메뉴 건너뛰기




Volumn 20, Issue 3, 2011, Pages 597-609

A secretory system for bacterial production of high-profile protein targets

Author keywords

Escherichia coli; Extracellular protein expression; High throughput protein expression; OmpA; OmpF; OsmY

Indexed keywords

MEMBRANE PROTEIN; OSMOTICALLY INDUCIBLE PROTEIN Y; OUTER MEMBRANE PROTEIN A; OUTER MEMBRANE PROTEIN F; RECOMBINANT PROTEIN; UNCLASSIFIED DRUG;

EID: 79952174790     PISSN: 09618368     EISSN: 1469896X     Source Type: Journal    
DOI: 10.1002/pro.593     Document Type: Article
Times cited : (36)

References (60)
  • 1
    • 41449117607 scopus 로고    scopus 로고
    • Thioredoxins and glutaredoxins as facilitators of protein folding
    • Berndt C, Lillig CH, Holmgren A (2008) Thioredoxins and glutaredoxins as facilitators of protein folding. Biochim Biophys Acta 1783:641-650.
    • (2008) Biochim Biophys Acta , vol.1783 , pp. 641-650
    • Berndt, C.1    Lillig, C.H.2    Holmgren, A.3
  • 2
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant protein folding and misfolding in Escherichia coli
    • Baneyx F, Mujacic M (2004) Recombinant protein folding and misfolding in Escherichia coli. Nat Biotechnol 22:1399-1408.
    • (2004) Nat Biotechnol , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 3
    • 0023734585 scopus 로고
    • Pore-forming colicins: Synthesis, extracellular release, mode of action, immunity
    • Lazdunski CJ (1988) Pore-forming colicins: synthesis, extracellular release, mode of action, immunity. Biochimie 70:1291-1296.
    • (1988) Biochimie , vol.70 , pp. 1291-1296
    • Lazdunski, C.J.1
  • 4
    • 0036589160 scopus 로고    scopus 로고
    • Use of colicin-based genetic tools for studying bacterial protein transport
    • DOI 10.1016/S0300-9084(02)01412-8, PII S0300908402014128
    • Filloux A, Voulhoux R, Ize B, Gerard F, Ball G, Wu LF (2002) Use of colicin-based genetic tools for studying bacterial protein transport. Biochimie 84:489-497. (Pubitemid 35350880)
    • (2002) Biochimie , vol.84 , Issue.5-6 , pp. 489-497
    • Filloux, A.1    Voulhoux, R.2    Ize, B.3    Gerard, F.4    Ball, G.5    Wu, L.F.6
  • 5
    • 0026911135 scopus 로고
    • E. coli hemolysin interactions with prokaryotic and eukaryotic cell membranes
    • Hughes C, Stanley P, Koronakis V (1992) E. coli hemolysin interactions with prokaryotic and eukaryotic cell membranes. Bioessays 14:519-525.
    • (1992) Bioessays , vol.14 , pp. 519-525
    • Hughes, C.1    Stanley, P.2    Koronakis, V.3
  • 6
    • 53549088613 scopus 로고    scopus 로고
    • Proteome-based identification of fusion partner for high-level extracellular production of recombinant proteins in Escherichia coli
    • Qian ZG, Xia XX, Choi JH, Lee SY (2008) Proteome-based identification of fusion partner for high-level extracellular production of recombinant proteins in Escherichia coli. Biotechnol Bioeng 101:587-601.
    • (2008) Biotechnol Bioeng , vol.101 , pp. 587-601
    • Qian, Z.G.1    Xia, X.X.2    Choi, J.H.3    Lee, S.Y.4
  • 7
    • 44649118664 scopus 로고    scopus 로고
    • Comparison of the extracellular proteomes of Escherichia coli B and K-12 strains during high cell density cultivation
    • Xia XX, Han MJ, Lee SY, Yoo JS (2008) Comparison of the extracellular proteomes of Escherichia coli B and K-12 strains during high cell density cultivation. Proteomics 8:2089-2103.
    • (2008) Proteomics , vol.8 , pp. 2089-2103
    • Xia, X.X.1    Han, M.J.2    Lee, S.Y.3    Yoo, J.S.4
  • 8
    • 33646550516 scopus 로고    scopus 로고
    • Proteomic analysis of extracellular proteins from Escherichia coli W3110
    • DOI 10.1021/pr050401j
    • Nandakumar MP, Cheung A, Marten MR (2006) Proteomic analysis of extracellular proteins from Escherichia coli W3110. J Proteome Res 5:1155-1161. (Pubitemid 43727793)
    • (2006) Journal of Proteome Research , vol.5 , Issue.5 , pp. 1155-1161
    • Nandakumar, M.P.1    Cheung, A.2    Marten, M.M.3
  • 9
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • DOI 10.1007/s00253-004-1559-9
    • Choi JH, Lee SY (2004) Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol 64:625-635. (Pubitemid 38822625)
    • (2004) Applied Microbiology and Biotechnology , vol.64 , Issue.5 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 10
  • 11
    • 0024604846 scopus 로고
    • Use of Bacteriocin Release Protein in E. Coli for Excretion of Human Growth-Hormone into the Culture-Medium
    • Hsiung HM, Cantrell A, Luirink J, Oudega B, Veros AJ, Becker GW (1989) Use of Bacteriocin Release Protein in E. Coli for Excretion of Human Growth-Hormone into the Culture-Medium. Biotechnol 7:267-271.
    • (1989) Biotechnol , vol.7 , pp. 267-271
    • Hsiung, H.M.1    Cantrell, A.2    Luirink, J.3    Oudega, B.4    Veros, A.J.5    Becker, G.W.6
  • 12
    • 0023177768 scopus 로고
    • Construction of an excretion vector and extracellular production of human growth hormone from Escherichia coli
    • DOI 10.1016/0378-1119(87)90487-2
    • Kato C, Kobayashi T, Kudo T, Furusato T, Murakami Y, Tanaka T, Baba H, Oishi T, Ohtsuka E, Ikehara M, Yanagida T, Kato H, Moriyama S, Horikoshi K (1987) Construction of an excretion vector and extracellular production of human growth hormone from Escherichia coli. Gene 54:197-202. (Pubitemid 17100371)
    • (1987) Gene , vol.54 , Issue.2-3 , pp. 197-202
    • Kato, C.1    Kobayashi, T.2    Kudo, T.3
  • 13
    • 30544435865 scopus 로고    scopus 로고
    • Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli
    • DOI 10.1038/nbt1174, PII NBT1174
    • Zhang G, Brokx S, Weiner JH (2006) Extracellular accumulation of recombinant proteins fused to the carrier protein YebF in Escherichia coli. Nat Biotechnol 24:100-104. (Pubitemid 43083173)
    • (2006) Nature Biotechnology , vol.24 , Issue.1 , pp. 100-104
    • Zhang, G.1    Brokx, S.2    Weiner, J.H.3
  • 14
    • 0036793640 scopus 로고    scopus 로고
    • Excretion of human beta-endorphin into culture medium by using outer membrane protein F as a fusion partner in recombinant Escherichia coli
    • DOI 10.1128/AEM.68.10.4979-4985.2002
    • Jeong KJ, Lee SY (2002) Excretion of human beta-endorphin into culture medium by using outer membrane protein F as a fusion partner in recombinant Escherichia coli. Appl Environ Microbiol 68:4979-4985. (Pubitemid 35154808)
    • (2002) Applied and Environmental Microbiology , vol.68 , Issue.10 , pp. 4979-4985
    • Jeong, K.J.1    Lee, S.Y.2
  • 15
    • 0031904157 scopus 로고    scopus 로고
    • One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-alpha) from Escherichia coli caused by the synergistic effects of glycine and Triton X-100
    • Yang J, Moyana T, MacKenzie S, Xia Q, Xiang J (1998) One hundred seventy-fold increase in excretion of an FV fragment-tumor necrosis factor alpha fusion protein (sFV/TNF-alpha) from Escherichia coli caused by the synergistic effects of glycine and triton X-100. Appl Environ Microbiol 64:2869-2874. (Pubitemid 28363154)
    • (1998) Applied and Environmental Microbiology , vol.64 , Issue.8 , pp. 2869-2874
    • Yang, J.1    Moyana, T.2    Mackenzie, S.3    Xia, Q.4    Xiang, J.5
  • 16
    • 77049098063 scopus 로고    scopus 로고
    • Efficient production of extracellular proteins with Escherichia coli by means of optimized coexpression of bacteriocin release proteins
    • Sommer B, Friehs K, Flaschel E (2010) Efficient production of extracellular proteins with Escherichia coli by means of optimized coexpression of bacteriocin release proteins. J Biotechnol 145:350-358.
    • (2010) J Biotechnol , vol.145 , pp. 350-358
    • Sommer, B.1    Friehs, K.2    Flaschel, E.3
  • 17
    • 44049095603 scopus 로고    scopus 로고
    • SRP and Sec pathway leader peptides for antibody phage display and antibody fragment production in E. coli
    • DOI 10.1016/j.nbt.2008.01.001, PII S1871678408000022
    • Thie H, Schirrmann T, Paschke M, Dubel S, Hust M (2008) SRP and Sec pathway leader peptides for antibody phage display and antibody fragment production in E. coli. Nat Biotechnol 25:49-54. (Pubitemid 351713600)
    • (2008) New Biotechnology , vol.25 , Issue.1 , pp. 49-54
    • Thie, H.1    Schirrmann, T.2    Paschke, M.3    Dubel, S.4    Hust, M.5
  • 18
    • 0037294121 scopus 로고    scopus 로고
    • Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli
    • Shokri A, Sanden AM, Larsson G (2003) Cell and process design for targeting of recombinant protein into the culture medium of Escherichia coli. Appl Microbiol Biotechnol 60:654-664. (Pubitemid 36286671)
    • (2003) Applied Microbiology and Biotechnology , vol.60 , Issue.6 , pp. 654-664
    • Shokri, A.1    Sanden, A.M.2    Larsson, G.3
  • 21
    • 0035040679 scopus 로고    scopus 로고
    • Formation of disulphide bonds during secretion of proteins through the periplasmic-independent type I pathway
    • DOI 10.1046/j.1365-2958.2001.02410.x
    • Fernandez LA, de Lorenzo V (2001) Formation of disulphide bonds during secretion of proteins through the periplasmic-independent type I pathway. Mol Microbiol 40:332-346. (Pubitemid 32391629)
    • (2001) Molecular Microbiology , vol.40 , Issue.2 , pp. 332-346
    • Fernandez, L.A.1    De, L.V.2
  • 22
    • 0033760702 scopus 로고    scopus 로고
    • Specific secretion of active single-chain Fv antibodies into the supernatants of Escherichia coli cultures by use of the hemolysin system
    • Fernandez LA, Sola I, Enjuanes L, de Lorenzo V (2000) Specific secretion of active single-chain Fv antibodies into the supernatants of Escherichia coli cultures by use of the hemolysin system. Appl Environ Microbiol 66:5024-5029.
    • (2000) Appl Environ Microbiol , vol.66 , pp. 5024-5029
    • Fernandez, L.A.1    Sola, I.2    Enjuanes, L.3    De Lorenzo, V.4
  • 26
    • 0030893407 scopus 로고    scopus 로고
    • Protein folding in the bacterial periplasm
    • Missiakas D, Raina S (1997) Protein folding in the bacterial periplasm. J Bacteriol 179:2465-2471. (Pubitemid 27164541)
    • (1997) Journal of Bacteriology , vol.179 , Issue.8 , pp. 2465-2471
    • Missiakas, D.1    Raina, S.2
  • 28
    • 0036412057 scopus 로고    scopus 로고
    • Cloning and hemolysin-mediated secretory expression of a codon-optimized synthetic human interleukin-6 gene in Escherichia coli
    • DOI 10.1016/S1046-5928(02)00028-1, PII S1046592802000281
    • Li Y, Chen CX, von Specht BU, Hahn HP (2002) Cloning and hemolysin-mediated secretory expression of a codon-optimized synthetic human interleukin-6 gene in Escherichia coli. Protein Expr Purif 25:437-447. (Pubitemid 35293972)
    • (2002) Protein Expression and Purification , vol.25 , Issue.3 , pp. 437-447
    • Li, Y.1    Chen, C.X.2    Von, S.B.-U.3    Hahn, H.P.4
  • 29
    • 55649116633 scopus 로고    scopus 로고
    • Factors that influence the extracellular expression of streptavidin in Escherichia coli using a bacteriocin release protein
    • Miksch G, Ryu S, Risse JM, Flaschel E (2008) Factors that influence the extracellular expression of streptavidin in Escherichia coli using a bacteriocin release protein. Appl Microbiol Biotechnol 81:319-326.
    • (2008) Appl Microbiol Biotechnol , vol.81 , pp. 319-326
    • Miksch, G.1    Ryu, S.2    Risse, J.M.3    Flaschel, E.4
  • 31
    • 0033842544 scopus 로고    scopus 로고
    • Secretion of virulence determinants by the general secretory pathway in Gram-negative pathogens: An evolving story
    • DOI 10.1016/S1286-4579(00)01260-0
    • Stathopoulos C, Hendrixson DR, Thanassi DG, Hultgren SJ, St Geme JW, Curtiss R (2000) Secretion of virulence determinants by the general secretory pathway in Gram-negative pathogens: an evolving story. Microbes Infect 2:1061-1072. (Pubitemid 30664220)
    • (2000) Microbes and Infection , vol.2 , Issue.9 , pp. 1061-1072
    • Stathopoulos, C.1    Hendrixson, D.R.2    Thanassi, D.G.3    Hultgren, S.J.4    St III, G.J.W.5    Curtiss III, R.6
  • 32
    • 0029924909 scopus 로고    scopus 로고
    • The cryptic general secretory pathway (gsp) operon of Escherichia coli K-12 encodes functional proteins
    • Francetic O, Pugsley AP (1996) The cryptic general secretory pathway (gsp) operon of Escherichia coli K-12 encodes functional proteins. J Bacteriol 178:3544-3549.
    • (1996) J Bacteriol , vol.178 , pp. 3544-3549
    • Francetic, O.1    Pugsley, A.P.2
  • 33
    • 0031733336 scopus 로고    scopus 로고
    • Structure of the outer membrane protein A transmembrane domain
    • DOI 10.1038/2983
    • Pautsch A, Schulz GE (1998) Structure of the outer membrane protein A transmembrane domain. Nat Struct Biol 5:1013-1017. (Pubitemid 28506635)
    • (1998) Nature Structural Biology , vol.5 , Issue.11 , pp. 1013-1017
    • Pautsch, A.1    Schulz, G.E.2
  • 34
    • 0023035811 scopus 로고
    • An Outer-Membrane Protein (Ompa) of Escherichia-Coli K-12 Undergoes a Conformational Change during Export
    • Freudl R, Schwarz H, Stierhof Y, Gamon K, Hindennach I, Henning U (1986) An Outer-Membrane Protein (Ompa) of Escherichia-Coli K-12 Undergoes a Conformational Change during Export. J Biol Chem 261:1355-1361.
    • (1986) J Biol Chem , vol.261 , pp. 1355-1361
    • Freudl, R.1    Schwarz, H.2    Stierhof, Y.3    Gamon, K.4    Hindennach, I.5    Henning, U.6
  • 35
    • 0025833095 scopus 로고
    • Trimerization of an in vitro synthesized OmpF porin of Escherichia coli outer membrane
    • Sen K, Nikaido H (1991) Trimerization of an Invitro Synthesized Ompf Porin of Escherichia-Coli Outer-Membrane. J Biol Chem 266:11295-11300. (Pubitemid 21906946)
    • (1991) Journal of Biological Chemistry , vol.266 , Issue.17 , pp. 11295-11300
    • Sen, K.1    Nikaido, H.2
  • 36
    • 0042878499 scopus 로고    scopus 로고
    • Membrane protein folding on the example of outer membrane protein A of Escherichia coli
    • Kleinschmidt JH (2003) Membrane protein folding on the example of outer membrane protein A of Escherichia coli. Cell Mol Life Sci 60:1547-1558.
    • (2003) Cell Mol Life Sci , vol.60 , pp. 1547-1558
    • Kleinschmidt, J.H.1
  • 38
    • 0025970549 scopus 로고
    • Lipopolysaccharide Structure Required for Invitro Trimerization of Escherichia-Coli Ompf Porin
    • Sen K, Nikaido H (1991) Lipopolysaccharide Structure Required for Invitro Trimerization of Escherichia-Coli Ompf Porin. J Bacteriol 173:926-928.
    • (1991) J Bacteriol , vol.173 , pp. 926-928
    • Sen, K.1    Nikaido, H.2
  • 39
    • 0029886388 scopus 로고    scopus 로고
    • A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins
    • DOI 10.1111/j.1365-2958.1996.tb02473.x
    • Chen R, Henning U (1996) A periplasmic protein (Skp) of Escherichia coli selectively binds a class of outer membrane proteins. Mol Microbiol 19:1287-1294. (Pubitemid 26112812)
    • (1996) Molecular Microbiology , vol.19 , Issue.6 , pp. 1287-1294
    • Chen, R.1    Henning, U.2
  • 40
    • 0025041015 scopus 로고
    • A protein with sequence identity to Skp (FirA) supports protein translocation into plasma membrane vesicles of Escherichia coli
    • DOI 10.1016/0014-5793(90)81132-8
    • Thome BM, Hoffschulte HK, Schiltz E, Muller M (1990) A protein with sequence identity to Skp (FirA) supports protein translocation into plasma membrane vesicles of Escherichia coli. FEBS Lett 269:113-116. (Pubitemid 20245330)
    • (1990) FEBS Letters , vol.269 , Issue.1 , pp. 113-116
    • Thome, B.M.1    Hoffschulte, H.K.2    Schiltz, E.3    Muller, M.4
  • 41
    • 0346457133 scopus 로고    scopus 로고
    • Incorporation of Heterologous Outer Membrane and Periplasmic Proteins into Escherichia coli Outer Membrane Vesicles
    • DOI 10.1074/jbc.M307628200
    • Kesty NC, Kuehn MJ (2004) Incorporation of heterologous outer membrane and periplasmic proteins into Escherichia coli outer membrane vesicles. J Biol Chem 279:2069-2076. (Pubitemid 38084479)
    • (2004) Journal of Biological Chemistry , vol.279 , Issue.3 , pp. 2069-2076
    • Kesty, N.C.1    Kuehn, M.J.2
  • 42
    • 0038148722 scopus 로고    scopus 로고
    • The BON domain: A putative membrane-binding domain
    • DOI 10.1016/S0968-0004(03)00115-4
    • Yeats C, Bateman A (2003) The BON domain: a putative membrane-binding domain. Trends Biochem Sci 28:352-355. (Pubitemid 36851614)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.7 , pp. 352-355
    • Yeats, C.1    Bateman, A.2
  • 44
    • 84891371714 scopus 로고    scopus 로고
    • Mycobacterium tuberculosis Rv0899 adopts a mixed alpha/beta-structure and does not form a transmembrane beta-barrel
    • Teriete P, Yao Y, Kolodzik A, Yu J, Song H, Niederweis M, Marassi FM (2010) Mycobacterium tuberculosis Rv0899 adopts a mixed alpha/beta-structure and does not form a transmembrane beta-barrel. Biochemistry 49:2768-2777.
    • (2010) Biochemistry , vol.49 , pp. 2768-2777
    • Teriete, P.1    Yao, Y.2    Kolodzik, A.3    Yu, J.4    Song, H.5    Niederweis, M.6    Marassi, F.M.7
  • 46
    • 34547907049 scopus 로고    scopus 로고
    • Expression and purification of bioactive high-purity mouse monokine induced by IFN-gamma in Escherichia coli
    • DOI 10.1016/j.pep.2007.04.004, PII S1046592807000988
    • Lu H, Yu M, Sun Y, Mao W, Wang Q, Wu M, Han W (2007) Expression and purification of bioactive high-purity mouse monokine induced by IFN-gamma in Escherichia coli. Protein Expr Purif 55:132-138. (Pubitemid 47259687)
    • (2007) Protein Expression and Purification , vol.55 , Issue.1 , pp. 132-138
    • Lu, H.1    Yu, M.2    Sun, Y.3    Mao, W.4    Wang, Q.5    Wu, M.6    Han, W.7
  • 49
    • 14544281936 scopus 로고    scopus 로고
    • Soluble CPG15 expressed during early development rescues cortical progenitors from apoptosis
    • DOI 10.1038/nn1407
    • Putz U, Harwell C, Nedivi E (2005) Soluble CPG15 expressed during early development rescues cortical progenitors from apoptosis. Nat Neurosci 8:322-331. (Pubitemid 40300189)
    • (2005) Nature Neuroscience , vol.8 , Issue.3 , pp. 322-331
    • Putz, U.1    Harwell, C.2    Nedivi, E.3
  • 50
    • 37349118993 scopus 로고    scopus 로고
    • Type I receptor binding of bone morphogenetic protein 6 is dependent on N-glycosylation of the ligand
    • DOI 10.1111/j.1742-4658.2007.06187.x
    • Saremba S, Nickel J, Seher A, Kotzsch A, Sebald W, Mueller TD (2008) Type I receptor binding of bone morphogenetic protein 6 is dependent on N-glycosylation of the ligand. FEBS J 275:172-183. (Pubitemid 350294073)
    • (2008) FEBS Journal , vol.275 , Issue.1 , pp. 172-183
    • Saremba, S.1    Nickel, J.2    Seher, A.3    Kotzsch, A.4    Sebald, W.5    Mueller, T.D.6
  • 51
    • 33645410951 scopus 로고    scopus 로고
    • Expression of the human activin type I and II receptor extracellular domains in Pichia pastoris
    • Daly R, Hearn MT (2006) Expression of the human activin type I and II receptor extracellular domains in Pichia pastoris. Protein Expr Purif 46:456-467.
    • (2006) Protein Expr Purif , vol.46 , pp. 456-467
    • Daly, R.1    Hearn, M.T.2
  • 52
    • 65649129324 scopus 로고    scopus 로고
    • An E. coli over-expression system for multiply-phosphorylated proteins and its use in a study of calcium phosphate sequestration by novel recombinant phosphopeptides
    • Clegg RA, Holt C (2009) An E. coli over-expression system for multiply-phosphorylated proteins and its use in a study of calcium phosphate sequestration by novel recombinant phosphopeptides. Protein Expr Purif 67:23-34.
    • (2009) Protein Expr Purif , vol.67 , pp. 23-34
    • Clegg, R.A.1    Holt, C.2
  • 53
    • 39049161655 scopus 로고    scopus 로고
    • Identification of osteopontin phosphorylation sites involved in bone remodeling and inhibition of pathological calcification
    • DOI 10.1002/jcb.21453
    • Saad FA, Salih E, Glimcher MJ (2008) Identification of osteopontin phosphorylation sites involved in bone remodeling and inhibition of pathological calcification. J Cell Biochem 103:852-856. (Pubitemid 351240620)
    • (2008) Journal of Cellular Biochemistry , vol.103 , Issue.3 , pp. 852-856
    • Saad, F.A.1    Salih, E.2    Glimcher, M.J.3
  • 54
    • 0030438013 scopus 로고    scopus 로고
    • Generation and use of recombinant human bone sialoprotein and osteopontin for hydroxyapatite studies
    • Stubbs JT, III (1996) Generation and use of recombinant human bone sialoprotein and osteopontin for hydroxyapatite studies. Connect Tissue Res 35:393-399.
    • (1996) Connect Tissue Res , vol.35 , pp. 393-399
    • Stubbs III, J.T.1
  • 56
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • DOI 10.1023/A:1011254402785
    • Marley J, Lu M, Bracken C (2001) A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 20:71-75. (Pubitemid 32519656)
    • (2001) Journal of Biomolecular NMR , vol.20 , Issue.1 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 57
    • 67849133359 scopus 로고    scopus 로고
    • ProteinCCD: Enabling the design of protein truncation constructs for expression and crystallization experiments
    • Mooij WT, Mitsiki E, Perrakis A (2009) ProteinCCD: enabling the design of protein truncation constructs for expression and crystallization experiments. Nucleic Acids Res 37:W402-405.
    • (2009) Nucleic Acids Res , vol.37
    • Mooij, W.T.1    Mitsiki, E.2    Perrakis, A.3
  • 58
    • 77955428012 scopus 로고    scopus 로고
    • A software tool to accelerate design of protein constructs for recombinant expression
    • Sagemark J, Kraulis P, Weigelt J (2010) A software tool to accelerate design of protein constructs for recombinant expression. Protein Expr Purif 72:175-178.
    • (2010) Protein Expr Purif , vol.72 , pp. 175-178
    • Sagemark, J.1    Kraulis, P.2    Weigelt, J.3
  • 60


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.