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Volumn 392, Issue 1-2, 2014, Pages 175-186

An improved method and cost effective strategy for soluble expression and purification of human N-myristoyltransferase 1 in E. coli

Author keywords

Auto induction; Myristoylation; N myristoyltransferase (NMT); Protein purification; Soluble expression; T7 expression system

Indexed keywords

ANTINEOPLASTIC AGENT; ISOENZYME; ISOPROPYL BETA DEXTRO 1 THIOGALACTOPYRANOSIDE; N MYRISTOYLTRANSFERASE 1; PROTEIN N MYRISTOYLTRANSFERASE; PYRANOSIDE; UNCLASSIFIED DRUG; ACYLTRANSFERASE; GLYCYLPEPTIDE N-TETRADECANOYLTRANSFERASE; PRIMER DNA; RECOMBINANT PROTEIN;

EID: 84905191726     PISSN: 03008177     EISSN: 15734919     Source Type: Journal    
DOI: 10.1007/s11010-014-2029-z     Document Type: Article
Times cited : (5)

References (57)
  • 2
    • 33646264815 scopus 로고    scopus 로고
    • Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events
    • doi:10.1073/pnas.0600824103
    • Vilas GL, Corvi MM, Plummer GJ, Seime AM, Lambkin GR, Berthiaume LG (2006) Posttranslational myristoylation of caspase-activated p21-activated protein kinase 2 (PAK2) potentiates late apoptotic events. Proc Natl Acad Sci USA 103:6542-6547. doi:10.1073/pnas.0600824103
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6542-6547
    • Vilas, G.L.1    Corvi, M.M.2    Plummer, G.J.3    Seime, A.M.4    Lambkin, G.R.5    Berthiaume, L.G.6
  • 3
    • 76649115299 scopus 로고    scopus 로고
    • Protein myristoylation in health and disease
    • doi:10.1007/s12154-009-0032-8
    • Wright MH, Heal WP, Mann DJ, Tate EW (2010) Protein myristoylation in health and disease. J Chem Biol 3:19-35. doi:10.1007/s12154-009-0032-8
    • (2010) J Chem Biol , vol.3 , pp. 19-35
    • Wright, M.H.1    Heal, W.P.2    Mann, D.J.3    Tate, E.W.4
  • 4
    • 84859341928 scopus 로고    scopus 로고
    • Targeting protein lipidation in disease
    • Resh MD (2012) Targeting protein lipidation in disease. Trends Mol Med 18:206-214
    • (2012) Trends Mol Med , vol.18 , pp. 206-214
    • Resh, M.D.1
  • 5
    • 84862596361 scopus 로고    scopus 로고
    • Inhibition of protein N-myristoylation: A therapeutic protocol in developing anticancer agents
    • Das U, Kumar S, Dimmock JR, Sharma RK (2012) Inhibition of protein N-myristoylation: a therapeutic protocol in developing anticancer agents. Curr Cancer Drug Targets 12:667-692
    • (2012) Curr Cancer Drug Targets , vol.12 , pp. 667-692
    • Das, U.1    Kumar, S.2    Dimmock, J.R.3    Sharma, R.K.4
  • 8
    • 84867757397 scopus 로고    scopus 로고
    • Design and synthesis of inhibitors of Plasmodium falciparum N-myristoyltransferase, a promising target for antimalarial drug discovery
    • doi:10.1021/jm301160h
    • Yu Z, Brannigan JA, Moss DK, Brzozowski AM, Wilkinson AJ, Holder AA, Tate EW, Leatherbarrow RJ (2012) Design and synthesis of inhibitors of Plasmodium falciparum N-myristoyltransferase, a promising target for antimalarial drug discovery. J Med Chem 55:8879-8890. doi:10.1021/jm301160h
    • (2012) J Med Chem , vol.55 , pp. 8879-8890
    • Yu, Z.1    Brannigan, J.A.2    Moss, D.K.3    Brzozowski, A.M.4    Wilkinson, A.J.5    Holder, A.A.6    Tate, E.W.7    Leatherbarrow, R.J.8
  • 11
    • 0028972680 scopus 로고
    • Increased N-myristoyltransferase activity observed in rat and human colonic tumors
    • doi:10.1093/jnci/87.21.1630
    • Magnuson BA, Raju RVS, Moyana TN, Sharma RK (1995) Increased N-myristoyltransferase activity observed in rat and human colonic tumors. J Natl Cancer Inst 87:1630-1635. doi:10.1093/jnci/87.21.1630
    • (1995) J Natl Cancer Inst , vol.87 , pp. 1630-1635
    • Magnuson, B.A.1    Raju, R.V.S.2    Moyana, T.N.3    Sharma, R.K.4
  • 12
    • 0031586342 scopus 로고    scopus 로고
    • N-myristoyltransferase overexpression in human colorectal adenocarcinomas
    • DOI 10.1006/excr.1997.3679
    • Raju RVS, Moyana TN, Sharma RK (1997) N-myristoyltransferase overexpression in human colorectal adenocarcinomas. Exp Cell Res 235:145-154. doi:10.1006/excr.1997.3679 (Pubitemid 27381692)
    • (1997) Experimental Cell Research , vol.235 , Issue.1 , pp. 145-154
    • Raju, R.V.S.1    Moyana, T.N.2    Sharma, R.K.3
  • 13
    • 24144464240 scopus 로고    scopus 로고
    • Two N-myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis
    • DOI 10.1158/1541-7786.MCR-05-0037
    • Ducker CE, Upson JJ, French KJ, Smith CD (2005) Two N- myristoyltransferase isozymes play unique roles in protein myristoylation, proliferation, and apoptosis. Mol Cancer Res 3:463-476. doi:10.1158/1541-7786. mcr-05-0037 (Pubitemid 41232608)
    • (2005) Molecular Cancer Research , vol.3 , Issue.8 , pp. 463-476
    • Ducker, C.E.1    Upson, J.J.2    French, K.J.3    Smith, C.D.4
  • 15
    • 33751162632 scopus 로고    scopus 로고
    • The role of myristoylation in the membrane association of the Lassa virus matrix protein Z
    • Strecker T, Maisa A, Daffis S, Eichler R, Lenz O, Garten W (2006) The role of myristoylation in the membrane association of the Lassa virus matrix protein Z. Virol J 3:93
    • (2006) Virol J , vol.3 , pp. 93
    • Strecker, T.1    Maisa, A.2    Daffis, S.3    Eichler, R.4    Lenz, O.5    Garten, W.6
  • 16
    • 4644243004 scopus 로고    scopus 로고
    • Myristoylation of the RING finger Z protein is essential for arenavirus budding
    • DOI 10.1128/JVI.78.20.11443-11448.2004
    • Perez M, Greenwald DL, de La Torre JC (2004) Myristoylation of the RING finger Z protein is essential for arenavirus budding. J Virol 78:11443-11448. doi:10.1128/jvi.78.20.11443-11448.2004 (Pubitemid 39299691)
    • (2004) Journal of Virology , vol.78 , Issue.20 , pp. 11443-11448
    • Perez, M.1    Greenwald, D.L.2    De La, T.J.C.3
  • 17
    • 84861318525 scopus 로고    scopus 로고
    • The myristate moiety and amino terminus of vaccinia virus L1 constitute a bipartite functional region needed for entry
    • doi:10.1128/jvi.06703-11
    • Foo CH, Whitbeck JC, Ponce-de-León M, Saw WT, Cohen GH, Eisenberg RJ (2012) The myristate moiety and amino terminus of vaccinia virus L1 constitute a bipartite functional region needed for entry. J Virol 86:5437-5451. doi:10.1128/jvi.06703-11
    • (2012) J Virol , vol.86 , pp. 5437-5451
    • Foo, C.H.1    Whitbeck, J.C.2    Ponce-de-León, M.3    Saw, W.T.4    Cohen, G.H.5    Eisenberg, R.J.6
  • 18
    • 0032549571 scopus 로고    scopus 로고
    • A second mammalian N-myristoyltransferase
    • DOI 10.1074/jbc.273.12.6595
    • Giang DK, Cravatt BF (1998) A second mammalian N-myristoyltransferase. J Biol Chem 273:6595-6598. doi:10.1074/jbc.273.12.6595 (Pubitemid 28160313)
    • (1998) Journal of Biological Chemistry , vol.273 , Issue.12 , pp. 6595-6598
    • Giang, D.K.1    Cravatt, B.F.2
  • 19
    • 0030657584 scopus 로고    scopus 로고
    • Human N-Myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction
    • DOI 10.1074/jbc.272.45.28680
    • Glover CJ, Hartman KD, Felsted RL (1997) Human N-myristoyltransferase amino-terminal domain involved in targeting the enzyme to the ribosomal subcellular fraction. J Biol Chem 272:28680-28689. doi:10.1074/jbc.272.45.28680 (Pubitemid 27517824)
    • (1997) Journal of Biological Chemistry , vol.272 , Issue.45 , pp. 28680-28689
    • Glover, C.J.1    Hartman, K.D.2    Felsted, R.L.3
  • 20
    • 0026544934 scopus 로고
    • Mutations of human myristoyl-CoA:Protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae
    • doi:10.1073/pnas.89.9.4129
    • Duronio RJ, Reed SI, Gordon JI (1992) Mutations of human myristoyl-CoA:protein N-myristoyltransferase cause temperature-sensitive myristic acid auxotrophy in Saccharomyces cerevisiae. Proc Natl Acad Sci USA 89:4129-4133. doi:10.1073/pnas.89.9.4129
    • (1992) Proc Natl Acad Sci USA , vol.89 , pp. 4129-4133
    • Duronio, R.J.1    Reed, S.I.2    Gordon, J.I.3
  • 21
    • 38349075225 scopus 로고    scopus 로고
    • N-myristoyltransferase isozymes exhibit differential specificity for human immunodeficiency virus type 1 Gag and Nef
    • doi:10.1099/vir.0.83412-0
    • Seaton KE, Smith CD (2008) N-myristoyltransferase isozymes exhibit differential specificity for human immunodeficiency virus type 1 Gag and Nef. J Gen Virol 89:288-296. doi:10.1099/vir.0.83412-0
    • (2008) J Gen Virol , vol.89 , pp. 288-296
    • Seaton, K.E.1    Smith, C.D.2
  • 22
    • 39749131702 scopus 로고    scopus 로고
    • HIV-1 production is specifically associated with human NMT1 long form in human NMT isozymes
    • doi:10.1016/j.micinf.2007.10.015
    • Takamune N, Gota K, Misumi S, Tanaka K, Okinaka S, Shoji S (2008) HIV-1 production is specifically associated with human NMT1 long form in human NMT isozymes. Microbes Infect 10:143-150. doi:10.1016/j.micinf.2007.10.015
    • (2008) Microbes Infect , vol.10 , pp. 143-150
    • Takamune, N.1    Gota, K.2    Misumi, S.3    Tanaka, K.4    Okinaka, S.5    Shoji, S.6
  • 23
    • 0032884573 scopus 로고    scopus 로고
    • Recombinant protein expression in Escherichia coli
    • doi:10.1016/S0958-1669(99)00003-8
    • Baneyx F (1999) Recombinant protein expression in Escherichia coli. Curr Opin Biotechnol 10:411-421. doi:10.1016/S0958-1669(99)00003-8
    • (1999) Curr Opin Biotechnol , vol.10 , pp. 411-421
    • Baneyx, F.1
  • 24
    • 38549143777 scopus 로고    scopus 로고
    • Production of active eukaryotic proteins through bacterial expression systems: A review of the existing biotechnology strategies
    • DOI 10.1007/s11010-007-9603-6
    • Sahdev S, Khattar SK, Saini KS (2008) Production of active eukaryotic proteins through bacterial expression systems: a review of the existing biotechnology strategies. Mol Cell Biochem 307:249-264 (Pubitemid 50006245)
    • (2008) Molecular and Cellular Biochemistry , vol.307 , Issue.1-2 , pp. 249-264
    • Sahdev, S.1    Khattar, S.K.2    Saini, K.S.3
  • 25
    • 13644262805 scopus 로고    scopus 로고
    • Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli
    • Sørensen H, Mortensen K (2005) Soluble expression of recombinant proteins in the cytoplasm of Escherichia coli. Microb Cell Fact 4:1
    • (2005) Microb Cell Fact , vol.4 , pp. 1
    • Sørensen, H.1    Mortensen, K.2
  • 26
    • 79957875229 scopus 로고    scopus 로고
    • Tuning different expression parameters to achieve soluble recombinant proteins in E. coli: Advantages of high-throughput screening
    • doi:10.1002/biot.201100025
    • Correa A, Oppezzo P (2011) Tuning different expression parameters to achieve soluble recombinant proteins in E. coli: advantages of high-throughput screening. Biotechnol J 6:715-730. doi:10.1002/biot.201100025
    • (2011) Biotechnol J , vol.6 , pp. 715-730
    • Correa, A.1    Oppezzo, P.2
  • 27
    • 33751419975 scopus 로고    scopus 로고
    • Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost
    • DOI 10.1016/j.pep.2006.06.024, PII S1046592806001951
    • Peti W, Page R (2007) Strategies to maximize heterologous protein expression in Escherichia coli with minimal cost. Protein Expr Purif 51:1-10. doi:10.1016/j.pep.2006.06.024 (Pubitemid 44821862)
    • (2007) Protein Expression and Purification , vol.51 , Issue.1 , pp. 1-10
    • Peti, W.1    Page, R.2
  • 28
    • 0028871804 scopus 로고
    • How to measure and predict the molar absorption coefficient of a protein
    • doi:10.1002/pro.5560041120
    • Pace CN, Vajdos F, Fee L, Grimsley G, Gray T (1995) How to measure and predict the molar absorption coefficient of a protein. Protein Sci 4:2411-2423. doi:10.1002/pro.5560041120
    • (1995) Protein Sci , vol.4 , pp. 2411-2423
    • Pace, C.N.1    Vajdos, F.2    Fee, L.3    Grimsley, G.4    Gray, T.5
  • 29
    • 25844437437 scopus 로고    scopus 로고
    • Proteome analysis of embryo and endosperm from germinating tomato seeds
    • DOI 10.1002/pmic.200401209
    • Sheoran IS, Olson DJH, Ross ARS, Sawhney VK (2005) Proteome analysis of embryo and endosperm from germinating tomato seeds. Proteomics 5:3752-3764. doi:10.1002/pmic.200401209 (Pubitemid 41393306)
    • (2005) Proteomics , vol.5 , Issue.14 , pp. 3752-3764
    • Sheoran, I.S.1    Olson, D.J.H.2    Ross, A.R.S.3    Sawhney, V.K.4
  • 30
    • 0028244655 scopus 로고
    • Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA:Protein N-myristoyltransferase. Determinants of binding energy and catalytic discrimination among acyl-CoA and peptide ligands
    • Bhatnagar RS, Jackson-Machelski E, McWherter CA, Gordon JI (1994) Isothermal titration calorimetric studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. Determinants of binding energy and catalytic discrimination among acyl-CoA and peptide ligands. J Biol Chem 269:11045-11053
    • (1994) J Biol Chem , vol.269 , pp. 11045-11053
    • Bhatnagar, R.S.1    Jackson-Machelski, E.2    McWherter, C.A.3    Gordon, J.I.4
  • 32
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • doi:10.1016/0022-2836(86)90385-2
    • Studier FW, Moffatt BA (1986) Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J Mol Biol 189:113-130. doi:10.1016/0022-2836(86)90385-2
    • (1986) J Mol Biol , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 33
    • 0026279733 scopus 로고
    • Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system
    • doi:10.1016/0022-2836(91)90855-Z
    • Studier FW (1991) Use of bacteriophage T7 lysozyme to improve an inducible T7 expression system. J Mol Biol 219:37-44. doi:10.1016/0022-2836(91) 90855-Z
    • (1991) J Mol Biol , vol.219 , pp. 37-44
    • Studier, F.W.1
  • 34
    • 0026305697 scopus 로고
    • Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor
    • doi:10.1016/0022-2836(91)90856-2
    • Dubendorf JW, Studier FW (1991) Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor. J Mol Biol 219:45-59. doi:10.1016/0022-2836(91)90856-2
    • (1991) J Mol Biol , vol.219 , pp. 45-59
    • Dubendorf, J.W.1    Studier, F.W.2
  • 35
    • 0025359849 scopus 로고
    • Structural and functional studies of Saccharomyces cerevisiae myristoyl-CoA:Protein N-myristoyltransferase produced in Escherichia coli. Evidence for an acyl-enzyme intermediate
    • Rudnick DA, McWherter CA, Adams SP, Ropson IJ, Duronio RJ, Gordon JI (1990) Structural and functional studies of Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase produced in Escherichia coli. Evidence for an acyl-enzyme intermediate. J Biol Chem 265:13370-13378
    • (1990) J Biol Chem , vol.265 , pp. 13370-13378
    • Rudnick, D.A.1    McWherter, C.A.2    Adams, S.P.3    Ropson, I.J.4    Duronio, R.J.5    Gordon, J.I.6
  • 37
    • 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
  • 38
    • 10644255526 scopus 로고    scopus 로고
    • Advanced genetic strategies for recombinant protein expression in Escherichia coli
    • DOI 10.1016/j.jbiotec.2004.08.004, PII S0168165604004560
    • Sørensen HP, Mortensen KK (2005) Advanced genetic strategies for recombinant protein expression in Escherichia coli. J Biotechnol 115:113-128. doi:10.1016/j.jbiotec.2004.08.004 (Pubitemid 39656438)
    • (2005) Journal of Biotechnology , vol.115 , Issue.2 , pp. 113-128
    • Sorensen, H.P.1    Mortensen, K.K.2
  • 39
    • 34548012600 scopus 로고    scopus 로고
    • Engineering cell physiology to enhance recombinant protein production in Escherichia coli
    • doi:10.1007/s00253-007-1039-0
    • Chou CP (2007) Engineering cell physiology to enhance recombinant protein production in Escherichia coli. Appl Microbiol Biotechnol 76:521-532. doi:10.1007/s00253-007-1039-0
    • (2007) Appl Microbiol Biotechnol , vol.76 , pp. 521-532
    • Chou, C.P.1
  • 40
    • 8844219685 scopus 로고    scopus 로고
    • Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli
    • DOI 10.1002/bit.20227
    • Han M-J, Park SJ, Park TJ, Lee SY (2004) Roles and applications of small heat shock proteins in the production of recombinant proteins in Escherichia coli. Biotechnol Bioeng 88:426-436. doi:10.1002/bit.20227 (Pubitemid 39536545)
    • (2004) Biotechnology and Bioengineering , vol.88 , Issue.4 , pp. 426-436
    • Han, M.-J.1    Park, S.J.2    Park, T.J.3    Lee, S.Y.4
  • 42
    • 0028298347 scopus 로고
    • Characterization of a polyhistidine-tagged form of human myristoyl- CoA:protein N-myristoyltransferase produced in Escherichia coli
    • DOI 10.1111/j.1432-1033.1994.tb18851.x
    • McIlhinney RAJ, Patel PB, McGlone K (1994) Characterization of a polyhistidine-tagged form of human myristoyl-CoA:protein N-myristoyltransferase produced in Escherichia coli. Eur J Biochem 222:137-146. doi:10.1111/j.1432- 1033.1994.tb18851.x (Pubitemid 24161335)
    • (1994) European Journal of Biochemistry , vol.222 , Issue.1 , pp. 137-146
    • McIlhinney, R.A.J.1    Patel, P.B.2    McGlone, K.3
  • 43
    • 0028072831 scopus 로고
    • Fatty acyl transfer by human N-myristyl transferase is dependent upon conserved cysteine and histidine residues
    • Peseckis SM, Resh MD (1994) Fatty acyl transfer by human N-myristyl transferase is dependent upon conserved cysteine and histidine residues. J Biol Chem 269:30888-30892 (Pubitemid 24377573)
    • (1994) Journal of Biological Chemistry , vol.269 , Issue.49 , pp. 30888-30892
    • Peseckis, S.M.1    Resh, M.D.2
  • 44
    • 0027276545 scopus 로고
    • A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA:protein N- myristoyltransferase
    • Rocque WJ, McWherter CA, Wood DC, Gordon JI (1993) A comparative analysis of the kinetic mechanism and peptide substrate specificity of human and Saccharomyces cerevisiae myristoyl-CoA:protein N-myristoyltransferase. J Biol Chem 268:9964-9971 (Pubitemid 23150169)
    • (1993) Journal of Biological Chemistry , vol.268 , Issue.14 , pp. 9964-9971
    • Rocque, W.J.1    McWherter, C.A.2    Wood, D.C.3    Gordon, J.I.4
  • 45
    • 0033814819 scopus 로고    scopus 로고
    • Purification of proteins using polyhistidine affinity tags
    • Bornhorst JA, Falke JJ (2000) Purification of proteins using polyhistidine affinity tags. Methods Enzymol 326:245-254
    • (2000) Methods Enzymol , vol.326 , pp. 245-254
    • Bornhorst, J.A.1    Falke, J.J.2
  • 46
    • 33847714692 scopus 로고    scopus 로고
    • Cautionary tail: The presence of an N-terminal tag on dynein light-chain roadblock/LC7 affects its interaction with a functional partner
    • DOI 10.2174/092986607780090801
    • Song J, Markley JL (2007) Cautionary tail: the presence of an N-terminal tag on dynein light-chain Roadblock/LC7 affects its interaction with a functional partner. Protein Pept Lett 14:265-268 (Pubitemid 46376858)
    • (2007) Protein and Peptide Letters , vol.14 , Issue.3 , pp. 265-268
    • Song, J.1    Markley, J.L.2
  • 48
    • 70450284404 scopus 로고    scopus 로고
    • Interactions between EB1 and microtubules: Dramatic effect of affinity tags and evidence for cooperative behavior
    • Zhu ZC, Gupta KK, Slabbekoorn AR, Paulson BA, Folker ES, Goodson HV (2009) Interactions between EB1 and microtubules: dramatic effect of affinity tags and evidence for cooperative behavior. J Biol Chem 284:32651-32661
    • (2009) J Biol Chem , vol.284 , pp. 32651-32661
    • Zhu, Z.C.1    Gupta, K.K.2    Slabbekoorn, A.R.3    Paulson, B.A.4    Folker, E.S.5    Goodson, H.V.6
  • 50
    • 74549196928 scopus 로고    scopus 로고
    • Current strategies for polypeptide fusion tags removal
    • Xie H, Yang C, Chen LE (2009) Current strategies for polypeptide fusion tags removal. Prog Biochem Biophys 36:1364-1369
    • (2009) Prog Biochem Biophys , vol.36 , pp. 1364-1369
    • Xie, H.1    Yang, C.2    Chen, L.E.3
  • 51
    • 0025283867 scopus 로고
    • Use of T7 RNA polymerase to direct expression of cloned genes
    • DOI 10.1016/0076-6879(90)85008-C
    • Studier FW, Rosenberg AH, Dunn JJ, Dubendorff JW (1990) Use of T7 RNA polymerase to direct expression of cloned genes. In: Goeddel DV (ed) Methods in enzymology. Academic Press, New York, pp 60-89 (Pubitemid 20219811)
    • (1990) Methods in Enzymology , vol.185 , pp. 60-89
    • Studier, F.W.1    Rosenberg, A.H.2    Dunn, J.J.3    Dubendorff, J.W.4
  • 52
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier FW (2005) Protein production by auto-induction in high density shaking cultures. Protein Expr Purif 41:207-234
    • (2005) Protein Expr Purif , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 53
    • 36749071435 scopus 로고    scopus 로고
    • Escherichia coli physiology in Luria-Bertani broth
    • DOI 10.1128/JB.01368-07
    • Sezonov G, Joseleau-Petit D, D'Ari R (2007) Escherichia coli physiology in Luria-Bertani broth. J Bacteriol 189:8746-8749. doi:10.1128/jb.01368-07 (Pubitemid 350210047)
    • (2007) Journal of Bacteriology , vol.189 , Issue.23 , pp. 8746-8749
    • Sezonov, G.1    Joseleau-Petit, D.2    D'Ari, R.3
  • 54
    • 0032536841 scopus 로고    scopus 로고
    • Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability
    • DOI 10.1016/S0378-1119(98)00020-1, PII S0378111998000201
    • Grossman TH, Kawasaki ES, Punreddy SR, Osburne MS (1998) Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability. Gene 209:95-103 (Pubitemid 28149625)
    • (1998) Gene , vol.209 , Issue.1-2 , pp. 95-103
    • Grossman, T.H.1    Kawasaki, E.S.2    Punreddy, S.R.3    Osburne, M.S.4
  • 55
    • 79952664822 scopus 로고    scopus 로고
    • Recombinant Escherichia coli GMP reductase: Kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme-ligand binary complex formation
    • Martinelli LKB, Ducati RG, Rosado LA, Breda A, Selbach BP, Santos DS, Basso LA (2011) Recombinant Escherichia coli GMP reductase: kinetic, catalytic and chemical mechanisms, and thermodynamics of enzyme-ligand binary complex formation. Mol BioSyst 7:1289-1305
    • (2011) Mol BioSyst , vol.7 , pp. 1289-1305
    • Martinelli, L.K.B.1    Ducati, R.G.2    Rosado, L.A.3    Breda, A.4    Selbach, B.P.5    Santos, D.S.6    Basso, L.A.7
  • 56
    • 76749150421 scopus 로고    scopus 로고
    • Structural and functional analyses of Mycobacterium tuberculosis Rv3315c-encoded metal-dependent homotetrameric cytidine deaminase
    • doi:10.1016/j.jsb.2009.12.019
    • Sánchez-Quitian ZA, Schneider CZ, Ducati RG, de Azevedo WF Jr, Bloch C Jr, Basso LA, Santos DS (2010) Structural and functional analyses of Mycobacterium tuberculosis Rv3315c-encoded metal-dependent homotetrameric cytidine deaminase. J Struct Biol 169:413-423. doi:10.1016/j.jsb.2009.12.019
    • (2010) J Struct Biol , vol.169 , pp. 413-423
    • Sánchez-Quitian, Z.A.1    Schneider, C.Z.2    Ducati, R.G.3    De Azevedo Jr., W.F.4    Bloch Jr., C.5    Basso, L.A.6    Santos, D.S.7
  • 57
    • 34848838957 scopus 로고    scopus 로고
    • The overnight express autoinduction system: High-density cell growth and protein expression while you sleep
    • Grabski A, Mehler M, Drott D (2005) The overnight express autoinduction system: high-density cell growth and protein expression while you sleep. Nat Methods 2:233-235
    • (2005) Nat Methods , vol.2 , pp. 233-235
    • Grabski, A.1    Mehler, M.2    Drott, D.3


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