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Volumn 8, Issue 5, 2013, Pages

Production of Recombinant Disulfide-Rich Venom Peptides for Structural and Functional Analysis via Expression in the Periplasm of E. coli

Author keywords

[No Author keywords available]

Indexed keywords

BUFFER; CARBON 13; CENTIPEDE VENOM; DISULFIDE RICH VENOM PEPTIDE; HYBRID PROTEIN; NITROGEN 15; SCORPION VENOM; SEA ANEMONE TOXIN; SPIDER VENOM; UNCLASSIFIED DRUG; VENOM;

EID: 84877129926     PISSN: None     EISSN: 19326203     Source Type: Journal    
DOI: 10.1371/journal.pone.0063865     Document Type: Article
Times cited : (134)

References (111)
  • 1
    • 78751585262 scopus 로고    scopus 로고
    • Venomics: a new paradigm for natural products-based drug discovery
    • Vetter I, Davis JL, Rash LD, Anangi R, Mobli M, et al. (2011) Venomics: a new paradigm for natural products-based drug discovery. Amino Acids 40: 15-28.
    • (2011) Amino Acids , vol.40 , pp. 15-28
    • Vetter, I.1    Davis, J.L.2    Rash, L.D.3    Anangi, R.4    Mobli, M.5
  • 2
    • 80053645532 scopus 로고    scopus 로고
    • Venoms as a platform for human drugs: translating toxins into therapeutics
    • King GF, (2011) Venoms as a platform for human drugs: translating toxins into therapeutics. Expert Opin Biol Ther 11: 1469-1484.
    • (2011) Expert Opin Biol Ther , vol.11 , pp. 1469-1484
    • King, G.F.1
  • 4
    • 0242331757 scopus 로고    scopus 로고
    • Therapeutic potential of venom peptides
    • Lewis RJ, Garcia ML, (2003) Therapeutic potential of venom peptides. Nat Rev Drug Discov 2: 790-802.
    • (2003) Nat Rev Drug Discov , vol.2 , pp. 790-802
    • Lewis, R.J.1    Garcia, M.L.2
  • 5
    • 84872130087 scopus 로고    scopus 로고
    • Spider-venom peptides: structure, pharmacology, and potential for control of insect pests
    • King GF, Hardy MC (2012) Spider-venom peptides: structure, pharmacology, and potential for control of insect pests. Annu Rev Entomol: 475-496.
    • (2012) Annu Rev Entomol , pp. 475-496
    • King, G.F.1    Hardy, M.C.2
  • 8
    • 66949177983 scopus 로고    scopus 로고
    • Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3
    • Jensen JE, Durek T, Alewood PF, Adams DJ, King GF, et al. (2009) Chemical synthesis and folding of APETx2, a potent and selective inhibitor of acid sensing ion channel 3. Toxicon 54: 56-61.
    • (2009) Toxicon , vol.54 , pp. 56-61
    • Jensen, J.E.1    Durek, T.2    Alewood, P.F.3    Adams, D.J.4    King, G.F.5
  • 9
    • 61949466107 scopus 로고    scopus 로고
    • Integrated oxidative folding of cysteine/selenocysteine containing peptides: improving chemical synthesis of conotoxins
    • Walewska A, Zhang MM, Skalicky JJ, Yoshikami D, Olivera BM, et al. (2009) Integrated oxidative folding of cysteine/selenocysteine containing peptides: improving chemical synthesis of conotoxins. Angew Chem Int Ed 48: 2221-2224.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 2221-2224
    • Walewska, A.1    Zhang, M.M.2    Skalicky, J.J.3    Yoshikami, D.4    Olivera, B.M.5
  • 11
    • 0029828233 scopus 로고    scopus 로고
    • Strategies for achieving high-level expression of genes in Escherichia coli
    • Makrides SC, (1996) Strategies for achieving high-level expression of genes in Escherichia coli. Microbiol Rev 60: 512-538.
    • (1996) Microbiol Rev , vol.60 , pp. 512-538
    • Makrides, S.C.1
  • 12
    • 0030046574 scopus 로고    scopus 로고
    • In vitro folding of inclusion body proteins
    • Rudolph R, Lilie H, (1996) In vitro folding of inclusion body proteins. FASEB J 10: 49-56.
    • (1996) FASEB J , vol.10 , pp. 49-56
    • Rudolph, R.1    Lilie, H.2
  • 13
    • 79957793254 scopus 로고    scopus 로고
    • Tuned Escherichia coli as a host for the expression of disulfide-rich proteins
    • Salinas G, Pellizza L, Margenat M, Fló M, Fernández C, (2011) Tuned Escherichia coli as a host for the expression of disulfide-rich proteins. Biotechnol J 6: 686-699.
    • (2011) Biotechnol J , vol.6 , pp. 686-699
    • Salinas, G.1    Pellizza, L.2    Margenat, M.3    Fló, M.4    Fernández, C.5
  • 14
    • 3042660198 scopus 로고    scopus 로고
    • Secretory and extracellular production of recombinant proteins using Escherichia coli
    • Choi JH, Lee SY, (2004) Secretory and extracellular production of recombinant proteins using Escherichia coli. Appl Microbiol Biotechnol 64: 625-635.
    • (2004) Appl Microbiol Biotechnol , vol.64 , pp. 625-635
    • Choi, J.H.1    Lee, S.Y.2
  • 15
    • 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
  • 17
    • 79951919101 scopus 로고    scopus 로고
    • Macromolecular NMR spectroscopy for the non-spectroscopist
    • Kwan AH, Mobli M, Gooley PR, King GF, Mackay JP, (2011) Macromolecular NMR spectroscopy for the non-spectroscopist. FEBS J 278: 687-703.
    • (2011) FEBS J , vol.278 , pp. 687-703
    • Kwan, A.H.1    Mobli, M.2    Gooley, P.R.3    King, G.F.4    Mackay, J.P.5
  • 18
    • 84877114884 scopus 로고    scopus 로고
    • Determination of peptide and protein structures using NMR spectroscopy
    • In: Mander L, Liu H-W, editors, Oxford:Elsevier
    • King GF, Mobli M (2010) Determination of peptide and protein structures using NMR spectroscopy. In: Mander L, Liu H-W, editors. Comprehensive Natural Products Chemistry II: Chemistry and Biology. Oxford:Elsevier. pp. 279-325.
    • (2010) Comprehensive Natural Products Chemistry II: Chemistry and Biology , pp. 279-325
    • King, G.F.1    Mobli, M.2
  • 19
    • 79951931431 scopus 로고    scopus 로고
    • Macromolecular NMR spectroscopy for the non-spectroscopist: beyond macromolecular solution structure determination
    • Bieri M, Kwan AH, Mobli M, King GF, Mackay JP, et al. (2011) Macromolecular NMR spectroscopy for the non-spectroscopist: beyond macromolecular solution structure determination. FEBS J 278: 704-715.
    • (2011) FEBS J , vol.278 , pp. 704-715
    • Bieri, M.1    Kwan, A.H.2    Mobli, M.3    King, G.F.4    Mackay, J.P.5
  • 20
    • 80054777668 scopus 로고    scopus 로고
    • A dynamic pharmacophore drives the interaction between psalmotoxin-1 and the putative drug target acid-sensing ion channel 1a
    • Saez NJ, Mobli M, Bieri M, Chassagnon IR, Malde AK, et al. (2011) A dynamic pharmacophore drives the interaction between psalmotoxin-1 and the putative drug target acid-sensing ion channel 1a. Mol Pharmacol 80: 796-808.
    • (2011) Mol Pharmacol , vol.80 , pp. 796-808
    • Saez, N.J.1    Mobli, M.2    Bieri, M.3    Chassagnon, I.R.4    Malde, A.K.5
  • 21
    • 40649099110 scopus 로고    scopus 로고
    • Expression and purification of maltose-binding protein fusions
    • In: Ausubel FM, editor, Beverly Massachusetts, USA John Wiley & Sons, Inc., Unit 16
    • Riggs P (2001) Expression and purification of maltose-binding protein fusions. In: Ausubel FM, editor. Current Protocols in Molecular Biology.Beverly Massachusetts, USA John Wiley & Sons, Inc., Unit 16. 16.
    • (2001) Current Protocols in Molecular Biology , pp. 16
    • Riggs, P.1
  • 22
    • 19444373996 scopus 로고    scopus 로고
    • Making the most of affinity tags
    • Waugh DS, (2005) Making the most of affinity tags. Trends Biotech 23: 316-320.
    • (2005) Trends Biotech , vol.23 , pp. 316-320
    • Waugh, D.S.1
  • 23
    • 0023806075 scopus 로고
    • Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase
    • Smith DB, Johnson KS, (1988) Single-step purification of polypeptides expressed in Escherichia coli as fusions with glutathione S-transferase. Gene 67: 31-40.
    • (1988) Gene , vol.67 , pp. 31-40
    • Smith, D.B.1    Johnson, K.S.2
  • 24
    • 0025977037 scopus 로고
    • Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase
    • Guan KL, Dixon JE, (1991) Eukaryotic proteins expressed in Escherichia coli: an improved thrombin cleavage and purification procedure of fusion proteins with glutathione S-transferase. Anal Biochem 192: 262-267.
    • (1991) Anal Biochem , vol.192 , pp. 262-267
    • Guan, K.L.1    Dixon, J.E.2
  • 25
    • 0023680201 scopus 로고
    • Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein
    • di Guan C, Li P, Riggs PD, Inouye H, (1988) Vectors that facilitate the expression and purification of foreign peptides in Escherichia coli by fusion to maltose-binding protein. Gene 67: 21-30.
    • (1988) Gene , vol.67 , pp. 21-30
    • di Guan, C.1    Li, P.2    Riggs, P.D.3    Inouye, H.4
  • 26
    • 0032787876 scopus 로고    scopus 로고
    • Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused
    • Kapust RB, Waugh DS, (1999) Escherichia coli maltose-binding protein is uncommonly effective at promoting the solubility of polypeptides to which it is fused. Protein Sci 8: 1668-1674.
    • (1999) Protein Sci , vol.8 , pp. 1668-1674
    • Kapust, R.B.1    Waugh, D.S.2
  • 27
    • 0033589826 scopus 로고    scopus 로고
    • New fusion protein systems designed to give soluble expression in Escherichia coli
    • Davis GD, Elisee C, Newham DM, Harrison RG, (1999) New fusion protein systems designed to give soluble expression in Escherichia coli. Biotech Bioeng 65: 382-388.
    • (1999) Biotech Bioeng , vol.65 , pp. 382-388
    • Davis, G.D.1    Elisee, C.2    Newham, D.M.3    Harrison, R.G.4
  • 28
    • 4444378435 scopus 로고    scopus 로고
    • The solubility and stability of recombinant proteins are increased by their fusion to NusA
    • De Marco V, Stier G, Blandin S, de Marco A, (2004) The solubility and stability of recombinant proteins are increased by their fusion to NusA. Biochem Biophys Res Commun 322: 766-771.
    • (2004) Biochem Biophys Res Commun , vol.322 , pp. 766-771
    • De Marco, V.1    Stier, G.2    Blandin, S.3    de Marco, A.4
  • 29
    • 0035975859 scopus 로고    scopus 로고
    • The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins
    • Einhauer A, Jungbauer A, (2001) The FLAG peptide, a versatile fusion tag for the purification of recombinant proteins. J Biochem Biophys Methods 49: 455-465.
    • (2001) J Biochem Biophys Methods , vol.49 , pp. 455-465
    • Einhauer, A.1    Jungbauer, A.2
  • 30
    • 0039310043 scopus 로고
    • Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli
    • Schatz PJ, (1993) Use of peptide libraries to map the substrate specificity of a peptide-modifying enzyme: a 13 residue consensus peptide specifies biotinylation in Escherichia coli. Biotechnology (NY) 11: 1138-1143.
    • (1993) Biotechnology (NY) , vol.11 , pp. 1138-1143
    • Schatz, P.J.1
  • 31
    • 0035975923 scopus 로고    scopus 로고
    • Perspectives of immobilized-metal affinity chromatography
    • Gaberc-Porekar V, Menart V, (2001) Perspectives of immobilized-metal affinity chromatography. J Biochem Biophys Methods 49: 335-360.
    • (2001) J Biochem Biophys Methods , vol.49 , pp. 335-360
    • Gaberc-Porekar, V.1    Menart, V.2
  • 32
    • 0027991404 scopus 로고
    • One-step affinity purification of bacterially produced proteins by means of the "Strep tag" and immobilized recombinant core streptavidin
    • Schmidt TG, Skerra A, (1994) One-step affinity purification of bacterially produced proteins by means of the "Strep tag" and immobilized recombinant core streptavidin. J Chromatogr A 676: 337-345.
    • (1994) J Chromatogr A , vol.676 , pp. 337-345
    • Schmidt, T.G.1    Skerra, A.2
  • 33
    • 34250766201 scopus 로고    scopus 로고
    • The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins
    • Schmidt TG, Skerra A, (2007) The Strep-tag system for one-step purification and high-affinity detection or capturing of proteins. Nat Protocols 2: 1528-1535.
    • (2007) Nat Protocols , vol.2 , pp. 1528-1535
    • Schmidt, T.G.1    Skerra, A.2
  • 34
    • 3142609724 scopus 로고    scopus 로고
    • Protein aggregation during overexpression limited by peptide extensions with large net negative charge
    • Zhang YB, Howitt J, McCorkle S, Lawrence P, Springer K, et al. (2004) Protein aggregation during overexpression limited by peptide extensions with large net negative charge. Protein Expr Purif 36: 207-216.
    • (2004) Protein Expr Purif , vol.36 , pp. 207-216
    • Zhang, Y.B.1    Howitt, J.2    McCorkle, S.3    Lawrence, P.4    Springer, K.5
  • 35
    • 0026577811 scopus 로고
    • A single step purification for recombinant proteins. Characterization of a microtubule associated protein (MAP 2) fragment which associates with the type II cAMP-dependent protein kinase
    • Stofko-Hahn RE, Carr DW, Scott JD, (1992) A single step purification for recombinant proteins. Characterization of a microtubule associated protein (MAP 2) fragment which associates with the type II cAMP-dependent protein kinase. FEBS Lett 302: 274-278.
    • (1992) FEBS Lett , vol.302 , pp. 274-278
    • Stofko-Hahn, R.E.1    Carr, D.W.2    Scott, J.D.3
  • 36
    • 0031579473 scopus 로고    scopus 로고
    • A new expression vector for high level protein production, one step purification and direct isotopic labeling of calmodulin-binding peptide fusion proteins
    • Zheng CF, Simcox T, Xu L, Vaillancourt P, (1997) A new expression vector for high level protein production, one step purification and direct isotopic labeling of calmodulin-binding peptide fusion proteins. Gene 186: 55-60.
    • (1997) Gene , vol.186 , pp. 55-60
    • Zheng, C.F.1    Simcox, T.2    Xu, L.3    Vaillancourt, P.4
  • 37
    • 13244265563 scopus 로고    scopus 로고
    • Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression
    • Dyson M, Shadbolt SP, Vincent K, Perera R, McCafferty J, (2004) Production of soluble mammalian proteins in Escherichia coli: identification of protein features that correlate with successful expression. BMC Biotechnol 4: 32.
    • (2004) BMC Biotechnol , vol.4 , pp. 32
    • Dyson, M.1    Shadbolt, S.P.2    Vincent, K.3    Perera, R.4    McCafferty, J.5
  • 38
    • 84860309632 scopus 로고    scopus 로고
    • Recombinant protein expression and purification: A comprehensive review of affinity tags and microbial applications
    • Young CL, Britton ZT, Robinson AS, (2012) Recombinant protein expression and purification: A comprehensive review of affinity tags and microbial applications. Biotechnol J 7: 620-634.
    • (2012) Biotechnol J , vol.7 , pp. 620-634
    • Young, C.L.1    Britton, Z.T.2    Robinson, A.S.3
  • 39
    • 0033762662 scopus 로고    scopus 로고
    • Production of stable isotope enriched antimicrobial peptides in Escherichia coli: An application to the production of a 15N-enriched fragment of lactoferrin
    • Majerle A, Kidrič J, Jerala R, (2000) Production of stable isotope enriched antimicrobial peptides in Escherichia coli: An application to the production of a 15N-enriched fragment of lactoferrin. J Biomol NMR 18: 145-151.
    • (2000) J Biomol NMR , vol.18 , pp. 145-151
    • Majerle, A.1    Kidrič, J.2    Jerala, R.3
  • 41
    • 33750489405 scopus 로고    scopus 로고
    • Incorporating a TEV cleavage site reduces the solubility of nine recombinant mouse proteins
    • Kurz M, Cowieson NP, Robin G, Hume DA, Martin JL, et al. (2006) Incorporating a TEV cleavage site reduces the solubility of nine recombinant mouse proteins. Protein Expr Purif 50: 68-73.
    • (2006) Protein Expr Purif , vol.50 , pp. 68-73
    • Kurz, M.1    Cowieson, N.P.2    Robin, G.3    Hume, D.A.4    Martin, J.L.5
  • 42
    • 0028228301 scopus 로고
    • Efficient and rapid affinity purification of proteins using recombinant fusion proteases
    • Walker PA, Leong LE, Ng PW, Tan SH, Waller S, et al. (1994) Efficient and rapid affinity purification of proteins using recombinant fusion proteases. Biotechnology (NY) 12: 601-605.
    • (1994) Biotechnology (NY) , vol.12 , pp. 601-605
    • Walker, P.A.1    Leong, L.E.2    Ng, P.W.3    Tan, S.H.4    Waller, S.5
  • 43
  • 44
    • 80054052318 scopus 로고    scopus 로고
    • An overview of enzymatic reagents for the removal of affinity tags
    • Waugh DS, (2011) An overview of enzymatic reagents for the removal of affinity tags. Protein Expr Purif 80: 283-293.
    • (2011) Protein Expr Purif , vol.80 , pp. 283-293
    • Waugh, D.S.1
  • 45
    • 0141539517 scopus 로고    scopus 로고
    • A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa
    • Jenny RJ, Mann KG, Lundblad RL, (2003) A critical review of the methods for cleavage of fusion proteins with thrombin and factor Xa. Protein Expr Purif 31: 1-11.
    • (2003) Protein Expr Purif , vol.31 , pp. 1-11
    • Jenny, R.J.1    Mann, K.G.2    Lundblad, R.L.3
  • 46
    • 0026692625 scopus 로고
    • An evaluation of different enzymatic cleavage methods for recombinant fusion proteins, applied on des(1-3)insulin-like growth factor I
    • Forsberg G, Baastrup B, Rondahl H, Holmgren E, Pohl G, et al. (1992) An evaluation of different enzymatic cleavage methods for recombinant fusion proteins, applied on des(1-3)insulin-like growth factor I. J Prot Chem 11: 201-211.
    • (1992) J Prot Chem , vol.11 , pp. 201-211
    • Forsberg, G.1    Baastrup, B.2    Rondahl, H.3    Holmgren, E.4    Pohl, G.5
  • 47
    • 77954002740 scopus 로고    scopus 로고
    • Gene optimization mechanisms: a multi-gene study reveals a high success rate of full-length human proteins expressed in Escherichia coli
    • Maertens B, Spriestersbach A, von Groll U, Roth U, Kubicek J, et al. (2010) Gene optimization mechanisms: a multi-gene study reveals a high success rate of full-length human proteins expressed in Escherichia coli. Protein Sci 19: 1312-1326.
    • (2010) Protein Sci , vol.19 , pp. 1312-1326
    • Maertens, B.1    Spriestersbach, A.2    von Groll, U.3    Roth, U.4    Kubicek, J.5
  • 48
    • 33645471986 scopus 로고    scopus 로고
    • A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production
    • Cabrita LD, Dai W, Bottomley SP, (2006) A family of E. coli expression vectors for laboratory scale and high throughput soluble protein production. BMC Biotechnol 6: 12.
    • (2006) BMC Biotechnol , vol.6 , pp. 12
    • Cabrita, L.D.1    Dai, W.2    Bottomley, S.P.3
  • 49
    • 0025292412 scopus 로고
    • Export of the periplasmic maltose-binding protein of Escherichia coli
    • Bassford PJ Jr, (1990) Export of the periplasmic maltose-binding protein of Escherichia coli. J Bioenerg Biomembr 22: 401-439.
    • (1990) J Bioenerg Biomembr , vol.22 , pp. 401-439
    • Bassford Jr., P.J.1
  • 50
    • 11944271430 scopus 로고
    • Solubility as a function of protein structure and solvent components
    • Schein CH, (1990) Solubility as a function of protein structure and solvent components. Biotechnology (NY) 8: 308-317.
    • (1990) Biotechnology (NY) , vol.8 , pp. 308-317
    • Schein, C.H.1
  • 51
    • 14744271625 scopus 로고
    • Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation
    • Kiefhaber T, Rudolph R, Kohler HH, Buchner J, (1991) Protein aggregation in vitro and in vivo: a quantitative model of the kinetic competition between folding and aggregation. Biotechnology (NY) 9: 825-829.
    • (1991) Biotechnology (NY) , vol.9 , pp. 825-829
    • Kiefhaber, T.1    Rudolph, R.2    Kohler, H.H.3    Buchner, J.4
  • 52
    • 0000671329 scopus 로고
    • Low temperatures stabilize interferon α-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli
    • Chesshyre JA, Hipkiss AR, (1989) Low temperatures stabilize interferon α-2 against proteolysis in Methylophilus methylotrophus and Escherichia coli. Appl Microbiol Biotech 31: 158-162.
    • (1989) Appl Microbiol Biotech , vol.31 , pp. 158-162
    • Chesshyre, J.A.1    Hipkiss, A.R.2
  • 53
    • 0028878615 scopus 로고
    • Tight transcriptional control mechanism ensures stable high-level expression from T7 promoter-based expression plasmids
    • Mertens N, Remaut E, Fiers W, (1995) Tight transcriptional control mechanism ensures stable high-level expression from T7 promoter-based expression plasmids. Biotechnology (NY) 13: 175-179.
    • (1995) Biotechnology (NY) , vol.13 , pp. 175-179
    • Mertens, N.1    Remaut, E.2    Fiers, W.3
  • 54
    • 65649135871 scopus 로고    scopus 로고
    • Practical protocols for production of very high yields of recombinant proteins using Escherichia coli
    • Sivashanmugam A, Murray V, Cui C, Zhang Y, Wang J, et al. (2009) Practical protocols for production of very high yields of recombinant proteins using Escherichia coli. Protein Sci 18: 936-948.
    • (2009) Protein Sci , vol.18 , pp. 936-948
    • Sivashanmugam, A.1    Murray, V.2    Cui, C.3    Zhang, Y.4    Wang, J.5
  • 55
    • 0034992645 scopus 로고    scopus 로고
    • A method for efficient isotopic labeling of recombinant proteins
    • Marley J, Lu M, Bracken C, (2001) A method for efficient isotopic labeling of recombinant proteins. J Biomol NMR 20: 71-75.
    • (2001) J Biomol NMR , vol.20 , pp. 71-75
    • Marley, J.1    Lu, M.2    Bracken, C.3
  • 56
    • 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 RC, Sreenath HK, Singh S, Aceti DJ, Bingman CA, et al. (2005) 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: 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
  • 57
    • 0028431597 scopus 로고
    • A novel isotope labeling protocol for bacterially expressed proteins
    • Reilly D, Fairbrother WJ, (1994) A novel isotope labeling protocol for bacterially expressed proteins. J Biomol NMR 4: 459-462.
    • (1994) J Biomol NMR , vol.4 , pp. 459-462
    • Reilly, D.1    Fairbrother, W.J.2
  • 58
    • 0030095165 scopus 로고    scopus 로고
    • High-level production of uniformly 15N- and 13C-enriched fusion proteins in Escherichia coli
    • Jansson M, Li YC, Jendeberg L, Anderson S, Montelione GT, et al. (1996) High-level production of uniformly 15N- and 13C-enriched fusion proteins in Escherichia coli. J Biomol NMR 7: 131-141.
    • (1996) J Biomol NMR , vol.7 , pp. 131-141
    • Jansson, M.1    Li, Y.C.2    Jendeberg, L.3    Anderson, S.4    Montelione, G.T.5
  • 59
    • 0030749281 scopus 로고    scopus 로고
    • Isotope labelling of macromolecules for structural determinations
    • Kainosho M, (1997) Isotope labelling of macromolecules for structural determinations. Nat Struct Biol 4: 858-861.
    • (1997) Nat Struct Biol , vol.4 , pp. 858-861
    • Kainosho, M.1
  • 60
    • 0016786847 scopus 로고
    • Parameters affecting the rate of synthesis of ribosomes and RNA polymerase in bacteria
    • Bremer H, (1975) Parameters affecting the rate of synthesis of ribosomes and RNA polymerase in bacteria. J Theoret Biol 53: 115-124.
    • (1975) J Theoret Biol , vol.53 , pp. 115-124
    • Bremer, H.1
  • 63
    • 72949086430 scopus 로고    scopus 로고
    • Direct visualization of disulfide bonds through diselenide proxies using 77Se NMR spectroscopy
    • Mobli M, de Araujo AD, Lambert LK, Pierens GK, Windley MJ, et al. (2009) Direct visualization of disulfide bonds through diselenide proxies using 77Se NMR spectroscopy. Angew Chem Int Ed 48: 9312-9314.
    • (2009) Angew Chem Int Ed , vol.48 , pp. 9312-9314
    • Mobli, M.1    de Araujo, A.D.2    Lambert, L.K.3    Pierens, G.K.4    Windley, M.J.5
  • 64
    • 76549170704 scopus 로고
    • The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts
    • Neu HC, Heppel LA, (1965) The release of enzymes from Escherichia coli by osmotic shock and during the formation of spheroplasts. J Biol Chem 240: 3685-3692.
    • (1965) J Biol Chem , vol.240 , pp. 3685-3692
    • Neu, H.C.1    Heppel, L.A.2
  • 65
    • 33749538062 scopus 로고    scopus 로고
    • Recombinant protein expression and solubility screening in Escherichia coli: a comparative study
    • Berrow NS, Bussow K, Coutard B, Diprose J, Ekberg M, et al. (2006) Recombinant protein expression and solubility screening in Escherichia coli: a comparative study. Acta Crystallogr D 62: 1218-1226.
    • (2006) Acta Crystallogr D , vol.62 , pp. 1218-1226
    • Berrow, N.S.1    Bussow, K.2    Coutard, B.3    Diprose, J.4    Ekberg, M.5
  • 66
  • 67
    • 77951296511 scopus 로고    scopus 로고
    • The optimization of in vitro high-throughput chemical lysis of Escherichia coli. Application to ACP domain of the polyketide synthase ppsC from Mycobacterium tuberculosis
    • Listwan P, Pedelacq JD, Lockard M, Bell C, Terwilliger TC, et al. (2010) The optimization of in vitro high-throughput chemical lysis of Escherichia coli. Application to ACP domain of the polyketide synthase ppsC from Mycobacterium tuberculosis. J Struct Funct Genomics 11: 41-49.
    • (2010) J Struct Funct Genomics , vol.11 , pp. 41-49
    • Listwan, P.1    Pedelacq, J.D.2    Lockard, M.3    Bell, C.4    Terwilliger, T.C.5
  • 68
    • 44049098410 scopus 로고    scopus 로고
    • Mechanical/physical methods of cell disruption and tissue homogenization
    • Goldberg S, (2008) Mechanical/physical methods of cell disruption and tissue homogenization. Methods Mol Biol 424: 3-22.
    • (2008) Methods Mol Biol , vol.424 , pp. 3-22
    • Goldberg, S.1
  • 69
    • 0024215242 scopus 로고
    • An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein
    • Maina CV, Riggs PD, Grandea AG, Slatko BE, Moran LS, et al. (1988) An Escherichia coli vector to express and purify foreign proteins by fusion to and separation from maltose-binding protein. Gene 74: 365-373.
    • (1988) Gene , vol.74 , pp. 365-373
    • Maina, C.V.1    Riggs, P.D.2    Grandea, A.G.3    Slatko, B.E.4    Moran, L.S.5
  • 70
    • 28144464877 scopus 로고    scopus 로고
    • Potential for using histidine tags in purification of proteins at large scale
    • Gaberc-Porekar V, Menart V, (2005) Potential for using histidine tags in purification of proteins at large scale. Chem Eng Tech 28: 1306-1314.
    • (2005) Chem Eng Tech , vol.28 , pp. 1306-1314
    • Gaberc-Porekar, V.1    Menart, V.2
  • 71
    • 84877101480 scopus 로고    scopus 로고
    • Macromolecular Crystallography Laboratory, USA, National Cancer Institute. (accessed 20130220)
    • Waugh DS (2010) TEV protease FAQ. Macromolecular Crystallography Laboratory, USA, National Cancer Institute. (http://mcl1.ncifcrf.gov/waugh_tech/faq/tev.pdf accessed 20130220).
    • (2010) TEV protease FAQ
    • Waugh, D.S.1
  • 72
    • 0035371184 scopus 로고    scopus 로고
    • Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple
    • Schafer FQ, Buettner GR, (2001) Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radical Biol Med 30: 1191-1212.
    • (2001) Free Radical Biol Med , vol.30 , pp. 1191-1212
    • Schafer, F.Q.1    Buettner, G.R.2
  • 73
    • 0014139748 scopus 로고
    • The standard redox potential of cysteine-cystine from the thiol-disulphide exchange reaction with glutathione and lipoic acid
    • Jocelyn PC, (1967) The standard redox potential of cysteine-cystine from the thiol-disulphide exchange reaction with glutathione and lipoic acid. Eur J Biochem 2: 327-331.
    • (1967) Eur J Biochem , vol.2 , pp. 327-331
    • Jocelyn, P.C.1
  • 75
    • 0025249194 scopus 로고
    • Amino acid analysis
    • Ozols J, (1990) Amino acid analysis. Methods Enzymol 182: 587-601.
    • (1990) Methods Enzymol , vol.182 , pp. 587-601
    • Ozols, J.1
  • 76
    • 79953282914 scopus 로고    scopus 로고
    • Quantitative amino acid analysis
    • In: Coligan JE, editor, John Wiley & Sons, Inc., Unit 3.2
    • Rutherfurd SM, Dunn BM (2011) Quantitative amino acid analysis In: Coligan JE, editor. Current Protocols in Protein Science John Wiley & Sons, Inc., Unit 3.2.
    • (2011) Current Protocols in Protein Science
    • Rutherfurd, S.M.1    Dunn, B.M.2
  • 77
    • 0012382504 scopus 로고    scopus 로고
    • Protein determination by UV absorption
    • In: Walker JM, editor, Humana Press
    • Aitken A, Learmonth M (2002) Protein determination by UV absorption. In: Walker JM, editor. The Protein Protocols Handbook:Humana Press. pp. 3-6.
    • (2002) The Protein Protocols Handbook , pp. 3-6
    • Aitken, A.1    Learmonth, M.2
  • 78
    • 0017184389 scopus 로고
    • A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding
    • Bradford MM, (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 72: 248-254.
    • (1976) Anal Biochem , vol.72 , pp. 248-254
    • Bradford, M.M.1
  • 79
    • 61349139504 scopus 로고    scopus 로고
    • Microvolume spectrophotometric and fluorometric determination of protein concentration
    • In: Coligan JE, editor, John Wiley & Sons, Inc
    • Desjardins P, Hansen JB, Allen M (2009) Microvolume spectrophotometric and fluorometric determination of protein concentration In: Coligan JE, editor. Current Protocols in Protein Science John Wiley & Sons, Inc.
    • (2009) Current Protocols in Protein Science
    • Desjardins, P.1    Hansen, J.B.2    Allen, M.3
  • 81
    • 0037048624 scopus 로고    scopus 로고
    • Low-conductivity buffers for high-sensitivity NMR measurements
    • Kelly AE, Ou HD, Withers R, Dötsch V, (2002) Low-conductivity buffers for high-sensitivity NMR measurements. J Am Chem Soc 124: 12013-12019.
    • (2002) J Am Chem Soc , vol.124 , pp. 12013-12019
    • Kelly, A.E.1    Ou, H.D.2    Withers, R.3    Dötsch, V.4
  • 82
    • 33846094119 scopus 로고    scopus 로고
    • Improving NMR sensitivity by use of salt-tolerant cryogenically cooled probes
    • Robosky LC, Reily MD, Avizonis D, (2007) Improving NMR sensitivity by use of salt-tolerant cryogenically cooled probes. Anal Bioanal Chem 387: 529-532.
    • (2007) Anal Bioanal Chem , vol.387 , pp. 529-532
    • Robosky, L.C.1    Reily, M.D.2    Avizonis, D.3
  • 83
    • 0027350599 scopus 로고
    • Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS
    • Anglister J, Grzesiek S, Ren H, Klee CB, Bax A, (1993) Isotope-edited multidimensional NMR of calcineurin B in the presence of the non-deuterated detergent CHAPS. J Biomol NMR 3: 121-126.
    • (1993) J Biomol NMR , vol.3 , pp. 121-126
    • Anglister, J.1    Grzesiek, S.2    Ren, H.3    Klee, C.B.4    Bax, A.5
  • 84
    • 0029400890 scopus 로고
    • Measuring protein self-association using pulsed-field gradient NMR spectroscopy: application to myosin light chain 2
    • Dingley AJ, Mackay JP, Chapman BE, Morris MB, Kuchel PW, et al. (1995) Measuring protein self-association using pulsed-field gradient NMR spectroscopy: application to myosin light chain 2. J Biomol NMR 6: 321-328.
    • (1995) J Biomol NMR , vol.6 , pp. 321-328
    • Dingley, A.J.1    Mackay, J.P.2    Chapman, B.E.3    Morris, M.B.4    Kuchel, P.W.5
  • 85
    • 3242798849 scopus 로고    scopus 로고
    • A simple method for improving protein solubility and long-term stability
    • Golovanov AP, Hautbergue GM, Wilson SA, Lian L-Y, (2004) A simple method for improving protein solubility and long-term stability. J Am Chem Soc 126: 8933-8939.
    • (2004) J Am Chem Soc , vol.126 , pp. 8933-8939
    • Golovanov, A.P.1    Hautbergue, G.M.2    Wilson, S.A.3    Lian, L.-Y.4
  • 86
    • 33646269969 scopus 로고    scopus 로고
    • Domain architecture and structure of the bacterial cell division protein DivIB
    • Robson SA, King GF, (2006) Domain architecture and structure of the bacterial cell division protein DivIB. Proc Natl Acad Sci USA 103: 6700-6705.
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6700-6705
    • Robson, S.A.1    King, G.F.2
  • 87
    • 0027155345 scopus 로고
    • Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins
    • Otting G, Liepinsh E, Wüthrich K, (1993) Disulfide bond isomerization in BPTI and BPTI(G36S): an NMR study of correlated mobility in proteins. Biochemistry 32: 3571-3582.
    • (1993) Biochemistry , vol.32 , pp. 3571-3582
    • Otting, G.1    Liepinsh, E.2    Wüthrich, K.3
  • 88
    • 33751408438 scopus 로고    scopus 로고
    • An improved strategy for high-level production of TEV protease in Escherichia coli and its purification and characterization
    • Fang L, Jia KZ, Tang YL, Ma DY, Yu M, et al. (2007) An improved strategy for high-level production of TEV protease in Escherichia coli and its purification and characterization. Protein Expr Purif 51: 102-109.
    • (2007) Protein Expr Purif , vol.51 , pp. 102-109
    • Fang, L.1    Jia, K.Z.2    Tang, Y.L.3    Ma, D.Y.4    Yu, M.5
  • 90
    • 0036027440 scopus 로고    scopus 로고
    • Novel insecticidal toxins from the venom of the spider Segestria florentina
    • Lipkin A, Kozlov S, Nosyreva E, Blake A, Windass JD, et al. (2002) Novel insecticidal toxins from the venom of the spider Segestria florentina. Toxicon 40: 125-130.
    • (2002) Toxicon , vol.40 , pp. 125-130
    • Lipkin, A.1    Kozlov, S.2    Nosyreva, E.3    Blake, A.4    Windass, J.D.5
  • 91
    • 84876666595 scopus 로고    scopus 로고
    • The insecticidal toxin Aps III is an atypical knottin peptide that potently blocks insect voltage-gated sodium channels
    • in press
    • Bende N, Kang E, Herzig V, Bosmans F, Nicholson GM, et al. (2013) The insecticidal toxin Aps III is an atypical knottin peptide that potently blocks insect voltage-gated sodium channels. Biochem Pharmacol, in press.
    • (2013) Biochem Pharmacol
    • Bende, N.1    Kang, E.2    Herzig, V.3    Bosmans, F.4    Nicholson, G.M.5
  • 92
    • 77953271751 scopus 로고    scopus 로고
    • A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain
    • Bohlen CJ, Priel A, Zhou S, King D, Siemens J, et al. (2010) A bivalent tarantula toxin activates the capsaicin receptor, TRPV1, by targeting the outer pore domain. Cell 141: 834-845.
    • (2010) Cell , vol.141 , pp. 834-845
    • Bohlen, C.J.1    Priel, A.2    Zhou, S.3    King, D.4    Siemens, J.5
  • 94
    • 0031618814 scopus 로고    scopus 로고
    • Novel insecticidal peptides from Tegenaria agrestis spider venom may have a direct effect on the insect central nervous system
    • Johnson JH, Bloomquist JR, Krapcho KJ, Kral RM Jr, Trovato R, et al. (1998) Novel insecticidal peptides from Tegenaria agrestis spider venom may have a direct effect on the insect central nervous system. Arch Insect Biochem Physiol 38: 19-31.
    • (1998) Arch Insect Biochem Physiol , vol.38 , pp. 19-31
    • Johnson, J.H.1    Bloomquist, J.R.2    Krapcho, K.J.3    Kral Jr., R.M.4    Trovato, R.5
  • 95
    • 0026630034 scopus 로고
    • Identification of insecticidal peptides from venom of the trap-door spider, Aptostichus schlingeri (Ctenizidae)
    • Skinner WS, Dennis PA, Li JP, Quistad GB, (1992) Identification of insecticidal peptides from venom of the trap-door spider, Aptostichus schlingeri (Ctenizidae). Toxicon 30: 1043-1050.
    • (1992) Toxicon , vol.30 , pp. 1043-1050
    • Skinner, W.S.1    Dennis, P.A.2    Li, J.P.3    Quistad, G.B.4
  • 96
    • 0028365066 scopus 로고
    • Isolation and sequencing of insecticidal peptides from the primitive hunting spider, Plectreurys tristis (Simon)
    • Quistad GB, Skinner WS, (1994) Isolation and sequencing of insecticidal peptides from the primitive hunting spider, Plectreurys tristis (Simon). J Biol Chem 269: 11098-11101.
    • (1994) J Biol Chem , vol.269 , pp. 11098-11101
    • Quistad, G.B.1    Skinner, W.S.2
  • 97
    • 4143069335 scopus 로고    scopus 로고
    • Isolation and characterization of Psalmopeotoxin I and II: two novel antimalarial peptides from the venom of the tarantula Psalmopoeus cambridgei
    • Choi SJ, Parent R, Guillaume C, Deregnaucourt C, Delarbre C, et al. (2004) Isolation and characterization of Psalmopeotoxin I and II: two novel antimalarial peptides from the venom of the tarantula Psalmopoeus cambridgei. FEBS Lett 572: 109-117.
    • (2004) FEBS Lett , vol.572 , pp. 109-117
    • Choi, S.J.1    Parent, R.2    Guillaume, C.3    Deregnaucourt, C.4    Delarbre, C.5
  • 98
    • 31044432475 scopus 로고    scopus 로고
    • Four novel tarantula toxins as selective modulators of voltage-gated sodium channel subtypes
    • Bosmans F, Rash L, Zhu S, Diochot S, Lazdunski M, et al. (2006) Four novel tarantula toxins as selective modulators of voltage-gated sodium channel subtypes. Mol Pharmacol 69: 419-429.
    • (2006) Mol Pharmacol , vol.69 , pp. 419-429
    • Bosmans, F.1    Rash, L.2    Zhu, S.3    Diochot, S.4    Lazdunski, M.5
  • 99
    • 0037126684 scopus 로고    scopus 로고
    • Two tarantula peptides inhibit activation of multiple sodium channels
    • Middleton RE, Warren VA, Kraus RL, Hwang JC, Liu CJ, et al. (2002) Two tarantula peptides inhibit activation of multiple sodium channels. Biochemistry 41: 14734-14747.
    • (2002) Biochemistry , vol.41 , pp. 14734-14747
    • Middleton, R.E.1    Warren, V.A.2    Kraus, R.L.3    Hwang, J.C.4    Liu, C.J.5
  • 100
    • 17644381598 scopus 로고    scopus 로고
    • Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel
    • Jung HJ, Lee JY, Kim SH, Eu YJ, Shin SY, et al. (2005) Solution structure and lipid membrane partitioning of VSTx1, an inhibitor of the KvAP potassium channel. Biochemistry 44: 6015-6023.
    • (2005) Biochemistry , vol.44 , pp. 6015-6023
    • Jung, H.J.1    Lee, J.Y.2    Kim, S.H.3    Eu, Y.J.4    Shin, S.Y.5
  • 101
    • 2942650423 scopus 로고    scopus 로고
    • Modulation of Kv4.2 channels by a peptide isolated from the venom of the giant bird-eating tarantula Theraphosa leblondi
    • Ebbinghaus J, Legros C, Nolting A, Guette C, Celerier ML, et al. (2004) Modulation of Kv4.2 channels by a peptide isolated from the venom of the giant bird-eating tarantula Theraphosa leblondi. Toxicon 43: 923-932.
    • (2004) Toxicon , vol.43 , pp. 923-932
    • Ebbinghaus, J.1    Legros, C.2    Nolting, A.3    Guette, C.4    Celerier, M.L.5
  • 102
    • 0029379657 scopus 로고
    • Characterization and cloning of insecticidal peptides from the primitive weaving spider Diguetia canities
    • Krapcho KJ, Kral RM Jr, Vanwagenen BC, Eppler KG, Morgan TK, (1995) Characterization and cloning of insecticidal peptides from the primitive weaving spider Diguetia canities. Insect Biochem Mol Biol 25: 991-1000.
    • (1995) Insect Biochem Mol Biol , vol.25 , pp. 991-1000
    • Krapcho, K.J.1    Kral Jr., R.M.2    Vanwagenen, B.C.3    Eppler, K.G.4    Morgan, T.K.5
  • 103
    • 0037408077 scopus 로고    scopus 로고
    • Purification and characterization of Hainantoxin-V, a tetrodotoxin-sensitive sodium channel inhibitor from the venom of the spider Selenocosmia hainana
    • Xiao YC, Liang SP, (2003) Purification and characterization of Hainantoxin-V, a tetrodotoxin-sensitive sodium channel inhibitor from the venom of the spider Selenocosmia hainana. Toxicon 41: 643-650.
    • (2003) Toxicon , vol.41 , pp. 643-650
    • Xiao, Y.C.1    Liang, S.P.2
  • 104
    • 0347816398 scopus 로고    scopus 로고
    • Inhibition of neuronal tetrodotoxin-sensitive Na+ channels by two spider toxins: hainantoxin-III and hainantoxin-IV
    • Xiao Y, Liang S, (2003) Inhibition of neuronal tetrodotoxin-sensitive Na+ channels by two spider toxins: hainantoxin-III and hainantoxin-IV. Eur J Pharmacol 477: 1-7.
    • (2003) Eur J Pharmacol , vol.477 , pp. 1-7
    • Xiao, Y.1    Liang, S.2
  • 105
    • 0346996705 scopus 로고    scopus 로고
    • Function and solution structure of hainantoxin-I, a novel insect sodium channel inhibitor from the Chinese bird spider Selenocosmia hainana
    • Li D, Xiao Y, Hu W, Xie J, Bosmans F, et al. (2003) Function and solution structure of hainantoxin-I, a novel insect sodium channel inhibitor from the Chinese bird spider Selenocosmia hainana. FEBS Lett 555: 616-622.
    • (2003) FEBS Lett , vol.555 , pp. 616-622
    • Li, D.1    Xiao, Y.2    Hu, W.3    Xie, J.4    Bosmans, F.5
  • 106
    • 33750873334 scopus 로고    scopus 로고
    • Spider toxins activate the capsaicin receptor to produce inflammatory pain
    • Siemens J, Zhou S, Piskorowski R, Nikai T, Lumpkin EA, et al. (2006) Spider toxins activate the capsaicin receptor to produce inflammatory pain. Nature 444: 208-212.
    • (2006) Nature , vol.444 , pp. 208-212
    • Siemens, J.1    Zhou, S.2    Piskorowski, R.3    Nikai, T.4    Lumpkin, E.A.5
  • 107
    • 0027465984 scopus 로고
    • Purification and amino acid sequences of six Tx3 type neurotoxins from the venom of the Brazilian 'armed' spider Phoneutria nigriventer (Keys)
    • Cordeiro Mdo N, de Figueiredo SG, Valentim Ado C, Diniz CR, von Eickstedt VR, et al. (1993) Purification and amino acid sequences of six Tx3 type neurotoxins from the venom of the Brazilian 'armed' spider Phoneutria nigriventer (Keys). Toxicon 31: 35-42.
    • (1993) Toxicon , vol.31 , pp. 35-42
    • Cordeiro Mdo, N.1    de Figueiredo, S.G.2    Valentim Ado, C.3    Diniz, C.R.4    von Eickstedt, V.R.5
  • 108
    • 33745249950 scopus 로고    scopus 로고
    • Potent modulation of the voltage-gated sodium channel Nav1.7 by OD1, a toxin from the scorpion Odonthobuthus doriae
    • Maertens C, Cuypers E, Amininasab M, Jalali A, Vatanpour H, et al. (2006) Potent modulation of the voltage-gated sodium channel Nav1.7 by OD1, a toxin from the scorpion Odonthobuthus doriae. Mol Pharmacol 70: 405-414.
    • (2006) Mol Pharmacol , vol.70 , pp. 405-414
    • Maertens, C.1    Cuypers, E.2    Amininasab, M.3    Jalali, A.4    Vatanpour, H.5
  • 109
    • 34548056414 scopus 로고    scopus 로고
    • AChBP-targeted α-conotoxin correlates distinct binding orientations with nAChR subtype selectivity
    • Dutertre S, Ulens C, Buttner R, Fish A, van Elk R, et al. (2007) AChBP-targeted α-conotoxin correlates distinct binding orientations with nAChR subtype selectivity. EMBO J 26: 3858-3867.
    • (2007) EMBO J , vol.26 , pp. 3858-3867
    • Dutertre, S.1    Ulens, C.2    Buttner, R.3    Fish, A.4    van Elk, R.5
  • 110
  • 111
    • 84865708220 scopus 로고    scopus 로고
    • Chemical punch packed in venoms makes centipedes excellent predators
    • Yang S, Liu Z, Xiao Y, Li Y, Rong M, et al. (2012) Chemical punch packed in venoms makes centipedes excellent predators. Mol Cell Proteomics 11: 640-650.
    • (2012) Mol Cell Proteomics , vol.11 , pp. 640-650
    • Yang, S.1    Liu, Z.2    Xiao, Y.3    Li, Y.4    Rong, M.5


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