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Volumn 10, Issue 3, 2005, Pages 187-197

Thick filament proteins and performance in human heart failure

Author keywords

Cardiomyopathy; Myosin; Myosin binding protein C; Titin

Indexed keywords

ADENOSINE TRIPHOSPHATASE (MAGNESIUM); CALCIUM ION; ISOPROTEIN; MUSCLE PROTEIN; MYOSIN ADENOSINE TRIPHOSPHATASE; MYOSIN HEAVY CHAIN ALPHA; MYOSIN HEAVY CHAIN BETA; MYOSIN LIGHT CHAIN;

EID: 30944461059     PISSN: 13824147     EISSN: None     Source Type: Journal    
DOI: 10.1007/s10741-005-5249-1     Document Type: Review
Times cited : (46)

References (104)
  • 1
    • 0008800145 scopus 로고
    • Contractility of actomyosin bands prepared from normal and failing human hearts
    • 1:CAS:528:DyaG1cXlslCjsQ%3D%3D
    • Kako K, Bing RJ. Contractility of actomyosin bands prepared from normal and failing human hearts. J Clin Invest 1958;37(3):465-470. 1:CAS:528:DyaG1cXlslCjsQ%3D%3D
    • (1958) J Clin Invest , vol.37 , Issue.3 , pp. 465-470
    • Kako, K.1    Bing, R.J.2
  • 2
    • 73649183082 scopus 로고
    • Myofibrillar adenosine triphosphatase activity in congestive heart failure
    • 1:CAS:528:DyaF38Xkt1GrsL0%3D
    • Alpert NR, Gordon MS. Myofibrillar adenosine triphosphatase activity in congestive heart failure. Am J Physiol 1962;202:940-946. 1:CAS:528:DyaF38Xkt1GrsL0%3D
    • (1962) Am J Physiol , vol.202 , pp. 940-946
    • Alpert, N.R.1    Gordon, M.S.2
  • 3
    • 0031735281 scopus 로고    scopus 로고
    • Congestive heart failure: Role of cross-bridge cycle kinetics
    • 1:CAS:528:DyaK1cXnvVWlsLk%3D
    • de Tombe PP. Congestive heart failure: Role of cross-bridge cycle kinetics. Cardiovasc Res 1998;40(3):440-443.
    • (1998) Cardiovasc Res , vol.40 , Issue.3 , pp. 440-443
    • de Tombe, P.P.1
  • 4
    • 0032609762 scopus 로고    scopus 로고
    • The C-protein (myosin binding protein C) family: Regulators of contraction and sarcomere formation?
    • 1:CAS:528:DyaK1MXktVejsb0%3D
    • Bennett PM, Furst DO, Gautel M. The C-protein (myosin binding protein C) family: Regulators of contraction and sarcomere formation? Rev Physiol Biochem Pharmacol 1999;138:203-234. 1:CAS:528:DyaK1MXktVejsb0%3D
    • (1999) Rev Physiol Biochem Pharmacol , vol.138 , pp. 203-234
    • Bennett, P.M.1    Furst, D.O.2    Gautel, M.3
  • 5
    • 0032853632 scopus 로고    scopus 로고
    • Tuning the human heart molecular motors by myosin light chains
    • 10.1007/s001099900031
    • Morano I. Tuning the human heart molecular motors by myosin light chains. J Mol Med 1999;77(7):544-555. 10.1007/s001099900031
    • (1999) J Mol Med , vol.77 , Issue.7 , pp. 544-555
    • Morano, I.1
  • 6
    • 0036220357 scopus 로고    scopus 로고
    • The failing human heart
    • 10.1016/S0008-6363(02)00248-1
    • Alpert NR, Mulieri LA, Warshaw D. The failing human heart. Cardiovasc Res 2002;54(1):1-10. 10.1016/S0008-6363(02)00248-1
    • (2002) Cardiovasc Res , vol.54 , Issue.1 , pp. 1-10
    • Alpert, N.R.1    Mulieri, L.A.2    Warshaw, D.3
  • 7
    • 12244249137 scopus 로고    scopus 로고
    • The effect of myosin light chain 2 dephosphorylation on Ca2+ -sensitivity of force is enhanced in failing human hearts
    • 1:CAS:528:DC%2BD3sXptFCmsg%3D%3D
    • van der Velden J, Papp Z, Boontje NM, Zaremba R, de Jong JW, Janssen PM, et al. The effect of myosin light chain 2 dephosphorylation on Ca2+ -sensitivity of force is enhanced in failing human hearts. Cardiovasc Res 2003;57(2):505-514. 1:CAS:528:DC%2BD3sXptFCmsg%3D%3D
    • (2003) Cardiovasc Res , vol.57 , Issue.2 , pp. 505-514
    • van der Velden, J.1    Papp, Z.2    Boontje, N.M.3    Zaremba, R.4    de Jong, J.W.5    Janssen, P.M.6
  • 8
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling, and disease
    • 10.1161/01.RES.0000117769.88862.F8
    • Granzier HL, Labeit S. The giant protein titin: A major player in myocardial mechanics, signaling, and disease. Circ Res 2004;94(3):284-295. 10.1161/01.RES.0000117769.88862.F8
    • (2004) Circ Res , vol.94 , Issue.3 , pp. 284-295
    • Granzier, H.L.1    Labeit, S.2
  • 9
    • 0032459586 scopus 로고    scopus 로고
    • Muscle thick filaments are rigid coupled tubules, not flexible ropes
    • 10.1002/(SICI)1097-0169(1998)41:3<195::AID-CM1>3.0.CO;2-7
    • Schmid MF, Epstein HF. Muscle thick filaments are rigid coupled tubules, not flexible ropes. Cell Motil Cytoskeleton 1998;41(3):195-201. 10.1002/ (SICI)1097-0169(1998)41:3<195::AID-CM1>3.0.CO;2-7
    • (1998) Cell Motil Cytoskeleton , vol.41 , Issue.3 , pp. 195-201
    • Schmid, M.F.1    Epstein, H.F.2
  • 10
    • 0031707518 scopus 로고    scopus 로고
    • Myosin rod-packing schemes in vertebrate muscle thick filaments
    • 1:CAS:528:DyaK1cXmtVSru70%3D
    • Squire J, Cantino M, Chew M, Denny R, Harford J, Hudson L, et al. Myosin rod-packing schemes in vertebrate muscle thick filaments. J Struct Biol 1998;122(1/2):128-138. 1:CAS:528:DyaK1cXmtVSru70%3D
    • (1998) J Struct Biol , vol.122 , Issue.1-2 , pp. 128-138
    • Squire, J.1    Cantino, M.2    Chew, M.3    Denny, R.4    Harford, J.5    Hudson, L.6
  • 11
    • 0029162081 scopus 로고
    • Compliance of thin filaments in skinned fibers of rabbit skeletal muscle
    • 1:CAS:528:DyaK2MXnsl2rt7s%3D
    • Higuchi H, Yanagida T, Goldman YE. Compliance of thin filaments in skinned fibers of rabbit skeletal muscle. Biophys J 1995;69(3):1000-1110. 1:CAS:528:DyaK2MXnsl2rt7s%3D
    • (1995) Biophys J , vol.69 , Issue.3 , pp. 1000-1110
    • Higuchi, H.1    Yanagida, T.2    Goldman, Y.E.3
  • 12
    • 0028081493 scopus 로고
    • X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle
    • 1:CAS:528:DyaK2MXisVajurc%3D
    • Huxley HE, Stewart A, Sosa H, Irving T. X-ray diffraction measurements of the extensibility of actin and myosin filaments in contracting muscle. Biophys J 1994;67(6):2411-2421. 1:CAS:528:DyaK2MXisVajurc%3D
    • (1994) Biophys J , vol.67 , Issue.6 , pp. 2411-2421
    • Huxley, H.E.1    Stewart, A.2    Sosa, H.3    Irving, T.4
  • 13
    • 0028081494 scopus 로고
    • X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction
    • 1:CAS:528:DyaK2MXisVaju74%3D
    • Wakabayashi K, Sugimoto Y, Tanaka H, Ueno Y, Takezawa Y, Amemiya Y. X-ray diffraction evidence for the extensibility of actin and myosin filaments during muscle contraction. Biophys J 1994;67(6):2422-2435. 1:CAS:528:DyaK2MXisVaju74%3D
    • (1994) Biophys J , vol.67 , Issue.6 , pp. 2422-2435
    • Wakabayashi, K.1    Sugimoto, Y.2    Tanaka, H.3    Ueno, Y.4    Takezawa, Y.5    Amemiya, Y.6
  • 14
    • 0036152427 scopus 로고    scopus 로고
    • The myosin power stroke
    • 10.1002/cm.10014
    • Tyska MJ, Warshaw DM. The myosin power stroke. Cell Motil Cytoskeleton 2002;51(1):1-15. 10.1002/cm.10014
    • (2002) Cell Motil Cytoskeleton , vol.51 , Issue.1 , pp. 1-15
    • Tyska, M.J.1    Warshaw, D.M.2
  • 15
    • 0015214368 scopus 로고
    • Mechanism of adenosine triphosphate hydrolysis by actomyosin
    • 10.1021/bi00801a004
    • Lymn RW, Taylor EW. Mechanism of adenosine triphosphate hydrolysis by actomyosin. Biochemistry 1971;10(25):4617-4624. 10.1021/bi00801a004
    • (1971) Biochemistry , vol.10 , Issue.25 , pp. 4617-4624
    • Lymn, R.W.1    Taylor, E.W.2
  • 16
    • 0017851095 scopus 로고
    • A cross-bridge model of muscle contraction
    • 1:CAS:528:DyaE1cXhs1OitLw%3D
    • Eisenberg E, Hill TL. A cross-bridge model of muscle contraction. Prog Biophys Mol Biol 1978;33(1):55-82. 1:CAS:528:DyaE1cXhs1OitLw%3D
    • (1978) Prog Biophys Mol Biol , vol.33 , Issue.1 , pp. 55-82
    • Eisenberg, E.1    Hill, T.L.2
  • 17
    • 0022400802 scopus 로고
    • Relationship between myosin isoenzyme composition, hemodynamics, and myocardial structure in various forms of human cardiac hypertrophy
    • 1:CAS:528:DyaL2MXmtFalsrY%3D
    • Hirzel HO, Tuchschmid CR, Schneider J, Krayenbuehl HP, Schaub MC. Relationship between myosin isoenzyme composition, hemodynamics, and myocardial structure in various forms of human cardiac hypertrophy. Circ Res 1985;57(5):729-740. 1:CAS:528:DyaL2MXmtFalsrY%3D
    • (1985) Circ Res , vol.57 , Issue.5 , pp. 729-740
    • Hirzel, H.O.1    Tuchschmid, C.R.2    Schneider, J.3    Krayenbuehl, H.P.4    Schaub, M.C.5
  • 18
    • 0023814263 scopus 로고
    • Changes in myofibrillar content and Mg-ATPase activity in ventricular tissues from patients with heart failure caused by coronary artery disease, cardiomyopathy, or mitral valve insufficiency
    • 1:CAS:528:DyaL1cXlt1Kktr0%3D
    • Pagani ED, Alousi AA, Grant AM, Older TM, Dziuban SW, Jr., Allen PD. Changes in myofibrillar content and Mg-ATPase activity in ventricular tissues from patients with heart failure caused by coronary artery disease, cardiomyopathy, or mitral valve insufficiency. Circ Res 1988;63(2):380-385. 1:CAS:528:DyaL1cXlt1Kktr0%3D
    • (1988) Circ Res , vol.63 , Issue.2 , pp. 380-385
    • Pagani, E.D.1    Alousi, A.A.2    Grant, A.M.3    Older, T.M.4    Dziuban Jr., S.W.5    Allen, P.D.6
  • 19
    • 0023871819 scopus 로고
    • Human myocardial adenosine triphosphatase activities in health and heart failure
    • 1:STN:280:BieC3czit1I%3D
    • Unverferth DV, Lee SW, Wallick ET. Human myocardial adenosine triphosphatase activities in health and heart failure. Am Heart J 1988;115(1 Pt 1):139-146. 1:STN:280:BieC3czit1I%3D
    • (1988) Am Heart J , vol.115 , Issue.1 PART 1 , pp. 139-146
    • Unverferth, D.V.1    Lee, S.W.2    Wallick, E.T.3
  • 20
    • 0026551226 scopus 로고
    • Alteration of contractile function and excitation-contraction coupling in dilated cardiomyopathy
    • 1:STN:280:By2B2cfos1A%3D
    • Hasenfuss G, Mulieri LA, Leavitt BJ, Allen PD, Haeberle JR, Alpert NR. Alteration of contractile function and excitation-contraction coupling in dilated cardiomyopathy. Circ Res 1992;70(6):1225-1232. 1:STN:280:By2B2cfos1A%3D
    • (1992) Circ Res , vol.70 , Issue.6 , pp. 1225-1232
    • Hasenfuss, G.1    Mulieri, L.A.2    Leavitt, B.J.3    Allen, P.D.4    Haeberle, J.R.5    Alpert, N.R.6
  • 21
    • 0031739057 scopus 로고    scopus 로고
    • A mechanistic analysis of the force-frequency relation in non-failing and progressively failing human myocardium
    • 9833127
    • Alpert NR, Leavitt BJ, Ittleman FP, Hasenfuss G, Pieske B, Mulieri LA. A mechanistic analysis of the force-frequency relation in non-failing and progressively failing human myocardium. Basic Res Cardiol 1998;93 (Suppl 1):23-32. 9833127
    • (1998) Basic Res Cardiol , vol.93 , Issue.SUPPL. 1 , pp. 23-32
    • Alpert, N.R.1    Leavitt, B.J.2    Ittleman, F.P.3    Hasenfuss, G.4    Pieske, B.5    Mulieri, L.A.6
  • 22
    • 0025339307 scopus 로고
    • Reduced cardiac myofibrillar Mg-ATPase activity without changes in myosin isozymes in patients with end-stage heart failure
    • 10.1007/BF00228455
    • Alousi AA, Grant AM, Etzler JR, Cofer BR, Van der Bel-Kahn J, Melvin D. Reduced cardiac myofibrillar Mg-ATPase activity without changes in myosin isozymes in patients with end-stage heart failure. Mol Cell Biochem 1990;96(1):79-88. 10.1007/BF00228455
    • (1990) Mol Cell Biochem , vol.96 , Issue.1 , pp. 79-88
    • Alousi, A.A.1    Grant, A.M.2    Etzler, J.R.3    Cofer, B.R.4    Van der Bel-Kahn, J.5    Melvin, D.6
  • 23
    • 0030056230 scopus 로고    scopus 로고
    • Maximal actomyosin ATPase activity and in vitro myosin motility are unaltered in human mitral regurgitation heart failure
    • 1:CAS:528:DyaK28Xkslyiurs%3D
    • Nguyen TT, Hayes E, Mulieri LA, Leavitt BJ, ter Keurs HE, Alpert NR, et al. Maximal actomyosin ATPase activity and in vitro myosin motility are unaltered in human mitral regurgitation heart failure. Circ Res 1996;79(2):222-226. 1:CAS:528:DyaK28Xkslyiurs%3D
    • (1996) Circ Res , vol.79 , Issue.2 , pp. 222-226
    • Nguyen, T.T.1    Hayes, E.2    Mulieri, L.A.3    Leavitt, B.J.4    ter Keurs, H.E.5    Alpert, N.R.6
  • 24
    • 0033034564 scopus 로고    scopus 로고
    • Isometric tension development and its calcium sensitivity in skinned myocyte-sized preparations from different regions of the human heart
    • 10.1016/S0008-6363(98)00337-X
    • van der Velden J, Klein LJ, van der Bijl M, Huybregts MA, Stooker W, Witkop J, et al. Isometric tension development and its calcium sensitivity in skinned myocyte-sized preparations from different regions of the human heart. Cardiovasc Res 1999;42(3):706-719. 10.1016/ S0008-6363(98)00337-X
    • (1999) Cardiovasc Res , vol.42 , Issue.3 , pp. 706-719
    • van der Velden, J.1    Klein, L.J.2    van der Bijl, M.3    Huybregts, M.A.4    Stooker, W.5    Witkop, J.6
  • 25
    • 0037215834 scopus 로고    scopus 로고
    • Myosin from failing and non-failing human ventricles exhibit similar contractile properties
    • 10.1016/S0022-2828(02)00282-1
    • Noguchi T, Camp P, Jr., Alix SL, Gorga JA, Begin KJ, Leavitt BJ, et al. Myosin from failing and non-failing human ventricles exhibit similar contractile properties. J Mol Cell Cardiol 2003;35(1):91-97. 10.1016/ S0022-2828(02)00282-1
    • (2003) J Mol Cell Cardiol , vol.35 , Issue.1 , pp. 91-97
    • Noguchi, T.1    Camp Jr., P.2    Alix, S.L.3    Gorga, J.A.4    Begin, K.J.5    Leavitt, B.J.6
  • 27
    • 0020551639 scopus 로고
    • Myosin isoenzymes in normal and hypertrophied human ventricular myocardium
    • 1:CAS:528:DyaL3sXks1ynsrk%3D
    • Mercadier JJ, Bouveret P, Gorza L, Schiaffino S, Clark WA, Zak R, et al. Myosin isoenzymes in normal and hypertrophied human ventricular myocardium. Circ Res 1983;53(1):52-62. 1:CAS:528:DyaL3sXks1ynsrk%3D
    • (1983) Circ Res , vol.53 , Issue.1 , pp. 52-62
    • Mercadier, J.J.1    Bouveret, P.2    Gorza, L.3    Schiaffino, S.4    Clark, W.A.5    Zak, R.6
  • 28
    • 0021273032 scopus 로고
    • Myosin types in the human heart. An immunofluorescence study of normal and hypertrophied atrial and ventricular myocardium
    • 1:CAS:528:DyaL2MXht12kuro%3D
    • Gorza L, Mercadier JJ, Schwartz K, Thornell LE, Sartore S, Schiaffino S. Myosin types in the human heart. An immunofluorescence study of normal and hypertrophied atrial and ventricular myocardium. Circ Res 1984;54(6):694-702. 1:CAS:528:DyaL2MXht12kuro%3D
    • (1984) Circ Res , vol.54 , Issue.6 , pp. 694-702
    • Gorza, L.1    Mercadier, J.J.2    Schwartz, K.3    Thornell, L.E.4    Sartore, S.5    Schiaffino, S.6
  • 29
    • 0024535042 scopus 로고
    • Distribution pattern of alpha and beta myosin in normal and diseased human ventricular myocardium
    • 10.1007/BF01907006
    • Bouvagnet P, Mairhofer H, Leger JO, Puech P, Leger JJ. Distribution pattern of alpha and beta myosin in normal and diseased human ventricular myocardium. Basic Res Cardiol 1989;84(1):91-102. 10.1007/ BF01907006
    • (1989) Basic Res Cardiol , vol.84 , Issue.1 , pp. 91-102
    • Bouvagnet, P.1    Mairhofer, H.2    Leger, J.O.3    Puech, P.4    Leger, J.J.5
  • 30
    • 0034599128 scopus 로고    scopus 로고
    • Myosin heavy chain isoform expression in the failing and nonfailing human heart
    • 1:CAS:528:DC%2BD3cXhvVektLY%3D
    • Miyata S, Minobe W, Bristow MR, Leinwand LA. Myosin heavy chain isoform expression in the failing and nonfailing human heart. Circ Res 2000;86(4):386-390. 1:CAS:528:DC%2BD3cXhvVektLY%3D
    • (2000) Circ Res , vol.86 , Issue.4 , pp. 386-390
    • Miyata, S.1    Minobe, W.2    Bristow, M.R.3    Leinwand, L.A.4
  • 31
    • 0035017153 scopus 로고    scopus 로고
    • Human cardiac myosin heavy chain isoforms in fetal and failing adult atria and ventricles
    • 1:CAS:528:DC%2BD3MXjtV2itL4%3D
    • Reiser PJ, Portman MA, Ning XH, Schomisch Moravec C. Human cardiac myosin heavy chain isoforms in fetal and failing adult atria and ventricles. Am J Physiol Heart Circ Physiol 2001;280(4):H1814-1820. 1:CAS:528:DC%2BD3MXjtV2itL4%3D
    • (2001) Am J Physiol Heart Circ Physiol , vol.280 , Issue.4
    • Reiser, P.J.1    Portman, M.A.2    Ning, X.H.3    Schomisch Moravec, C.4
  • 32
    • 0021669797 scopus 로고
    • Myosin isoenzymes in human hypertrophic hearts. Shift in atrial myosin heavy chains and in ventricular myosin light chains
    • 1:CAS:528:DyaL2MXkt1Slt74%3D
    • Schaub MC, Tuchschmid CR, Srihari T, Hirzel HO. Myosin isoenzymes in human hypertrophic hearts. Shift in atrial myosin heavy chains and in ventricular myosin light chains. Eur Heart J 1984;5 (Suppl F):85-93. 1:CAS:528:DyaL2MXkt1Slt74%3D
    • (1984) Eur Heart J , vol.5 , Issue.SUPPL. F , pp. 85-93
    • Schaub, M.C.1    Tuchschmid, C.R.2    Srihari, T.3    Hirzel, H.O.4
  • 33
    • 0028983138 scopus 로고
    • Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro
    • 1:CAS:528:DyaK2MXntFartLc%3D
    • VanBuren P, Harris DE, Alpert NR, Warshaw DM. Cardiac V1 and V3 myosins differ in their hydrolytic and mechanical activities in vitro. Circ Res 1995;77(2):439-444. 1:CAS:528:DyaK2MXntFartLc%3D
    • (1995) Circ Res , vol.77 , Issue.2 , pp. 439-444
    • VanBuren, P.1    Harris, D.E.2    Alpert, N.R.3    Warshaw, D.M.4
  • 34
    • 0033546224 scopus 로고    scopus 로고
    • Effects of myosin heavy chain isoform switching on Ca2+-activated tension development in single adult cardiac myocytes
    • 1:CAS:528:DyaK1MXjslelt7k%3D
    • Metzger JM, Wahr PA, Michele DE, Albayya F, Westfall MV. Effects of myosin heavy chain isoform switching on Ca2+-activated tension development in single adult cardiac myocytes. Circ Res 1999;84(11):1310-1317. 1:CAS:528:DyaK1MXjslelt7k%3D
    • (1999) Circ Res , vol.84 , Issue.11 , pp. 1310-1317
    • Metzger, J.M.1    Wahr, P.A.2    Michele, D.E.3    Albayya, F.4    Westfall, M.V.5
  • 35
    • 0037076795 scopus 로고    scopus 로고
    • Small amounts of alpha-myosin heavy chain isoform expression significantly increase power output of rat cardiac myocyte fragments
    • 10.1161/01.RES.0000022879.57270.11
    • Herron TJ, McDonald KS. Small amounts of alpha-myosin heavy chain isoform expression significantly increase power output of rat cardiac myocyte fragments. Circ Res 2002;90(11):1150-1152. 10.1161/ 01.RES.0000022879.57270.11
    • (2002) Circ Res , vol.90 , Issue.11 , pp. 1150-1152
    • Herron, T.J.1    McDonald, K.S.2
  • 36
    • 23744469807 scopus 로고    scopus 로고
    • Power output is linearly related to MyHC content in rat skinned myocytes and isolated working hearts
    • Korte FS, Herron TJ, Rovetto MJ, McDonald KS. Power output is linearly related to MyHC content in rat skinned myocytes and isolated working hearts. Am J Physiol Heart Circ Physiol 2005;289(2):H801-812.
    • (2005) Am J Physiol Heart Circ Physiol , vol.289 , Issue.2
    • Korte, F.S.1    Herron, T.J.2    Rovetto, M.J.3    McDonald, K.S.4
  • 37
    • 21844463045 scopus 로고    scopus 로고
    • Alpha-myosin heavy chain: A sarcomeric gene associated with dilated and hypertrophic phenotypes of cardiomyopathy
    • 10.1161/CIRCULATIONAHA.104.507699
    • Carniel E, Taylor MR, Sinagra G, Di Lenarda A, Ku L, Fain PR, et al. Alpha-myosin heavy chain: A sarcomeric gene associated with dilated and hypertrophic phenotypes of cardiomyopathy. Circulation 2005;112(1):54-59. 10.1161/CIRCULATIONAHA.104.507699
    • (2005) Circulation , vol.112 , Issue.1 , pp. 54-59
    • Carniel, E.1    Taylor, M.R.2    Sinagra, G.3    Di Lenarda, A.4    Ku, L.5    Fain, P.R.6
  • 38
    • 0030685743 scopus 로고    scopus 로고
    • Changes in gene expression in the intact human heart. Downregulation of alpha-myosin heavy chain in hypertrophied, failing ventricular myocardium
    • 1:CAS:528:DyaK2sXnt1GgsLc%3D
    • Lowes BD, Minobe W, Abraham WT, Rizeq MN, Bohlmeyer TJ, Quaife RA, et al. Changes in gene expression in the intact human heart. Downregulation of alpha-myosin heavy chain in hypertrophied, failing ventricular myocardium. J Clin Invest 1997;100(9):2315-2324. 1:CAS:528:DyaK2sXnt1GgsLc%3D
    • (1997) J Clin Invest , vol.100 , Issue.9 , pp. 2315-2324
    • Lowes, B.D.1    Minobe, W.2    Abraham, W.T.3    Rizeq, M.N.4    Bohlmeyer, T.J.5    Quaife, R.A.6
  • 39
    • 0030671503 scopus 로고    scopus 로고
    • Myosin heavy chain gene expression in human heart failure
    • 1:CAS:528:DyaK2sXnt1Ggsbs%3D
    • Nakao K, Minobe W, Roden R, Bristow MR, Leinwand LA. Myosin heavy chain gene expression in human heart failure. J Clin Invest 1997;100(9):2362-2370. 1:CAS:528:DyaK2sXnt1Ggsbs%3D
    • (1997) J Clin Invest , vol.100 , Issue.9 , pp. 2362-2370
    • Nakao, K.1    Minobe, W.2    Roden, R.3    Bristow, M.R.4    Leinwand, L.A.5
  • 40
    • 0242585474 scopus 로고    scopus 로고
    • Coordinate changes in Myosin heavy chain isoform gene expression are selectively associated with alterations in dilated cardiomyopathy phenotype
    • 1:CAS:528:DC%2BD3sXps1Wkuw%3D%3D
    • Abraham WT, Gilbert EM, Lowes BD, Minobe WA, Larrabee P, Roden RL, et al. Coordinate changes in Myosin heavy chain isoform gene expression are selectively associated with alterations in dilated cardiomyopathy phenotype. Mol Med 2002;8(11):750-760. 1:CAS:528:DC%2BD3sXps1Wkuw%3D%3D
    • (2002) Mol Med , vol.8 , Issue.11 , pp. 750-760
    • Abraham, W.T.1    Gilbert, E.M.2    Lowes, B.D.3    Minobe, W.A.4    Larrabee, P.5    Roden, R.L.6
  • 41
    • 0345806493 scopus 로고    scopus 로고
    • Microarray gene expression profiles in dilated and hypertrophic cardiomyopathic end-stage heart failure
    • 1:CAS:528:DC%2BD38XmsFait74%3D
    • Hwang JJ, Allen PD, Tseng GC, Lam CW, Fananapazir L, Dzau VJ, et al. Microarray gene expression profiles in dilated and hypertrophic cardiomyopathic end-stage heart failure. Physiol Genomics 2002;10(1):31-44. 1:CAS:528:DC%2BD38XmsFait74%3D
    • (2002) Physiol Genomics , vol.10 , Issue.1 , pp. 31-44
    • Hwang, J.J.1    Allen, P.D.2    Tseng, G.C.3    Lam, C.W.4    Fananapazir, L.5    Dzau, V.J.6
  • 42
    • 4544372627 scopus 로고    scopus 로고
    • The Ku protein complex interacts with YY1, is up-regulated in human heart failure, and represses alpha myosin heavy-chain gene expression
    • 10.1128/MCB.24.19.8705-8715.2004
    • Sucharov CC, Helmke SM, Langer SJ, Perryman MB, Bristow M, Leinwand L. The Ku protein complex interacts with YY1, is up-regulated in human heart failure, and represses alpha myosin heavy-chain gene expression. Mol Cell Biol 2004;24(19):8705-8715. 10.1128/MCB.24.19.8705-8715.2004
    • (2004) Mol Cell Biol , vol.24 , Issue.19 , pp. 8705-8715
    • Sucharov, C.C.1    Helmke, S.M.2    Langer, S.J.3    Perryman, M.B.4    Bristow, M.5    Leinwand, L.6
  • 43
    • 0030709438 scopus 로고    scopus 로고
    • Molecular remodeling of cardiac contractile function
    • 1:CAS:528:DyaK2sXnsVClu7Y%3D
    • James J, Robbins J. Molecular remodeling of cardiac contractile function. Am J Physiol 1997;273(5 Pt 2):H2105-2118. 1:CAS:528:DyaK2sXnsVClu7Y%3D
    • (1997) Am J Physiol , vol.273 , Issue.5 PART 2
    • James, J.1    Robbins, J.2
  • 44
    • 17744416349 scopus 로고    scopus 로고
    • Changes in essential myosin light chain isoform expression provide a molecular basis for isometric force regulation in the failing human heart
    • 10.1006/jmcc.1996.0353
    • Morano I, Hadicke K, Haase H, Bohm M, Erdmann E, Schaub MC. Changes in essential myosin light chain isoform expression provide a molecular basis for isometric force regulation in the failing human heart. J Mol Cell Cardiol 1997;29(4):1177-1187. 10.1006/jmcc.1996.0353
    • (1997) J Mol Cell Cardiol , vol.29 , Issue.4 , pp. 1177-1187
    • Morano, I.1    Hadicke, K.2    Haase, H.3    Bohm, M.4    Erdmann, E.5    Schaub, M.C.6
  • 45
    • 0030038230 scopus 로고    scopus 로고
    • Regulation of human heart contractility by essential myosin light chain isoforms
    • 1:CAS:528:DyaK28XksFCltrg%3D
    • Morano M, Zacharzowski U, Maier M, Lange PE, Alexi-Meskishvili V, Haase H, et al. Regulation of human heart contractility by essential myosin light chain isoforms. J Clin Invest 1996;98(2):467-473. 1:CAS:528:DyaK28XksFCltrg%3D
    • (1996) J Clin Invest , vol.98 , Issue.2 , pp. 467-473
    • Morano, M.1    Zacharzowski, U.2    Maier, M.3    Lange, P.E.4    Alexi-Meskishvili, V.5    Haase, H.6
  • 46
    • 0000266364 scopus 로고    scopus 로고
    • Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms
    • 10.1016/S0008-6363(97)00258-7
    • Schaub MC, Hefti MA, Zuellig RA, Morano I. Modulation of contractility in human cardiac hypertrophy by myosin essential light chain isoforms. Cardiovasc Res 1998;37(2):381-404. 10.1016/S0008-6363(97)00258-7
    • (1998) Cardiovasc Res , vol.37 , Issue.2 , pp. 381-404
    • Schaub, M.C.1    Hefti, M.A.2    Zuellig, R.A.3    Morano, I.4
  • 47
    • 0030976482 scopus 로고    scopus 로고
    • Different actin affinities of human cardiac essential myosin light chain isoforms
    • 10.1016/S0014-5793(97)00390-6
    • Morano I, Haase H. Different actin affinities of human cardiac essential myosin light chain isoforms. FEBS Lett 1997;408(1):71-74. 10.1016/ S0014-5793(97)00390-6
    • (1997) FEBS Lett , vol.408 , Issue.1 , pp. 71-74
    • Morano, I.1    Haase, H.2
  • 48
    • 0035806920 scopus 로고    scopus 로고
    • Effects of calcium, inorganic phosphate, and pH on isometric force in single skinned cardiomyocytes from donor and failing human hearts
    • 1:STN:280:DC%2BD3MvpvFOnsw%3D%3D
    • van der Velden J, Klein LJ, Zaremba R, Boontje NM, Huybregts MA, Stooker W, et al. Effects of calcium, inorganic phosphate, and pH on isometric force in single skinned cardiomyocytes from donor and failing human hearts. Circulation 2001;104(10):1140-1146. 1:STN:280:DC%2BD3MvpvFOnsw%3D%3D
    • (2001) Circulation , vol.104 , Issue.10 , pp. 1140-1146
    • van der Velden, J.1    Klein, L.J.2    Zaremba, R.3    Boontje, N.M.4    Huybregts, M.A.5    Stooker, W.6
  • 49
    • 0037216694 scopus 로고    scopus 로고
    • Increased Ca2+-sensitivity of the contractile apparatus in end-stage human heart failure results from altered phosphorylation of contractile proteins
    • 1:CAS:528:DC%2BD38XpslSlsrg%3D
    • van der Velden J, Papp Z, Zaremba R, Boontje NM, de Jong JW, Owen VJ, et al. Increased Ca2+-sensitivity of the contractile apparatus in end-stage human heart failure results from altered phosphorylation of contractile proteins. Cardiovasc Res 2003;57(1):37-47. 1:CAS:528:DC%2BD38XpslSlsrg%3D
    • (2003) Cardiovasc Res , vol.57 , Issue.1 , pp. 37-47
    • van der Velden, J.1    Papp, Z.2    Zaremba, R.3    Boontje, N.M.4    de Jong, J.W.5    Owen, V.J.6
  • 50
    • 0023762259 scopus 로고
    • Increased calcium sensitivity of chemically skinned human atria by myosin light chain kinase
    • 10.1007/BF02005820
    • Morano I, Bachle-Stolz C, Katus A, Ruegg JC. Increased calcium sensitivity of chemically skinned human atria by myosin light chain kinase. Basic Res Cardiol 1988;83(4):350-359. 10.1007/BF02005820
    • (1988) Basic Res Cardiol , vol.83 , Issue.4 , pp. 350-359
    • Morano, I.1    Bachle-Stolz, C.2    Katus, A.3    Ruegg, J.C.4
  • 51
    • 4944235675 scopus 로고    scopus 로고
    • Passive stiffness changes caused by upregulation of compliant titin isoforms in human dilated cardiomyopathy hearts
    • 10.1161/01.RES.0000143901.37063.2f
    • Makarenko I, Opitz CA, Leake MC, Neagoe C, Kulke M, Gwathmey JK, et al. Passive stiffness changes caused by upregulation of compliant titin isoforms in human dilated cardiomyopathy hearts. Circ Res 2004;95(7):708-716. 10.1161/01.RES.0000143901.37063.2f
    • (2004) Circ Res , vol.95 , Issue.7 , pp. 708-716
    • Makarenko, I.1    Opitz, C.A.2    Leake, M.C.3    Neagoe, C.4    Kulke, M.5    Gwathmey, J.K.6
  • 52
    • 0242331661 scopus 로고    scopus 로고
    • Damped elastic recoil of the titin spring in myofibrils of human myocardium
    • 10.1073/pnas.2133733100
    • Opitz CA, Kulke M, Leake MC, Neagoe C, Hinssen H, Hajjar RJ, et al. Damped elastic recoil of the titin spring in myofibrils of human myocardium. Proc Natl Acad Sci USA 2003;100(22):12688-12693. 10.1073/ pnas.2133733100
    • (2003) Proc Natl Acad Sci USA , vol.100 , Issue.22 , pp. 12688-12693
    • Opitz, C.A.1    Kulke, M.2    Leake, M.C.3    Neagoe, C.4    Hinssen, H.5    Hajjar, R.J.6
  • 53
    • 0037056083 scopus 로고    scopus 로고
    • Titin isoform switch in ischemic human heart disease
    • 10.1161/01.CIR.0000029803.93022.93
    • Neagoe C, Kulke M, del Monte F, Gwathmey JK, de Tombe PP, Hajjar RJ, et al. Titin isoform switch in ischemic human heart disease. Circulation 2002;106(11):1333-1341. 10.1161/01.CIR.0000029803.93022.93
    • (2002) Circulation , vol.106 , Issue.11 , pp. 1333-1341
    • Neagoe, C.1    Kulke, M.2    del Monte, F.3    Gwathmey, J.K.4    de Tombe, P.P.5    Hajjar, R.J.6
  • 54
    • 3142672018 scopus 로고    scopus 로고
    • Altered titin expression, myocardial stiffness, and left ventricular function in patients with dilated cardiomyopathy
    • 10.1161/01.CIR.0000135591.37759.AF
    • Nagueh SF, Shah G, Wu Y, Torre-Amione G, King NM, Lahmers S, et al. Altered titin expression, myocardial stiffness, and left ventricular function in patients with dilated cardiomyopathy. Circulation 2004;110(2):155-162. 10.1161/01.CIR.0000135591.37759.AF
    • (2004) Circulation , vol.110 , Issue.2 , pp. 155-162
    • Nagueh, S.F.1    Shah, G.2    Wu, Y.3    Torre-Amione, G.4    King, N.M.5    Lahmers, S.6
  • 56
    • 0028339341 scopus 로고
    • Titin, myosin light chains and C-protein in the developing and failing human heart
    • 10.1006/jmcc.1994.1045
    • Morano I, Hadicke K, Grom S, Koch A, Schwinger RH, Bohm M, et al. Titin, myosin light chains and C-protein in the developing and failing human heart. J Mol Cell Cardiol 1994;26(3):361-368. 10.1006/jmcc.1994.1045
    • (1994) J Mol Cell Cardiol , vol.26 , Issue.3 , pp. 361-368
    • Morano, I.1    Hadicke, K.2    Grom, S.3    Koch, A.4    Schwinger, R.H.5    Bohm, M.6
  • 57
    • 0036793597 scopus 로고    scopus 로고
    • It takes "heart" to win: What makes the heart powerful?
    • 12270954
    • McDonald KS, Herron TJ. It takes "heart" to win: What makes the heart powerful? News Physiol Sci 2002;17:185-190. 12270954
    • (2002) News Physiol Sci , vol.17 , pp. 185-190
    • McDonald, K.S.1    Herron, T.J.2
  • 58
  • 59
    • 0019995903 scopus 로고
    • Altered myosin isozyme patterns from pressure-overloaded and thyrotoxic hypertrophied rabbit hearts
    • 1:STN:280:Bi2B3cbgtVw%3D
    • Litten RZ, 3rd, Martin BJ, Low RB, Alpert NR. Altered myosin isozyme patterns from pressure-overloaded and thyrotoxic hypertrophied rabbit hearts. Circ Res 1982;50(6):856-864. 1:STN:280:Bi2B3cbgtVw%3D
    • (1982) Circ Res , vol.50 , Issue.6 , pp. 856-864
    • Litten III, R.Z.1    Martin, B.J.2    Low, R.B.3    Alpert, N.R.4
  • 60
    • 0031902620 scopus 로고    scopus 로고
    • Functional characterization of cardiac myosin isoforms
    • 10.2170/jjphysiol.48.173
    • Sugiura S, Yamashita H. Functional characterization of cardiac myosin isoforms. Jpn J Physiol 1998;48(3):173-179. 10.2170/jjphysiol.48.173
    • (1998) Jpn J Physiol , vol.48 , Issue.3 , pp. 173-179
    • Sugiura, S.1    Yamashita, H.2
  • 61
    • 9744230560 scopus 로고    scopus 로고
    • Cardiac myosin isoforms from different species have unique enzymatic and mechanical properties
    • 10.1021/bi0495329
    • Malmqvist UP, Aronshtam A, Lowey S. Cardiac myosin isoforms from different species have unique enzymatic and mechanical properties. Biochemistry 2004;43(47):15058-15065. 10.1021/bi0495329
    • (2004) Biochemistry , vol.43 , Issue.47 , pp. 15058-15065
    • Malmqvist, U.P.1    Aronshtam, A.2    Lowey, S.3
  • 62
    • 0034721806 scopus 로고    scopus 로고
    • Strongly binding myosin crossbridges regulate loaded shortening and power output in cardiac myocytes
    • 1:CAS:528:DC%2BD3cXnvVOlu70%3D
    • McDonald KS, Moss RL. Strongly binding myosin crossbridges regulate loaded shortening and power output in cardiac myocytes. Circ Res 2000;87(9):768-773. 1:CAS:528:DC%2BD3cXnvVOlu70%3D
    • (2000) Circ Res , vol.87 , Issue.9 , pp. 768-773
    • McDonald, K.S.1    Moss, R.L.2
  • 63
    • 0032533986 scopus 로고    scopus 로고
    • Role of myosin heavy chain composition in kinetics of force development and relaxation in rat myocardium
    • 1:CAS:528:DyaK1cXotFCitrc%3D
    • Fitzsimons DP, Patel JR, Moss RL. Role of myosin heavy chain composition in kinetics of force development and relaxation in rat myocardium. J Physiol 1998;513 (Pt 1):171-183. 1:CAS:528:DyaK1cXotFCitrc%3D
    • (1998) J Physiol , vol.513 , Issue.PART 1 , pp. 171-183
    • Fitzsimons, D.P.1    Patel, J.R.2    Moss, R.L.3
  • 64
    • 0028261701 scopus 로고
    • Single myosin molecule mechanics: Piconewton forces and nanometre steps
    • 10.1038/368113a0
    • Finer JT, Simmons RM, Spudich JA. Single myosin molecule mechanics: Piconewton forces and nanometre steps. Nature 1994;368(6467):113-119. 10.1038/368113a0
    • (1994) Nature , vol.368 , Issue.6467 , pp. 113-119
    • Finer, J.T.1    Simmons, R.M.2    Spudich, J.A.3
  • 65
    • 0025881496 scopus 로고
    • Protein friction exerted by motor enzymes through a weak-binding interaction
    • 1:CAS:528:DyaK3MXmtVWgtbs%3D
    • Tawada K, Sekimoto K. Protein friction exerted by motor enzymes through a weak-binding interaction. J Theor Biol 1991;150(2):193-200. 1:CAS:528:DyaK3MXmtVWgtbs%3D
    • (1991) J Theor Biol , vol.150 , Issue.2 , pp. 193-200
    • Tawada, K.1    Sekimoto, K.2
  • 66
    • 0026006251 scopus 로고
    • Equilibrium muscle cross-bridge behavior. Theoretical considerations. II. Model describing the behavior of strongly-binding cross-bridges when both heads of myosin bind to the actin filament
    • 1:CAS:528:DyaK3MXlvVSgtrw%3D
    • Schoenberg M. Equilibrium muscle cross-bridge behavior. Theoretical considerations. II. Model describing the behavior of strongly-binding cross-bridges when both heads of myosin bind to the actin filament. Biophys J 1991;60(3):679-689. 1:CAS:528:DyaK3MXlvVSgtrw%3D
    • (1991) Biophys J , vol.60 , Issue.3 , pp. 679-689
    • Schoenberg, M.1
  • 67
    • 12344324461 scopus 로고    scopus 로고
    • Impact of beta-myosin heavy chain isoform expression on cross-bridge cycling kinetics
    • 1:CAS:528:DC%2BD2MXhsFelsrs%3D
    • Rundell VL, Manaves V, Martin AF, de Tombe PP. Impact of beta-myosin heavy chain isoform expression on cross-bridge cycling kinetics. Am J Physiol Heart Circ Physiol 2005;288(2):H896-903. 1:CAS:528:DC%2BD2MXhsFelsrs%3D
    • (2005) Am J Physiol Heart Circ Physiol , vol.288 , Issue.2
    • Rundell, V.L.1    Manaves, V.2    Martin, A.F.3    de Tombe, P.P.4
  • 68
    • 0026782733 scopus 로고
    • Sliding velocity of isolated rabbit cardiac myosin correlates with isozyme distribution
    • 1:CAS:528:DyaK38Xls1ymsro%3D
    • Yamashita H, Sugiura S, Serizawa T, Sugimoto T, Iizuka M, Katayama E, et al. Sliding velocity of isolated rabbit cardiac myosin correlates with isozyme distribution. Am J Physiol 1992;263(2 Pt 2):H464-472. 1:CAS:528:DyaK38Xls1ymsro%3D
    • (1992) Am J Physiol , vol.263 , Issue.2 PART 2
    • Yamashita, H.1    Sugiura, S.2    Serizawa, T.3    Sugimoto, T.4    Iizuka, M.5    Katayama, E.6
  • 69
    • 0032104084 scopus 로고    scopus 로고
    • Comparison of unitary displacements and forces between 2 cardiac myosin isoforms by the optical trap technique: Molecular basis for cardiac adaptation
    • 1:CAS:528:DyaK1cXjslSjtrs%3D
    • Sugiura S, Kobayakawa N, Fujita H, Yamashita H, Momomura S, Chaen S, et al. Comparison of unitary displacements and forces between 2 cardiac myosin isoforms by the optical trap technique: Molecular basis for cardiac adaptation. Circ Res 1998;82(10):1029-1034. 1:CAS:528:DyaK1cXjslSjtrs%3D
    • (1998) Circ Res , vol.82 , Issue.10 , pp. 1029-1034
    • Sugiura, S.1    Kobayakawa, N.2    Fujita, H.3    Yamashita, H.4    Momomura, S.5    Chaen, S.6
  • 70
    • 0033198519 scopus 로고    scopus 로고
    • Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms
    • 1:CAS:528:DyaK1MXmslGjsbo%3D
    • Palmiter KA, Tyska MJ, Dupuis DE, Alpert NR, Warshaw DM. Kinetic differences at the single molecule level account for the functional diversity of rabbit cardiac myosin isoforms. J Physiol 1999;519 (Pt 3):669-678.
    • (1999) J Physiol , vol.519 , Issue.PART 3 , pp. 669-678
    • Palmiter, K.A.1    Tyska, M.J.2    Dupuis, D.E.3    Alpert, N.R.4    Warshaw, D.M.5
  • 71
    • 0029099958 scopus 로고
    • Force-velocity relations of rat cardiac myosin isozymes sliding on algal cell actin cables in vitro
    • 7640292
    • Sugiura S, Yamashita H, Sata M, Momomura S, Serizawa T, Oiwa K, et al. Force-velocity relations of rat cardiac myosin isozymes sliding on algal cell actin cables in vitro. Biochim Biophys Acta 1995;1231(1):69-75. 7640292
    • (1995) Biochim Biophys Acta , vol.1231 , Issue.1 , pp. 69-75
    • Sugiura, S.1    Yamashita, H.2    Sata, M.3    Momomura, S.4    Serizawa, T.5    Oiwa, K.6
  • 72
    • 0014103605 scopus 로고
    • ATPase activity of myosin correlated with speed of muscle shortening
    • 4227924
    • Barany M. ATPase activity of myosin correlated with speed of muscle shortening. J Gen Physiol 1967;50(6):(Suppl):197-218. 4227924
    • (1967) J Gen Physiol , vol.50 , Issue.6 SUPPL. , pp. 197-218
    • Barany, M.1
  • 73
    • 0026019522 scopus 로고
    • Energetics of isometric force development in control and volume-overload human myocardium. Comparison with animal species
    • 1:STN:280:By2D2snlslM%3D
    • Hasenfuss G, Mulieri LA, Blanchard EM, Holubarsch C, Leavitt BJ, Ittleman F, et al. Energetics of isometric force development in control and volume-overload human myocardium. Comparison with animal species. Circ Res 1991;68(3):836-846. 1:STN:280:By2D2snlslM%3D
    • (1991) Circ Res , vol.68 , Issue.3 , pp. 836-846
    • Hasenfuss, G.1    Mulieri, L.A.2    Blanchard, E.M.3    Holubarsch, C.4    Leavitt, B.J.5    Ittleman, F.6
  • 74
    • 0026721368 scopus 로고
    • Contractile protein function in failing and nonfailing human myocardium
    • 1:CAS:528:DyaK3sXnvVemtg%3D%3D
    • Hasenfuss G, Mulieri LA, Leavitt BJ, Allen PD, Holubarsch C, Just H, et al. Contractile protein function in failing and nonfailing human myocardium. Basic Res Cardiol 1992;87 (Suppl 1):107-116. 1:CAS:528:DyaK3sXnvVemtg%3D%3D
    • (1992) Basic Res Cardiol , vol.87 , Issue.SUPPL. 1 , pp. 107-116
    • Hasenfuss, G.1    Mulieri, L.A.2    Leavitt, B.J.3    Allen, P.D.4    Holubarsch, C.5    Just, H.6
  • 75
    • 0021916285 scopus 로고
    • The economy of isometric force development, myosin isoenzyme pattern and myofibrillar ATPase activity in normal and hypothyroid rat myocardium
    • 1:STN:280:BiqD1MbnsFc%3D
    • Holubarsch C, Goulette RP, Litten RZ, Martin BJ, Mulieri LA, Alpert NR. The economy of isometric force development, myosin isoenzyme pattern and myofibrillar ATPase activity in normal and hypothyroid rat myocardium. Circ Res 1985;56(1):78-86. 1:STN:280:BiqD1MbnsFc%3D
    • (1985) Circ Res , vol.56 , Issue.1 , pp. 78-86
    • Holubarsch, C.1    Goulette, R.P.2    Litten, R.Z.3    Martin, B.J.4    Mulieri, L.A.5    Alpert, N.R.6
  • 76
    • 0020471098 scopus 로고
    • Heat, mechanics, and myosin ATPase in normal and hypertrophied heart muscle
    • 1:CAS:528:DyaL38XhtVWktbk%3D
    • Alpert NR, Mulieri LA. Heat, mechanics, and myosin ATPase in normal and hypertrophied heart muscle. Fed Proc 1982;41(2):192-198. 1:CAS:528:DyaL38XhtVWktbk%3D
    • (1982) Fed Proc , vol.41 , Issue.2 , pp. 192-198
    • Alpert, N.R.1    Mulieri, L.A.2
  • 77
    • 0034711237 scopus 로고    scopus 로고
    • The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever
    • 10.1074/jbc.M006438200
    • Warshaw DM, Guilford WH, Freyzon Y, Krementsova E, Palmiter KA, Tyska MJ, et al. The light chain binding domain of expressed smooth muscle heavy meromyosin acts as a mechanical lever. J Biol Chem 2000;275(47):37167-37172. 10.1074/jbc.M006438200
    • (2000) J Biol Chem , vol.275 , Issue.47 , pp. 37167-37172
    • Warshaw, D.M.1    Guilford, W.H.2    Freyzon, Y.3    Krementsova, E.4    Palmiter, K.A.5    Tyska, M.J.6
  • 79
    • 20644440418 scopus 로고    scopus 로고
    • The kinase domain of titin controls muscle gene expression and protein turnover
    • 10.1126/science.1110463
    • Lange S, Xiang F, Yakovenko A, Vihola A, Hackman P, Rostkova E, et al. The kinase domain of titin controls muscle gene expression and protein turnover. Science 2005;308(5728):1599-1603. 10.1126/science.1110463
    • (2005) Science , vol.308 , Issue.5728 , pp. 1599-1603
    • Lange, S.1    Xiang, F.2    Yakovenko, A.3    Vihola, A.4    Hackman, P.5    Rostkova, E.6
  • 80
    • 0030052266 scopus 로고    scopus 로고
    • A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy
    • 1:CAS:528:DyaK28Xotlagug%3D%3D
    • Freiburg A, Gautel M. A molecular map of the interactions between titin and myosin-binding protein C. Implications for sarcomeric assembly in familial hypertrophic cardiomyopathy. Eur J Biochem 1996;235(1/ 2):317-323. 1:CAS:528:DyaK28Xotlagug%3D%3D
    • (1996) Eur J Biochem , vol.235 , Issue.1-2 , pp. 317-323
    • Freiburg, A.1    Gautel, M.2
  • 81
    • 0029823455 scopus 로고    scopus 로고
    • Titin develops restoring force in rat cardiac myocytes
    • 1:CAS:528:DyaK28XlsVOns7s%3D
    • Helmes M, Trombitas K, Granzier H. Titin develops restoring force in rat cardiac myocytes. Circ Res 1996;79(3):619-626. 1:CAS:528:DyaK28XlsVOns7s%3D
    • (1996) Circ Res , vol.79 , Issue.3 , pp. 619-626
    • Helmes, M.1    Trombitas, K.2    Granzier, H.3
  • 82
    • 0029886571 scopus 로고    scopus 로고
    • Elastic properties of single titin molecules made visible through fluorescent F-actin binding
    • 10.1006/bbrc.1996.0624
    • Kellermayer MS, Granzier HL. Elastic properties of single titin molecules made visible through fluorescent F-actin binding. Biochem Biophys Res Commun 1996;221(3):491-497. 10.1006/bbrc.1996.0624
    • (1996) Biochem Biophys Res Commun , vol.221 , Issue.3 , pp. 491-497
    • Kellermayer, M.S.1    Granzier, H.L.2
  • 83
    • 0037192845 scopus 로고    scopus 로고
    • Molecular mechanics of cardiac titin's PEVK and N2B spring elements
    • 10.1074/jbc.M200356200
    • Watanabe K, Nair P, Labeit D, Kellermayer MS, Greaser M, Labeit S, et al. Molecular mechanics of cardiac titin's PEVK and N2B spring elements. J Biol Chem 2002;277(13):11549-11558. 10.1074/jbc.M200356200
    • (2002) J Biol Chem , vol.277 , Issue.13 , pp. 11549-11558
    • Watanabe, K.1    Nair, P.2    Labeit, D.3    Kellermayer, M.S.4    Greaser, M.5    Labeit, S.6
  • 84
    • 0037194788 scopus 로고    scopus 로고
    • Reverse engineering of the giant muscle protein titin
    • 10.1038/nature00938
    • Li H, Linke WA, Oberhauser AF, Carrion-Vazquez M, Kerkvliet JG, Lu H, et al. Reverse engineering of the giant muscle protein titin. Nature 2002;418(6901):998-1002. 10.1038/nature00938
    • (2002) Nature , vol.418 , Issue.6901 , pp. 998-1002
    • Li, H.1    Linke, W.A.2    Oberhauser, A.F.3    Carrion-Vazquez, M.4    Kerkvliet, J.G.5    Lu, H.6
  • 85
    • 0036443942 scopus 로고    scopus 로고
    • PEVK domain of titin: An entropic spring with actin-binding properties
    • 1:CAS:528:DC%2BD38XksVygsLs%3D
    • Linke WA, Kulke M, Li H, Fujita-Becker S, Neagoe C, Manstein DJ, et al. PEVK domain of titin: An entropic spring with actin-binding properties. J Struct Biol 2002;137(1/2):194-205. 1:CAS:528:DC%2BD38XksVygsLs%3D
    • (2002) J Struct Biol , vol.137 , Issue.1-2 , pp. 194-205
    • Linke, W.A.1    Kulke, M.2    Li, H.3    Fujita-Becker, S.4    Neagoe, C.5    Manstein, D.J.6
  • 86
    • 0037056103 scopus 로고    scopus 로고
    • Changes in titin isoform expression in pacing-induced cardiac failure give rise to increased passive muscle stiffness
    • 10.1161/01.CIR.0000029804.61510.02
    • Wu Y, Bell SP, Trombitas K, Witt CC, Labeit S, LeWinter MM, et al. Changes in titin isoform expression in pacing-induced cardiac failure give rise to increased passive muscle stiffness. Circulation 2002;106(11):1384-1389. 10.1161/01.CIR.0000029804.61510.02
    • (2002) Circulation , vol.106 , Issue.11 , pp. 1384-1389
    • Wu, Y.1    Bell, S.P.2    Trombitas, K.3    Witt, C.C.4    Labeit, S.5    LeWinter, M.M.6
  • 87
    • 0002854866 scopus 로고
    • Polypeptide chains of intermediate molecular weight in myosin preparations
    • 10.1016/0014-5793(71)80075-3
    • Starr R, Offer G. Polypeptide chains of intermediate molecular weight in myosin preparations. FEBS Lett 1971;15(1):40-44. 10.1016/ 0014-5793(71)80075-3
    • (1971) FEBS Lett , vol.15 , Issue.1 , pp. 40-44
    • Starr, R.1    Offer, G.2
  • 88
    • 0033612182 scopus 로고    scopus 로고
    • Cardiac myosin binding protein
    • 1:CAS:528:DyaK1MXjsVygsr0%3D
    • Winegrad S. Cardiac myosin binding protein C. Circ Res 1999;84(10):1117-1126. 1:CAS:528:DyaK1MXjsVygsr0%3D
    • (1999) C Circ Res , vol.84 , Issue.10 , pp. 1117-1126
    • Winegrad, S.1
  • 89
    • 0022899276 scopus 로고
    • The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle
    • 10.1007/BF01753571
    • Bennett P, Craig R, Starr R, Offer G. The ultrastructural location of C-protein, X-protein and H-protein in rabbit muscle. J Muscle Res Cell Motil 1986;7(6):550-567. 10.1007/BF01753571
    • (1986) J Muscle Res Cell Motil , vol.7 , Issue.6 , pp. 550-567
    • Bennett, P.1    Craig, R.2    Starr, R.3    Offer, G.4
  • 90
    • 0017234893 scopus 로고
    • The location of C-protein in rabbit skeletal muscle
    • 1:STN:280:CSmC2snltVc%3D
    • Craig R, Offer G. The location of C-protein in rabbit skeletal muscle. Proc R Soc Lond B Biol Sci 1976;192(1109):451-461. 1:STN:280:CSmC2snltVc%3D
    • (1976) Proc R Soc Lond B Biol Sci , vol.192 , Issue.1109 , pp. 451-461
    • Craig, R.1    Offer, G.2
  • 91
    • 0016818769 scopus 로고
    • Interaction of C-protein with myosin, myosin rod and light meromyosin
    • 1:CAS:528:DyaE2MXmtVaht7c%3D
    • Moos C, Offer G, Starr R, Bennett P. Interaction of C-protein with myosin, myosin rod and light meromyosin. J Mol Biol 1975;97(1):1-9. 1:CAS:528:DyaE2MXmtVaht7c%3D
    • (1975) J Mol Biol , vol.97 , Issue.1 , pp. 1-9
    • Moos, C.1    Offer, G.2    Starr, R.3    Bennett, P.4
  • 92
    • 0017826080 scopus 로고
    • The interaction of C-protein with heavy meromyosin and subfragment-2
    • 1:CAS:528:DyaE1cXlslGhsrc%3D
    • Starr R, Offer G. The interaction of C-protein with heavy meromyosin and subfragment-2. Biochem J 1978;171(3):813-816. 1:CAS:528:DyaE1cXlslGhsrc%3D
    • (1978) Biochem J , vol.171 , Issue.3 , pp. 813-816
    • Starr, R.1    Offer, G.2
  • 93
    • 0042093724 scopus 로고    scopus 로고
    • Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain
    • 10.1016/S0022-2836(03)00781-2
    • Squire JM, Luther PK, Knupp C. Structural evidence for the interaction of C-protein (MyBP-C) with actin and sequence identification of a possible actin-binding domain. J Mol Biol 2003;331(3):713-724. 10.1016/ S0022-2836(03)00781-2
    • (2003) J Mol Biol , vol.331 , Issue.3 , pp. 713-724
    • Squire, J.M.1    Luther, P.K.2    Knupp, C.3
  • 94
    • 0344736754 scopus 로고    scopus 로고
    • Effect of MyBP-C binding to actin on contractility in heart muscle
    • 10.1085/jgp.200308941
    • Kulikovskaya I, McClellan G, Flavigny J, Carrier L, Winegrad S. Effect of MyBP-C binding to actin on contractility in heart muscle. J Gen Physiol 2003;122(6):761-774. 10.1085/jgp.200308941
    • (2003) J Gen Physiol , vol.122 , Issue.6 , pp. 761-774
    • Kulikovskaya, I.1    McClellan, G.2    Flavigny, J.3    Carrier, L.4    Winegrad, S.5
  • 95
    • 0037131207 scopus 로고    scopus 로고
    • Identification of novel interactions between domains of Myosin binding protein-C that are modulated by hypertrophic cardiomyopathy missense mutations
    • 10.1161/01.RES.0000036750.81083.83
    • Moolman-Smook J, Flashman E, de Lange W, Li Z, Corfield V, Redwood C, et al. Identification of novel interactions between domains of Myosin binding protein-C that are modulated by hypertrophic cardiomyopathy missense mutations. Circ Res 2002;91(8):704-711. 10.1161/ 01.RES.0000036750.81083.83
    • (2002) Circ Res , vol.91 , Issue.8 , pp. 704-711
    • Moolman-Smook, J.1    Flashman, E.2    de Lange, W.3    Li, Z.4    Corfield, V.5    Redwood, C.6
  • 96
    • 2642572455 scopus 로고    scopus 로고
    • Cardiac myosin binding protein C: Its role in physiology and disease
    • 10.1161/01.RES.0000127175.21818.C2
    • Flashman E, Redwood C, Moolman-Smook J, Watkins H. Cardiac myosin binding protein C: Its role in physiology and disease. Circ Res 2004;94(10):1279-1289. 10.1161/01.RES.0000127175.21818.C2
    • (2004) Circ Res , vol.94 , Issue.10 , pp. 1279-1289
    • Flashman, E.1    Redwood, C.2    Moolman-Smook, J.3    Watkins, H.4
  • 97
    • 0030030825 scopus 로고    scopus 로고
    • The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle
    • 1:CAS:528:DyaK28XosVahuw%3D%3D
    • Gilbert R, Kelly MG, Mikawa T, Fischman DA. The carboxyl terminus of myosin binding protein C (MyBP-C, C-protein) specifies incorporation into the A-band of striated muscle. J Cell Sci 1996;109 (Pt 1):101-111. 1:CAS:528:DyaK28XosVahuw%3D%3D
    • (1996) J Cell Sci , vol.109 , Issue.PART 1 , pp. 101-111
    • Gilbert, R.1    Kelly, M.G.2    Mikawa, T.3    Fischman, D.A.4
  • 98
    • 0037155775 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy in cardiac myosin binding protein-C knockout mice
    • 10.1161/01.RES.0000012222.70819.64
    • Harris SP, Bartley CR, Hacker TA, McDonald KS, Douglas PS, Greaser ML, et al. Hypertrophic cardiomyopathy in cardiac myosin binding protein-C knockout mice. Circ Res 2002;90(5):594-601. 10.1161/ 01.RES.0000012222.70819.64
    • (2002) Circ Res , vol.90 , Issue.5 , pp. 594-601
    • Harris, S.P.1    Bartley, C.R.2    Hacker, T.A.3    McDonald, K.S.4    Douglas, P.S.5    Greaser, M.L.6
  • 99
    • 4544268066 scopus 로고    scopus 로고
    • Effect of cardiac myosin-binding protein C on stability of the thick filament
    • 10.1016/j.yjmcc.2004.05.023
    • McClellan G, Kulikovskaya I, Flavigny J, Carrier L, Winegrad S. Effect of cardiac myosin-binding protein C on stability of the thick filament. J Mol Cell Cardiol 2004;37(4):823-835. 10.1016/j.yjmcc.2004.05.023
    • (2004) J Mol Cell Cardiol , vol.37 , Issue.4 , pp. 823-835
    • McClellan, G.1    Kulikovskaya, I.2    Flavigny, J.3    Carrier, L.4    Winegrad, S.5
  • 100
    • 3042721428 scopus 로고    scopus 로고
    • Reduced cross-bridge dependent stiffness of skinned myocardium from mice lacking cardiac myosin binding protein-C
    • 10.1023/B:MCBI.0000041849.60591.45
    • Palmer BM, McConnell BK, Li GH, Seidman CE, Seidman JG, Irving TC, et al. Reduced cross-bridge dependent stiffness of skinned myocardium from mice lacking cardiac myosin binding protein-C. Mol Cell Biochem 2004;263(1/2):73-80. 10.1023/B:MCBI.0000041849.60591.45
    • (2004) Mol Cell Biochem , vol.263 , Issue.1-2 , pp. 73-80
    • Palmer, B.M.1    McConnell, B.K.2    Li, G.H.3    Seidman, C.E.4    Seidman, J.G.5    Irving, T.C.6
  • 101
    • 2442698889 scopus 로고    scopus 로고
    • Role of cardiac myosin binding protein C in sustaining left ventricular systolic stiffening
    • 10.1161/01.RES.0000126898.95550.31
    • Palmer BM, Georgakopoulos D, Janssen PM, Wang Y, Alpert NR, Belardi DF, et al. Role of cardiac myosin binding protein C in sustaining left ventricular systolic stiffening. Circ Res 2004;94(9):1249-1255. 10.1161/ 01.RES.0000126898.95550.31
    • (2004) Circ Res , vol.94 , Issue.9 , pp. 1249-1255
    • Palmer, B.M.1    Georgakopoulos, D.2    Janssen, P.M.3    Wang, Y.4    Alpert, N.R.5    Belardi, D.F.6
  • 102
    • 0142024741 scopus 로고    scopus 로고
    • Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C
    • 10.1161/01.RES.0000096363.85588.9A
    • Korte FS, McDonald KS, Harris SP, Moss RL. Loaded shortening, power output, and rate of force redevelopment are increased with knockout of cardiac myosin binding protein-C. Circ Res 2003;93(8):752-758. 10.1161/ 01.RES.0000096363.85588.9A
    • (2003) Circ Res , vol.93 , Issue.8 , pp. 752-758
    • Korte, F.S.1    McDonald, K.S.2    Harris, S.P.3    Moss, R.L.4
  • 103
    • 0029029027 scopus 로고
    • Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: A modulator of cardiac contraction?
    • 1:CAS:528:DyaK2MXlvVCqsr8%3D
    • Gautel M, Zuffardi O, Freiburg A, Labeit S. Phosphorylation switches specific for the cardiac isoform of myosin binding protein-C: A modulator of cardiac contraction? Embo J 1995;14(9):1952-1960. 1:CAS:528:DyaK2MXlvVCqsr8%3D
    • (1995) Embo J , vol.14 , Issue.9 , pp. 1952-1960
    • Gautel, M.1    Zuffardi, O.2    Freiburg, A.3    Labeit, S.4
  • 104
    • 0037444566 scopus 로고    scopus 로고
    • Troponin I in the murine myocardium: Influence on length-dependent activation and interfilament spacing
    • 1:CAS:528:DC%2BD3sXjt1Slt7g%3D
    • Konhilas JP, Irving TC, Wolska BM, Jweied EE, Martin AF, Solaro RJ, et al. Troponin I in the murine myocardium: Influence on length-dependent activation and interfilament spacing. J Physiol 2003;547(Pt 3):951-961. 1:CAS:528:DC%2BD3sXjt1Slt7g%3D
    • (2003) J Physiol , vol.547 , Issue.PART 3 , pp. 951-961
    • Konhilas, J.P.1    Irving, T.C.2    Wolska, B.M.3    Jweied, E.E.4    Martin, A.F.5    Solaro, R.J.6


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