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Volumn 32, Issue 3, 2011, Pages 203-208

The 3-state model of muscle regulation revisited: Is a fourth state involved?

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM; MYOSIN;

EID: 82955195877     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-011-9263-8     Document Type: Review
Times cited : (28)

References (41)
  • 1
    • 79951828756 scopus 로고    scopus 로고
    • Enhanced active cross-bridges during diastole: Molecular pathogenesis of tropomyosin's HCM mutations
    • 21320446 1:CAS:528:DC%2BC3MXhvFKgtbg%3D 10.1016/j.bpj.2011.01.001
    • F Bai A Weis AK Takeda PB Chase M Kawai 2011 Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin's HCM mutations Biophys J 100 4 1014 1023 21320446 1:CAS:528:DC%2BC3MXhvFKgtbg%3D 10.1016/j.bpj.2011.01.001
    • (2011) Biophys J , vol.100 , Issue.4 , pp. 1014-1023
    • Bai, F.1    Weis, A.2    Takeda, A.K.3    Chase, P.B.4    Kawai, M.5
  • 2
    • 0015525066 scopus 로고
    • Cooperation within actin filament in vertebrate skeletal muscle
    • 4261616 1:CAS:528:DyaE38XkvFyjsbk%3D
    • RD Bremel A Weber 1972 Cooperation within actin filament in vertebrate skeletal muscle Nature New Biol 238 97 101 4261616 1:CAS:528:DyaE38XkvFyjsbk%3D
    • (1972) Nature New Biol , vol.238 , pp. 97-101
    • Bremel, R.D.1    Weber, A.2
  • 3
    • 0036995623 scopus 로고    scopus 로고
    • Regulation of striated muscle contraction: A discussion
    • DOI 10.1023/A:1022066922922
    • JM Chalovich 2002 Regulation of striated muscle contraction: a discussion J Muscle Res Cell Motil 23 4 353 361 12630710 1:CAS:528:DC%2BD3sXkvFejtQ%3D%3D 10.1023/A:1022066922922 (Pubitemid 36223037)
    • (2002) Journal of Muscle Research and Cell Motility , vol.23 , Issue.4 , pp. 353-361
    • Chalovich, J.M.1
  • 4
    • 26644464382 scopus 로고    scopus 로고
    • Functional consequences of hypertrophic and dilated cardiomyopathy- causing mutations in α-tropomyosin
    • DOI 10.1074/jbc.M505014200
    • AN Chang K Harada MJ Ackerman JD Potter 2005 Functional consequences of hypertrophic and dilated cardiomyopathy-causing mutations in alpha-tropomyosin J Biol Chem 280 40 34343 34349 16043485 1:CAS:528:DC%2BD2MXhtVKitrzP 10.1074/jbc.M505014200 (Pubitemid 41443160)
    • (2005) Journal of Biological Chemistry , vol.280 , Issue.40 , pp. 34343-34349
    • Chang, A.N.1    Harada, K.2    Ackerman, M.J.3    Potter, J.D.4
  • 5
    • 33750290244 scopus 로고    scopus 로고
    • Functional homodimers and heterodimers of recombinant smooth muscle tropomyosin
    • DOI 10.1021/bi0613224
    • A Coulton SS Lehrer MA Geeves 2006 Functional homodimers and heterodimers of recombinant smooth muscle tropomyosin Biochemistry 45 42 12853 12858 17042503 1:CAS:528:DC%2BD28XhtVWkurbO 10.1021/bi0613224 (Pubitemid 44630871)
    • (2006) Biochemistry , vol.45 , Issue.42 , pp. 12853-12858
    • Coulton, A.1    Lehrer, S.S.2    Geeves, M.A.3
  • 6
    • 0030592154 scopus 로고    scopus 로고
    • Calcium-induced conformational change in cardiac troponin C studied by fluorescence probes attached to Cys-84
    • DOI 10.1016/0167-4838(96)00028-3
    • WJ Dong HC Cheung 1996 Calcium-induced conformational change in cardiac troponin C studied by fluorescence probes attached to Cys-84 Biochim Biophys Acta 1295 2 139 146 8695639 10.1016/0167-4838(96)00028-3 (Pubitemid 26233242)
    • (1996) Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology , vol.1295 , Issue.2 , pp. 139-146
    • Dong, W.-J.1    Cheung, H.C.2
  • 7
    • 0033998842 scopus 로고    scopus 로고
    • An interdomain distance in cardiac troponin C determined by fluorescence spectroscopy
    • W-J Dong JM Robinson J Xing PK Umeda HC Cheung 2000 an interdomain distance in cardiac troponin C determined by fluorescence spectroscopy Protein Sci 9 280 289 10716180 1:CAS:528:DC%2BD3cXhs12rsro%3D 10.1110/ps.9.2.280 (Pubitemid 30127001)
    • (2000) Protein Science , vol.9 , Issue.2 , pp. 280-289
    • Dong, W.-J.1    Robinson, J.M.2    Xing, J.3    Umeda, P.K.4    Cheung, H.C.5
  • 9
    • 0028340236 scopus 로고
    • Dynamics of the muscle thin filament regulatory switch: The size of the cooperative unit
    • MA Geeves SS Lehrer 1994 Dynamics of the muscle thin filament regulatory switch: the size of the cooperative unit Biophys J 67 1 273 282 7918995 1:CAS:528:DyaK2cXlsFWmtLs%3D 10.1016/S0006-3495(94)80478-3 (Pubitemid 24197892)
    • (1994) Biophysical Journal , vol.67 , Issue.1 , pp. 273-282
    • Geeves, M.A.1    Lehrer, S.S.2
  • 10
    • 0034622584 scopus 로고    scopus 로고
    • Inhibition of actin-myosin subfragment 1 ATPase activity by troponin I and IC: Relationship to the thin filament states of muscle
    • DOI 10.1021/bi0002232
    • MA Geeves M Chai SS Lehrer 2000 Inhibition of actin-myosin subfragment 1 ATPase activity by troponin I and IC: relationship to the thin filament states of muscle Biochemistry 39 31 9345 9350 10924128 1:CAS:528:DC%2BD3cXksleisL0%3D 10.1021/bi0002232 (Pubitemid 30626325)
    • (2000) Biochemistry , vol.39 , Issue.31 , pp. 9345-9350
    • Geeves, M.A.1    Chai, M.2    Lehrer, S.S.3
  • 11
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • AM Gordon E Homsher M Regnier 2000 Regulation of contraction in striated muscle Physiol Rev 80 2 853 924 10747208 1:CAS:528:DC%2BD3cXisFSgsr8%3D (Pubitemid 30164950)
    • (2000) Physiological Reviews , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 13
    • 33644863664 scopus 로고    scopus 로고
    • Maximal activation of skeletal muscle thin filaments requires both rigor myosin S1 and calcium
    • DOI 10.1074/jbc.M505549200
    • DH Heeley B Belknap HD White 2006 Maximal activation of skeletal muscle thin filaments requires both rigor myosin S1 and calcium J Biol Chem 281 1 668 676 16186114 1:CAS:528:DC%2BD28Xht1Cgsw%3D%3D 10.1074/jbc.M505549200 (Pubitemid 43671230)
    • (2006) Journal of Biological Chemistry , vol.281 , Issue.1 , pp. 668-676
    • Heeley, D.H.1    Belknap, B.2    White, H.D.3
  • 14
    • 0016610748 scopus 로고
    • Regulation of muscle contraction: Bindings of troponin and its components to actin and tropomyosin
    • 126151 1:CAS:528:DyaE2MXhsFSrtbs%3D 10.1111/j.1432-1033.1975.tb03993.x
    • SE Hitchcock 1975 Regulation of muscle contraction: bindings of troponin and its components to actin and tropomyosin Eur J Biochem 52 2 255 263 126151 1:CAS:528:DyaE2MXhsFSrtbs%3D 10.1111/j.1432-1033.1975.tb03993.x
    • (1975) Eur J Biochem , vol.52 , Issue.2 , pp. 255-263
    • Hitchcock, S.E.1
  • 16
    • 77958482912 scopus 로고    scopus 로고
    • Mechanism of regulation of native cardiac muscle thin filaments by rigor cardiac myosin-S1 and calcium
    • 20696756 1:CAS:528:DC%2BC3cXht12nu7%2FJ 10.1074/jbc.M109.098228
    • A Houmeida DH Heeley B Belknap HD White 2010 Mechanism of regulation of native cardiac muscle thin filaments by rigor cardiac myosin-S1 and calcium J Biol Chem 285 43 32760 32769 20696756 1:CAS:528:DC%2BC3cXht12nu7%2FJ 10.1074/jbc.M109.098228
    • (2010) J Biol Chem , vol.285 , Issue.43 , pp. 32760-32769
    • Houmeida, A.1    Heeley, D.H.2    Belknap, B.3    White, H.D.4
  • 17
    • 15544390385 scopus 로고    scopus 로고
    • Calcium, thin filaments, and the integrative biology of cardiac contractility
    • DOI 10.1146/annurev.physiol.67.040403.114025
    • T Kobayashi RJ Solaro 2005 Calcium, thin filaments, and the integrative biology of cardiac contractility Annu Rev Physiol 67 39 67 15709952 1:CAS:528:DC%2BD2MXjsFelu78%3D 10.1146/annurev.physiol.67.040403.114025 (Pubitemid 40404485)
    • (2005) Annual Review of Physiology , vol.67 , pp. 39-67
    • Kobayashi, T.1    Solaro, R.J.2
  • 19
    • 0032540229 scopus 로고    scopus 로고
    • The muscle thin filament as a classical cooperative/allosteric regulatory system
    • DOI 10.1006/jmbi.1998.1654
    • SS Lehrer MA Geeves 1998 The muscle thin filament as a classical cooperative/allosteric regulatory system J Mol Biol 277 5 1081 1089 9571024 1:CAS:528:DyaK1cXivF2ntbo%3D 10.1006/jmbi.1998.1654 (Pubitemid 28190848)
    • (1998) Journal of Molecular Biology , vol.277 , Issue.5 , pp. 1081-1089
    • Lehrer, S.S.1    Geeves, M.A.2
  • 20
    • 0020490904 scopus 로고
    • Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase
    • 6123507 1:CAS:528:DyaL38XkvVOksL4%3D
    • SS Lehrer EP Morris 1982 Dual effects of tropomyosin and troponin-tropomyosin on actomyosin subfragment 1 ATPase J Biol Chem 257 14 8073 8080 6123507 1:CAS:528:DyaL38XkvVOksL4%3D
    • (1982) J Biol Chem , vol.257 , Issue.14 , pp. 8073-8080
    • Lehrer, S.S.1    Morris, E.P.2
  • 21
    • 0030838333 scopus 로고    scopus 로고
    • Actin-tropomyosin activation of myosin subfragment 1 ATPase and thin filament cooperativity. The role of tropomyosin flexibility and end-to-end interactions
    • DOI 10.1021/bi971568w
    • SS Lehrer NL Golitsina MA Geeves 1997 Actin-tropomyosin activation of myosin subfragment 1 ATPase and thin filament cooperativity. The role of tropomyosin flexibility and end-to-end interactions Biochemistry 36 44 13449 13454 9354612 1:CAS:528:DyaK2sXms1SqsL4%3D 10.1021/bi971568w (Pubitemid 27481590)
    • (1997) Biochemistry , vol.36 , Issue.44 , pp. 13449-13454
    • Lehrer, S.S.1    Golitsina, N.L.2    Geeves, M.A.3
  • 22
    • 0037470225 scopus 로고    scopus 로고
    • Differential regulation of the actomyosin interaction by skeletal and cardiac troponin isoforms
    • DOI 10.1074/jbc.M210690200
    • R Maytum B Westerdorf K Jaquet MA Geeves 2003 Differential regulation of the actomyosin interaction by skeletal and cardiac troponin isoforms J Biol Chem 278 9 6696 6701 12475978 1:CAS:528:DC%2BD3sXhsVKjtLg%3D 10.1074/jbc.M210690200 (Pubitemid 36800656)
    • (2003) Journal of Biological Chemistry , vol.278 , Issue.9 , pp. 6696-6701
    • Maytum, R.1    Westerdorf, B.2    Jaquet, K.3    Geeves, M.A.4
  • 23
    • 0027234056 scopus 로고
    • Regulation of the interaction between actin and myosin subfragment 1: Evidence for three states of the thin filament
    • DF McKillop MA Geeves 1993 Regulation of the interaction between actin and myosin subfragment 1: evidence for three states of the thin filament Biophys J 65 2 693 701 8218897 1:CAS:528:DyaK2cXhsFKqs7k%3D 10.1016/S0006-3495(93) 81110-X (Pubitemid 23263882)
    • (1993) Biophysical Journal , vol.65 , Issue.2 , pp. 693-701
    • McKillop, D.F.A.1    Geeves, M.A.2
  • 24
    • 2642583071 scopus 로고    scopus 로고
    • Myosin crossbridge activation of cardiac thin filaments: Implications for myocardial function in health and disease
    • DOI 10.1161/01.RES.0000127125.61647.4F
    • RL Moss M Razumova DP Fitzsimons 2004 Myosin crossbridge activation of cardiac thin filaments: implications for myocardial function in health and disease Circ Res 94 10 1290 1300 15166116 1:CAS:528:DC%2BD2cXktFSltbY%3D 10.1161/01.RES.0000127125.61647.4F (Pubitemid 38724474)
    • (2004) Circulation Research , vol.94 , Issue.10 , pp. 1290-1300
    • Moss, R.L.1    Razumova, M.2    Fitzsimons, D.P.3
  • 25
    • 65649150702 scopus 로고    scopus 로고
    • 2+-dependent photocrosslinking of tropomyosin residue 146 to residues 157-163 in the C-terminal domain of troponin i in reconstituted skeletal muscle thin filaments
    • 19379756 1:CAS:528:DC%2BD1MXms1aitb0%3D 10.1016/j.jmb.2009.04.027
    • 2+-dependent photocrosslinking of tropomyosin residue 146 to residues 157-163 in the C-terminal domain of troponin I in reconstituted skeletal muscle thin filaments J Mol Biol 389 3 575 583 19379756 1:CAS:528:DC%2BD1MXms1aitb0%3D 10.1016/j.jmb.2009.04.027
    • (2009) J Mol Biol , vol.389 , Issue.3 , pp. 575-583
    • Mudalige, W.A.1    Tao, T.C.2    Lehrer, S.S.3
  • 26
    • 0020024384 scopus 로고
    • Studies on co-operative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethylmaleimide-treated and untreated species of myosin subfragment 1
    • DOI 10.1016/0022-2836(82)90479-X
    • H Nagashima S Asakura 1982 Studies on cooperative properties of tropomyosin-actin and tropomyosin-troponin-actin complexes by the use of N-ethyl maleimide-treated and untreated species of myosin subfragment 1 J Mol Biol 155 409 428 7086898 1:CAS:528:DyaL38XktVans7c%3D 10.1016/0022-2836(82)90479-X (Pubitemid 12117709)
    • (1982) Journal of Molecular Biology , vol.155 , Issue.4 , pp. 409-428
    • Nagashima, H.1    Asakura, S.2
  • 27
    • 0033044797 scopus 로고    scopus 로고
    • Troponin I: Inhibitor or facilitator
    • SV Perry 1999 Troponin I: inhibitor or facilitator Mol Cell Biochem 190 1-2 9 32 10098965 1:CAS:528:DyaK1MXisVyksrs%3D 10.1023/A:1006939307715 (Pubitemid 29094983)
    • (1999) Molecular and Cellular Biochemistry , vol.190 , Issue.1-2 , pp. 9-32
    • Perry, S.V.1
  • 28
    • 0016213363 scopus 로고
    • Troponin, tropomyosin and actin interactions in the regulation of muscle contraction
    • 4847540 1:CAS:528:DyaE2MXksFCrsbo%3D 10.1021/bi00710a007
    • JD Potter J Gergely 1974 Troponin, tropomyosin and actin interactions in the regulation of muscle contraction Biochemistry 13 2697 2703 4847540 1:CAS:528:DyaE2MXksFCrsbo%3D 10.1021/bi00710a007
    • (1974) Biochemistry , vol.13 , pp. 2697-2703
    • Potter, J.D.1    Gergely, J.2
  • 29
    • 0028858949 scopus 로고
    • 2+ regulation of muscle contraction
    • 7852318 1:CAS:528:DyaK2MXjs1Kmt74%3D 10.1074/jbc.270.6.2557
    • 2+ regulation of muscle contraction J Biol Chem 270 6 2557 2562 7852318 1:CAS:528: DyaK2MXjs1Kmt74%3D 10.1074/jbc.270.6.2557
    • (1995) J Biol Chem , vol.270 , Issue.6 , pp. 2557-2562
    • Potter, J.D.1    Sheng, Z.2    Pan, B.S.3    Zhao, J.4
  • 30
    • 4143067982 scopus 로고    scopus 로고
    • Structural dynamics of actin during active interaction with myosin: Different effects of weakly and strongly bound myosin heads
    • DOI 10.1021/bi049914e
    • E Prochniewicz TF Walseth DD Thomas 2004 Structural dynamics of actin during active interaction with myosin: different effects of weakly and strongly bound myosin heads Biochemistry 43 33 10642 10652 15311925 1:CAS:528: DC%2BD2cXmtVKksb0%3D 10.1021/bi049914e (Pubitemid 39096706)
    • (2004) Biochemistry , vol.43 , Issue.33 , pp. 10642-10652
    • Prochniewicz, E.1    Walseth, T.F.2    Thomas, D.D.3
  • 31
    • 37349042936 scopus 로고    scopus 로고
    • Dilated and hypertrophic cardiomyopathy mutations in troponin and α-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments
    • DOI 10.1161/CIRCRESAHA.107.156380, PII 0000301220071207000009
    • P Robinson PJ Griffiths H Watkins CS Redwood 2007 Dilated and Hypertrophic Cardiomyopathy Mutations in Troponin and {alpha}-Tropomyosin Have Opposing Effects on the Calcium Affinity of Cardiac Thin Filaments Circ Res 101 12 1266 1273 17932326 1:CAS:528:DC%2BD2sXhtlOjsLzK 10.1161/CIRCRESAHA.107.156380 (Pubitemid 350294643)
    • (2007) Circulation Research , vol.101 , Issue.12 , pp. 1266-1273
    • Robinson, P.1    Griffiths, P.J.2    Watkins, H.3    Redwood, C.S.4
  • 32
    • 33644795360 scopus 로고    scopus 로고
    • Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin
    • DOI 10.1016/j.str.2005.09.016, PII S0969212605003965
    • A Singh SE Hitchcock-DeGregori 2006 Dual requirement for flexibility and specificity for binding of the coiled-coil tropomyosin to its target, actin Structure 14 1 43 50 16407064 1:CAS:528:DC%2BD28XksVWruw%3D%3D 10.1016/j.str.2005.09.016 (Pubitemid 43350072)
    • (2006) Structure , vol.14 , Issue.1 , pp. 43-50
    • Singh, A.1    Hitchcock-Degregori, S.E.2
  • 33
    • 15544368953 scopus 로고    scopus 로고
    • R.J. Solaro R.L. Moss (eds). Advances in Muscle Research Kluwer, Dordrecht
    • Solaro RJ, Moss RL (eds) (2002) Molecular control mechanisms in striated muscle contraction, vol 1. Advances in Muscle Research, Kluwer, Dordrecht
    • (2002) Molecular Control Mechanisms in Striated Muscle Contraction , vol.1
  • 34
    • 31744435681 scopus 로고    scopus 로고
    • Activation dependence of stretch activation in mouse skinned myocardium: Implications for ventricular function
    • DOI 10.1085/jgp.200509432
    • JE Stelzer L Larsson DP Fitzsimons RL Moss 2006 Activation dependence of stretch activation in mouse skinned myocardium: implications for ventricular function J Gen Physiol 127 2 95 107 16446502 1:CAS:528:DC%2BD28XhvVantLc%3D 10.1085/jgp.200509432 (Pubitemid 43177133)
    • (2006) Journal of General Physiology , vol.127 , Issue.2 , pp. 95-107
    • Stelzer, J.E.1    Larsson, L.2    Fitzsimons, D.P.3    Moss, R.L.4
  • 35
    • 77951623260 scopus 로고    scopus 로고
    • The molecular basis of the steep force-calcium relation in heart muscle
    • 10.1016/j.yjmcc.2009.11.019
    • YB Sun M Irving 2009 The molecular basis of the steep force-calcium relation in heart muscle J Mol Cell Cardiol 48 5 859 865 10.1016/j.yjmcc.2009. 11.019
    • (2009) J Mol Cell Cardiol , vol.48 , Issue.5 , pp. 859-865
    • Sun, Y.B.1    Irving, M.2
  • 36
    • 0036787723 scopus 로고    scopus 로고
    • Relaxation kinetics following sudden Ca(2+) reduction in single myofibrils from skeletal muscle
    • 12324431 1:CAS:528:DC%2BD38XnslSrtrw%3D 10.1016/S0006-3495(02)73974-X
    • C Tesi N Piroddi F Colomo C Poggesi 2002 Relaxation kinetics following sudden Ca(2+) reduction in single myofibrils from skeletal muscle Biophys J 83 4 2142 2151 12324431 1:CAS:528:DC%2BD38XnslSrtrw%3D 10.1016/S0006-3495(02)73974-X
    • (2002) Biophys J , vol.83 , Issue.4 , pp. 2142-2151
    • Tesi, C.1    Piroddi, N.2    Colomo, F.3    Poggesi, C.4
  • 37
    • 0034623058 scopus 로고    scopus 로고
    • A new model of cooperative myosin-thin filament binding
    • 10864931 1:CAS:528:DC%2BD3cXmsVKltbg%3D
    • LS Tobacman CA Butters 2000 A new model of cooperative myosin-thin filament binding J Biol Chem 275 36 27587 27593 10864931 1:CAS:528: DC%2BD3cXmsVKltbg%3D
    • (2000) J Biol Chem , vol.275 , Issue.36 , pp. 27587-27593
    • Tobacman, L.S.1    Butters, C.A.2
  • 39
    • 0031566964 scopus 로고    scopus 로고
    • Steric-model for activation of muscle thin filaments
    • DOI 10.1006/jmbi.1996.0800
    • P Vibert R Craig W Lehman 1997 Steric-model for activation of muscle thin filaments J Mol Biol 266 1 8 14 9054965 1:CAS:528:DyaK2sXhsVKgs78%3D 10.1006/jmbi.1996.0800 (Pubitemid 27170513)
    • (1997) Journal of Molecular Biology , vol.266 , Issue.1 , pp. 8-14
    • Vibert, P.1    Craig, R.2    Lehman, W.3
  • 40
    • 0022367130 scopus 로고
    • Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle
    • CK Wang HC Cheung 1985 Energetics of the binding of calcium and troponin I to troponin C from rabbit skeletal muscle Biophys J 48 5 727 739 4074834 1:CAS:528:DyaL28XisVaj 10.1016/S0006-3495(85)83831-5 (Pubitemid 16199600)
    • (1985) Biophysical Journal , vol.48 , Issue.5 , pp. 727-739
    • Wang, C.-K.1    Cheung, H.C.2
  • 41
    • 0034620545 scopus 로고    scopus 로고
    • Binding of troponin I and the troponin I-troponin C complex to actin- tropomyosin. Dissociation by myosin subfragment 1
    • DOI 10.1021/bi992327m
    • X Zhou EP Morris SS Lehrer 2000 Binding of troponin I and the troponin I-troponin C complex to actin-tropomyosin. Dissociation by myosin subfragment 1 Biochemistry 39 5 1128 1132 10653659 1:CAS:528:DC%2BD3cXit1Wjsg%3D%3D 10.1021/bi992327m (Pubitemid 30075342)
    • (2000) Biochemistry , vol.39 , Issue.5 , pp. 1128-1132
    • Zhou, X.1    Morris, E.P.2    Lehrer, S.S.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.