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Volumn 76, Issue 1, 2011, Pages 25-35

Optimization of Escherichia coli cultivation methods for high yield neuropeptide y receptor type 2 production

Author keywords

Escherichia coli; G protein coupled receptor; Inclusion body; Minimal media; Neuropeptide Y receptor type 2

Indexed keywords

NEUROPEPTIDE Y RECEPTOR; NEUROPEPTIDE Y2 RECEPTOR; RECOMBINANT PROTEIN;

EID: 78650168714     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2010.10.012     Document Type: Article
Times cited : (15)

References (63)
  • 1
    • 0016689007 scopus 로고
    • Molecular-structure of membrane-bound rhodopsin
    • N.W. Downer, and S.W. Englander Molecular-structure of membrane-bound rhodopsin Nature 254 1975 625 627
    • (1975) Nature , vol.254 , pp. 625-627
    • Downer, N.W.1    Englander, S.W.2
  • 2
    • 42149181885 scopus 로고    scopus 로고
    • Structural diversity of g protein-coupled receptors and significance for drug discovery
    • M.C. Lagerstrom, and H.B. Schioth Structural diversity of g protein-coupled receptors and significance for drug discovery Nat. Rev. Drug. Discov. 7 2008 339 357
    • (2008) Nat. Rev. Drug. Discov. , vol.7 , pp. 339-357
    • Lagerstrom, M.C.1    Schioth, H.B.2
  • 3
    • 34250306407 scopus 로고    scopus 로고
    • Heterologous GPCR expression: A bottleneck to obtaining crystal structures
    • DOI 10.1021/bp060349b
    • E.C. McCusker, S.E. Bane, M.A. O'Malley, and A.S. Robinson Heterologous GPCR expression: a bottleneck to obtaining crystal structures Biotechnol. Prog. 23 2007 540 547 (Pubitemid 46911176)
    • (2007) Biotechnology Progress , vol.23 , Issue.3 , pp. 540-547
    • McCusker, E.C.1    Bane, S.E.2    O'Malley, M.A.3    Robinson, A.S.4
  • 4
    • 33749987003 scopus 로고    scopus 로고
    • 2a receptor yields in Saccharomyces cerevisiae
    • DOI 10.1021/bp050431r
    • A. Wedekind, M.A. O'Malley, R.T. Niebauer, and A.S. Robinson Optimization of the human adenosine A(2)a receptor yields in Saccharomyces cerevisiae Biotechnol. Prog. 22 2006 1249 1255 (Pubitemid 44568798)
    • (2006) Biotechnology Progress , vol.22 , Issue.5 , pp. 1249-1255
    • Wedekind, A.1    O'Malley, M.A.2    Niebauer, R.T.3    Robinson, A.S.4
  • 5
    • 0037333304 scopus 로고    scopus 로고
    • Membrane proteins: The 'Wild West' of structural biology
    • DOI 10.1016/S0968-0004(03)00026-4
    • J. Torres, T.J. Stevens, and M. Samso Membrane proteins: the 'Wild West' of structural biology Trends Biochem. Sci. 28 2003 137 144 (Pubitemid 36293851)
    • (2003) Trends in Biochemical Sciences , vol.28 , Issue.3 , pp. 137-144
    • Torres, J.1    Stevens, T.J.2    Samso, M.3
  • 7
    • 76749100307 scopus 로고    scopus 로고
    • Preparation of stable isotope-labeled peripheral cannabinoid receptor CB2 by bacterial fermentation
    • C. Berger, J.T.C. Ho, T. Kimura, S. Hess, K. Gawrisch, and A. Yeliseev Preparation of stable isotope-labeled peripheral cannabinoid receptor CB2 by bacterial fermentation Protein Expr. Purif. 70 2010 236 247
    • (2010) Protein Expr. Purif. , vol.70 , pp. 236-247
    • Berger, C.1    Ho, J.T.C.2    Kimura, T.3    Hess, S.4    Gawrisch, K.5    Yeliseev, A.6
  • 8
    • 21744449334 scopus 로고    scopus 로고
    • Comparison of class A and D G protein-coupled receptors: Common features in structure and activation
    • DOI 10.1021/bi047316u
    • M. Eilers, V. Hornak, S.O. Smith, and J.B. Konopka Comparison of class A and D G protein-coupled receptors: common features in structure and activation Biochemistry 44 2005 8959 8975 (Pubitemid 40943213)
    • (2005) Biochemistry , vol.44 , Issue.25 , pp. 8959-8975
    • Eilers, M.1    Hornak, V.2    Smith, S.O.3    Konopka, J.B.4
  • 9
    • 36549050758 scopus 로고    scopus 로고
    • On the hierarchical classification of G protein-coupled receptors
    • DOI 10.1093/bioinformatics/btm506
    • M.N. Davies, A. Secker, A.A. Freitas, M. Mendao, J. Timmis, and D.R. Flower On the hierarchical classification of G protein-coupled receptors Bioinformatics 23 2007 3113 3118 (Pubitemid 350187511)
    • (2007) Bioinformatics , vol.23 , Issue.23 , pp. 3113-3118
    • Davies, M.N.1    Secker, A.2    Freitas, A.A.3    Mendao, M.4    Timmis, J.5    Flower, D.R.6
  • 10
    • 0027328091 scopus 로고
    • Molecular-basis of muscarinic acetylcholine-receptor function
    • J. Wess Molecular-basis of muscarinic acetylcholine-receptor function Trends Pharmacol. Sci. 14 1993 308 313
    • (1993) Trends Pharmacol. Sci. , vol.14 , pp. 308-313
    • Wess, J.1
  • 11
    • 0032402450 scopus 로고    scopus 로고
    • Molecular basis of receptor/G-protein-coupling selectivity
    • DOI 10.1016/S0163-7258(98)00030-8, PII S0163725898000308
    • J. Wess Molecular basis of receptor/G-protein-coupling selectivity Pharmacol. Ther. 80 1998 231 264 (Pubitemid 28537822)
    • (1998) Pharmacology and Therapeutics , vol.80 , Issue.3 , pp. 231-264
    • Wess, J.1
  • 12
    • 0025834532 scopus 로고
    • Diversity of G-proteins in signal transduction
    • M.I. Simon, M.P. Strathmann, and N. Gautam Diversity of G-proteins in signal transduction Science 252 1991 802 808
    • (1991) Science , vol.252 , pp. 802-808
    • Simon, M.I.1    Strathmann, M.P.2    Gautam, N.3
  • 14
    • 4344581120 scopus 로고    scopus 로고
    • The retinal conformation and its environment in rhodopsin in light of a new 2.2 A crystal structure
    • DOI 10.1016/j.jmb.2004.07.044, PII S0022283604008733
    • T. Okada, M. Sugihara, A.N. Bondar, M. Elstner, P. Entel, and V. Buss The retinal conformation and its environment in rhodopsin in light of a new 2.2 angstrom crystal structure J. Mol. Biol. 342 2004 571 583 (Pubitemid 39149759)
    • (2004) Journal of Molecular Biology , vol.342 , Issue.2 , pp. 571-583
    • Okada, T.1    Sugihara, M.2    Bondar, A.-N.3    Elstner, M.4    Entel, P.5    Buss, V.6
  • 15
    • 5044235587 scopus 로고    scopus 로고
    • Electron crystallography reveals the structure of metarhodopsin I
    • DOI 10.1038/sj.emboj.7600374
    • J.J. Ruprecht, T. Mielke, R. Vogel, C. Villa, and G.F.X. Schertler Electron crystallography reveals the structure of metarhodopsin I EMBO J. 23 2004 3609 3620 (Pubitemid 39336283)
    • (2004) EMBO Journal , vol.23 , Issue.18 , pp. 3609-3620
    • Ruprecht, J.J.1    Mielke, T.2    Vogel, R.3    Villa, C.4    Schertler, G.F.X.5
  • 20
    • 38749131545 scopus 로고    scopus 로고
    • New G-protein-coupled receptor crystal structures: Insights and limitations
    • B. Kobilka, and G.F.X. Schertler New G-protein-coupled receptor crystal structures: insights and limitations Trends Pharmacol. Sci. 29 2008 79 83
    • (2008) Trends Pharmacol. Sci. , vol.29 , pp. 79-83
    • Kobilka, B.1    Schertler, G.F.X.2
  • 21
    • 0030612833 scopus 로고    scopus 로고
    • Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution
    • K. Pervushin, R. Riek, G. Wider, and K. Wuthrich Attenuated T-2 relaxation by mutual cancellation of dipole-dipole coupling and chemical shift anisotropy indicates an avenue to NMR structures of very large biological macromolecules in solution Proc. Natl. Acad. Sci. USA 94 1997 12366 12371
    • (1997) Proc. Natl. Acad. Sci. USA , vol.94 , pp. 12366-12371
    • Pervushin, K.1    Riek, R.2    Wider, G.3    Wuthrich, K.4
  • 22
    • 37849009111 scopus 로고    scopus 로고
    • Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy
    • K. Werner, C. Richter, J. Klein-Seetharaman, and H. Schwalbe Isotope labeling of mammalian GPCRs in HEK293 cells and characterization of the C-terminus of bovine rhodopsin by high resolution liquid NMR spectroscopy J. Biomol. NMR 40 2008 49 53
    • (2008) J. Biomol. NMR , vol.40 , pp. 49-53
    • Werner, K.1    Richter, C.2    Klein-Seetharaman, J.3    Schwalbe, H.4
  • 23
    • 19944375100 scopus 로고    scopus 로고
    • Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR
    • DOI 10.1016/j.pnmrs.2005.01.001, PII S0079656505000026
    • D. Huster Investigations of the structure and dynamics of membrane-associated peptides by magic angle spinning NMR Prog. Nucl. Magn. Reson. Spectrosc. 46 2005 79 107 (Pubitemid 40749325)
    • (2005) Progress in Nuclear Magnetic Resonance Spectroscopy , vol.46 , Issue.2-3 , pp. 79-107
    • Huster, D.1
  • 25
    • 0038024615 scopus 로고    scopus 로고
    • The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints
    • DOI 10.1124/mol.63.6.1256
    • R. Fredriksson, M.C. Lagerstrom, L.G. Lundin, and H.B. Schioth The G-protein-coupled receptors in the human genome form five main families. Phylogenetic analysis, paralogon groups, and fingerprints Mol. Pharmacol. 63 2003 1256 1272 (Pubitemid 36627220)
    • (2003) Molecular Pharmacology , vol.63 , Issue.6 , pp. 1256-1272
    • Fredriksson, R.1    Lagerstrom, M.C.2    Lundin, L.-G.3    Schioth, H.B.4
  • 27
    • 63049084192 scopus 로고    scopus 로고
    • Effect of neuropeptide y Y2 receptor deletion on emotional stress-induced neuronal activation in mice
    • N.K. Nguyen, S.B. Sartori, H. Herzog, R. Tasan, G. Sperk, and N. Singewald Effect of neuropeptide Y Y2 receptor deletion on emotional stress-induced neuronal activation in mice Synapse 63 2009 236 246
    • (2009) Synapse , vol.63 , pp. 236-246
    • Nguyen, N.K.1    Sartori, S.B.2    Herzog, H.3    Tasan, R.4    Sperk, G.5    Singewald, N.6
  • 29
    • 67749108153 scopus 로고    scopus 로고
    • NPY revealed as a critical modulator of osteoblast function in vitro: New insights into the role of Y1 and Y2 receptors
    • L. Teixeira, D.M. Sousa, A.F. Nunes, M.M. Sousa, H. Herzog, and M. Lamghari NPY revealed as a critical modulator of osteoblast function in vitro: new insights into the role of Y1 and Y2 receptors J. Cell. Biochem. 107 2009 908 916
    • (2009) J. Cell. Biochem. , vol.107 , pp. 908-916
    • Teixeira, L.1    Sousa, D.M.2    Nunes, A.F.3    Sousa, M.M.4    Herzog, H.5    Lamghari, M.6
  • 32
    • 40649118484 scopus 로고    scopus 로고
    • Overview of protein expression in E. coli
    • P.F. Schendel Overview of protein expression in E. coli Curr. Protoc. Mol. Biol. Chapter 16 2001 1611 1613
    • (2001) Curr. Protoc. Mol. Biol. Chapter , vol.16 , pp. 1611-1613
    • Schendel, P.F.1
  • 33
    • 8344256552 scopus 로고    scopus 로고
    • Recombinant Protein Folding and Misfolding in Escherichia coli
    • F. Baneyx, and M. Mujacic Recombinant Protein Folding and Misfolding in Escherichia coli Nat. Biotechnol. 22 2004 1399 1408
    • (2004) Nat. Biotechnol. , vol.22 , pp. 1399-1408
    • Baneyx, F.1    Mujacic, M.2
  • 34
    • 15444367003 scopus 로고    scopus 로고
    • Escherichia coli: Media preparation and bacteriological tools
    • K. Elbing, and R. Brent Escherichia coli: media preparation and bacteriological tools Curr Protoc Mol Biol Chapter 1 2002 111 117
    • (2002) Curr Protoc Mol Biol Chapter , vol.1 , pp. 111-117
    • Elbing, K.1    Brent, R.2
  • 35
    • 33947356279 scopus 로고    scopus 로고
    • G protein coupled receptor structure and activation
    • DOI 10.1016/j.bbamem.2006.10.021, PII S0005273606003981
    • B.K. Kobilka G protein coupled receptor structure and activation Biochim. Biophys. Acta 1768 2007 794 807 (Pubitemid 46452546)
    • (2007) Biochimica et Biophysica Acta - Biomembranes , vol.1768 , Issue.4 , pp. 794-807
    • Kobilka, B.K.1
  • 36
    • 73249140429 scopus 로고    scopus 로고
    • Prokaryotic expression, in vitro folding, and molecular pharmacological characterization of the neuropeptide y receptor type 2
    • P. Schmidt, D. Lindner, C. Montag, S. Berndt, A.G. Beck-Sickinger, R. Rudolph, and D. Huster Prokaryotic expression, in vitro folding, and molecular pharmacological characterization of the neuropeptide Y receptor type 2 Biotechnol. Prog. 25 2009 1732 1739
    • (2009) Biotechnol. Prog. , vol.25 , pp. 1732-1739
    • Schmidt, P.1    Lindner, D.2    Montag, C.3    Berndt, S.4    Beck-Sickinger, A.G.5    Rudolph, R.6    Huster, D.7
  • 38
    • 33751269309 scopus 로고    scopus 로고
    • Improving the batch-to-batch reproducibility in microbial cultures during recombinant protein production by guiding the process along a predefined total biomass profile
    • DOI 10.1007/s00449-006-0080-1
    • M. Jenzsch, S. Gnoth, M. Kleinschmidt, R. Simutis, and A. Lubbert Improving the batch-to-batch reproducibility in microbial cultures during recombinant protein production by guiding the process along a predefined total biomass profile Bioprocess Biosyst. Eng. 29 2006 315 321 (Pubitemid 44800768)
    • (2006) Bioprocess and Biosystems Engineering , vol.29 , Issue.5-6 , pp. 315-321
    • Jenzsch, M.1    Gnoth, S.2    Kleinschmidt, M.3    Simutis, R.4    Lubbert, A.5
  • 39
    • 0001639179 scopus 로고
    • The growth of bacterial cultures
    • J. Monod The growth of bacterial cultures Annu. Rev. Microbiol. 3 1949 371 394
    • (1949) Annu. Rev. Microbiol. , vol.3 , pp. 371-394
    • Monod, J.1
  • 40
    • 33751290076 scopus 로고    scopus 로고
    • Open-loop control of the biomass concentration within the growth phase of recombinant protein production processes
    • DOI 10.1016/j.jbiotec.2006.06.004, PII S0168165606004780
    • M. Jenzsch, S. Gnoth, M. Beck, M. Kleinschmidt, R. Simutis, and A. Lubbert Open-loop control of the biomass concentration within the growth phase of recombinant protein production processes J. Biotechnol. 127 2006 84 94 (Pubitemid 46127428)
    • (2006) Journal of Biotechnology , vol.127 , Issue.1 , pp. 84-94
    • Jenzsch, M.1    Gnoth, S.2    Beck, M.3    Kleinschmidt, M.4    Simutis, R.5    Lubbert, A.6
  • 41
    • 0014949207 scopus 로고
    • Cleavage of structural proteins during assembly of head of bacteriophage-T4
    • U.K. Laemmli Cleavage of structural proteins during assembly of head of bacteriophage-T4 Nature 227 1970 680 685
    • (1970) Nature , vol.227 , pp. 680-685
    • Laemmli, U.K.1
  • 43
    • 0000920252 scopus 로고
    • The effect of the ph of the medium during growth on the enzymic activities of bacteria (Escherichia coli and Micrococcus Lysodeikticus) and the biological significance of the changes produced
    • E.F. Gale, and H.M. Epps The effect of the ph of the medium during growth on the enzymic activities of bacteria (Escherichia coli and Micrococcus Lysodeikticus) and the biological significance of the changes produced Biochem. J. 36 1942 600 618
    • (1942) Biochem. J. , vol.36 , pp. 600-618
    • Gale, E.F.1    Epps, H.M.2
  • 44
    • 37249066180 scopus 로고    scopus 로고
    • Control of cultivation processes for recombinant protein production: A review
    • DOI 10.1007/s00449-007-0163-7
    • S. Gnoth, M. Jenzsch, R. Simutis, and A. Lübbert Control of cultivation processes for recombinant protein production: a review Bioprocess Biosyst. Eng. 31 2008 21 39 (Pubitemid 350276242)
    • (2008) Bioprocess and Biosystems Engineering , vol.31 , Issue.1 , pp. 21-39
    • Gnoth, S.1    Jenzsch, M.2    Simutis, R.3    Lubbert, A.4
  • 45
    • 78650178369 scopus 로고    scopus 로고
    • Product formation kinetics in a recombinant protein production process, 10th international IFAC symposium on computer applications in biotechnology
    • S. Gnoth, M. Jenzsch, R. Simutis, and A. Lübbert Product formation kinetics in a recombinant protein production process, 10th international IFAC symposium on computer applications in biotechnology Preprints 1 2006 197 202
    • (2006) Preprints , vol.1 , pp. 197-202
    • Gnoth, S.1    Jenzsch, M.2    Simutis, R.3    Lübbert, A.4
  • 47
    • 33645415883 scopus 로고    scopus 로고
    • Exceptional total and functional yields of the human adenosine (A2a) receptor expressed in the yeast Saccharomyces Cerevisiae
    • R.T. Niebauer, and A.S. Robinson Exceptional total and functional yields of the human adenosine (A2a) receptor expressed in the yeast Saccharomyces Cerevisiae Protein Expr. Purif. 46 2006 204 211
    • (2006) Protein Expr. Purif. , vol.46 , pp. 204-211
    • Niebauer, R.T.1    Robinson, A.S.2
  • 48
    • 32944474906 scopus 로고    scopus 로고
    • Solubilization, purification, and mass spectrometry analysis of the human μ-opioid receptor expressed in Pichia Pastoris
    • V. Sarramegna, I. Muller, G. Mousseau, C. Froment, B. Monsarrat, A. Milon, and F. Talmont Solubilization, purification, and mass spectrometry analysis of the human μ-opioid receptor expressed in Pichia Pastoris Protein Expr. Purif. 43 2005 85 93
    • (2005) Protein Expr. Purif. , vol.43 , pp. 85-93
    • Sarramegna, V.1    Muller, I.2    Mousseau, G.3    Froment, C.4    Monsarrat, B.5    Milon, A.6    Talmont, F.7
  • 49
    • 11144234979 scopus 로고    scopus 로고
    • Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli
    • DOI 10.1110/ps.041022305
    • A. Korepanova, F.P. Gao, Y.Z. Hua, H.J. Qin, R.K. Nakamoto, and T.A. Cross Cloning and expression of multiple integral membrane proteins from Mycobacterium tuberculosis in Escherichia coli Protein Sci. 14 2005 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
  • 50
    • 68049103042 scopus 로고    scopus 로고
    • KKKKPLFGLFFGLF: A cationic peptide designed to exert antibacterial activity
    • E. Duval, C. Zatylny, M. Laurencin, M. Baudy-Floc'h, and J. Henry KKKKPLFGLFFGLF: a cationic peptide designed to exert antibacterial activity Peptides 30 2009 1608 1612
    • (2009) Peptides , vol.30 , pp. 1608-1612
    • Duval, E.1    Zatylny, C.2    Laurencin, M.3    Baudy-Floc'H, M.4    Henry, J.5
  • 53
    • 0015712889 scopus 로고
    • Nucleotide sequence of lactose messenger ribonucleic acid transcribed from UV5 promoter mutant of Escherichia coli
    • N.M. Maizels Nucleotide sequence of lactose messenger ribonucleic acid transcribed from UV5 promoter mutant of Escherichia coli Proc. Natl. Acad. Sci. USA 70 1973 3585 3589
    • (1973) Proc. Natl. Acad. Sci. USA , vol.70 , pp. 3585-3589
    • Maizels, N.M.1
  • 54
    • 0142231418 scopus 로고    scopus 로고
    • Growth rate regulation of lac operon expression in Escherichia Coli is cyclic AMP dependent
    • J.T. Kuo, Y.J. Chang, and C.P. Tseng Growth rate regulation of lac operon expression in Escherichia Coli is cyclic AMP dependent FEBS Lett. 553 2003 397 402
    • (2003) FEBS Lett. , vol.553 , pp. 397-402
    • Kuo, J.T.1    Chang, Y.J.2    Tseng, C.P.3
  • 55
    • 48749138481 scopus 로고
    • Membrane actions of water-soluble fusogens: Effect of dimethylsulfoxide, glycerol and sucrose on lipid bilayer order and fluidity
    • W.K. Surewicz Membrane actions of water-soluble fusogens: effect of dimethylsulfoxide, glycerol and sucrose on lipid bilayer order and fluidity Chem. Phys. Lipids 34 1984 363 372
    • (1984) Chem. Phys. Lipids , vol.34 , pp. 363-372
    • Surewicz, W.K.1
  • 56
    • 0021327428 scopus 로고
    • Dimethyl sulphoxide protects cells against polypeptide toxins and poliovirus
    • K. Sandvig, I.H. Madshus, and S. Olsnes Dimethylsulfoxide protects cells against polypeptide toxins and poliovirus Biochem. J. 219 1984 935 940 (Pubitemid 14141751)
    • (1984) Biochemical Journal , vol.219 , Issue.3 , pp. 935-940
    • Sandvig, K.1    Madshus, I.H.2    Olsnes, S.3
  • 57
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • R. Rudolph, and H. Lilie In vitro folding of inclusion body proteins FASEB J. 10 1996 49 56 (Pubitemid 26035506)
    • (1996) FASEB Journal , vol.10 , Issue.1 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 58
    • 0344653612 scopus 로고    scopus 로고
    • Responses of E. coli to osmotic stress: Large changes in amounts of cytoplasmic solutes and water
    • DOI 10.1016/S0968-0004(98)01196-7
    • M.T. Record, E.S. Courtenay, D.S. Cayley, and H.J. Guttman Responses of E. coli to osmotic stress: large changes in amounts of cytoplasmic solutes and water Trends Biochem. Sci. 23 1998 143 148 (Pubitemid 28189526)
    • (1998) Trends in Biochemical Sciences , vol.23 , Issue.4 , pp. 143-148
    • Record Jr., M.T.1    Courtenay, E.S.2    Cayley, D.S.3    Guttman, H.J.4
  • 59
    • 0021842726 scopus 로고
    • Allosteric regulation of glycerol kinase by enzyme III(glc) of the phosphotransferase system in Escherichia coli and Salmonella typhimurium
    • glc of the phosphotransferase system in Escherichia coli and Salmonella Typhimurium J. Bacteriol. 162 1985 810 816 (Pubitemid 15059762)
    • (1985) Journal of Bacteriology , vol.162 , Issue.2 , pp. 810-816
    • Novotny, M.J.1    Frederickson, W.L.2    Waygood, E.B.3    Saier Jr., M.H.4
  • 60
    • 0017330460 scopus 로고
    • Interaction of lac repressor with inducer. Kinetic and equilibrium measurements
    • B.E. Friedman, J.S. Olson, and K.S. Matthews Interaction of lac repressor with inducer - kinetic and equilibrium measurements J. Mol. Biol. 111 1977 27 39 (Pubitemid 8077907)
    • (1977) Journal of Molecular Biology , vol.111 , Issue.1 , pp. 27-39
    • Friedman, B.E.1    Olson, J.S.2    Matthews, K.S.3
  • 61
    • 18144400877 scopus 로고    scopus 로고
    • Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes: How well are protein folding and stability aspects coupled?
    • DOI 10.1074/jbc.M410947200
    • R. Mishra, R. Seckler, and R. Bhat Efficient refolding of aggregation-prone citrate synthase by polyol osmolytes - how well are protein folding and stability aspects coupled? J. Biol. Chem. 280 2005 15553 15560 (Pubitemid 40616671)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.16 , pp. 15553-15560
    • Mishra, R.1    Seckler, R.2    Bhat, R.3
  • 62
    • 0033028431 scopus 로고    scopus 로고
    • Molecular inroads into the regulation and metabolism of fatty acids, lessons from bacteria
    • DOI 10.1016/S0163-7827(98)00022-8, PII S0163782798000228
    • C.C. DiRusso, P.N. Black, and J.D. Weimar Molecular inroads into the regulation and metabolism of fatty acids, lessons from bacteria Prog. Lipid Res. 38 1999 129 197 (Pubitemid 29151326)
    • (1999) Progress in Lipid Research , vol.38 , Issue.2 , pp. 129-197
    • DiRusso, C.C.1    Black, P.N.2    Weimar, J.D.3
  • 63
    • 4944246094 scopus 로고    scopus 로고
    • Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins
    • DOI 10.1038/nature02899
    • L. Ferbitz, T. Maier, H. Patzelt, B. Bukau, E. Deuerling, and N. Ban Trigger factor in complex with the ribosome forms a molecular cradle for nascent proteins Nature 431 2004 590 596 (Pubitemid 39336342)
    • (2004) Nature , vol.431 , Issue.7008 , pp. 590-596
    • Ferbitz, L.1    Maier, T.2    Patzelt, H.3    Bukau, B.4    Deuerling, E.5    Ban, N.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.