메뉴 건너뛰기




Volumn 378, Issue 3, 2004, Pages 717-726

Diversity of folds in animal toxins acting on ion channels

Author keywords

Animal toxin; Disulphide bridging; Ion channel; Structural motif; Toxin fold

Indexed keywords

CELLS; MOLECULAR STRUCTURE; POLYPEPTIDES; PORE SIZE; POSITIVE IONS;

EID: 1642464613     PISSN: 02646021     EISSN: None     Source Type: Journal    
DOI: 10.1042/BJ20031860     Document Type: Review
Times cited : (217)

References (63)
  • 1
    • 0343671345 scopus 로고    scopus 로고
    • Functional architectures of animal toxins: A clue to drug design?
    • Ménez, A. (1998) Functional architectures of animal toxins: a clue to drug design? Toxicon 36, 1557-1572
    • (1998) Toxicon , vol.36 , pp. 1557-1572
    • Ménez, A.1
  • 2
    • 0037304388 scopus 로고    scopus 로고
    • Motions and structural variability within toxins: Implication for their use as scaffolds for protein engineering
    • Gilquin, B., Bourgoin, M., Ménez, R., Le Du, M. H., Servent, D., Zinn-Justin, S. and Ménez, A. (2003) Motions and structural variability within toxins: Implication for their use as scaffolds for protein engineering. Protein Sci. 12, 266-277
    • (2003) Protein Sci. , vol.12 , pp. 266-277
    • Gilquin, B.1    Bourgoin, M.2    Ménez, R.3    Le Du, M.H.4    Servent, D.5    Zinn-Justin, S.6    Ménez, A.7
  • 3
    • 0242331757 scopus 로고    scopus 로고
    • Therapeutic potential of venom peptides
    • Lewis, R. J. and Garcia, M. L. (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
  • 4
    • 6544291615 scopus 로고    scopus 로고
    • Sea anemone toxins as templates for the design of immunosuppressant drugs
    • Kem, W. R., Pennington, M. W. and Norton, R. S. (1999) Sea anemone toxins as templates for the design of immunosuppressant drugs. Perspect. Drug Discov. Des. 15/16, 111-129
    • (1999) Perspect. Drug Discov. Des. , vol.15-16 , pp. 111-129
    • Kem, W.R.1    Pennington, M.W.2    Norton, R.S.3
  • 5
    • 0032249498 scopus 로고    scopus 로고
    • Inhibition of T-type voltage-gated calcium channels by a new scorpion toxin
    • Chuang, R., Jaffe, H., Cribbs, L., Perez-Reyes, E. and Swartz, K. J. (1998) Inhibition of T-type voltage-gated calcium channels by a new scorpion toxin. Nat. Neurosci. 1, 668-674
    • (1998) Nat. Neurosci. , vol.1 , pp. 668-674
    • Chuang, R.1    Jaffe, H.2    Cribbs, L.3    Perez-Reyes, E.4    Swartz, K.J.5
  • 8
    • 0030783712 scopus 로고    scopus 로고
    • Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels
    • Blanc, E., Sabatier, J. M., Kharrat, R., Meunier, S., El Ayeb, M., Van Rietschoten, J. and Darbon, H. (1997) Solution structure of maurotoxin, a scorpion toxin from Scorpio maurus, with high affinity for voltage-gated potassium channels. Proteins 29, 321-333
    • (1997) Proteins , vol.29 , pp. 321-333
    • Blanc, E.1    Sabatier, J.M.2    Kharrat, R.3    Meunier, S.4    El Ayeb, M.5    Van Rietschoten, J.6    Darbon, H.7
  • 9
    • 0026726528 scopus 로고
    • Analysis of side-chain organization on a refined model of charybdotoxin: Structural and functional implications
    • Bontems, F., Gilquin, B., Roumestand, C., Ménez, A. and Toma, F. (1992) Analysis of side-chain organization on a refined model of charybdotoxin: structural and functional implications. Biochemistry 31, 7756-7764
    • (1992) Biochemistry , vol.31 , pp. 7756-7764
    • Bontems, F.1    Gilquin, B.2    Roumestand, C.3    Ménez, A.4    Toma, F.5
  • 12
    • 0031574335 scopus 로고    scopus 로고
    • Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA
    • Scanlon, M. J., Naranjo, D., Thomas, L., Alewood, P. F., Lewis, R. J. and Craik, D. J. (1997) Solution structure and proposed binding mechanism of a novel potassium channel toxin κ-conotoxin PVIIA. Structure 5, 1585-1597
    • (1997) Structure , vol.5 , pp. 1585-1597
    • Scanlon, M.J.1    Naranjo, D.2    Thomas, L.3    Alewood, P.F.4    Lewis, R.J.5    Craik, D.J.6
  • 13
    • 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. C., 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.C.9    Rowan, E.G.10
  • 14
    • 0029878263 scopus 로고    scopus 로고
    • Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone
    • Tudor, J. E., Pallaghy, P. K., Pennington, M. W. and Norton, R. S. (1996) Solution structure of ShK toxin, a novel potassium channel inhibitor from a sea anemone. Nat. Struct. Biol. 3, 317-320
    • (1996) Nat. Struct. Biol. , vol.3 , pp. 317-320
    • Tudor, J.E.1    Pallaghy, P.K.2    Pennington, M.W.3    Norton, R.S.4
  • 17
    • 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
  • 18
    • 0026418431 scopus 로고
    • Refined structure of charybdotoxin: Common motifs in scorpion toxins and insect defensins
    • Bontems, F., Roumestand, C., Gilquin, B., Ménez, A. and Toma, F. (1991) Refined structure of charybdotoxin: common motifs in scorpion toxins and insect defensins. Science 254, 1521-1523
    • (1991) Science , vol.254 , pp. 1521-1523
    • Bontems, F.1    Roumestand, C.2    Gilquin, B.3    Ménez, A.4    Toma, F.5
  • 19
    • 0028090517 scopus 로고
    • A common structural motif incorporating a cystine knot and a triple-stranded β-sheet in toxic and inhibitory peptides
    • 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 peptides. 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
  • 20
    • 0037033085 scopus 로고    scopus 로고
    • Function and solution structure of huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena
    • Peng, K., Shu, Q., Liu, Z. and Liang, S. (2002) Function and solution structure of huwentoxin-IV, a potent neuronal tetrodotoxin (TTX)-sensitive sodium channel antagonist from Chinese bird spider Selenocosmia huwena. J. Biol. Chem. 277, 47564-47571
    • (2002) J. Biol. Chem. , vol.277 , pp. 47564-47571
    • Peng, K.1    Shu, Q.2    Liu, Z.3    Liang, S.4
  • 21
    • 0030727613 scopus 로고    scopus 로고
    • The structure of versutoxin (delta-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 (delta-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
  • 22
    • 1642453564 scopus 로고    scopus 로고
    • The 'functional' dyad of scorpion toxin Pi1 is not by itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels
    • Mouhat, S., Mosbah, A., Visan, V., Wulff, H., Delepierre, M., Darbon, H., Grissmer, S., De Waard, M. and Sabatier, J. M. (2004) The 'functional' dyad of scorpion toxin Pi1 is not by itself a prerequisite for toxin binding to the voltage-gated Kv1.2 potassium channels. Biochem. J. 377, 25-36
    • (2004) Biochem. J. , vol.377 , pp. 25-36
    • Mouhat, S.1    Mosbah, A.2    Visan, V.3    Wulff, H.4    Delepierre, M.5    Darbon, H.6    Grissmer, S.7    De Waard, M.8    Sabatier, J.M.9
  • 23
    • 15644375485 scopus 로고    scopus 로고
    • Delineation of the functional site of α-dendrotoxin - The functional topographies of dendrotoxins are different but share a conserved core with those of other Kv1 potassium channel-blocking toxins
    • Gasparini, S., Danse, J. M., Lecoq, A., Pinkasfeld, S., Zinn-Justin, S., Young, L. C., de Meideros, C. C. L., Rowan, E. G., Harvey, A. and Ménez, A. (1998) Delineation of the functional site of α-dendrotoxin - The functional topographies of dendrotoxins are different but share a conserved core with those of other Kv1 potassium channel-blocking toxins. J. Biol. Chem. 273, 25393-25403
    • (1998) J. Biol. Chem. , vol.273 , pp. 25393-25403
    • Gasparini, S.1    Danse, J.M.2    Lecoq, A.3    Pinkasfeld, S.4    Zinn-Justin, S.5    Young, L.C.6    De Meideros, C.C.L.7    Rowan, E.G.8    Harvey, A.9    Ménez, A.10
  • 26
    • 0034096955 scopus 로고    scopus 로고
    • Structural basis for the biological activity of dendrotoxin-I, a potent potassium channels blocker
    • Katoh, E., Nishio, H., Inui, T., Nishiuchi, Y., Kimura, T., Sakakibara, S. and Yamazaki, T. (2000) Structural basis for the biological activity of dendrotoxin-I, a potent potassium channels blocker. Biopolymers 54, 44-57
    • (2000) Biopolymers , vol.54 , pp. 44-57
    • Katoh, E.1    Nishio, H.2    Inui, T.3    Nishiuchi, Y.4    Kimura, T.5    Sakakibara, S.6    Yamazaki, T.7
  • 30
    • 0037066147 scopus 로고    scopus 로고
    • Solution structures of the cis- and trans-Pro30 isomers of a novel 38-residue toxin from the venom of Hadronyche infensa sp. that contains a cystine-knot motif within its four disulfide bonds
    • Rosengren, K. J., Wilson, D., Daly, N. L., Alewood, P. F. and Craik, D. J. (2002) Solution structures of the cis- and trans-Pro30 isomers of a novel 38-residue toxin from the venom of Hadronyche infensa sp. that contains a cystine-knot motif within its four disulfide bonds. Biochemistry 41, 3294-3301
    • (2002) Biochemistry , vol.41 , pp. 3294-3301
    • Rosengren, K.J.1    Wilson, D.2    Daly, N.L.3    Alewood, P.F.4    Craik, D.J.5
  • 31
    • 0024790415 scopus 로고
    • Three-dimensional structure of the neurotoxin ATX la from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy
    • Widmer, H., Billeter, M. and Wuthrich, K. (1989) Three-dimensional structure of the neurotoxin ATX la from Anemonia sulcata in aqueous solution determined by nuclear magnetic resonance spectroscopy. Proteins 6, 357-371
    • (1989) Proteins , vol.6 , pp. 357-371
    • Widmer, H.1    Billeter, M.2    Wuthrich, K.3
  • 32
    • 0031584274 scopus 로고    scopus 로고
    • Structure of neurotoxin B-IV from the marine worm Cerebratulus lacteus: A helical hairpin cross-linked by disulphide bonding
    • Barnham, K. J., Dyke, T. R., Kem, W. R. and Norton, R. S. (1997) Structure of neurotoxin B-IV from the marine worm Cerebratulus lacteus: a helical hairpin cross-linked by disulphide bonding. J. Mol. Biol. 268, 886-902
    • (1997) J. Mol. Biol. , vol.268 , pp. 886-902
    • Barnham, K.J.1    Dyke, T.R.2    Kem, W.R.3    Norton, R.S.4
  • 33
    • 0028233375 scopus 로고
    • Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 Å resolution
    • Housset, D., Habersetzer-Rochat, C., Astier, J. P. and Fontecilla-Camps, J. C. (1994) Crystal structure of toxin II from the scorpion Androctonus australis Hector refined at 1.3 Å resolution. J. Mol. Biol. 238, 88-103
    • (1994) J. Mol. Biol. , vol.238 , pp. 88-103
    • Housset, D.1    Habersetzer-Rochat, C.2    Astier, J.P.3    Fontecilla-Camps, J.C.4
  • 35
    • 0032530987 scopus 로고    scopus 로고
    • An excitatory scorpion toxin with a distinctive feature: An additional alpha helix at the C-terminus and its implications for interaction with insect sodium channels
    • Oren, D. A., Froy, O., Amit, E., Kleinberger-Doron, N., Gurevitz, M. and Shaanan, B. (1998) An excitatory scorpion toxin with a distinctive feature: an additional alpha helix at the C-terminus and its implications for interaction with insect sodium channels. Structure 6, 1095-1103
    • (1998) Structure , vol.6 , pp. 1095-1103
    • Oren, D.A.1    Froy, O.2    Amit, E.3    Kleinberger-Doron, N.4    Gurevitz, M.5    Shaanan, B.6
  • 36
    • 0033731951 scopus 로고    scopus 로고
    • Structure and pharmacology of spider venom neurotoxins
    • Escoubas, P., Diochot, S. and Corzo, G. (2000) 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
  • 38
    • 0025915724 scopus 로고
    • Structure and structure-function relationships of sea anemone proteins that interact with the sodium channel
    • Norton, R. S. (1991) Structure and structure-function relationships of sea anemone proteins that interact with the sodium channel. Toxicon 29, 1051-1084
    • (1991) Toxicon , vol.29 , pp. 1051-1084
    • Norton, R.S.1
  • 39
    • 0003621201 scopus 로고    scopus 로고
    • Chemical synthesis and characterization of small proteins: Example of scorpion toxins
    • Rochat, H. and Martin-Eauclaire, M. F., eds, Birkhäuser Verlag, Basel, Boston and Berlin
    • Sabatier, J. M. (2000) Chemical synthesis and characterization of small proteins: example of scorpion toxins. In Animal Toxins (Rochat, H. and Martin-Eauclaire, M. F., eds), pp. 196-216, Birkhäuser Verlag, Basel, Boston and Berlin
    • (2000) Animal Toxins , pp. 196-216
    • Sabatier, J.M.1
  • 41
    • 0038606006 scopus 로고    scopus 로고
    • Importance of the conserved aromatic residues in the scorpion α-like toxin BmK M1: The hydrophobic surface region revisited
    • Sun, Y. M., Bosman, F., Zhu, R. H., Goudet, C., Xiong, Y. M., Tytgat, J. and Wang, D. C. (2003) Importance of the conserved aromatic residues in the scorpion α-like toxin BmK M1: The hydrophobic surface region revisited. J. Biol. Chem. 278, 24125-24131
    • (2003) J. Biol. Chem. , vol.278 , pp. 24125-24131
    • Sun, Y.M.1    Bosman, F.2    Zhu, R.H.3    Goudet, C.4    Xiong, Y.M.5    Tytgat, J.6    Wang, D.C.7
  • 42
    • 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
  • 43
    • 0027205407 scopus 로고
    • Solution structure of omega-conotoxin GVIA using 2-D NMR spectroscopy and relaxation matrix analysis
    • Davis, J. H., Bradley, E. K., Miljanich, G. P., Nadasdi, L., Ramachandran, J. and Basus, V. J. (1993) Solution structure of omega-conotoxin GVIA using 2-D NMR spectroscopy and relaxation matrix analysis. Biochemistry 32, 7396-7405
    • (1993) Biochemistry , vol.32 , pp. 7396-7405
    • Davis, J.H.1    Bradley, E.K.2    Miljanich, G.P.3    Nadasdi, L.4    Ramachandran, J.5    Basus, V.J.6
  • 44
    • 0029069121 scopus 로고
    • NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom
    • Albrand, J. P., Blackledge, M. J., Pascaud, F., Hollecker, M. and Marion, D. (1995) NMR and restrained molecular dynamics study of the three-dimensional solution structure of toxin FS2, a specific blocker of the L-type calcium channel, isolated from black mamba venom. Biochemistry 34, 5923-5937
    • (1995) Biochemistry , vol.34 , pp. 5923-5937
    • Albrand, J.P.1    Blackledge, M.J.2    Pascaud, F.3    Hollecker, M.4    Marion, D.5
  • 46
    • 0036207873 scopus 로고    scopus 로고
    • The virally encoded fungal toxin KP4 specifically blocks L-type voltage-gated calcium channels
    • Gage, M. J., Rane, S. G., Hockerman, G. H. and Smith, T. J. (2002) The virally encoded fungal toxin KP4 specifically blocks L-type voltage-gated calcium channels. Mol. Pharmacol. 61, 936-944
    • (2002) Mol. Pharmacol. , vol.61 , pp. 936-944
    • Gage, M.J.1    Rane, S.G.2    Hockerman, G.H.3    Smith, T.J.4
  • 47
    • 0036381024 scopus 로고    scopus 로고
    • Molecular moulds with multiple missions: Functional sites in three-finger toxins
    • Kini, R. M. (2002) Molecular moulds with multiple missions: functional sites in three-finger toxins. Clin. Exp. Pharmacol. Physiol. 29, 815-822
    • (2002) Clin. Exp. Pharmacol. Physiol. , vol.29 , pp. 815-822
    • Kini, R.M.1
  • 48
    • 0033152766 scopus 로고    scopus 로고
    • Roles of key functional groups in ω-conotoxin GVIA - Synthesis, structure and functional assay of selected peptide analogues
    • Flinn, J. P., Pallaghy, P. K., Lew, M. J., Murphy, R., Angus, J. A. and Norton, R. S. (1999) Roles of key functional groups in ω-conotoxin GVIA - Synthesis, structure and functional assay of selected peptide analogues. Eur. J. Biochem. 262, 447-455
    • (1999) Eur. J. Biochem. , vol.262 , pp. 447-455
    • Flinn, J.P.1    Pallaghy, P.K.2    Lew, M.J.3    Murphy, R.4    Angus, J.A.5    Norton, R.S.6
  • 49
    • 0028927315 scopus 로고
    • NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels
    • Lippens, G., Najib, J., Wodak, S. J. and Tartar, A. (1995) NMR sequential assignments and solution structure of chlorotoxin, a small scorpion toxin that blocks chloride channels. Biochemistry 34, 13-21
    • (1995) Biochemistry , vol.34 , pp. 13-21
    • Lippens, G.1    Najib, J.2    Wodak, S.J.3    Tartar, A.4
  • 51
    • 0033988543 scopus 로고    scopus 로고
    • The gene cloning and sequencing of Bm-12, a chlorotoxin-like peptide from the scorpion Buthus martensi Karsch
    • Wu, J. J., Dai, L., Lan, Z. D. and Chi, C. W. (2000) The gene cloning and sequencing of Bm-12, a chlorotoxin-like peptide from the scorpion Buthus martensi Karsch. Toxicon 38, 661-668
    • (2000) Toxicon , vol.38 , pp. 661-668
    • Wu, J.J.1    Dai, L.2    Lan, Z.D.3    Chi, C.W.4
  • 54
    • 0034672022 scopus 로고    scopus 로고
    • Maurotoxin compared with Pi1/HsTx1 scorpion toxins: Toward new insights in the understanding of their distinct disulfide bridge patterns
    • Fajloun, Z., Mosbah, A., Carlier, E., Mansuelle, P., Sandoz, G., Fathallah, M., di Luccio, E., Devaux, C., Rochat, H., Darbon, H. et al. (2000) Maurotoxin compared with Pi1/HsTx1 scorpion toxins: Toward new insights in the understanding of their distinct disulfide bridge patterns. J. Biol. Chem. 275, 39394-39402
    • (2000) J. Biol. Chem. , vol.275 , pp. 39394-39402
    • Fajloun, Z.1    Mosbah, A.2    Carlier, E.3    Mansuelle, P.4    Sandoz, G.5    Fathallah, M.6    Di Luccio, E.7    Devaux, C.8    Rochat, H.9    Darbon, H.10
  • 58
    • 0032538462 scopus 로고    scopus 로고
    • δ-Atracotoxins from Australian funnel-web spiders compete with scorpion α-toxin binding but differentially modulate alkaloid toxin activation of voltage-gated sodium channels
    • Little, M. J., Zappia, C., Gilles, N., Connor, M., Tyler, M. I., Martin-Eauclaire, M. F., Gordon, D. and Nicholson, G. M. (1998) δ-Atracotoxins from Australian funnel-web spiders compete with scorpion α-toxin binding but differentially modulate alkaloid toxin activation of voltage-gated sodium channels. J. Biol. Chem. 273, 27076-27083
    • (1998) J. Biol. Chem. , vol.273 , pp. 27076-27083
    • Little, M.J.1    Zappia, C.2    Gilles, N.3    Connor, M.4    Tyler, M.I.5    Martin-Eauclaire, M.F.6    Gordon, D.7    Nicholson, G.M.8
  • 62
    • 0034060567 scopus 로고    scopus 로고
    • Structure-activity relationships of ω-conotoxins at N-type voltage sensitive calcium channels
    • Nielsen, K. J., Schroeder, T. and Lewis, R. (2000) Structure-activity relationships of ω-conotoxins at N-type voltage sensitive calcium channels. J. Mol. Recogn. 13, 55-70
    • (2000) J. Mol. Recogn. , vol.13 , pp. 55-70
    • Nielsen, K.J.1    Schroeder, T.2    Lewis, R.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.