, S.1    Klein, M.2    Stolt-Bergner, P.C.3    Muenke, C.4    Roy, A.5    Michel, H.6
  • 57
    • 0029838532 scopus 로고    scopus 로고
    • Purification of a rat neurotensin receptor expressed in Escherichia coli
    • Tucker, J., and Grisshammer, R. (1996) Purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem J 317: 891-899. (Pubitemid 26308267)
    • (1996) Biochemical Journal , vol.317 , Issue.3 , pp. 891-899
    • Tucker, J.1    Grisshammer, R.2
  • 61
    • 0028834958 scopus 로고
    • Properties of N-terminal tails in G-protein coupled receptors - A statistical study
    • Wallin, E., and von Heijne, G. (1995) Properties of N-terminal tails in G-protein coupled receptors - a statistical study. Protein Eng 8: 693-698.
    • (1995) Protein Eng , vol.8 , pp. 693-698
    • Wallin, E.1    Von Heijne, G.2
  • 62
    • 0031954925 scopus 로고    scopus 로고
    • Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms
    • Wallin, E., and von Heijne, G. (1998) Genome-wide analysis of integral membrane proteins from eubacterial, archaean, and eukaryotic organisms. Protein Sci 7: 1029-1038. (Pubitemid 28216544)
    • (1998) Protein Science , vol.7 , Issue.4 , pp. 1029-1038
    • Wallin, E.1    Von Heijne, G.2
  • 64
    • 12244292640 scopus 로고    scopus 로고
    • Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli
    • Weiss, H.M., and Grisshammer, R. (2002) Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli. Eur J Biochem 269: 82-92.
    • (2002) Eur J Biochem , vol.269 , pp. 82-92
    • Weiss, H.M.1    Grisshammer, R.2
  • 65
    • 1942468187 scopus 로고    scopus 로고
    • Automated large-scale purification of a G protein-coupled receptor for neurotensin
    • DOI 10.1016/S0014-5793(04)00195-4, PII S0014579304001954
    • White, J.F., Trinh, L.B., Shiloach, J., and Grisshammer, R. (2004) Automated large-scale purification of a G protein-coupled receptor for neurotensin. FEBS Lett 564: 289-293. (Pubitemid 38520935)
    • (2004) FEBS Letters , vol.564 , Issue.3 , pp. 289-293
    • White, J.F.1    Trinh, L.B.2    Shiloach, J.3    Grisshammer, R.4
  • 66
    • 43049142194 scopus 로고    scopus 로고
    • High yield cell-free production of integral membrane proteins without refolding or detergents
    • Wuu, J.J., and Swartz, J.R. (2008) High yield cell-free production of integral membrane proteins without refolding or detergents. Biochim Biophys Acta 1778: 1237-1250.
    • (2008) Biochim Biophys Acta , vol.1778 , pp. 1237-1250
    • Wuu, J.J.1    Swartz, J.R.2
  • 67
    • 25844443463 scopus 로고    scopus 로고
    • Expression of human peripheral cannabinoid receptor for structural studies
    • DOI 10.1110/ps.051550305
    • Yeliseev, A.A., Wong, K.K., Soubias, O., and Gawrisch, K. (2005) Expression of human peripheral cannabinoid receptor for structural studies. Protein Sci 14: 2638-2653. (Pubitemid 41395590)
    • (2005) Protein Science , vol.14 , Issue.10 , pp. 2638-2653
    • Yeliseev, A.A.1    Wong, K.K.2    Soubias, O.3    Gawrisch, K.4


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