메뉴 건너뛰기




Volumn 51, Issue 19, 2012, Pages 4049-4061

Structure, function, and chemical synthesis of Vaejovis mexicanus peptide 24: A novel potent blocker of Kv1.3 potassium channels of human T lymphocytes

Author keywords

[No Author keywords available]

Indexed keywords

CHANNEL BLOCKERS; CHEMICAL SYNTHESIS; DISULFIDE BRIDGE; HUMAN LYMPHOCYTES; HUMAN T LYMPHOCYTES; ION CHANNEL; POTASSIUM CHANNELS; PROTEOMIC ANALYSIS; SEQUENCE ANALYSIS; STRUCTURAL FEATURE; THREE-DIMENSIONAL SOLUTIONS;

EID: 84861164829     PISSN: 00062960     EISSN: 15204995     Source Type: Journal    
DOI: 10.1021/bi300060n     Document Type: Article
Times cited : (52)

References (70)
  • 1
    • 70349162817 scopus 로고    scopus 로고
    • The functional network of ion channels in T lymphocytes
    • Cahalan, M. D. and Chandy, K. G. (2009) The functional network of ion channels in T lymphocytes Immunol. Rev. 231, 59-87
    • (2009) Immunol. Rev. , vol.231 , pp. 59-87
    • Cahalan, M.D.1    Chandy, K.G.2
  • 5
    • 0028983387 scopus 로고
    • +-channel-blocking peptides
    • +-channel- blocking peptides Neuron 15, 5-10
    • (1995) Neuron , vol.15 , pp. 5-10
    • Miller, C.1
  • 7
    • 84863779195 scopus 로고    scopus 로고
    • The UniProtKB/Swiss-Prot Tox-Prot program: A central hub of integrated venom protein data
    • Jungo, F., Bougueleret, L., Xenarios, I., and Poux, S. (2012) The UniProtKB/Swiss-Prot Tox-Prot program: A central hub of integrated venom protein data Toxicon DOI 10.1016/j.toxicon.2012.03.10
    • (2012) Toxicon
    • Jungo, F.1    Bougueleret, L.2    Xenarios, I.3    Poux, S.4
  • 8
    • 2942691708 scopus 로고    scopus 로고
    • Molecular basis of α-KTx specificity
    • Giangiacomo, K. M., Ceralde, Y., and Mullmann, T. J. (2004) Molecular basis of α-KTx specificity Toxicon 43, 877-886
    • (2004) Toxicon , vol.43 , pp. 877-886
    • Giangiacomo, K.M.1    Ceralde, Y.2    Mullmann, T.J.3
  • 10
    • 49649113677 scopus 로고    scopus 로고
    • Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease
    • Han, S., Yi, H., Yin, S. J., Chen, Z. Y., Liu, H., Cao, Z. J., Wu, Y. L., and Li, W. X. (2008) Structural basis of a potent peptide inhibitor designed for Kv1.3 channel, a therapeutic target of autoimmune disease J. Biol. Chem. 283, 19058-19065
    • (2008) J. Biol. Chem. , vol.283 , pp. 19058-19065
    • Han, S.1    Yi, H.2    Yin, S.J.3    Chen, Z.Y.4    Liu, H.5    Cao, Z.J.6    Wu, Y.L.7    Li, W.X.8
  • 19
    • 0034849408 scopus 로고    scopus 로고
    • MRBAYES: Bayesian inference of phylogenetic trees
    • Huelsenbeck, J. P. and Ronquist, F. (2001) MRBAYES: Bayesian inference of phylogenetic trees Bioinformatics 17, 754-755
    • (2001) Bioinformatics , vol.17 , pp. 754-755
    • Huelsenbeck, J.P.1    Ronquist, F.2
  • 20
    • 0041386108 scopus 로고    scopus 로고
    • MrBayes 3: Bayesian phylogenetic inference under mixed models
    • Ronquist, F. and Huelsenbeck, J. P. (2003) MrBayes 3: Bayesian phylogenetic inference under mixed models Bioinformatics 19, 1572-1574
    • (2003) Bioinformatics , vol.19 , pp. 1572-1574
    • Ronquist, F.1    Huelsenbeck, J.P.2
  • 21
    • 0019627519 scopus 로고
    • Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction
    • Sarin, V. K., Kent, S. B., Tam, J. P., and Merrifield, R. B. (1981) Quantitative monitoring of solid-phase peptide synthesis by the ninhydrin reaction Anal. Biochem. 117, 147-157
    • (1981) Anal. Biochem. , vol.117 , pp. 147-157
    • Sarin, V.K.1    Kent, S.B.2    Tam, J.P.3    Merrifield, R.B.4
  • 22
    • 0025103048 scopus 로고
    • A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis
    • King, D. S., Fields, C. G., and Fields, G. B. (1990) A cleavage method which minimizes side reactions following Fmoc solid phase peptide synthesis Int. J. Pept. Protein Res. 36, 255-266
    • (1990) Int. J. Pept. Protein Res. , vol.36 , pp. 255-266
    • King, D.S.1    Fields, C.G.2    Fields, G.B.3
  • 23
    • 0029400480 scopus 로고
    • NMRPIPE: A multidimensional spectral processing system based on UNIX pipes
    • Delaglio, F., Grzesiek, S., Vuister, G. W., Zhu, G., Pfeifer, J., and Bax, A. (1995) NMRPIPE: A multidimensional spectral processing system based on UNIX pipes J. Biomol. NMR 6, 277-293
    • (1995) J. Biomol. NMR , vol.6 , pp. 277-293
    • Delaglio, F.1    Grzesiek, S.2    Vuister, G.W.3    Zhu, G.4    Pfeifer, J.5    Bax, A.6
  • 24
    • 0343459675 scopus 로고
    • The program XEASY for computer-supported NMR spectral analysis of biological macromolecules
    • Bartels, C., Xia, T., Billeter, M., Guntert, P., and Wutrich, 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.2    Billeter, M.3    Guntert, P.4    Wutrich, K.5
  • 25
    • 0020475326 scopus 로고
    • 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor
    • 1H nuclear magnetic resonance spectra. Basic pancreatic trypsin inhibitor J. Mol. Biol. 155, 347-366
    • (1982) J. Mol. Biol. , vol.155 , pp. 347-366
    • Wagner, G.1    Wuthrich, K.2
  • 26
    • 0005963761 scopus 로고
    • Multiple quantum filters for elucidating NMR coupling networks
    • Piantini, U., Sorensen, O. W., and Ernst, R. R. (1982) Multiple quantum filters for elucidating NMR coupling networks J. Am. Chem. Soc. 104, 6800-6801
    • (1982) J. Am. Chem. Soc. , vol.104 , pp. 6800-6801
    • Piantini, U.1    Sorensen, O.W.2    Ernst, R.R.3
  • 27
    • 0344448273 scopus 로고
    • Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy
    • Braunschweiler, L. and Ernst, R. R. (1983) Coherence transfer by isotropic mixing: Application to proton correlation spectroscopy J. Magn. Reson. 53, 521-528
    • (1983) J. Magn. Reson. , vol.53 , pp. 521-528
    • Braunschweiler, L.1    Ernst, R.R.2
  • 28
    • 0343359244 scopus 로고
    • Investigation of exchange processes by two-dimensional NMR spectroscopy
    • Jeener, J., Meier, M. H., Bachmann, P., and Ernst, R. R. (1979) Investigation of exchange processes by two-dimensional NMR spectroscopy J. Chem. Phys. 71, 4546-4553
    • (1979) J. Chem. Phys. , vol.71 , pp. 4546-4553
    • Jeener, J.1    Meier, M.H.2    Bachmann, P.3    Ernst, R.R.4
  • 29
    • 0031576336 scopus 로고    scopus 로고
    • Torsion angle dynamics for NMR structure calculation with the new program DYANA
    • Guntert, P., Mumenthaler, C., and Wuthrich, K. (1997) Torsion angle dynamics for NMR structure calculation with the new program DYANA J. Mol. Biol. 273, 283-298
    • (1997) J. Mol. Biol. , vol.273 , pp. 283-298
    • Guntert, P.1    Mumenthaler, C.2    Wuthrich, K.3
  • 30
    • 0036873589 scopus 로고    scopus 로고
    • Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS
    • Herrmann, T., Guntert, P., and Wuthrich, K. (2002) Protein NMR structure determination with automated NOE-identification in the NOESY spectra using the new software ATNOS J. Biomol. NMR 24, 171-189
    • (2002) J. Biomol. NMR , vol.24 , pp. 171-189
    • Herrmann, T.1    Guntert, P.2    Wuthrich, K.3
  • 32
    • 33748518255 scopus 로고    scopus 로고
    • Comparison of multiple Amber force fields and development of improved protein backbone parameters
    • Hornak, V., Abel, R., Okur, A., Strockbine, B., Roitberg, A., and Simmerling, C. (2006) Comparison of multiple Amber force fields and development of improved protein backbone parameters Proteins 65, 712-725
    • (2006) Proteins , vol.65 , pp. 712-725
    • Hornak, V.1    Abel, R.2    Okur, A.3    Strockbine, B.4    Roitberg, A.5    Simmerling, C.6
  • 33
    • 0036234027 scopus 로고    scopus 로고
    • Comparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model, and with explicit water
    • Xia, B., Tsui, V., Case, D. A., Dyson, H. J., and Wright, P. E. (2002) Comparison of protein solution structures refined by molecular dynamics simulation in vacuum, with a generalized Born model, and with explicit water J. Biomol. NMR 22, 317-331
    • (2002) J. Biomol. NMR , vol.22 , pp. 317-331
    • Xia, B.1    Tsui, V.2    Case, D.A.3    Dyson, H.J.4    Wright, P.E.5
  • 34
    • 0022555607 scopus 로고
    • Voltage-gated potassium conductance in human T lymphocytes stimulated with phorbol ester
    • Deutsch, C., Krause, D., and Lee, S. C. (1986) Voltage-gated potassium conductance in human T lymphocytes stimulated with phorbol ester J. Physiol. 372, 405-423
    • (1986) J. Physiol. , vol.372 , pp. 405-423
    • Deutsch, C.1    Krause, D.2    Lee, S.C.3
  • 35
    • 0021260968 scopus 로고
    • K channels in T lymphocytes: A patch clamp study using monoclonal antibody adhesion
    • Matteson, D. R. and Deutsch, C. (1984) K channels in T lymphocytes: A patch clamp study using monoclonal antibody adhesion Nature 307, 468-471
    • (1984) Nature , vol.307 , pp. 468-471
    • Matteson, D.R.1    Deutsch, C.2
  • 36
    • 0019441262 scopus 로고
    • Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches
    • Hamill, O. P., Marty, A., Neher, E., Sakmann, B., and Sigworth, F. J. (1981) Improved patch-clamp techniques for high-resolution current recording from cells and cell-free membrane patches Pfluegers Arch. 391, 85-100
    • (1981) Pfluegers Arch. , vol.391 , pp. 85-100
    • Hamill, O.P.1    Marty, A.2    Neher, E.3    Sakmann, B.4    Sigworth, F.J.5
  • 37
    • 38849092210 scopus 로고    scopus 로고
    • A note on difficult structure alignment problems
    • Sippl, M. J. and Wiederstein, M. (2008) A note on difficult structure alignment problems Bioinformatics 24, 426-427
    • (2008) Bioinformatics , vol.24 , pp. 426-427
    • Sippl, M.J.1    Wiederstein, M.2
  • 38
    • 58149377754 scopus 로고    scopus 로고
    • Different residues in channel turret determining the selectivity of ADWX-1 inhibitor peptide between Kv1.1 and Kv1.3 channels
    • Yin, S. J., Jiang, L., Yi, H., Han, S., Yang, D. W., Liu, M. L., Liu, H., Cao, Z. J., Wu, Y. L., and Li, W. X. (2008) Different residues in channel turret determining the selectivity of ADWX-1 inhibitor peptide between Kv1.1 and Kv1.3 channels J. Proteome Res. 7, 4890-4897
    • (2008) J. Proteome Res. , vol.7 , pp. 4890-4897
    • Yin, S.J.1    Jiang, L.2    Yi, H.3    Han, S.4    Yang, D.W.5    Liu, M.L.6    Liu, H.7    Cao, Z.J.8    Wu, Y.L.9    Li, W.X.10
  • 39
    • 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
  • 40
    • 48449105393 scopus 로고    scopus 로고
    • The RosettaDock server for local protein-protein docking
    • Lyskov, S. and Gray, J. J. (2008) The RosettaDock server for local protein-protein docking Nucleic Acids Res. 36, W233-W238
    • (2008) Nucleic Acids Res. , vol.36
    • Lyskov, S.1    Gray, J.J.2
  • 41
    • 77954895219 scopus 로고    scopus 로고
    • Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement
    • Chen, X., Wang, Q., Ni, F., and Ma, J. (2010) Structure of the full-length Shaker potassium channel Kv1.2 by normal-mode-based X-ray crystallographic refinement Proc. Natl. Acad. Sci. U.S.A. 107, 11352-11357
    • (2010) Proc. Natl. Acad. Sci. U.S.A. , vol.107 , pp. 11352-11357
    • Chen, X.1    Wang, Q.2    Ni, F.3    Ma, J.4
  • 43
    • 34548232365 scopus 로고    scopus 로고
    • Inference of macromolecular assemblies from crystalline state
    • Krissinel, E. and Henrick, K. (2007) Inference of macromolecular assemblies from crystalline state J. Mol. Biol. 372, 774-797
    • (2007) J. Mol. Biol. , vol.372 , pp. 774-797
    • Krissinel, E.1    Henrick, K.2
  • 46
    • 0038161052 scopus 로고    scopus 로고
    • Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations
    • Gray, J. J., Moughon, S., Wang, C., Schueler-Furman, O., Kuhlman, B., Rohl, C. A., and Baker, D. (2003) Protein-protein docking with simultaneous optimization of rigid-body displacement and side-chain conformations J. Mol. Biol. 331, 281-299
    • (2003) J. Mol. Biol. , vol.331 , pp. 281-299
    • Gray, J.J.1    Moughon, S.2    Wang, C.3    Schueler-Furman, O.4    Kuhlman, B.5    Rohl, C.A.6    Baker, D.7
  • 47
    • 28544434796 scopus 로고    scopus 로고
    • Nuclear magnetic resonance structural studies of a potassium channel-Charybdotoxin complex
    • Yu, L., Sun, C., Song, D., Shen, J., Xu, N., Gunasekera, A., Hajduk, P. J., and Olejniczak, E. T. (2005) Nuclear magnetic resonance structural studies of a potassium channel-Charybdotoxin complex Biochemistry 44, 15834-15841
    • (2005) Biochemistry , vol.44 , pp. 15834-15841
    • Yu, L.1    Sun, C.2    Song, D.3    Shen, J.4    Xu, N.5    Gunasekera, A.6    Hajduk, P.J.7    Olejniczak, E.T.8
  • 49
    • 33745484721 scopus 로고    scopus 로고
    • Moving pieces in a taxonomic puzzle: Venom 2D-LC/MS and data clustering analyses to infer phylogenetic relationships in some scorpions from the Buthidae family (Scorpiones)
    • Nascimento, D. G., Rates, B., Santos, D. M., Verano-Braga, T., Barbosa-Silva, A., Dutra, A. A., Biondi, I., Martin-Eauclaire, M. F., De Lima, M. E., and Pimenta, A. M. (2006) Moving pieces in a taxonomic puzzle: Venom 2D-LC/MS and data clustering analyses to infer phylogenetic relationships in some scorpions from the Buthidae family (Scorpiones) Toxicon 47, 628-639
    • (2006) Toxicon , vol.47 , pp. 628-639
    • Nascimento, D.G.1    Rates, B.2    Santos, D.M.3    Verano-Braga, T.4    Barbosa-Silva, A.5    Dutra, A.A.6    Biondi, I.7    Martin-Eauclaire, M.F.8    De Lima, M.E.9    Pimenta, A.M.10
  • 56
    • 14044270108 scopus 로고    scopus 로고
    • Contribution of the functional dyad of animal toxins acting on voltage-gated Kv1-type channels
    • Mouhat, S., De Waard, M., and Sabatier, J. M. (2005) Contribution of the functional dyad of animal toxins acting on voltage-gated Kv1-type channels J. Pept. Sci. 11, 65-68
    • (2005) J. Pept. Sci. , vol.11 , pp. 65-68
    • Mouhat, S.1    De Waard, M.2    Sabatier, J.M.3
  • 58
    • 6944247603 scopus 로고    scopus 로고
    • Mapping of maurotoxin binding sites on hKv1.2, hKv1.3, and hIKCa1 channels
    • Visan, V., Fajloun, Z., Sabatier, J. M., and Grissmer, S. (2004) Mapping of maurotoxin binding sites on hKv1.2, hKv1.3, and hIKCa1 channels Mol. Pharmacol. 66, 1103-1112
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1103-1112
    • Visan, V.1    Fajloun, Z.2    Sabatier, J.M.3    Grissmer, S.4
  • 59
    • 0346458799 scopus 로고    scopus 로고
    • Evolutionary trace analysis of scorpion toxins specific for K-channels
    • Zhu, S., Huys, I., Dyason, K., Verdonck, F., and Tytgat, J. (2004) Evolutionary trace analysis of scorpion toxins specific for K-channels Proteins 54, 361-370
    • (2004) Proteins , vol.54 , pp. 361-370
    • Zhu, S.1    Huys, I.2    Dyason, K.3    Verdonck, F.4    Tytgat, J.5
  • 61
    • 22844448219 scopus 로고    scopus 로고
    • A variable residue in the pore of Kv1 channels is critical for the high affinity of blockers from sea anemones and scorpions
    • Gilquin, B., Braud, S., Eriksson, M. A., Roux, B., Bailey, T. D., Priest, B. T., Garcia, M. L., Ménez, A., and Gasparini, S. (2005) A variable residue in the pore of Kv1 channels is critical for the high affinity of blockers from sea anemones and scorpions J. Biol. Chem. 280, 27093-27102
    • (2005) J. Biol. Chem. , vol.280 , pp. 27093-27102
    • Gilquin, B.1    Braud, S.2    Eriksson, M.A.3    Roux, B.4    Bailey, T.D.5    Priest, B.T.6    Garcia, M.L.7    Ménez, A.8    Gasparini, S.9
  • 62
    • 0037999227 scopus 로고    scopus 로고
    • Interaction of Agitoxin2, Charybdotoxin, and Iberiotoxin with potassium channels: Selectivity between voltage-gated and maxi-K channels
    • Gao, Y. D. and Garcia, M. L. (2003) Interaction of Agitoxin2, Charybdotoxin, and Iberiotoxin with potassium channels: Selectivity between voltage-gated and maxi-K channels Proteins 52, 146-154
    • (2003) Proteins , vol.52 , pp. 146-154
    • Gao, Y.D.1    Garcia, M.L.2
  • 63
    • 0036840108 scopus 로고    scopus 로고
    • + channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles
    • + channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles Biophys. J. 83, 2595-2609
    • (2002) Biophys. J. , vol.83 , pp. 2595-2609
    • Eriksson, M.A.1    Roux, B.2
  • 64
    • 34248143507 scopus 로고    scopus 로고
    • Revealing the molecular determinants of neurotoxin specificity for calcium-activated versus voltage-dependent potassium channels
    • Giangiacomo, K. M., Becker, J., Garsky, C., Felix, J. P., Priest, B. T., Schmalhofer, W., Garcia, M. L., and Mullmann, T. J. (2007) Revealing the molecular determinants of neurotoxin specificity for calcium-activated versus voltage-dependent potassium channels Biochemistry 46, 5358-5364
    • (2007) Biochemistry , vol.46 , pp. 5358-5364
    • Giangiacomo, K.M.1    Becker, J.2    Garsky, C.3    Felix, J.P.4    Priest, B.T.5    Schmalhofer, W.6    Garcia, M.L.7    Mullmann, T.J.8
  • 65
    • 80053431062 scopus 로고    scopus 로고
    • Charybdotoxin unbinding from the mKv1.3 potassium channel: A combined computational and experimental study
    • Khabiri, M., Nikouee, A., Cwiklik, L., Grissmer, S., and Ettrich, R. (2011) Charybdotoxin unbinding from the mKv1.3 potassium channel: A combined computational and experimental study J. Phys. Chem. B 115, 11490-11500
    • (2011) J. Phys. Chem. B , vol.115 , pp. 11490-11500
    • Khabiri, M.1    Nikouee, A.2    Cwiklik, L.3    Grissmer, S.4    Ettrich, R.5
  • 66
    • 2942677403 scopus 로고    scopus 로고
    • Computational simulations of interactions of scorpion toxins with the voltage-gated potassium ion channel
    • Yu, K., Fu, W., Liu, H., Luo, X., Chen, K. X., Ding, J., Shen, J., and Jiang, H. (2004) Computational simulations of interactions of scorpion toxins with the voltage-gated potassium ion channel Biophys. J. 86, 3542-3555
    • (2004) Biophys. J. , vol.86 , pp. 3542-3555
    • Yu, K.1    Fu, W.2    Liu, H.3    Luo, X.4    Chen, K.X.5    Ding, J.6    Shen, J.7    Jiang, H.8
  • 67
    • 33645858263 scopus 로고    scopus 로고
    • Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR
    • Lange, A., Giller, K., Hornig, S., Martin-Eauclaire, M. F., Pongs, O., Becker, S., and Baldus, M. (2006) Toxin-induced conformational changes in a potassium channel revealed by solid-state NMR Nature 440, 959-962
    • (2006) Nature , vol.440 , pp. 959-962
    • Lange, A.1    Giller, K.2    Hornig, S.3    Martin-Eauclaire, M.F.4    Pongs, O.5    Becker, S.6    Baldus, M.7
  • 68
    • 84863393842 scopus 로고    scopus 로고
    • Developing a comparative docking protocol for the prediction of peptide selectivity profiles: Investigation of potassium channel toxins
    • Chen, P.-C. and Kuyucak, S. (2012) Developing a comparative docking protocol for the prediction of peptide selectivity profiles: Investigation of potassium channel toxins Toxins 4, 110-138
    • (2012) Toxins , vol.4 , pp. 110-138
    • Chen, P.-C.1    Kuyucak, S.2
  • 69
    • 6944247603 scopus 로고    scopus 로고
    • Mapping of maurotoxin binding sites on hKv1.2, hKv1.3, and hIKCa1 channels
    • Visan, V., Fajloun, Z., Sabatier, J. M., and Grissmer, S. (2004) Mapping of maurotoxin binding sites on hKv1.2, hKv1.3, and hIKCa1 channels Mol. Pharmacol. 66, 1103-1112
    • (2004) Mol. Pharmacol. , vol.66 , pp. 1103-1112
    • Visan, V.1    Fajloun, Z.2    Sabatier, J.M.3    Grissmer, S.4
  • 70
    • 0033406644 scopus 로고    scopus 로고
    • Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: Solution structure of the potassium channel inhibitor HsTX1
    • Savarin, P., Romi-Lebrun, R., Zinn-Justin, S., Lebrun, B., Nakajima, T., Gilquin, B., and Menez, A. (1999) Structural and functional consequences of the presence of a fourth disulfide bridge in the scorpion short toxins: Solution structure of the potassium channel inhibitor HsTX1 Protein Sci. 8, 2672-2685
    • (1999) Protein Sci. , vol.8 , pp. 2672-2685
    • Savarin, P.1    Romi-Lebrun, R.2    Zinn-Justin, S.3    Lebrun, B.4    Nakajima, T.5    Gilquin, B.6    Menez, A.7


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.