메뉴 건너뛰기




Volumn 12, Issue 7, 2003, Pages 1332-1343

Recombinant production and solution structure of PcTx1, the specific peptide inhibitor of ASIC1a proton-gated cation channels

Author keywords

ASIC; ICK motif; NMR structure; Spider toxin

Indexed keywords

ACID SENSING ION CHANNEL; CATION CHANNEL; CYSTINE; PEPTIDE; PROTON; PSALMOTOXIN 1; RECOMBINANT PROTEIN; SPIDER VENOM; TOXIN; UNCLASSIFIED DRUG;

EID: 0037634059     PISSN: 09618368     EISSN: None     Source Type: Journal    
DOI: 10.1110/ps.0307003     Document Type: Article
Times cited : (103)

References (73)
  • 1
    • 0024562287 scopus 로고
    • Two classes of channel-specific toxins from funnel web spider venom
    • Adams, M.E., Herold, E.E., and Venema, V.J. 1989. Two classes of channel-specific toxins from funnel web spider venom. J. Comp. Physiol. 164: 333-342.
    • (1989) J. Comp. Physiol. , vol.164 , pp. 333-342
    • Adams, M.E.1    Herold, E.E.2    Venema, V.J.3
  • 2
    • 0025055598 scopus 로고
    • ω-agatoxins: Novel calcium channel antagonists of two subtypes from funnel web spider (Agelenopsis aperta) venom
    • Adams, M.E., Bindokas, V.P., Hasegawa, L., and Venema, V.J. 1990. ω-agatoxins: Novel calcium channel antagonists of two subtypes from funnel web spider (Agelenopsis aperta) venom. J. Biol. Chem. 265: 861-867.
    • (1990) J. Biol. Chem. , vol.265 , pp. 861-867
    • Adams, M.E.1    Bindokas, V.P.2    Hasegawa, L.3    Venema, V.J.4
  • 3
    • 0027332134 scopus 로고
    • Structure and properties of ω-agatoxin IVB, a new antagonist of P-type calcium channels
    • Adams, M.E., Mintz, I.M., Reily, M.D., Thanabal, V., and Bean, B.P. 1993. Structure and properties of ω-agatoxin IVB, a new antagonist of P-type calcium channels. Mol. Pharmacol. 44: 681-688.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 681-688
    • Adams, M.E.1    Mintz, I.M.2    Reily, M.D.3    Thanabal, V.4    Bean, B.P.5
  • 5
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T.-H., Billeter, M., Güntert, P., and Wüthrich, K. 1995. The program XEASY for computer-supported NMR spectral analysis of biological macromolecules. J. Biomol. NMR 5: 1-10.
    • (1995) J. Biomol. NMR , vol.5 , pp. 1-10
    • Bartels, C.1    Xia, T.-H.2    Billeter, M.3    Güntert, P.4    Wüthrich, K.5
  • 6
    • 0034489434 scopus 로고    scopus 로고
    • Solution structure of HpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel
    • Bernard, C., Legros, C., Ferrat, G., Bischoff, U., Marquardt, A., Pongs, O., and Darbon, H. 2000. Solution structure of HpTX2, a toxin from Heteropoda venatoria spider that blocks Kv4.2 potassium channel. Protein Sci. 9: 2059-2067.
    • (2000) Protein Sci. , vol.9 , pp. 2059-2067
    • Bernard, C.1    Legros, C.2    Ferrat, G.3    Bischoff, U.4    Marquardt, A.5    Pongs, O.6    Darbon, H.7
  • 7
    • 0035980211 scopus 로고    scopus 로고
    • Solution structure of Ptu1, a toxin from the assassin bug Peirates turpis that blocks the voltage-sensitive calcium channel N-type
    • Bernard, C., Corzo, G., Mosbah, A., Nakajima, T., and Darbon, H. 2001. Solution structure of Ptu1, a toxin from the assassin bug Peirates turpis that blocks the voltage-sensitive calcium channel N-type. Biochemistry 40: 12795-12800.
    • (2001) Biochemistry , vol.40 , pp. 12795-12800
    • Bernard, C.1    Corzo, G.2    Mosbah, A.3    Nakajima, T.4    Darbon, H.5
  • 12
    • 0033833498 scopus 로고    scopus 로고
    • Isolation, synthesis and pharmacological characterization of 8-palutoxins IT, novel insecticidal toxins from the spider Paracoelotes luctuosus (Amaurobiidae)
    • Corzo, G., Escoubas, P., Stankiewicz, M., Pelhate, M., Kristensen, C.P., and Nakajima, T. 2000. Isolation, synthesis and pharmacological characterization of 8-palutoxins IT, novel insecticidal toxins from the spider Paracoelotes luctuosus (Amaurobiidae). Eur. J. Biochem. 267: 5783-5795.
    • (2000) Eur. J. Biochem. , vol.267 , pp. 5783-5795
    • Corzo, G.1    Escoubas, P.2    Stankiewicz, M.3    Pelhate, M.4    Kristensen, C.P.5    Nakajima, T.6
  • 13
    • 0035239222 scopus 로고    scopus 로고
    • The cystine knot motif in toxins and implications for drug design
    • Craik, D.J., Daly, N.L., and Waine, C. 2001. The cystine knot motif in toxins and implications for drug design. Toxicon 39: 43-60.
    • (2001) Toxicon , vol.39 , pp. 43-60
    • Craik, D.J.1    Daly, N.L.2    Waine, C.3
  • 14
    • 0035066437 scopus 로고    scopus 로고
    • Brownian dynamics simulations of interaction between scorpion toxin Lq2 and potassium ion channel
    • Cui, M., Shen, J., Briggs, J.M., Luo, X., Tan, X., Jiang, H., Chen, K., and Ji, R. 2001. Brownian dynamics simulations of interaction between scorpion toxin Lq2 and potassium ion channel. Biophys. J. 80: 1659-1669.
    • (2001) Biophys. J. , vol.80 , pp. 1659-1669
    • Cui, M.1    Shen, J.2    Briggs, J.M.3    Luo, X.4    Tan, X.5    Jiang, H.6    Chen, K.7    Ji, R.8
  • 15
    • 0036302289 scopus 로고    scopus 로고
    • Brownian dynamics simulations of the recognition of the scorpion toxin P05 with the small-conductance calcium-activated potassium channels
    • Cui, M., Shen, J., Briggs, J.M., Fu, W., Wu, J., Zhang, Y., Luo, X., Chi, Z., Ji, R., Jiang, H., et al. 2002. Brownian dynamics simulations of the recognition of the scorpion toxin P05 with the small-conductance calcium-activated potassium channels. J. Mol. Biol. 318: 417-428.
    • (2002) J. Mol. Biol. , vol.318 , pp. 417-428
    • Cui, M.1    Shen, J.2    Briggs, J.M.3    Fu, W.4    Wu, J.5    Zhang, Y.6    Luo, X.7    Chi, Z.8    Ji, R.9    Jiang, H.10
  • 16
    • 0033573844 scopus 로고    scopus 로고
    • A novel endogenous inhibitor of phenoloxidase from Musca domestica has a cystine motif commonly found in snail and spider toxins
    • Daquinag, A.C., Sato, T., Koda, H., Takao, T., Fukuda, M., Shimonishi, Y., and Tsukamoto, T. 1999. A novel endogenous inhibitor of phenoloxidase from Musca domestica has a cystine motif commonly found in snail and spider toxins. Biochemistry 38: 2179-2188.
    • (1999) Biochemistry , vol.38 , pp. 2179-2188
    • Daquinag, A.C.1    Sato, T.2    Koda, H.3    Takao, T.4    Fukuda, M.5    Shimonishi, Y.6    Tsukamoto, T.7
  • 17
    • 6544276937 scopus 로고    scopus 로고
    • On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures
    • Dauplais, M., Lecoq, A., Song, J., Cotton, J., Jamin, N., Gilquin, B., Roumestand, C., Vita, C., de Medeiros, C.L., Rowan, E.G., et al. 1997. On the convergent evolution of animal toxins. Conservation of a diad of functional residues in potassium channel-blocking toxins with unrelated structures. J. Biol. Chem. 272: 4302-4309.
    • (1997) J. Biol. Chem. , vol.272 , pp. 4302-4309
    • Dauplais, M.1    Lecoq, A.2    Song, J.3    Cotton, J.4    Jamin, N.5    Gilquin, B.6    Roumestand, C.7    Vita, C.8    De Medeiros, C.L.9    Rowan, E.G.10
  • 19
    • 0033731951 scopus 로고    scopus 로고
    • Structure and pharmacology of spider venom neurotoxins
    • Escoubas, P., Diochot, S., and Corzo, G. 2000b. Structure and pharmacology of spider venom neurotoxins. Biochimie 82: 893-907.
    • (2000) Biochimie , vol.82 , pp. 893-907
    • Escoubas, P.1    Diochot, S.2    Corzo, G.3
  • 20
    • 0036088553 scopus 로고    scopus 로고
    • Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies
    • Escoubas, P., Diochot, S., Célérier, M.L., Nakajima, T., and Lazdunski, M. 2002. Novel tarantula toxins for subtypes of voltage-dependent potassium channels in the Kv2 and Kv4 subfamilies. Mol. Pharmacol. 62: 48-57.
    • (2002) Mol. Pharmacol. , vol.62 , pp. 48-57
    • Escoubas, P.1    Diochot, S.2    Célérier, M.L.3    Nakajima, T.4    Lazdunski, M.5
  • 21
    • 0034798344 scopus 로고    scopus 로고
    • Venomous cone snails: Molecular phylogeny and the generation of toxin diversity
    • Espiritu, D.J., Watkins, M., Dia-Monje, V., Cartier, G.E., Cruz, L.J., and Olivera, B.M. 2001. Venomous cone snails: Molecular phylogeny and the generation of toxin diversity. Toxicon 39: 1899-1916.
    • (2001) Toxicon , vol.39 , pp. 1899-1916
    • Espiritu, D.J.1    Watkins, M.2    Dia-Monje, V.3    Cartier, G.E.4    Cruz, L.J.5    Olivera, B.M.6
  • 22
    • 0030727613 scopus 로고    scopus 로고
    • The structure of versutoxin (δ-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel
    • Fletcher, J.I., Chapman, B.E., Mackay, J.P., Howden, M.E., and King, G.F. 1997. The structure of versutoxin (δ-atracotoxin-Hv1) provides insights into the binding of site 3 neurotoxins to the voltage-gated sodium channel. Structure 5: 1525-1535.
    • (1997) Structure , vol.5 , pp. 1525-1535
    • Fletcher, J.I.1    Chapman, B.E.2    Mackay, J.P.3    Howden, M.E.4    King, G.F.5
  • 23
    • 2342642814 scopus 로고    scopus 로고
    • Dipole moments of scorpion toxins direct the interaction towards small- or large-conductance Ca++-activated K+ channels
    • Fremont, V., Blanc, E., Crest, M., Eauclaire, M.F., Gola, M., Darbon, H., and Van Rietscoten, J. 1997. Dipole moments of scorpion toxins direct the interaction towards small- or large-conductance Ca++-activated K+ channels. Lett. Peptide Sci. 4: 305-312.
    • (1997) Lett. Peptide Sci. , vol.4 , pp. 305-312
    • Fremont, V.1    Blanc, E.2    Crest, M.3    Eauclaire, M.F.4    Gola, M.5    Darbon, H.6    Van Rietscoten, J.7
  • 24
    • 0036841675 scopus 로고    scopus 로고
    • Brownian dynamics simulations of the recognition of the scorpion toxin maurotoxin with the voltage-gated potassium ion channels
    • Fu, W., Cui, M., Briggs, J.M., Huang, X., Xiong, B., Zhang, Y., Luo, X., Shen, J., Ji, R., Jiang, H., et al. 2002. Brownian dynamics simulations of the recognition of the scorpion toxin maurotoxin with the voltage-gated potassium ion channels. Biophys. J. 83: 2370-2385.
    • (2002) Biophys. J. , vol.83 , pp. 2370-2385
    • Fu, W.1    Cui, M.2    Briggs, J.M.3    Huang, X.4    Xiong, B.5    Zhang, Y.6    Luo, X.7    Shen, J.8    Ji, R.9    Jiang, H.10
  • 25
    • 0026259488 scopus 로고
    • Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints
    • Güntert, P. and Wüthrich, K. 1991. Improved efficiency of protein structure calculations from NMR data using the program DIANA with redundant dihedral angle constraints. J. Biomol. NMR 1: 447-456.
    • (1991) J. Biomol. NMR , vol.1 , pp. 447-456
    • Güntert, P.1    Wüthrich, K.2
  • 26
    • 0034608606 scopus 로고    scopus 로고
    • A new member of acid-sensing ion channels from pituitary gland
    • Grunder, S., Geissler, H.S., Bassler, E.L., and Ruppersberg, J.P. 2000. A new member of acid-sensing ion channels from pituitary gland. Neuroreport 11: 1607-1611.
    • (2000) Neuroreport , vol.11 , pp. 1607-1611
    • Grunder, S.1    Geissler, H.S.2    Bassler, E.L.3    Ruppersberg, J.P.4
  • 27
    • 0031569801 scopus 로고    scopus 로고
    • Solution structure of the sodium channel antagonist conotoxin GS: A new molecular caliper for probing sodium channel geometry
    • Hill, J.M., Alewood, P.F., and Craik, D.J. 1997. Solution structure of the sodium channel antagonist conotoxin GS: A new molecular caliper for probing sodium channel geometry. Structure 5: 571-583.
    • (1997) Structure , vol.5 , pp. 571-583
    • Hill, J.M.1    Alewood, P.F.2    Craik, D.J.3
  • 29
    • 0033848234 scopus 로고    scopus 로고
    • Expression of functional recombinant scorpion β-neurotoxin Css II in E. coli
    • Johnson, T.M., Quick, M.W., Sakai, T.T., and Krishna, N.R. 2000. Expression of functional recombinant scorpion β-neurotoxin Css II in E. coli. Peptides 21: 767-772.
    • (2000) Peptides , vol.21 , pp. 767-772
    • Johnson, T.M.1    Quick, M.W.2    Sakai, T.T.3    Krishna, N.R.4
  • 31
    • 0033051246 scopus 로고    scopus 로고
    • Capsaicin, protons and heat: New excitement about nociceptors
    • Kress, M. and Zeilhofer, H.U. 1999. Capsaicin, protons and heat: New excitement about nociceptors. Trends Pharmacol. Sci. 20: 112-118.
    • (1999) Trends Pharmacol. Sci. , vol.20 , pp. 112-118
    • Kress, M.1    Zeilhofer, H.U.2
  • 32
    • 0019522783 scopus 로고
    • Receptor for protons in the membrane of sensory neurons
    • Krishtal, O.A. and Pidoplichko, V.I. 1981. Receptor for protons in the membrane of sensory neurons. Brain Res. 214: 150-154.
    • (1981) Brain Res. , vol.214 , pp. 150-154
    • Krishtal, O.A.1    Pidoplichko, V.I.2
  • 33
    • 0019327003 scopus 로고
    • A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules
    • Kumar, A., Ernst, R.R., and Wuthrich, K. 1980. A two-dimensional nuclear Overhauser enhancement (2D NOE) experiment for the elucidation of complete proton-proton cross-relaxation networks in biological macromolecules. Biochem. Biophys. Res. Commun. 95: 1-6.
    • (1980) Biochem. Biophys. Res. Commun. , vol.95 , pp. 1-6
    • Kumar, A.1    Ernst, R.R.2    Wuthrich, K.3
  • 34
    • 0027186445 scopus 로고
    • Isolation and pharmacological characterization of ω-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses
    • Lampe, R.A., Defeo, P.A., Davison, M.D., Young, J., Herman, J.L., Spreen, R.C., Horn, M.B., Mangano, T.J., and Keith, R.A. 1993. Isolation and pharmacological characterization of ω-grammotoxin SIA, a novel peptide inhibitor of neuronal voltage-sensitive calcium channel responses. Mol. Pharmacol. 44: 451-460.
    • (1993) Mol. Pharmacol. , vol.44 , pp. 451-460
    • Lampe, R.A.1    Defeo, P.A.2    Davison, M.D.3    Young, J.4    Herman, J.L.5    Spreen, R.C.6    Horn, M.B.7    Mangano, T.J.8    Keith, R.A.9
  • 35
    • 0000243829 scopus 로고
    • A program to check the stereochemical quality of protein structures
    • Laskowski, R.A., MacArthur, M.W., Moss, D.M., and Thornton, J.M. 1993. A program to check the stereochemical quality of protein structures. J. Appl. Cryst. 26: 283-291.
    • (1993) J. Appl. Cryst. , vol.26 , pp. 283-291
    • Laskowski, R.A.1    MacArthur, M.W.2    Moss, D.M.3    Thornton, J.M.4
  • 36
    • 0030339738 scopus 로고    scopus 로고
    • AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR
    • Laskowski, R.A., Rullmannn, J.A., MacArthur, M.W., Kaptein, R.. and Thornton, J.M. 1996. AQUA and PROCHECK-NMR: Programs for checking the quality of protein structures solved by NMR. J. Biomol. NMR 8: 477-486.
    • (1996) J. Biomol. NMR , vol.8 , pp. 477-486
    • Laskowski, R.A.1    Rullmannn, J.A.2    MacArthur, M.W.3    Kaptein, R.4    Thornton, J.M.5
  • 37
    • 0030973424 scopus 로고    scopus 로고
    • Structure-function relationships of ω-conotoxin GVIA. Synthesis, structure, calcium channel binding, and functional assay of alanine-substituted analogues
    • Lew, M.J., Flinn, J.P., Pallaghy, P.K., Murphy, R., Whorlow, S.L., Wright, C.E., Norton, R.S., and Angus, J.A. 1997. Structure-function relationships of ω-conotoxin GVIA. Synthesis, structure, calcium channel binding, and functional assay of alanine-substituted analogues. J. Biol. Chem. 272: 12014-12023.
    • (1997) J. Biol. Chem. , vol.272 , pp. 12014-12023
    • Lew, M.J.1    Flinn, J.P.2    Pallaghy, P.K.3    Murphy, R.4    Whorlow, S.L.5    Wright, C.E.6    Norton, R.S.7    Angus, J.A.8
  • 38
    • 0033976795 scopus 로고    scopus 로고
    • Ion channel toxins and therapeutics: From cone snail venoms to ciguatera
    • Lewis, R.J. 2000. Ion channel toxins and therapeutics: From cone snail venoms to ciguatera. Ther. Drug. Monit. 22: 61-64.
    • (2000) Ther. Drug. Monit. , vol.22 , pp. 61-64
    • Lewis, R.J.1
  • 39
    • 0033990723 scopus 로고    scopus 로고
    • Cloning and functional expression of a synthetic gene encoding huwentoxin-I, a neurotoxin from the Chinese bird spider (Selenocosmia huwena)
    • Li, M., Li, L.Y., Wu, X., and Liang, S.P. 2000. Cloning and functional expression of a synthetic gene encoding huwentoxin-I, a neurotoxin from the Chinese bird spider (Selenocosmia huwena). Toxicon 38: 153-162.
    • (2000) Toxicon , vol.38 , pp. 153-162
    • Li, M.1    Li, L.Y.2    Wu, X.3    Liang, S.P.4
  • 41
    • 0037151037 scopus 로고    scopus 로고
    • Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function
    • Maggio, F. and King, G.F. 2002. Scanning mutagenesis of a Janus-faced atracotoxin reveals a bipartite surface patch that is essential for neurotoxic function. J. Biol. Chem. 277: 22806-22813.
    • (2002) J. Biol. Chem. , vol.277 , pp. 22806-22813
    • Maggio, F.1    King, G.F.2
  • 43
    • 0027508282 scopus 로고
    • Block of calcium channels in rat neurons by synthetic ω-Aga-IVA
    • Mintz, I.M. and Bean, B.P. 1993. Block of calcium channels in rat neurons by synthetic ω-Aga-IVA. Neuropharmacology 32: 1161-1169.
    • (1993) Neuropharmacology , vol.32 , pp. 1161-1169
    • Mintz, I.M.1    Bean, B.P.2
  • 44
    • 0034663625 scopus 로고    scopus 로고
    • A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel
    • Mosbah, A., Kharrat, R., Fajloun, Z., Renisio, J.G., Blanc, E., Sabatier, J.M., El Ayeb, M., and Darbon, H. 2000. A new fold in the scorpion toxin family, associated with an activity on a ryanodine-sensitive calcium channel. Proteins 40: 436-442.
    • (2000) Proteins , vol.40 , pp. 436-442
    • Mosbah, A.1    Kharrat, R.2    Fajloun, Z.3    Renisio, J.G.4    Blanc, E.5    Sabatier, J.M.6    El Ayeb, M.7    Darbon, H.8
  • 45
    • 0028695949 scopus 로고
    • Snail and spider toxins share a similar tertiary structure and "cystine motif."
    • Narasimhan, L., Singh, J., Humblet, C., Guruprasad, K., and Blundell, T. 1994. Snail and spider toxins share a similar tertiary structure and "cystine motif." Nat. Struct. Biol. 1: 850-852.
    • (1994) Nat. Struct. Biol. , vol.1 , pp. 850-852
    • Narasimhan, L.1    Singh, J.2    Humblet, C.3    Guruprasad, K.4    Blundell, T.5
  • 47
    • 0031796848 scopus 로고    scopus 로고
    • The cystine knot structure of ion channel toxins and related polypeptides
    • Norton, R.S. and Pallaghy, P.K. 1998. The cystine knot structure of ion channel toxins and related polypeptides. Toxicon 36: 1573-1583.
    • (1998) Toxicon , vol.36 , pp. 1573-1583
    • Norton, R.S.1    Pallaghy, P.K.2
  • 49
    • 0029986992 scopus 로고    scopus 로고
    • Three-dimensional structure analysis of μ-agatoxins: Further evidence for common motifs among neurotoxins with diverse ion channel specificities
    • Omecinsky, D.O., Holub, K.E., Adams, M.E., and Reily, M.D. 1996. Three-dimensional structure analysis of μ-agatoxins: Further evidence for common motifs among neurotoxins with diverse ion channel specificities. Biochemistry 35: 2836-2844.
    • (1996) Biochemistry , vol.35 , pp. 2836-2844
    • Omecinsky, D.O.1    Holub, K.E.2    Adams, M.E.3    Reily, M.D.4
  • 51
    • 0037072815 scopus 로고    scopus 로고
    • Solution structure of peptide toxins that block mechanosensitive ion channels
    • Oswald, R.E., Suchyna, T.M., McFeeters, R., Gottlieb, P., and Sachs, F. 2002. Solution structure of peptide toxins that block mechanosensitive ion channels. J. Biol. Chem. 277: 34443-34450.
    • (2002) J. Biol. Chem. , vol.277 , pp. 34443-34450
    • Oswald, R.E.1    Suchyna, T.M.2    McFeeters, R.3    Gottlieb, P.4    Sachs, F.5
  • 52
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides
    • Pallaghy, P.K., Nielsen, K.J., Craik, D.J., and Norton, R.S. 1994. A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory polypeptides. Protein Sci. 3: 1833-1839.
    • (1994) Protein Sci. , vol.3 , pp. 1833-1839
    • Pallaghy, P.K.1    Nielsen, K.J.2    Craik, D.J.3    Norton, R.S.4
  • 53
    • 0025966769 scopus 로고
    • Design, synthesis, and functional expression of a gene for charybdotoxin, a peptide blocker of K+ channels
    • Park, C.S., Hausdorff, S.F., and Miller, C. 1991. Design, synthesis, and functional expression of a gene for charybdotoxin, a peptide blocker of K+ channels. Proc. Natl. Acad. Sci. 88: 2046-2050.
    • (1991) Proc. Natl. Acad. Sci. , vol.88 , pp. 2046-2050
    • Park, C.S.1    Hausdorff, S.F.2    Miller, C.3
  • 54
    • 0142042688 scopus 로고    scopus 로고
    • The effect of Huwentoxin-I on Ca(2+) channels in differentiated NG108-15 cells, a patch-clamp study
    • Peng, K., Chen, X.D., and Liang, S.P. 2001. The effect of Huwentoxin-I on Ca(2+) channels in differentiated NG108-15 cells, a patch-clamp study. Toxicon 39: 491-498.
    • (2001) Toxicon , vol.39 , pp. 491-498
    • Peng, K.1    Chen, X.D.2    Liang, S.P.3
  • 55
    • 0026717289 scopus 로고
    • Synthesis and characterization of a disulfide bond isomer of ω-conotoxin GVIA
    • Pennington, M.W., Festin, S.M., Maccecchini, M.L., and Kem, W.R. 1992. Synthesis and characterization of a disulfide bond isomer of ω-conotoxin GVIA. Toxicon 30: 755-764.
    • (1992) Toxicon , vol.30 , pp. 755-764
    • Pennington, M.W.1    Festin, S.M.2    Maccecchini, M.L.3    Kem, W.R.4
  • 56
    • 3943076416 scopus 로고    scopus 로고
    • An essential binding surface for ShK toxin interaction with rat brain potassium channels
    • Pennington, M.W., Mahnir, V.M., Khaytin, I., Zaydenberg, I., Byrnes, M.E., and Kem, W.R. 1996a. An essential binding surface for ShK toxin interaction with rat brain potassium channels. Biochemistry 35: 16407-16411.
    • (1996) Biochemistry , vol.35 , pp. 16407-16411
    • Pennington, M.W.1    Mahnir, V.M.2    Khaytin, I.3    Zaydenberg, I.4    Byrnes, M.E.5    Kem, W.R.6
  • 57
    • 0029997350 scopus 로고    scopus 로고
    • Identification of three separate binding sites on SHK toxin, a potent inhibitor of voltage-dependent potassium channels in human T-lymphocytes and rat brain
    • Pennington, M.W., Mahnir, V.M., Krafte, D.S., Zaydenberg, I., Byrnes, M.E., Khaytin, I., Crowley, K., and Kem, W.R. 1996b. Identification of three separate binding sites on SHK toxin, a potent inhibitor of voltage-dependent potassium channels in human T-lymphocytes and rat brain. Biochem. Biophys. Res. Commun. 219: 696-701.
    • (1996) Biochem. Biophys. Res. Commun. , vol.219 , pp. 696-701
    • Pennington, M.W.1    Mahnir, V.M.2    Krafte, D.S.3    Zaydenberg, I.4    Byrnes, M.E.5    Khaytin, I.6    Crowley, K.7    Kem, W.R.8
  • 58
    • 0033742266 scopus 로고    scopus 로고
    • Peptides and genes coding for scorpion toxins that affect ion-channels
    • Possani, L.D., Merino, E., Corona, M., Bolivar, F., and Becerril, B. 2000. Peptides and genes coding for scorpion toxins that affect ion-channels. Biochimie 82: 861-868.
    • (2000) Biochimie , vol.82 , pp. 861-868
    • Possani, L.D.1    Merino, E.2    Corona, M.3    Bolivar, F.4    Becerril, B.5
  • 59
    • 0030459627 scopus 로고    scopus 로고
    • Tissue acidosis in nociception and pain
    • Reeh, P.W. and Steen, K.H. 1996. Tissue acidosis in nociception and pain. Prog. Brain Res. 113: 143-151.
    • (1996) Prog. Brain Res. , vol.113 , pp. 143-151
    • Reeh, P.W.1    Steen, K.H.2
  • 61
    • 0033613178 scopus 로고    scopus 로고
    • Synthesis, bioactivity, and cloning of the L-type calcium channel blocker ω-conotoxin TxVII
    • Sasaki, T., Feng, Z.P., Scott, R., Grigoriev, N., Syed, N.I., Fainzilber, M., and Sato, K. 1999. Synthesis, bioactivity, and cloning of the L-type calcium channel blocker ω-conotoxin TxVII. Biochemistry 38: 12876-12884.
    • (1999) Biochemistry , vol.38 , pp. 12876-12884
    • Sasaki, T.1    Feng, Z.P.2    Scott, R.3    Grigoriev, N.4    Syed, N.I.5    Fainzilber, M.6    Sato, K.7
  • 62
    • 0032554613 scopus 로고    scopus 로고
    • Three-dimensional structure of κ-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails
    • Savarin, P., Guenneugues, M., Gilquin, B., Lamthanh, H., Gasparini, S., Zinn-Justin, S., and Ménez, A. 1998. Three-dimensional structure of κ-conotoxin PVIIA, a novel potassium channel-blocking toxin from cone snails. Biochemistry 37: 5407-5416.
    • (1998) Biochemistry , vol.37 , pp. 5407-5416
    • Savarin, P.1    Guenneugues, M.2    Gilquin, B.3    Lamthanh, H.4    Gasparini, S.5    Zinn-Justin, S.6    Ménez, A.7
  • 63
    • 19044384234 scopus 로고    scopus 로고
    • K-Hefutoxin1, a novel toxin from the scorpion heterometrus fulvipes with unique structure and function: Importance of the functional diad in potassium channel selectivity
    • Srinivasan, K.N., Sivaraja, V., Huys, I., Sasaki, T., Cheng, B., Kumar, T.K., Sato, K., Tytgat, J., Yu, C., Brian Chia, C.S., et al. 2002. K-Hefutoxin1, a novel toxin from the scorpion heterometrus fulvipes with unique structure and function: Importance of the functional diad in potassium channel selectivity. J. Biol. Chem. 277: 30040-30047.
    • (2002) J. Biol. Chem. , vol.277 , pp. 30040-30047
    • Srinivasan, K.N.1    Sivaraja, V.2    Huys, I.3    Sasaki, T.4    Cheng, B.5    Kumar, T.K.6    Sato, K.7    Tytgat, J.8    Yu, C.9    Brian Chia, C.S.10
  • 64
    • 0028811258 scopus 로고
    • An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula
    • Swartz, K.J. and MacKinnon, R. 1995. An inhibitor of the Kv2.1 potassium channel isolated from the venom of a Chilean tarantula. Neuron 15: 941-949.
    • (1995) Neuron , vol.15 , pp. 941-949
    • Swartz, K.J.1    MacKinnon, R.2
  • 65
    • 44049114111 scopus 로고
    • Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets
    • Szyperski, T., Güntert, P., Otting, G., and Wüthrich, K. 1992. Determination of scalar coupling constants by inverse Fourier transformation of in-phase multiplets. J. Magn. Reson. 99: 552-560.
    • (1992) J. Magn. Reson. , vol.99 , pp. 552-560
    • Szyperski, T.1    Güntert, P.2    Otting, G.3    Wüthrich, K.4
  • 67
    • 0032103129 scopus 로고    scopus 로고
    • +-gated cation channels: Neuronal acid sensors in the NaC/DEG family of ion channels
    • +-gated cation channels: Neuronal acid sensors in the NaC/DEG family of ion channels. Curr. Opin. Neurobiol. 8: 418-424.
    • (1998) Curr. Opin. Neurobiol. , vol.8 , pp. 418-424
    • Waldmann, R.1    Lazdunski, M.2
  • 70
    • 0033199282 scopus 로고    scopus 로고
    • Structure-function studies of ω-atracotoxin, a potent antagonist of insect voltage-gated calcium channels
    • Wang, X., Smith, R., Fletcher, J.I., Wilson, H., Wood, C.J., Howden, M.E., and King, G.F. 1999. Structure-function studies of ω-atracotoxin, a potent antagonist of insect voltage-gated calcium channels. Eur. J. Biochem. 264: 488-494.
    • (1999) Eur. J. Biochem. , vol.264 , pp. 488-494
    • Wang, X.1    Smith, R.2    Fletcher, J.I.3    Wilson, H.4    Wood, C.J.5    Howden, M.E.6    King, G.F.7
  • 71
    • 0037176852 scopus 로고    scopus 로고
    • Gene expression, mutation, and structure-function relationship of scorpion toxin BmP05 active on SK(Ca) channels
    • Wu, J.J., He, L.L., Zhou, Z., and Chi, C.W. 2002. Gene expression, mutation, and structure-function relationship of scorpion toxin BmP05 active on SK(Ca) channels. Biochemistry 41: 2844-2849.
    • (2002) Biochemistry , vol.41 , pp. 2844-2849
    • Wu, J.J.1    He, L.L.2    Zhou, Z.3    Chi, C.W.4
  • 73
    • 0031941375 scopus 로고    scopus 로고
    • Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis
    • Yan, L. and Adams, M.E. 1998. Lycotoxins, antimicrobial peptides from venom of the wolf spider Lycosa carolinensis. J. Biol. Chem. 273: 2059-2066.
    • (1998) J. Biol. Chem. , vol.273 , pp. 2059-2066
    • Yan, L.1    Adams, M.E.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.