메뉴 건너뛰기




Volumn 64, Issue 1, 2009, Pages 32-38

Improved yield of a ligand-binding GPCR expressed in E. coli for structural studies

Author keywords

Autoinduction; G protein coupled receptor; GPCR; Neurotensin; Neurotensin receptor

Indexed keywords

BUFFER; G PROTEIN COUPLED RECEPTOR; HYBRID PROTEIN; LIGAND; NEUROTENSIN; NEUROTENSIN RECEPTOR; NEUROTENSIN TYPE 1 RECEPTOR; PHOSPHOLIPID;

EID: 57649105479     PISSN: 10465928     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.pep.2008.10.001     Document Type: Article
Times cited : (28)

References (56)
  • 1
    • 22844448355 scopus 로고    scopus 로고
    • Structural biology of G protein-coupled receptors
    • Lundstrom K. Structural biology of G protein-coupled receptors. Bioorg. Med. Chem. Lett. 15 (2005) 3654-3657
    • (2005) Bioorg. Med. Chem. Lett. , vol.15 , pp. 3654-3657
    • Lundstrom, K.1
  • 2
    • 17844400914 scopus 로고    scopus 로고
    • The repertoire of G-protein-coupled receptors in fully sequenced genomes
    • Fredriksson R., and Schioth H.B. The repertoire of G-protein-coupled receptors in fully sequenced genomes. Mol. Pharmacol. 67 (2005) 1414-1425
    • (2005) Mol. Pharmacol. , vol.67 , pp. 1414-1425
    • Fredriksson, R.1    Schioth, H.B.2
  • 3
    • 0033118334 scopus 로고    scopus 로고
    • Molecular tinkering of G protein-coupled receptors: an evolutionary success
    • Bockaert J., and Pin J.P. Molecular tinkering of G protein-coupled receptors: an evolutionary success. EMBO J. 18 (1999) 1723-1729
    • (1999) EMBO J. , vol.18 , pp. 1723-1729
    • Bockaert, J.1    Pin, J.P.2
  • 4
    • 0037082324 scopus 로고    scopus 로고
    • Target validation of G-protein coupled receptors
    • Wise A., Gearing K., and Rees S. Target validation of G-protein coupled receptors. Drug Discov. Today 7 (2002) 235-246
    • (2002) Drug Discov. Today , vol.7 , pp. 235-246
    • Wise, A.1    Gearing, K.2    Rees, S.3
  • 8
    • 0032504237 scopus 로고    scopus 로고
    • G protein-coupled receptors. I. Diversity of receptor-ligand interactions
    • Ji T.H., Grossmann M., and Ji I. G protein-coupled receptors. I. Diversity of receptor-ligand interactions. J. Biol. Chem. 273 (1998) 17299-17302
    • (1998) J. Biol. Chem. , vol.273 , pp. 17299-17302
    • Ji, T.H.1    Grossmann, M.2    Ji, I.3
  • 9
    • 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. Purification and characterization of the human adenosine A(2a) receptor functionally expressed in Escherichia coli. Eur. J. Biochem. 269 (2002) 82-92
    • (2002) Eur. J. Biochem. , vol.269 , pp. 82-92
    • Weiss, H.M.1    Grisshammer, R.2
  • 10
    • 0027361998 scopus 로고
    • Expression of a rat neurotensin receptor in Escherichia coli
    • Grisshammer R., Duckworth R., and Henderson R. Expression of a rat neurotensin receptor in Escherichia coli. Biochem. J. 295 Pt. 2 (1993) 571-576
    • (1993) Biochem. J. , vol.295 , Issue.PART 2 , pp. 571-576
    • Grisshammer, R.1    Duckworth, R.2    Henderson, R.3
  • 11
    • 25844443463 scopus 로고    scopus 로고
    • Expression of human peripheral cannabinoid receptor for structural studies
    • Yeliseev A.A., Wong K.K., Soubias O., and Gawrisch K. Expression of human peripheral cannabinoid receptor for structural studies. Protein Sci. 14 (2005) 2638-2653
    • (2005) Protein Sci. , vol.14 , pp. 2638-2653
    • Yeliseev, A.A.1    Wong, K.K.2    Soubias, O.3    Gawrisch, K.4
  • 12
    • 33747787335 scopus 로고    scopus 로고
    • Bacterial expression of functional, biotinylated peripheral cannabinoid receptor CB2
    • Krepkiy D., Wong K., Gawrisch K., and Yeliseev A. Bacterial expression of functional, biotinylated peripheral cannabinoid receptor CB2. Protein Expr. Purif. 49 (2006) 60-70
    • (2006) Protein Expr. Purif. , vol.49 , pp. 60-70
    • Krepkiy, D.1    Wong, K.2    Gawrisch, K.3    Yeliseev, A.4
  • 13
    • 0033631386 scopus 로고    scopus 로고
    • Expression of functional M2 muscarinic acetylcholine receptor in Escherichia coli
    • Furukawa H., and Haga T. Expression of functional M2 muscarinic acetylcholine receptor in Escherichia coli. J. Biochem. 127 (2000) 151-161
    • (2000) J. Biochem. , vol.127 , pp. 151-161
    • Furukawa, H.1    Haga, T.2
  • 14
    • 0032200201 scopus 로고    scopus 로고
    • Purification of recombinant M1 muscarinic acetylcholine receptor
    • Hulme E.C., and Curtis C.A. Purification of recombinant M1 muscarinic acetylcholine receptor. Biochem. Soc. Trans. 26 (1998) S361
    • (1998) Biochem. Soc. Trans. , vol.26
    • Hulme, E.C.1    Curtis, C.A.2
  • 15
    • 0026666760 scopus 로고
    • Functional expression of the human serotonin 5-HT1A receptor in Escherichia coli. Ligand binding properties and interaction with recombinant G protein alpha-subunits
    • Bertin B., Freissmuth M., Breyer R.M., Schutz W., Strosberg A.D., and Marullo S. Functional expression of the human serotonin 5-HT1A receptor in Escherichia coli. Ligand binding properties and interaction with recombinant G protein alpha-subunits. J. Biol. Chem. 267 (1992) 8200-8206
    • (1992) J. Biol. Chem. , vol.267 , pp. 8200-8206
    • Bertin, B.1    Freissmuth, M.2    Breyer, R.M.3    Schutz, W.4    Strosberg, A.D.5    Marullo, S.6
  • 16
    • 0033979165 scopus 로고    scopus 로고
    • Engineering of a proteolytically stable human beta 2-adrenergic receptor/maltose-binding protein fusion and production of the chimeric protein in Escherichia coli and baculovirus-infected insect cells
    • Hampe W., Voss R.H., Haase W., Boege F., Michel H., and Reilander H. Engineering of a proteolytically stable human beta 2-adrenergic receptor/maltose-binding protein fusion and production of the chimeric protein in Escherichia coli and baculovirus-infected insect cells. J. Biotechnol. 77 (2000) 219-234
    • (2000) J. Biotechnol. , vol.77 , pp. 219-234
    • Hampe, W.1    Voss, R.H.2    Haase, W.3    Boege, F.4    Michel, H.5    Reilander, H.6
  • 17
    • 0028652233 scopus 로고
    • Expression of rat NK-2 (neurokinin A) receptor in E. coli
    • Grisshammer R., Little J., and Aharony D. Expression of rat NK-2 (neurokinin A) receptor in E. coli. Receptors Channels 2 (1994) 295-302
    • (1994) Receptors Channels , vol.2 , pp. 295-302
    • Grisshammer, R.1    Little, J.2    Aharony, D.3
  • 18
    • 0027281985 scopus 로고
    • Functional expression of rat alpha 2B-adrenoceptor in Escherichia coli
    • Xia Y., Chhajlani V., and Wikberg J.E. Functional expression of rat alpha 2B-adrenoceptor in Escherichia coli. Eur. J. Pharmacol. 246 (1993) 129-133
    • (1993) Eur. J. Pharmacol. , vol.246 , pp. 129-133
    • Xia, Y.1    Chhajlani, V.2    Wikberg, J.E.3
  • 21
    • 0033105541 scopus 로고    scopus 로고
    • Expression of delta, kappa and mu human opioid receptors in Escherichia coli and reconstitution of the high-affinity state for agonist with heterotrimeric G proteins
    • Stanasila L., Massotte D., Kieffer B.L., and Pattus F. Expression of delta, kappa and mu human opioid receptors in Escherichia coli and reconstitution of the high-affinity state for agonist with heterotrimeric G proteins. Eur. J. Biochem. 260 (1999) 430-438
    • (1999) Eur. J. Biochem. , vol.260 , pp. 430-438
    • Stanasila, L.1    Massotte, D.2    Kieffer, B.L.3    Pattus, F.4
  • 22
    • 0029566092 scopus 로고
    • Ligand binding analysis of human neuropeptide Y1 receptor mutants expressed in E. coli
    • Munch G., Walker P., Shine J., and Herzog H. Ligand binding analysis of human neuropeptide Y1 receptor mutants expressed in E. coli. Receptors Channels 3 (1995) 291-297
    • (1995) Receptors Channels , vol.3 , pp. 291-297
    • Munch, G.1    Walker, P.2    Shine, J.3    Herzog, H.4
  • 23
    • 0033378616 scopus 로고    scopus 로고
    • Improved purification of a rat neurotensin receptor expressed in Escherichia coli
    • Grisshammer R., Averbeck P., and Sohal A.K. Improved purification of a rat neurotensin receptor expressed in Escherichia coli. Biochem. Soc. Trans. 27 (1999) 899-903
    • (1999) Biochem. Soc. Trans. , vol.27 , pp. 899-903
    • Grisshammer, R.1    Averbeck, P.2    Sohal, A.K.3
  • 24
    • 0031260369 scopus 로고    scopus 로고
    • Quantitative evaluation of neurotensin receptor purification by immobilized metal affinity chromatography
    • Grisshammer R., and Tucker J. Quantitative evaluation of neurotensin receptor purification by immobilized metal affinity chromatography. Protein. Expr. Purif. 11 (1997) 53-60
    • (1997) Protein. Expr. Purif. , vol.11 , pp. 53-60
    • Grisshammer, R.1    Tucker, J.2
  • 25
    • 26444581283 scopus 로고    scopus 로고
    • Large-scale expression and purification of a G-protein-coupled receptor for structure determination-an overview
    • Grisshammer R., White J.F., Trinh L.B., and Shiloach J. Large-scale expression and purification of a G-protein-coupled receptor for structure determination-an overview. J. Struct. Funct. Genomics 6 (2005) 159-163
    • (2005) J. Struct. Funct. Genomics , vol.6 , pp. 159-163
    • Grisshammer, R.1    White, J.F.2    Trinh, L.B.3    Shiloach, J.4
  • 26
    • 0023042283 scopus 로고
    • Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes
    • Studier F.W., and Moffatt B.A. Use of bacteriophage T7 RNA polymerase to direct selective high-level expression of cloned genes. J. Mol. Biol. 189 (1986) 113-130
    • (1986) J. Mol. Biol. , vol.189 , pp. 113-130
    • Studier, F.W.1    Moffatt, B.A.2
  • 27
    • 0030941829 scopus 로고    scopus 로고
    • The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm
    • Prinz W.A., Aslund F., Holmgren A., and Beckwith J. The role of the thioredoxin and glutaredoxin pathways in reducing protein disulfide bonds in the Escherichia coli cytoplasm. J. Biol. Chem. 272 (1997) 15661-15667
    • (1997) J. Biol. Chem. , vol.272 , pp. 15661-15667
    • Prinz, W.A.1    Aslund, F.2    Holmgren, A.3    Beckwith, J.4
  • 28
    • 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
    • Miroux B., and Walker J.E. 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 (1996) 289-298
    • (1996) J. Mol. Biol. , vol.260 , pp. 289-298
    • Miroux, B.1    Walker, J.E.2
  • 29
    • 0026305697 scopus 로고
    • Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor
    • Dubendorff J.W., and Studier F.W. Controlling basal expression in an inducible T7 expression system by blocking the target T7 promoter with lac repressor. J. Mol. Biol. 219 (1991) 45-59
    • (1991) J. Mol. Biol. , vol.219 , pp. 45-59
    • Dubendorff, J.W.1    Studier, F.W.2
  • 30
    • 0032536841 scopus 로고    scopus 로고
    • Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability
    • Grossman T.H., Kawasaki E.S., Punreddy S.R., and Osburne M.S. Spontaneous cAMP-dependent derepression of gene expression in stationary phase plays a role in recombinant expression instability. Gene 209 (1998) 95-103
    • (1998) Gene , vol.209 , pp. 95-103
    • Grossman, T.H.1    Kawasaki, E.S.2    Punreddy, S.R.3    Osburne, M.S.4
  • 32
    • 14844294424 scopus 로고    scopus 로고
    • Protein production by auto-induction in high density shaking cultures
    • Studier F.W. Protein production by auto-induction in high density shaking cultures. Protein Expr. Purif. 41 (2005) 207-234
    • (2005) Protein Expr. Purif. , vol.41 , pp. 207-234
    • Studier, F.W.1
  • 33
    • 33847145336 scopus 로고    scopus 로고
    • Expression of membrane proteins from Mycobacterium tuberculosis in Escherichia coli as fusions with maltose binding protein
    • Korepanova A., Moore J.D., Nguyen H.B., Hua Y., Cross T.A., and Gao F. Expression of membrane proteins from Mycobacterium tuberculosis in Escherichia coli as fusions with maltose binding protein. Protein Expr. Purif. 53 (2007) 24-30
    • (2007) Protein Expr. Purif. , vol.53 , pp. 24-30
    • Korepanova, A.1    Moore, J.D.2    Nguyen, H.B.3    Hua, Y.4    Cross, T.A.5    Gao, F.6
  • 34
    • 7044272757 scopus 로고    scopus 로고
    • Membrane proteins, lipids and detergents: not just a soap opera
    • Seddon A.M., Curnow P., and Booth P.J. Membrane proteins, lipids and detergents: not just a soap opera. Biochimica et Biophysica Acta 1666 (2004) 105-117
    • (2004) Biochimica et Biophysica Acta , vol.1666 , pp. 105-117
    • Seddon, A.M.1    Curnow, P.2    Booth, P.J.3
  • 36
    • 0041876269 scopus 로고    scopus 로고
    • Heterologous expression of G-protein-coupled receptors: comparison of expression systems fron the standpoint of large-scale production and purification
    • Sarramegna V., Talmont F., Demange P., and Milon A. Heterologous expression of G-protein-coupled receptors: comparison of expression systems fron the standpoint of large-scale production and purification. Cell. Mol. Life Sci. 60 (2003) 1529-1546
    • (2003) Cell. Mol. Life Sci. , vol.60 , pp. 1529-1546
    • Sarramegna, V.1    Talmont, F.2    Demange, P.3    Milon, A.4
  • 37
    • 0037648337 scopus 로고    scopus 로고
    • Structure-based analysis of GPCR function: conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1
    • Baneres J.L., Martin A., Hullot P., Girard J.P., Rossi J.C., and Parello J. Structure-based analysis of GPCR function: conformational adaptation of both agonist and receptor upon leukotriene B4 binding to recombinant BLT1. J. Mol. Biol. 329 (2003) 801-814
    • (2003) J. Mol. Biol. , vol.329 , pp. 801-814
    • Baneres, J.L.1    Martin, A.2    Hullot, P.3    Girard, J.P.4    Rossi, J.C.5    Parello, J.6
  • 38
    • 20144385917 scopus 로고    scopus 로고
    • Molecular characterization of a purified 5-HT4 receptor: a structural basis for drug efficacy
    • Baneres J.L., Mesnier D., Martin A., Joubert L., Dumuis A., and Bockaert J. Molecular characterization of a purified 5-HT4 receptor: a structural basis for drug efficacy. J. Biol. Chem. 280 (2005) 20253-20260
    • (2005) J. Biol. Chem. , vol.280 , pp. 20253-20260
    • Baneres, J.L.1    Mesnier, D.2    Martin, A.3    Joubert, L.4    Dumuis, A.5    Bockaert, J.6
  • 39
    • 0030467888 scopus 로고    scopus 로고
    • Expression of an olfactory receptor in Escherichia coli: purification, reconstitution, and ligand binding
    • Kiefer H., Krieger J., Olszewski J.D., Von Heijne G., Prestwich G.D., and Breer H. Expression of an olfactory receptor in Escherichia coli: purification, reconstitution, and ligand binding. Biochemistry 35 (1996) 16077-16084
    • (1996) Biochemistry , vol.35 , pp. 16077-16084
    • Kiefer, H.1    Krieger, J.2    Olszewski, J.D.3    Von Heijne, G.4    Prestwich, G.D.5    Breer, H.6
  • 40
    • 1942468187 scopus 로고    scopus 로고
    • Automated large-scale purification of a G protein-coupled receptor for neurotensin
    • White J.F., Trinh L.B., Shiloach J., and Grisshammer R. Automated large-scale purification of a G protein-coupled receptor for neurotensin. FEBS Lett. 564 (2004) 289-293
    • (2004) FEBS Lett. , vol.564 , pp. 289-293
    • White, J.F.1    Trinh, L.B.2    Shiloach, J.3    Grisshammer, R.4
  • 41
    • 57649111577 scopus 로고    scopus 로고
    • D. Kang, M. Thomas, D. Madelman, F. Katzen, J. Fletcher, A. Cullinan,W. Kudlicki, ADVERTISING FEATURE: MagicMedia™: a new E. coli growth media for higher yields in pET-based expression systems, Nat ure Application Notes. Available online 17 July 2006.
    • D. Kang, M. Thomas, D. Madelman, F. Katzen, J. Fletcher, A. Cullinan,W. Kudlicki, ADVERTISING FEATURE: MagicMedia™: a new E. coli growth media for higher yields in pET-based expression systems, Nat ure Application Notes. Available online 17 July 2006.
  • 42
    • 10844238943 scopus 로고    scopus 로고
    • Unattended high-density cell growth and induction of protein expression with overnight express autoinduction system
    • Grabski A., Mehler M., and Drott D. Unattended high-density cell growth and induction of protein expression with overnight express autoinduction system. InNovations 17 (2003) 3-8
    • (2003) InNovations , vol.17 , pp. 3-8
    • Grabski, A.1    Mehler, M.2    Drott, D.3
  • 43
    • 3543149006 scopus 로고    scopus 로고
    • The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3)
    • Dumon-Seignovert L., Cariot G., and Vuillard L. The toxicity of recombinant proteins in Escherichia coli: a comparison of overexpression in BL21(DE3), C41(DE3), and C43(DE3). Protein Expr. Purif. 37 (2004) 203-206
    • (2004) Protein Expr. Purif. , vol.37 , pp. 203-206
    • Dumon-Seignovert, L.1    Cariot, G.2    Vuillard, L.3
  • 44
    • 0034613080 scopus 로고    scopus 로고
    • Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F(1)F(o) ATP synthase
    • Arechaga I., Miroux B., Karrasch S., Huijbregts R., de Kruijff B., Runswick M.J., and Walker J.E. Characterisation of new intracellular membranes in Escherichia coli accompanying large scale over-production of the b subunit of F(1)F(o) ATP synthase. FEBS Lett. 482 (2000) 215-219
    • (2000) FEBS Lett. , vol.482 , pp. 215-219
    • Arechaga, I.1    Miroux, B.2    Karrasch, S.3    Huijbregts, R.4    de Kruijff, B.5    Runswick, M.J.6    Walker, J.E.7
  • 45
    • 29044449189 scopus 로고    scopus 로고
    • Solubilization, purification and reconstitution of Ca(2+)-ATPase from bovine pulmonary artery smooth muscle microsomes by different detergents: preservation of native structure and function of the enzyme by DHPC
    • Mandal A., Das S., Chakraborti T., Kar P., Ghosh B., and Chakraborti S. Solubilization, purification and reconstitution of Ca(2+)-ATPase from bovine pulmonary artery smooth muscle microsomes by different detergents: preservation of native structure and function of the enzyme by DHPC. Biochim. Biophys. Acta 1760 (2006) 20-31
    • (2006) Biochim. Biophys. Acta , vol.1760 , pp. 20-31
    • Mandal, A.1    Das, S.2    Chakraborti, T.3    Kar, P.4    Ghosh, B.5    Chakraborti, S.6
  • 46
    • 0026682998 scopus 로고
    • The essential role of specific Halobacterium halobium polar lipids in 2D-array formation of bacteriorhodopsin
    • Sternberg B., L'Hostis C., Whiteway C.A., and Watts A. The essential role of specific Halobacterium halobium polar lipids in 2D-array formation of bacteriorhodopsin. Biochim. Biophys. Acta 1108 (1992) 21-30
    • (1992) Biochim. Biophys. Acta , vol.1108 , pp. 21-30
    • Sternberg, B.1    L'Hostis, C.2    Whiteway, C.A.3    Watts, A.4
  • 47
    • 0024367272 scopus 로고
    • Membrane structure and dynamics
    • Watts A. Membrane structure and dynamics. Curr. Opin. Cell Biol. 1 (1989) 691-700
    • (1989) Curr. Opin. Cell Biol. , vol.1 , pp. 691-700
    • Watts, A.1
  • 48
    • 0031740077 scopus 로고    scopus 로고
    • Solid-state NMR approaches for studying the interaction of peptides and proteins with membranes
    • Watts A. Solid-state NMR approaches for studying the interaction of peptides and proteins with membranes. Biochim. Biophys. Acta 1376 (1998) 297-318
    • (1998) Biochim. Biophys. Acta , vol.1376 , pp. 297-318
    • Watts, A.1
  • 49
    • 33745633632 scopus 로고    scopus 로고
    • The biological significance of lipid-protein interactions
    • Findlay H.E., and Booth P.J. The biological significance of lipid-protein interactions. J. Phys.: Condens. Matter. 18 (2006) S1281-S1291
    • (2006) J. Phys.: Condens. Matter. , vol.18
    • Findlay, H.E.1    Booth, P.J.2
  • 52
    • 0038303147 scopus 로고    scopus 로고
    • A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: the cytochrome b6f complex of oxygenic photosynthesis
    • Zhang H., Kurisu G., Smith J.L., and Cramer W.A. A defined protein-detergent-lipid complex for crystallization of integral membrane proteins: the cytochrome b6f complex of oxygenic photosynthesis. Proc. Natl. Acad. Sci. USA 100 (2003) 5160-5163
    • (2003) Proc. Natl. Acad. Sci. USA , vol.100 , pp. 5160-5163
    • Zhang, H.1    Kurisu, G.2    Smith, J.L.3    Cramer, W.A.4
  • 53
    • 34250306407 scopus 로고    scopus 로고
    • Heterologous GPCR expression: a bottleneck to obtaining crystal structures
    • McCusker E.C., Bane S.E., O'Malley M.A., and Robinson A.S. Heterologous GPCR expression: a bottleneck to obtaining crystal structures. Biotechnol. Prog. 23 (2007) 540-547
    • (2007) Biotechnol. Prog. , vol.23 , pp. 540-547
    • McCusker, E.C.1    Bane, S.E.2    O'Malley, M.A.3    Robinson, A.S.4
  • 54
    • 0013805953 scopus 로고
    • Lipid composition of the normal human brain: gray matter, white matter, and myelin
    • O'Brien J.S., and Sampson E.L. Lipid composition of the normal human brain: gray matter, white matter, and myelin. J. Lipid Res. 6 (1965) 537-544
    • (1965) J. Lipid Res. , vol.6 , pp. 537-544
    • O'Brien, J.S.1    Sampson, E.L.2
  • 55
    • 14844337509 scopus 로고    scopus 로고
    • Auto-induction medium for the production of [U-15N]- and [U-13C, U-15N]-labeled proteins for NMR screening and structure determination
    • Tyler R.C., Sreenath H.K., Singh S., Aceti D.J., Bingman C.A., Markley J.L., and Fox B.G. Auto-induction medium for the production of [U-15N]- and [U-13C, U-15N]-labeled proteins for NMR screening and structure determination. Protein Expr. Purif. 40 (2005) 268-278
    • (2005) Protein Expr. Purif. , vol.40 , pp. 268-278
    • Tyler, R.C.1    Sreenath, H.K.2    Singh, S.3    Aceti, D.J.4    Bingman, C.A.5    Markley, J.L.6    Fox, B.G.7
  • 56
    • 34548158514 scopus 로고    scopus 로고
    • Neurotensin receptor type 1: Escherichia coli expression, purification, characterization and biophysical study
    • Harding P.J., Attrill H., Ross S., Koeppe J.R., Kapanidis A.N., and Watts A. Neurotensin receptor type 1: Escherichia coli expression, purification, characterization and biophysical study. Biochem. Soc. Trans. 35 (2007) 760-763
    • (2007) Biochem. Soc. Trans. , vol.35 , pp. 760-763
    • Harding, P.J.1    Attrill, H.2    Ross, S.3    Koeppe, J.R.4    Kapanidis, A.N.5    Watts, A.6


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.