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Volumn 43, Issue 8, 2004, Pages 865-875

Current views on scorpion toxins specific for K+-channels

Author keywords

Amino acid sequence; Evolution; K+ channel; Scorpion toxin

Indexed keywords

AGITOXIN; BUTANTOXIN; CALCIUM ACTIVATED POTASSIUM CHANNEL; CHARYBDOTOXIN; COBATOXIN; HEFUTOXIN; HONGOTOXIN; IBERIOTOXIN; INSECTOXIN; KALIOTOXIN; LEIUROTOXIN I; LIMBATOTOXIN; MARGATOXIN; MARTENTOXIN; MAUROTOXIN; NEUROTOXIN; NOXIUSTOXIN; PEPTIDE; POTASSIUM CHANNEL; SCORPION VENOM; SLOTOXIN; TAMULUSTOXIN; UNCLASSIFIED DRUG;

EID: 17744406515     PISSN: 00410101     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.toxicon.2004.03.022     Document Type: Review
Times cited : (317)

References (63)
  • 1
    • 0026584910 scopus 로고
    • Scyllatoxin, a blocker of Ca(2+)-activated K+ channels: Structure-function relationships and brain localization of the binding sites
    • Auguste P., Hugues M., Mourre C., Moinier D., Tartar A., Lazdunski M. Scyllatoxin, a blocker of Ca(2+)-activated K+ channels: structure-function relationships and brain localization of the binding sites. Biochemistry. 31:1992;648-654
    • (1992) Biochemistry , vol.31 , pp. 648-654
    • Auguste, P.1    Hugues, M.2    Mourre, C.3    Moinier, D.4    Tartar, A.5    Lazdunski, M.6
  • 2
    • 0034624201 scopus 로고    scopus 로고
    • Tc1, from Tityus cambridgei, is the first member of a new sub-family of scorpion toxin that blocks K+-channels
    • Batista C.V.F., Gómez-Lagunas F., Lucas S., Possani L.D. Tc1, from Tityus cambridgei, is the first member of a new sub-family of scorpion toxin that blocks K+-channels. FEBS Lett. 486:2000;117-120
    • (2000) FEBS Lett. , vol.486 , pp. 117-120
    • Batista, C.V.F.1    Gómez-Lagunas, F.2    Lucas, S.3    Possani, L.D.4
  • 4
    • 0020026499 scopus 로고
    • Selective blockage of voltage-dependent K+ channels by a novel scorpion toxin
    • Carbone E., Wanke E., Prestipino G., Possani L.D., Maelicke A. Selective blockage of voltage-dependent K+ channels by a novel scorpion toxin. Nature. 296:1982;90-91
    • (1982) Nature , vol.296 , pp. 90-91
    • Carbone, E.1    Wanke, E.2    Prestipino, G.3    Possani, L.D.4    Maelicke, A.5
  • 7
    • 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., Ji R. Brownian dynamics simulations of interaction between scorpion toxin Lq2 and potassium ion channel. Biophys. J. 80:2001;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
  • 8
    • 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., Chen K. Brownian dynamics simulations of the recognition of the scorpion toxin P05 with the small-conductance calcium-activated potassium channels. J. Mol. Biol. 318:2002;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    Chen, K.11
  • 10
    • 0027466723 scopus 로고
    • Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion
    • DeBin J.A., Maggio J.E., Strichartz G.R. Purification and characterization of chlorotoxin, a chloride channel ligand from the venom of the scorpion. Am. J. Physiol. 264:1993;C361-C369
    • (1993) Am. J. Physiol. , vol.264
    • Debin, J.A.1    Maggio, J.E.2    Strichartz, G.R.3
  • 11
    • 0033592869 scopus 로고    scopus 로고
    • Pi7, an orphan peptide from the scorpion Pandinus imperator: A 1H-NMR analysis using a nano-NMR probe
    • Delepierre M., Prochnicka-Chalufour A., Boisbouvier J., Possani L.D. Pi7, an orphan peptide from the scorpion Pandinus imperator: a 1H-NMR analysis using a nano-NMR probe. Biochemistry. 38:1999;16756-16765
    • (1999) Biochemistry , vol.38 , pp. 16756-16765
    • Delepierre, M.1    Prochnicka-Chalufour, A.2    Boisbouvier, J.3    Possani, L.D.4
  • 12
    • 0037468668 scopus 로고    scopus 로고
    • BTK-2, a new inhibitor of the Kv1.1 potassium channel purified from Indian scorpion Buthus tamulus
    • Dhawan R., Varshney A., Mathew M.K., Lala A.K. BTK-2, a new inhibitor of the Kv1.1 potassium channel purified from Indian scorpion Buthus tamulus. FEBS Lett. 539:2003;7-13
    • (2003) FEBS Lett. , vol.539 , pp. 7-13
    • Dhawan, R.1    Varshney, A.2    Mathew, M.K.3    Lala, A.K.4
  • 13
    • 0036840108 scopus 로고    scopus 로고
    • Modelling the structure of agitoxin in complex with the Shaker K+ channel: A computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles
    • Eriksson M.A., Roux B. Modelling the structure of agitoxin in complex with the Shaker K+ channel: a computational approach based on experimental distance restraints extracted from thermodynamic mutant cycles. Biophys. J. 83:2002;2595-2609
    • (2002) Biophys. J. , vol.83 , pp. 2595-2609
    • Eriksson, M.A.1    Roux, B.2
  • 14
    • 0035111045 scopus 로고    scopus 로고
    • Synthetic undecapeptide (NTX 10-20) of Noxiustoxin blocks completely the IA current of cerebellum granular cells
    • Frau A., Pisciotta M., Gurrola G., Possani L.D., Prestipiono G. Synthetic undecapeptide (NTX 10-20) of Noxiustoxin blocks completely the IA current of cerebellum granular cells. Eur. Biophys. J. 29:2001;569-573
    • (2001) Eur. Biophys. J. , vol.29 , pp. 569-573
    • Frau, A.1    Pisciotta, M.2    Gurrola, G.3    Possani, L.D.4    Prestipiono, G.5
  • 16
    • 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., Chen K. Brownian dynamics simulations of the recognition of the scorpion toxin maurotoxin with the voltage-gated potassium ion channels. Biophys. J. 83:2002;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    Chen, K.11
  • 17
    • 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., Garcia M.L. Interaction of agitoxin2, charybdotoxin, and iberiotoxin with potassium channels: selectivity between voltage-gated and Maxi-K channels. Proteins. 52:2003;146-154
    • (2003) Proteins , vol.52 , pp. 146-154
    • Gao, Y.D.1    Garcia, M.L.2
  • 19
    • 0035928946 scopus 로고    scopus 로고
    • Slotoxin, alphaKTx1.11, a new scorpion peptide blocker of MaxiK channels that differentiates between alpha and alpha plus beta (beta1 or beta4) complexes
    • Garcia-Valdes J., Zamudio F.Z., Toro L., Possani L.D. Slotoxin, alphaKTx1.11, a new scorpion peptide blocker of MaxiK channels that differentiates between alpha and alpha plus beta (beta1 or beta4) complexes. FEBS Lett. 505:2001;369-373
    • (2001) FEBS Lett. , vol.505 , pp. 369-373
    • Garcia-Valdes, J.1    Zamudio, F.Z.2    Toro, L.3    Possani, L.D.4
  • 20
    • 0036709305 scopus 로고    scopus 로고
    • An overview of toxins and genes from the venom of the Asian scorpion Buthus martensi Karsch
    • Goudet C., Chi C.W., Tytgat J. An overview of toxins and genes from the venom of the Asian scorpion Buthus martensi Karsch. Toxicon. 40:2002;1239-1258
    • (2002) Toxicon , vol.40 , pp. 1239-1258
    • Goudet, C.1    Chi, C.W.2    Tytgat, J.3
  • 23
    • 0035239235 scopus 로고    scopus 로고
    • Twenty years of dendrotoxins
    • Harvey A.L. Twenty years of dendrotoxins. Toxicon. 39:2001;15-26
    • (2001) Toxicon , vol.39 , pp. 15-26
    • Harvey, A.L.1
  • 24
    • 0038054249 scopus 로고    scopus 로고
    • Evidence for function-specific mutation in the neurotoxin, parabutoxin 3
    • Huys I., Tytgat J. Evidence for function-specific mutation in the neurotoxin, parabutoxin 3. Eur. J. Neurosci. 17:2003;1786-1792
    • (2003) Eur. J. Neurosci. , vol.17 , pp. 1786-1792
    • Huys, I.1    Tytgat, J.2
  • 26
    • 1642546220 scopus 로고    scopus 로고
    • BmTx3, a scorpion toxin with two putative functional faces separately active on A-type K+ and HERG currents
    • Huys I., Xu C.Q., Wang C.Z., Vacher H., Martin-Eauclaire M.F., Chi C.W., Tytgat J. BmTx3, a scorpion toxin with two putative functional faces separately active on A-type K+ and HERG currents. Biochem. J. 378:2004;745-752
    • (2004) Biochem. J. , vol.378 , pp. 745-752
    • Huys, I.1    Xu, C.Q.2    Wang, C.Z.3    Vacher, H.4    Martin-Eauclaire, M.F.5    Chi, C.W.6    Tytgat, J.7
  • 28
    • 0029881007 scopus 로고    scopus 로고
    • MOLMOL: A program for display and analysis of macromolecular structures
    • Koradi R., Billeter M., Wüthrich K. MOLMOL: a program for display and analysis of macromolecular structures. J. Mol. Graphics. 14:1996;51-55
    • (1996) J. Mol. Graphics , vol.14 , pp. 51-55
    • Koradi, R.1    Billeter, M.2    Wüthrich, K.3
  • 33
    • 0345055320 scopus 로고    scopus 로고
    • Evidence for a new class of scorpion toxins active against K+ channels
    • Legros C., Céard B., Bougis P.E., Martin-Eauclaire M.-F. Evidence for a new class of scorpion toxins active against K+ channels. FEBS Lett. 431:1998;375-380
    • (1998) FEBS Lett. , vol.431 , pp. 375-380
    • Legros, C.1    Céard, B.2    Bougis, P.E.3    Martin-Eauclaire, M.-F.4
  • 34
    • 0036845677 scopus 로고    scopus 로고
    • Structural and functional role of the extracellular s5-p linker in the HERG potassium channel
    • Liu J., Zhang M., Jiang M., Tseng G.N. Structural and functional role of the extracellular s5-p linker in the HERG potassium channel. J. Gen. Physiol. 120:2002;723-737
    • (2002) J. Gen. Physiol. , vol.120 , pp. 723-737
    • Liu, J.1    Zhang, M.2    Jiang, M.3    Tseng, G.N.4
  • 35
    • 0242657337 scopus 로고    scopus 로고
    • Potassium channels
    • MacKinnon R. Potassium channels. FEBS Lett. 55:2004;62-65
    • (2004) FEBS Lett. , vol.55 , pp. 62-65
    • MacKinnon, R.1
  • 36
    • 0032478696 scopus 로고    scopus 로고
    • Structural conservation in prokaryotic and eukaryotic potassium channels
    • MacKinnon R., Cohen S.L., Kuo A., Lee A., Chait B.T. Structural conservation in prokaryotic and eukaryotic potassium channels. Science. 280:1998;106-109
    • (1998) Science , vol.280 , pp. 106-109
    • MacKinnon, R.1    Cohen, S.L.2    Kuo, A.3    Lee, A.4    Chait, B.T.5
  • 37
  • 40
    • 0343671345 scopus 로고    scopus 로고
    • Functional architectures of animal toxins: A clue to drug design?
    • Menez A. Functional architectures of animal toxins: a clue to drug design? Toxicon. 36:1998;1557-1572
    • (1998) Toxicon , vol.36 , pp. 1557-1572
    • Menez, A.1
  • 41
    • 0028983387 scopus 로고
    • The Charybdotoxin family of K+ channel-blocking peptides
    • Miller C. The Charybdotoxin family of K+ channel-blocking peptides. Neuron. 15:1995;5-10
    • (1995) Neuron , vol.15 , pp. 5-10
    • Miller, C.1
  • 42
    • 33747646924 scopus 로고    scopus 로고
    • An overview of the potassium channel family
    • reviews 0004
    • Miller C. An overview of the potassium channel family. Genome Biol. 1:2000;. reviews 0004
    • (2000) Genome Biol. , vol.1
    • Miller, C.1
  • 43
    • 0021918550 scopus 로고
    • Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle
    • Miller C., Moczydlowski E., Latorre R., Phillips M. Charybdotoxin, a protein inhibitor of single Ca2+-activated K+ channels from mammalian skeletal muscle. Nature. 313:1985;316-318
    • (1985) Nature , vol.313 , pp. 316-318
    • Miller, C.1    Moczydlowski, E.2    Latorre, R.3    Phillips, M.4
  • 44
    • 1642453564 scopus 로고    scopus 로고
    • The 'functional' dyad of scorpion toxin Pi1 is not a prerequisite for toxin binding to the voltage-gated KV1.2 potassium channels
    • Mouhat S., Mosbah A., Visan V., Wulff H., Delepierre M., Dabon H., Grissmer S., De Waard M., Sabatier J.-M. The 'functional' dyad of scorpion toxin Pi1 is not a prerequisite for toxin binding to the voltage-gated KV1.2 potassium channels. Biochem. J. 377:2004;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    Dabon, H.6    Grissmer, S.7    De Waard, M.8    Sabatier, J.-M.9
  • 45
    • 0035998345 scopus 로고    scopus 로고
    • A short-chain peptide toxin isolated from Centruroides sculpturatus scorpion venom inhibits ether-ago-go-related gene K(+) channels
    • Nastainczyk W., Meves H., Watt D.D. A short-chain peptide toxin isolated from Centruroides sculpturatus scorpion venom inhibits ether-ago-go-related gene K(+) channels. Toxicon. 40:2002;1053-1058
    • (2002) Toxicon , vol.40 , pp. 1053-1058
    • Nastainczyk, W.1    Meves, H.2    Watt, D.D.3
  • 46
    • 0037053276 scopus 로고    scopus 로고
    • Mapping the binding site of a HERG-specific peptide toxin (ErgTx) to the channel's outer vestibule
    • Pardo-López L., Zhang M., Liu J., Jiang M., Possani L.D., Tseng G.N. Mapping the binding site of a HERG-specific peptide toxin (ErgTx) to the channel's outer vestibule. J. Biol. Chem. 277:2002;16403-16411
    • (2002) J. Biol. Chem. , vol.277 , pp. 16403-16411
    • Pardo-López, L.1    Zhang, M.2    Liu, J.3    Jiang, M.4    Possani, L.D.5    Tseng, G.N.6
  • 47
    • 0037195936 scopus 로고    scopus 로고
    • Tamapin, a venom peptide from the Indian red scorpion (Mesobuthus tamulus) that targets small conductance Ca2+-activated K+ channels and after hyperpolarization currents in central neurons
    • Pedarzani P., D'hoedt D., Doorty K.B., Wadsworth J.D., Joseph J.S., Jeyaseelan K., Kini R.M., Gadre S.V., Sapatnekar S.M., Stocker M., Strong P.N. Tamapin, a venom peptide from the Indian red scorpion (Mesobuthus tamulus) that targets small conductance Ca2+-activated K+ channels and after hyperpolarization currents in central neurons. J. Biol. Chem. 277:2002;46101-46109
    • (2002) J. Biol. Chem. , vol.277 , pp. 46101-46109
    • Pedarzani, P.1    D'Hoedt, D.2    Doorty, K.B.3    Wadsworth, J.D.4    Joseph, J.S.5    Jeyaseelan, K.6    Kini, R.M.7    Gadre, S.V.8    Sapatnekar, S.M.9    Stocker, M.10    Strong, P.N.11
  • 49
    • 0034730474 scopus 로고    scopus 로고
    • Fast K+ currents from cerebellum granular cells are completely blocked by a peptide purified from Androctonus australis Garzoni scorpion venom
    • Pisciotta M., Coronas F.I., Bloch C., Prestipino G., Possani L.D. Fast K+ currents from cerebellum granular cells are completely blocked by a peptide purified from Androctonus australis Garzoni scorpion venom. Biochim. Biophys. Acta. 1468:2000;203-212
    • (2000) Biochim. Biophys. Acta , vol.1468 , pp. 203-212
    • Pisciotta, M.1    Coronas, F.I.2    Bloch, C.3    Prestipino, G.4    Possani, L.D.5
  • 50
    • 51849183464 scopus 로고
    • The primary structure of Noxiustoxin: A K+ channel blocking peptide from the venom of the scorpion Centruroides noxius Hoffmann
    • Possani L.D., Martin B., Svendsen I. The primary structure of Noxiustoxin: a K+ channel blocking peptide from the venom of the scorpion Centruroides noxius Hoffmann. Carlsberg Res. Commun. 47:1982;285-289
    • (1982) Carlsberg Res. Commun. , vol.47 , pp. 285-289
    • Possani, L.D.1    Martin, B.2    Svendsen, I.3
  • 51
    • 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., Becerril B. Peptides and genes coding for scorpion toxins that affect ion-channels. Biochimie. 82:2000;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
  • 55
    • 0242458492 scopus 로고    scopus 로고
    • Structural basis of the KcsA K+ channel and Agitoxin2 pore-blocking toxin interaction by using the transferred cross-saturation method
    • Takeuchi K., Yokogawa M., Matsuda T., Sugai M., Kawano S., Kohno T., Nakamura H., Takahashi H., Shimada S. Structural basis of the KcsA K+ channel and Agitoxin2 pore-blocking toxin interaction by using the transferred cross-saturation method. Structure. 11:2003;1381-1392
    • (2003) Structure , vol.11 , pp. 1381-1392
    • Takeuchi, K.1    Yokogawa, M.2    Matsuda, T.3    Sugai, M.4    Kawano, S.5    Kohno, T.6    Nakamura, H.7    Takahashi, H.8    Shimada, S.9
  • 56
    • 0031574072 scopus 로고    scopus 로고
    • The CLUSTAL_X windows interface: Flexible strategies for multiple sequence alignment aided by quality analysis tools
    • Thompson J.D., Gibson T.J., Plewniak F., Jeanmougin F., Higgins D.G. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res. 25:1997;4876-4882
    • (1997) Nucleic Acids Res. , vol.25 , pp. 4876-4882
    • Thompson, J.D.1    Gibson, T.J.2    Plewniak, F.3    Jeanmougin, F.4    Higgins, D.G.5
  • 57
    • 0034733876 scopus 로고    scopus 로고
    • The blocking effect of BmP02, one novel short-chain peptide on transient outward K+ channel of adult rat ventricular myocyte
    • Tong Q.-C., Zhang Y., Li D.-P., Zhou Z.-N., Ji Y.-H. The blocking effect of BmP02, one novel short-chain peptide on transient outward K+ channel of adult rat ventricular myocyte. Peptides. 90:2000;85-92
    • (2000) Peptides , vol.90 , pp. 85-92
    • Tong, Q.-C.1    Zhang, Y.2    Li, D.-P.3    Zhou, Z.-N.4    Ji, Y.-H.5
  • 59
    • 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., Chi C.W. Gene expression, mutation, and structure-function relationship of scorpion toxin BmP05 active on SK(Ca) channels. Biochemistry. 41:2002;2844-2849
    • (2002) Biochemistry , vol.41 , pp. 2844-2849
    • Wu, J.J.1    He, L.L.2    Zhou, Z.3    Chi, C.W.4
  • 60
    • 0042880941 scopus 로고    scopus 로고
    • Turret and pore block of K+ channels: What is the difference?
    • Xu C.Q., Zhu S.Y., Chi C.W., Tytgat J. Turret and pore block of K+ channels: what is the difference? Trends Pharmacol. Sci. 24:2003;446-448
    • (2003) Trends Pharmacol. Sci. , vol.24 , pp. 446-448
    • Xu, C.Q.1    Zhu, S.Y.2    Chi, C.W.3    Tytgat, J.4
  • 61
    • 0038523849 scopus 로고    scopus 로고
    • BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1
    • Zhang M., Korolkova Y.V., Liu J., Jiang M., Grishin E.V., Tseng G.N. BeKm-1 is a HERG-specific toxin that shares the structure with ChTx but the mechanism of action with ErgTx1. Biophys. J. 84:2003;3022-3036
    • (2003) Biophys. J. , vol.84 , pp. 3022-3036
    • Zhang, M.1    Korolkova, Y.V.2    Liu, J.3    Jiang, M.4    Grishin, E.V.5    Tseng, G.N.6
  • 62
    • 0032883778 scopus 로고    scopus 로고
    • Molecular cloning and sequencing of two 'short chain' and two 'long chain' K(+) channel-blocking peptides from the Chinese scorpion Buthus martensii Karsch
    • Zhu S., Li W., Zeng X., Jiang D., Mao X., Liu H. Molecular cloning and sequencing of two 'short chain' and two 'long chain' K(+) channel-blocking peptides from the Chinese scorpion Buthus martensii Karsch. FEBS Lett. 457:1999;509-514
    • (1999) FEBS Lett. , vol.457 , pp. 509-514
    • Zhu, S.1    Li, W.2    Zeng, X.3    Jiang, D.4    Mao, X.5    Liu, H.6
  • 63
    • 0346458799 scopus 로고    scopus 로고
    • Evolutionary trace analysis of scorpion toxins specific for K-channels
    • Zhu S., Huys I., Dyason K., Verdonck F., Tytgat J. Evolutionary trace analysis of scorpion toxins specific for K-channels. Proteins. 54:2004;361-370
    • (2004) Proteins , vol.54 , pp. 361-370
    • Zhu, S.1    Huys, I.2    Dyason, K.3    Verdonck, F.4    Tytgat, J.5


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.