메뉴 건너뛰기




Volumn 1818, Issue 2, 2012, Pages 286-293

Water wires in atomistic models of the Hv1 proton channel

Author keywords

Membrane proteins; Molecular dynamics simulations; Voltage gated ion channels; Voltage sensing domains

Indexed keywords

VOLTAGE GATED POTASSIUM CHANNEL; WATER;

EID: 84855438589     PISSN: 00052736     EISSN: 18792642     Source Type: Journal    
DOI: 10.1016/j.bbamem.2011.07.045     Document Type: Article
Times cited : (59)

References (69)
  • 1
    • 33646229810 scopus 로고    scopus 로고
    • A voltage-sensor domain protein is a voltage-gated proton channel
    • M. Sasaki, M. Takagi, and Y. Okamura A voltage-sensor domain protein is a voltage-gated proton channel Science 312 2006 589 592
    • (2006) Science , vol.312 , pp. 589-592
    • Sasaki, M.1    Takagi, M.2    Okamura, Y.3
  • 2
    • 33646358260 scopus 로고    scopus 로고
    • A voltage-gated proton-selective channel lacking the pore domain
    • I.S. Ramsey, M.M. Moran, J.A. Chong, and D.E. Clapham A voltage-gated proton-selective channel lacking the pore domain Nature 440 2006 1213 1216
    • (2006) Nature , vol.440 , pp. 1213-1216
    • Ramsey, I.S.1    Moran, M.M.2    Chong, J.A.3    Clapham, D.E.4
  • 3
    • 66149104077 scopus 로고    scopus 로고
    • Hv1 proton channels are required for high-level NADPH oxidase-dependent superoxide production during the phagocyte respiratory burst
    • S.I. Ramsey, E. Ruchti, J.S. Kaczmarek, and D.E. Clapham Hv1 proton channels are required for high-level NADPH oxidase-dependent superoxide production during the phagocyte respiratory burst Proc. Natl. Acad. Sci. U.S.A. 106 2009 7642 7647
    • (2009) Proc. Natl. Acad. Sci. U.S.A. , vol.106 , pp. 7642-7647
    • Ramsey, S.I.1    Ruchti, E.2    Kaczmarek, J.S.3    Clapham, D.E.4
  • 5
    • 76149085162 scopus 로고    scopus 로고
    • VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification
    • A. El Chemaly, Y. Okochi, M. Sasaki, S. Arnaudeau, Y. Okamura, and N. Demaurex VSOP/Hv1 proton channels sustain calcium entry, neutrophil migration, and superoxide production by limiting cell depolarization and acidification J. Exp. Med. 207 2010 129 139
    • (2010) J. Exp. Med. , vol.207 , pp. 129-139
    • El Chemaly, A.1    Okochi, Y.2    Sasaki, M.3    Arnaudeau, S.4    Okamura, Y.5    Demaurex, N.6
  • 8
    • 75749122696 scopus 로고    scopus 로고
    • Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel
    • P.V. Lishko, I.L. Botchkina, A. Fedorenko, and Y. Kirichok Acid extrusion from human spermatozoa is mediated by flagellar voltage-gated proton channel Cell 140 2010 327 337
    • (2010) Cell , vol.140 , pp. 327-337
    • Lishko, P.V.1    Botchkina, I.L.2    Fedorenko, A.3    Kirichok, Y.4
  • 9
    • 77954346297 scopus 로고    scopus 로고
    • Function of the HVCN1 proton channel in airway epithelia and a naturally occurring mutation, M91T
    • D. Iovannisci, B. Illek, and H. Fischer Function of the HVCN1 proton channel in airway epithelia and a naturally occurring mutation, M91T J. Gen. Physiol. 136 2010 35 46
    • (2010) J. Gen. Physiol. , vol.136 , pp. 35-46
    • Iovannisci, D.1    Illek, B.2    Fischer, H.3
  • 11
    • 43449139690 scopus 로고    scopus 로고
    • The Voltage-Gated Proton Channel Hv1 Has Two Pores, Each Controlled by One Voltage Sensor
    • DOI 10.1016/j.neuron.2008.03.026, PII S0896627308003000
    • F. Tombola, M.H. Ulbrich, and E.Y. Isacoff The voltage-gated proton channel Hv1 has two pores, each controlled by one voltage sensor Neuron 58 2008 546 556 (Pubitemid 351672357)
    • (2008) Neuron , vol.58 , Issue.4 , pp. 546-556
    • Tombola, F.1    Ulbrich, M.H.2    Isacoff, E.Y.3
  • 13
    • 0030175348 scopus 로고    scopus 로고
    • + channel
    • DOI 10.1016/S0896-6273(00)80143-9
    • + channel Neuron 16 1996 1169 1177 (Pubitemid 26227238)
    • (1996) Neuron , vol.16 , Issue.6 , pp. 1169-1177
    • Aggarwal, S.K.1    MacKinnon, R.2
  • 14
    • 0026594721 scopus 로고
    • The size of gating charge in wild-type and mutant Shaker potassium channels
    • N.E. Schoppa, K. McCormack, M.A. Tanouye, and F.J. Sigworth The size of gating charge in wild-type and mutant Shaker potassium channels Science 255 1992 1712 1715
    • (1992) Science , vol.255 , pp. 1712-1715
    • Schoppa, N.E.1    McCormack, K.2    Tanouye, M.A.3    Sigworth, F.J.4
  • 16
    • 77449143196 scopus 로고    scopus 로고
    • Strong cooperativity between subunits in voltage-gated proton channels
    • C. Gonzalez, H.P. Koch, B.M. Drum, and H.P. Larsson Strong cooperativity between subunits in voltage-gated proton channels Nat. Struct. Mol. Biol. 17 2010 51 56
    • (2010) Nat. Struct. Mol. Biol. , vol.17 , pp. 51-56
    • Gonzalez, C.1    Koch, H.P.2    Drum, B.M.3    Larsson, H.P.4
  • 17
    • 77449091709 scopus 로고    scopus 로고
    • I. E.Y., the opening of the two pores of the Hv1 voltage-gated proton channel is tuned by cooperativity, Nature Struct
    • F. Tombola, M.H. Ulbrich, and S.C. Kohout I. E.Y., The opening of the two pores of the Hv1 voltage-gated proton channel is tuned by cooperativity, Nature Struct Mol. Biol. 17 2010 44 50
    • (2010) Mol. Biol. , vol.17 , pp. 44-50
    • Tombola, F.1    Ulbrich, M.H.2    Kohout, S.C.3
  • 18
    • 0030070436 scopus 로고    scopus 로고
    • Transmembrane movement of the Shaker K+ channel S4
    • B. Larsson, O.S. Baker, D.S. Dhillon, and E.Y. Isacoff Transmembrane movement of the Shaker K+ channel S4 Neuron 16 1996 387 397
    • (1996) Neuron , vol.16 , pp. 387-397
    • Larsson, B.1    Baker, O.S.2    Dhillon, D.S.3    Isacoff, E.Y.4
  • 19
    • 0030048243 scopus 로고    scopus 로고
    • Direct physical measure of conformational rearrangement underlying potassium channel gating
    • L.M. Mannuzzu, M.M. Moronne, and E.Y. Isacoff Direct physical measure of conformational rearrangement underlying potassium channel gating Science 271 1996 213 216 (Pubitemid 26033303)
    • (1996) Science , vol.271 , Issue.5246 , pp. 213-216
    • Mannuzzu, L.M.1    Moronne, M.M.2    Isacoff, E.Y.3
  • 20
    • 27544516349 scopus 로고    scopus 로고
    • Calibrated measurement of gating-charge arginine
    • V. Ruta, J. Chen, and R. MacKinnon Calibrated measurement of gating-charge arginine Cell 123 2005 463 475
    • (2005) Cell , vol.123 , pp. 463-475
    • Ruta, V.1    Chen, J.2    MacKinnon, R.3
  • 22
    • 36248946187 scopus 로고    scopus 로고
    • Portability of paddle motif function and pharmacology in voltage sensors
    • A.R. Alabi, M.I. Bahamonde, H.J. Jung, J.I. Kin, and K.J. Swartz Portability of paddle motif function and pharmacology in voltage sensors Nature 450 2007 370 376
    • (2007) Nature , vol.450 , pp. 370-376
    • Alabi, A.R.1    Bahamonde, M.I.2    Jung, H.J.3    Kin, J.I.4    Swartz, K.J.5
  • 24
    • 1142274549 scopus 로고    scopus 로고
    • A proton pore in a potassium channel voltage sensor reveals a focused electric field
    • DOI 10.1038/nature02270
    • D.M. Starace, and F. Bezanilla A proton pore in a potassium channel voltage sensor reveals a focused electric field Nature 427 2004 548 553 (Pubitemid 38209113)
    • (2004) Nature , vol.427 , Issue.6974 , pp. 548-553
    • Starace, D.M.1    Bezanilla, F.2
  • 25
    • 33846688821 scopus 로고    scopus 로고
    • The twisted ion-permeation pathway of a resting voltage-sensing domain
    • DOI 10.1038/nature05396, PII NATURE05396
    • F. Tombola, M.M. Pathak, P. Gorostiza, and E.Y. Isacoff The twisted ion-permeation pathway of a resting voltage-sensing domain Nature 445 2007 546 549 (Pubitemid 46197635)
    • (2007) Nature , vol.445 , Issue.7127 , pp. 546-549
    • Tombola, F.1    Pathak, M.M.2    Gorostiza, P.3    Isacoff, E.Y.4
  • 26
    • 13244272072 scopus 로고    scopus 로고
    • Voltage-sensing arginines in a potassium channel permeate and occlude cation-selective pores
    • DOI 10.1016/j.neuron.2004.12.047, PII S0896627305000188
    • F. Tombola, M.M. Pathak, and E.Y. Isacoff Voltage-sensing arginines in a potassium channel permeate and occlude cation-selective pores Neuron 45 2005 379 388 (Pubitemid 40188206)
    • (2005) Neuron , vol.45 , Issue.3 , pp. 379-388
    • Tombola, F.1    Pathak, M.M.2    Isacoff, E.Y.3
  • 28
    • 22544439334 scopus 로고    scopus 로고
    • Ion permeation through a voltage-sensitive gating pore in brain sodium channels having voltage sensor mutations
    • DOI 10.1016/j.neuron.2005.06.012, PII S0896627305005179
    • S. Sokolov, T. Scheuer, and W.A. Catterall Ion permeation through a voltage-sensitive gating pore in brain sodium channels having voltage sensor mutations Neuron 47 2005 183 189 (Pubitemid 41019250)
    • (2005) Neuron , vol.47 , Issue.2 , pp. 183-189
    • Sokolov, S.1    Scheuer, T.2    Catterall, W.A.3
  • 29
    • 33847344389 scopus 로고    scopus 로고
    • Gating pore current in an inherited ion channelopathy
    • DOI 10.1038/nature05598, PII NATURE05598
    • S. Sokolov, T. Scheuer, and W.A. Caterall Gating pore current in an inherited ion channelopathy Nature 446 2007 76 78 (Pubitemid 46348048)
    • (2007) Nature , vol.446 , Issue.7131 , pp. 76-78
    • Sokolov, S.1    Scheuer, T.2    Catterall, W.A.3
  • 30
    • 34347211819 scopus 로고    scopus 로고
    • + channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore
    • DOI 10.1085/jgp.200709755
    • A.F. Struyk, and S.C. Cannon A Na+ channel mutation linked to hypokalemic periodic paralysis exposes a proton-selective gating pore J. Gen. Physiol. 130 2007 11 20 (Pubitemid 47001069)
    • (2007) Journal of General Physiology , vol.130 , Issue.1 , pp. 11-20
    • Struyk, A.F.1    Cannon, S.C.2
  • 31
    • 38749112951 scopus 로고    scopus 로고
    • A Common Pathway for Charge Transport through Voltage-Sensing Domains
    • DOI 10.1016/j.neuron.2008.01.015, PII S0896627308000767
    • B. Chanda, and F. Bezanilla A common pathway for charge transport through voltage-sensing domains Neuron 57 2008 345 351 (Pubitemid 351179168)
    • (2008) Neuron , vol.57 , Issue.3 , pp. 345-351
    • Chanda, B.1    Bezanilla, F.2
  • 35
    • 33748456949 scopus 로고    scopus 로고
    • The barrier for proton transport in aquaporins as a challenge for electrostatic models: The role of protein relaxation in mutational calculations
    • DOI 10.1002/prot.21012
    • M. Kato, A.V. Pisliakov, and A. Warshel The barrier for proton transport in aquaporins as a challenge for electrostatic models: The role of protein relaxation in mutational calculations Proteins Struct. Funct. Bioinform. 64 2006 829 844 (Pubitemid 44420926)
    • (2006) Proteins: Structure, Function and Genetics , vol.64 , Issue.4 , pp. 829-844
    • Kato, M.1    Pisliakov, A.V.2    Warshel, A.3
  • 36
    • 0344825877 scopus 로고    scopus 로고
    • What Really Prevents Proton Transport through Aquaporin? Charge Self-Energy versus Proton Wire Proposals
    • A. Burykin, and A. Warshel What really prevents proton transport through aquaporin? Charge self-energy versus proton wire proposals Biophys. J. 85 2003 3696 3706 (Pubitemid 37492952)
    • (2003) Biophysical Journal , vol.85 , Issue.6 , pp. 3696-3706
    • Burykin, A.1    Warshel, A.2
  • 37
    • 12344277810 scopus 로고    scopus 로고
    • Realistic simulations of proton transport along the gramicidin channel: Demonstrating the importance of solvation effects
    • DOI 10.1021/jp0465783
    • S. Braun-Sand, A. Burykin, Z.T. Chu, and A. Warshel Realistic simulations of proton transport along the gramicidin channel: demonstrating the importance of solvation effects J. Phys. Chem. B 109 2005 583 592 (Pubitemid 40121005)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.1 , pp. 583-592
    • Braun-Sand, S.1    Burykin, A.2    Chu, Z.T.3    Warshel, A.4
  • 38
    • 36248982122 scopus 로고    scopus 로고
    • + channel in a lipid membrane-like environment
    • DOI 10.1038/nature06265, PII NATURE06265
    • + channel in a lipid membrane-like environment Nature 450 2007 376 382 (Pubitemid 350126743)
    • (2007) Nature , vol.450 , Issue.7168 , pp. 376-382
    • Long, S.B.1    Tao, X.2    Campbell, E.B.3    MacKinnon, R.4
  • 39
    • 0027136282 scopus 로고
    • Comparative protein modelling by satisfaction of spatial restraints
    • DOI 10.1006/jmbi.1993.1626
    • A. Sali, and T.L. Blundell Comparative protein modelling by satisfaction of spatial restraints J. Mol. Biol. 234 1993 779 815 (Pubitemid 24007801)
    • (1993) Journal of Molecular Biology , vol.234 , Issue.3 , pp. 779-815
    • Sali, A.1    Blundell, T.L.2
  • 42
    • 15744368593 scopus 로고    scopus 로고
    • An ab initio study on the torsional surface of alkanes and its effect on molecular simulations of alkanes and a DPPC bilayer
    • DOI 10.1021/jp0468096
    • J.B. Klauda, B.R. Brooks, A.D. MacKerell Jr., R.M. Venable, and R.W. Pastor An ab initio study on the torsional surface of alkanes and its effect on molecular simulations of alkanes and a DPPC bilayer J. Phys. Chem. B 109 2005 5300 5311 (Pubitemid 40407752)
    • (2005) Journal of Physical Chemistry B , vol.109 , Issue.11 , pp. 5300-5311
    • Klauda, J.B.1    Brooks, B.R.2    MacKerell Jr., A.D.3    Venable, R.M.4    Pastor, R.W.5
  • 45
    • 33846823909 scopus 로고
    • Particle mesh Ewald: An N•log(N) method for Ewald sums in large systems
    • T. Darden, D. York, and L. Pedersen Particle mesh Ewald: an N•log(N) method for Ewald sums in large systems J. Chem. Phys. 98 1993 10089 10092
    • (1993) J. Chem. Phys. , vol.98 , pp. 10089-10092
    • Darden, T.1    York, D.2    Pedersen, L.3
  • 46
    • 84963146276 scopus 로고
    • Generalized Verlet algorithm for efficient molecular dynamics simulations with long-range interactions
    • H. Grubmüller, H. Heller, A. Windemuth, and K. Schulten Generalized Verlet algorithm for efficient molecular dynamics simulations with long-range interactions Mol. Simul. 6 1991 121 142
    • (1991) Mol. Simul. , vol.6 , pp. 121-142
    • Grubmüller, H.1    Heller, H.2    Windemuth, A.3    Schulten, K.4
  • 47
    • 33646940952 scopus 로고
    • Numerical integration of the Cartesian equations of motion of a system with constraints: Molecular dynamics of n-alkanes
    • J.-P. Ryckaert, G. Ciccotti, and H.J.C. Berendsen Numerical integration of the Cartesian equations of motion of a system with constraints: molecular dynamics of n-alkanes J. Comput. Phys. 23 1977 327 341
    • (1977) J. Comput. Phys. , vol.23 , pp. 327-341
    • Ryckaert, J.-P.1    Ciccotti, G.2    Berendsen, H.J.C.3
  • 48
    • 84986440341 scopus 로고
    • An analytical version of the SHAKE and RATTLE algorithm for rigid water models
    • S. Miyamoto, and P. Kollman An analytical version of the SHAKE and RATTLE algorithm for rigid water models J. Comput. Chem. 13 1992 952 962
    • (1992) J. Comput. Chem. , vol.13 , pp. 952-962
    • Miyamoto, S.1    Kollman, P.2
  • 49
    • 36449003554 scopus 로고
    • Constant-pressure molecular-dynamics algorithms
    • G.J. Martyna, D.J. Tobias, and M.L. Klein Constant-pressure molecular-dynamics algorithms J. Chem. Phys. 101 1994 4177 4189
    • (1994) J. Chem. Phys. , vol.101 , pp. 4177-4189
    • Martyna, G.J.1    Tobias, D.J.2    Klein, M.L.3
  • 50
    • 36449007836 scopus 로고
    • Constant pressure molecular dynamics simulation: The Langevin piston method
    • S.E. Feller, Y. Zhang, R.W. Pastor, and B.R. Brooks Constant pressure molecular dynamics simulation: the Langevin piston method J. Chem. Phys. 103 1995 4613 4621
    • (1995) J. Chem. Phys. , vol.103 , pp. 4613-4621
    • Feller, S.E.1    Zhang, Y.2    Pastor, R.W.3    Brooks, B.R.4
  • 52
    • 42749105522 scopus 로고    scopus 로고
    • Collective diffusion model for water permeation through microscopic channels
    • 224501-224501 to 224501-224504
    • F. Zhu, E. Tajkhorshid, and K. Schulten Collective diffusion model for water permeation through microscopic channels Phys. Rev. Lett. 93 2004 224501-224501 to 224501-224504
    • (2004) Phys. Rev. Lett. , vol.93
    • Zhu, F.1    Tajkhorshid, E.2    Schulten, K.3
  • 55
    • 34547628129 scopus 로고    scopus 로고
    • + channel in a membrane environment
    • DOI 10.1529/biophysj.107.112540
    • V. Jogini, and B. Roux Dynamics of the Kv1.2 voltage-gated K1 channel in a membrane Biophys. J. 93 2007 3070 3082 (Pubitemid 350097098)
    • (2007) Biophysical Journal , vol.93 , Issue.9 , pp. 3070-3082
    • Jogini, V.1    Roux, B.2
  • 56
    • 33846785439 scopus 로고    scopus 로고
    • How Does a Voltage Sensor Interact with a Lipid Bilayer? Simulations of a Potassium Channel Domain
    • DOI 10.1016/j.str.2007.01.004, PII S0969212607000330
    • Z.A. Sands, and M.S.P. Sansom How does a voltage sensor interact with a lipid bilayer? Simulations of a potassium channel domain Structure 15 2007 235 244 (Pubitemid 46209817)
    • (2007) Structure , vol.15 , Issue.2 , pp. 235-244
    • Sands, Z.A.1    Sansom, M.S.P.2
  • 57
    • 33646135082 scopus 로고    scopus 로고
    • Environment of the gating charges in the Kv1.2 Shaker potassium channel
    • W. Treptow, and M. Tarek Environment of the gating charges in the Kv1.2 Shaker potassium channel. Biophys. J. 90 2006 L64 L66
    • (2006) Biophys. J. , vol.90
    • Treptow, W.1    Tarek, M.2
  • 61
    • 33646251373 scopus 로고    scopus 로고
    • Single-channel water permeabilities of Escherichia coli aquaporins AqpZ and GllF
    • M. Jensen, and O.G. Mouritsen Single-channel water permeabilities of Escherichia coli aquaporins AqpZ and GllF Biophys. J. 90 2006 2270 2284
    • (2006) Biophys. J. , vol.90 , pp. 2270-2284
    • Jensen, M.1    Mouritsen, O.G.2
  • 62
    • 34447325646 scopus 로고    scopus 로고
    • Water transport in aquaporins: Osmotic permeability matrix analysis of molecular dynamics simulations
    • DOI 10.1529/biophysj.106.101170
    • M. Hashido, A. Kidera, and M. Ikeguchi Water transport in aquaporins: osmotic permeability matrix analysis of molecular dynamics simulations Biophys. J. 93 2007 373 385 (Pubitemid 47057805)
    • (2007) Biophysical Journal , vol.93 , Issue.2 , pp. 373-385
    • Hashido, M.1    Kidera, A.2    Ikeguchi, M.3
  • 63
    • 26844501325 scopus 로고    scopus 로고
    • Comparative simulations of aquaporin family: AQP1, AQPZ, AQP0 and GlpF
    • DOI 10.1016/j.febslet.2005.09.018, PII S0014579305011233
    • M. Hashido, M. Ikeguchi, and A. Kidera Comparative simulations of aquaporin family: AQP1, AQPZ, AQP0 and GlpF FEBS Lett. 579 2005 5549 5552 (Pubitemid 41455629)
    • (2005) FEBS Letters , vol.579 , Issue.25 , pp. 5549-5552
    • Hashido, M.1    Ikeguchi, M.2    Kidera, A.3
  • 64
    • 55749105149 scopus 로고    scopus 로고
    • Dynamic control of slow water transport by aquaporin 0: Implications for hydration and junction stability in the eye lens
    • M.O. Jensen, R.O. Dror, H.F. Xu, D.W. Borhani, I.T. Arkin, M.P. Eastwood, and D.E. Shaw Dynamic control of slow water transport by aquaporin 0: implications for hydration and junction stability in the eye lens Proc. Natl. Acad. Sci. U.S.A. 105 2008 14430 14435
    • (2008) Proc. Natl. Acad. Sci. U.S.A. , vol.105 , pp. 14430-14435
    • Jensen, M.O.1    Dror, R.O.2    Xu, H.F.3    Borhani, D.W.4    Arkin, I.T.5    Eastwood, M.P.6    Shaw, D.E.7
  • 66
    • 0037379781 scopus 로고    scopus 로고
    • Voltage-gated proton channels and other proton transfer pathways
    • T.E. Decoursey Voltage-gated proton channels and other proton transfer pathways Physiol. Rev. 83 2003 475 579 (Pubitemid 36382892)
    • (2003) Physiological Reviews , vol.83 , Issue.2 , pp. 475-579
    • Decoursey, T.E.1
  • 68
    • 40049094627 scopus 로고    scopus 로고
    • Structural Dynamics of an Isolated Voltage-Sensor Domain in a Lipid Bilayer
    • DOI 10.1016/j.str.2007.12.015, PII S096921260800021X
    • S. Chakrapani, L.G. Cuello, D.M. Cortes, and E. Perozo Structural dynamics of an isolated voltage-sensor domain in a lipid bilayer Structure 16 2008 398 409 (Pubitemid 351324110)
    • (2008) Structure , vol.16 , Issue.3 , pp. 398-409
    • Chakrapani, S.1    Cuello, L.G.2    Cortes, D.M.3    Perozo, E.4
  • 69
    • 0029972071 scopus 로고    scopus 로고
    • Mechanism of unassisted ion transport across membrane bilayers
    • DOI 10.1021/ja9540381
    • M.A. Wilson, and A. Pohorille Mechanism of unassisted ion transport across membrane bilayers J. Am. Chem. Soc. 118 1996 6580 6587 (Pubitemid 26248152)
    • (1996) Journal of the American Chemical Society , vol.118 , Issue.28 , pp. 6580-6587
    • Wilson, M.A.1    Pohorille, A.2


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.