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Volumn 34, Issue 3-4, 2013, Pages 285-294

Alpha-tropomyosin mutations in inherited cardiomyopathies

Author keywords

Cardiomyopathy; Mutation; Tropomyosin

Indexed keywords

TROPOMYOSIN;

EID: 84890102055     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-013-9358-5     Document Type: Review
Times cited : (79)

References (88)
  • 2
    • 0037407012 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: A paradigm for myocardial energy depletion
    • 10.1016/S0168-9525(03)00081-7 12711218 10.1016/S0168-9525(03)00081-7 1:CAS:528:DC%2BD3sXjtFeqt78%3D
    • Ashrafian H, Redwood C, Blair E, Watkins H (2003) Hypertrophic cardiomyopathy: a paradigm for myocardial energy depletion. Trends Genet 19(5):263-268. doi: 10.1016/S0168-9525(03)00081-7
    • (2003) Trends Genet , vol.19 , Issue.5 , pp. 263-268
    • Ashrafian, H.1    Redwood, C.2    Blair, E.3    Watkins, H.4
  • 3
    • 79951828756 scopus 로고    scopus 로고
    • Enhanced active cross-bridges during diastole: Molecular pathogenesis of tropomyosin's HCM mutations
    • 10.1016/j.bpj.2011.01.001 21320446 10.1016/j.bpj.2011.01.001 1:CAS:528:DC%2BC3MXhvFKgtbg%3D
    • Bai F, Weis A, Takeda AK, Chase PB, Kawai M (2011) Enhanced active cross-bridges during diastole: molecular pathogenesis of tropomyosin's HCM mutations. Biophys J 100(4):1014-1023. doi: 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
  • 4
    • 84867552914 scopus 로고    scopus 로고
    • DCM-related tropomyosin mutants E40K/E54K over-inhibit the actomyosin interaction and lead to a decrease in the number of cycling cross-bridges
    • 10.1371/journal.pone.0047471 23077624 10.1371/journal.pone.0047471 1:CAS:528:DC%2BC38Xhs1Wht7zL
    • Bai F, Groth HL, Kawai M (2012) DCM-related tropomyosin mutants E40K/E54K over-inhibit the actomyosin interaction and lead to a decrease in the number of cycling cross-bridges. PLoS One 7(10):e47471. doi: 10.1371/journal.pone.0047471
    • (2012) PLoS One , vol.7 , Issue.10 , pp. 47471
    • Bai, F.1    Groth, H.L.2    Kawai, M.3
  • 5
    • 84864241713 scopus 로고    scopus 로고
    • Structure of the rigor actin-tropomyosin-myosin complex
    • 10.1016/j.cell.2012.05.037 22817895 10.1016/j.cell.2012.05.037 1:CAS:528:DC%2BC38XhtVyms7jI
    • Behrmann E, Muller M, Penczek PA, Mannherz HG, Manstein DJ, Raunser S (2012) Structure of the rigor actin-tropomyosin-myosin complex. Cell 150(2):327-338. doi: 10.1016/j.cell.2012.05.037
    • (2012) Cell , vol.150 , Issue.2 , pp. 327-338
    • Behrmann, E.1    Muller, M.2    Penczek, P.A.3    Mannherz, H.G.4    Manstein, D.J.5    Raunser, S.6
  • 7
    • 0033851629 scopus 로고    scopus 로고
    • Effect of hypertrophic cardiomyopathy mutations in human cardiac muscle alpha-tropomyosin (Asp175Asn and Glu180Gly) on the regulatory properties of human cardiac troponin determined by in vitro motility assay
    • 10.1006/jmcc.2000.1182 10900175 10.1006/jmcc.2000.1182 1:CAS:528:DC%2BD3cXkvVKksL8%3D
    • Bing W, Knott A, Redwood C, Esposito G, Purcell I, Watkins H, Marston S (2000) Effect of hypertrophic cardiomyopathy mutations in human cardiac muscle alpha-tropomyosin (Asp175Asn and Glu180Gly) on the regulatory properties of human cardiac troponin determined by in vitro motility assay. J Mol Cell Cardiol 32(8):1489-1498. doi: 10.1006/jmcc.2000.1182
    • (2000) J Mol Cell Cardiol , vol.32 , Issue.8 , pp. 1489-1498
    • Bing, W.1    Knott, A.2    Redwood, C.3    Esposito, G.4    Purcell, I.5    Watkins, H.6    Marston, S.7
  • 8
    • 69849090616 scopus 로고    scopus 로고
    • The effect of the dilated cardiomyopathy-causing mutation Glu54Lys of alpha-tropomyosin on actin-myosin interactions during the ATPase cycle
    • 10.1016/j.abb.2009.07.018 19646950 10.1016/j.abb.2009.07.018 1:CAS:528:DC%2BD1MXhtFagurrO
    • Borovikov YS, Karpicheva OE, Avrova SV, Robinson P, Redwood CS (2009a) The effect of the dilated cardiomyopathy-causing mutation Glu54Lys of alpha-tropomyosin on actin-myosin interactions during the ATPase cycle. Arch Biochem Biophys 489(1-2):20-24. doi: 10.1016/j.abb.2009.07.018
    • (2009) Arch Biochem Biophys , vol.489 , Issue.1-2 , pp. 20-24
    • Borovikov, Y.S.1    Karpicheva, O.E.2    Avrova, S.V.3    Robinson, P.4    Redwood, C.S.5
  • 9
    • 62049085300 scopus 로고    scopus 로고
    • Dilated cardiomyopathy mutations in alpha-tropomyosin inhibit its movement during the ATPase cycle
    • 10.1016/j.bbrc.2009.02.054 19222994 10.1016/j.bbrc.2009.02.054 1:CAS:528:DC%2BD1MXjsFahtbY%3D
    • Borovikov YS, Karpicheva OE, Chudakova GA, Robinson P, Redwood CS (2009b) Dilated cardiomyopathy mutations in alpha-tropomyosin inhibit its movement during the ATPase cycle. Biochem Biophys Res Commun 381(3):403-406. doi: 10.1016/j.bbrc.2009.02.054
    • (2009) Biochem Biophys Res Commun , vol.381 , Issue.3 , pp. 403-406
    • Borovikov, Y.S.1    Karpicheva, O.E.2    Chudakova, G.A.3    Robinson, P.4    Redwood, C.S.5
  • 10
    • 79961128342 scopus 로고    scopus 로고
    • The effect of the dilated cardiomyopathy-causing Glu40Lys TPM1 mutation on actin-myosin interactions during the ATPase cycle
    • 10.1016/j.bbrc.2011.06.138 21741356 10.1016/j.bbrc.2011.06.138 1:CAS:528:DC%2BC3MXpvFGhtb4%3D
    • Borovikov YS, Avrova SV, Karpicheva OE, Robinson P, Redwood CS (2011a) The effect of the dilated cardiomyopathy-causing Glu40Lys TPM1 mutation on actin-myosin interactions during the ATPase cycle. Biochem Biophys Res Commun 411(3):496-500. doi: 10.1016/j.bbrc.2011.06.138
    • (2011) Biochem Biophys Res Commun , vol.411 , Issue.3 , pp. 496-500
    • Borovikov, Y.S.1    Avrova, S.V.2    Karpicheva, O.E.3    Robinson, P.4    Redwood, C.S.5
  • 11
    • 79953164261 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy-causing Asp175asn and Glu180gly Tpm1 mutations shift tropomyosin strands further towards the open position during the ATPase cycle
    • 10.1016/j.bbrc.2011.02.139 21376702 10.1016/j.bbrc.2011.02.139 1:CAS:528:DC%2BC3MXkt1Kjt7Y%3D
    • Borovikov YS, Rysev NA, Karpicheva OE, Redwood CS (2011b) Hypertrophic cardiomyopathy-causing Asp175asn and Glu180gly Tpm1 mutations shift tropomyosin strands further towards the open position during the ATPase cycle. Biochem Biophys Res Commun 407(1):197-201. doi: 10.1016/j.bbrc.2011.02.139
    • (2011) Biochem Biophys Res Commun , vol.407 , Issue.1 , pp. 197-201
    • Borovikov, Y.S.1    Rysev, N.A.2    Karpicheva, O.E.3    Redwood, C.S.4
  • 12
    • 0031883848 scopus 로고    scopus 로고
    • A mutant tropomyosin that causes hypertrophic cardiomyopathy is expressed in vivo and associated with an increased calcium sensitivity
    • 9440709 10.1161/01.RES.82.1.106 1:CAS:528:DyaK1cXlsVGhsw%3D%3D
    • Bottinelli R, Coviello DA, Redwood CS, Pellegrino MA, Maron BJ, Spirito P, Watkins H, Reggiani C (1998) A mutant tropomyosin that causes hypertrophic cardiomyopathy is expressed in vivo and associated with an increased calcium sensitivity. Circ Res 82(1):106-115
    • (1998) Circ Res , vol.82 , Issue.1 , pp. 106-115
    • Bottinelli, R.1    Coviello, D.A.2    Redwood, C.S.3    Pellegrino, M.A.4    Maron, B.J.5    Spirito, P.6    Watkins, H.7    Reggiani, C.8
  • 13
    • 26644464382 scopus 로고    scopus 로고
    • Functional consequences of hypertrophic and dilated cardiomyopathy- causing mutations in alpha-tropomyosin
    • 10.1074/jbc.M505014200 16043485 10.1074/jbc.M505014200 1:CAS:528:DC%2BD2MXhtVKitrzP
    • Chang AN, Harada K, Ackerman MJ, Potter JD (2005) Functional consequences of hypertrophic and dilated cardiomyopathy-causing mutations in alpha-tropomyosin. J Biol Chem 280(40):34343-34349. doi: 10.1074/jbc.M505014200
    • (2005) J Biol Chem , vol.280 , Issue.40 , pp. 34343-34349
    • Chang, A.N.1    Harada, K.2    Ackerman, M.J.3    Potter, J.D.4
  • 17
    • 0025040392 scopus 로고
    • A molecular basis for familial hypertrophic cardiomyopathy: A beta cardiac myosin heavy chain gene missense mutation
    • 1975517 10.1016/0092-8674(90)90274-I 1:CAS:528:DyaK3cXmtVGqs7w%3D
    • Geisterfer-Lowrance AA, Kass S, Tanigawa G, Vosberg HP, McKenna W, Seidman CE, Seidman JG (1990) A molecular basis for familial hypertrophic cardiomyopathy: a beta cardiac myosin heavy chain gene missense mutation. Cell 62(5):999-1006
    • (1990) Cell , vol.62 , Issue.5 , pp. 999-1006
    • Geisterfer-Lowrance, A.A.1    Kass, S.2    Tanigawa, G.3    Vosberg, H.P.4    McKenna, W.5    Seidman, C.E.6    Seidman, J.G.7
  • 18
    • 0030933128 scopus 로고    scopus 로고
    • Effects of two familial hypertrophic cardiomyopathy-causing mutations on alpha-tropomyosin structure and function
    • 10.1021/bi962970y 9109674 10.1021/bi962970y 1:STN:280: DyaK2s3mtlOmuw%3D%3D
    • Golitsina N, An Y, Greenfield NJ, Thierfelder L, Iizuka K, Seidman JG, Seidman CE, Lehrer SS, Hitchcock-DeGregori SE (1997) Effects of two familial hypertrophic cardiomyopathy-causing mutations on alpha-tropomyosin structure and function. Biochemistry 36(15):4637-4642. doi: 10.1021/bi962970y
    • (1997) Biochemistry , vol.36 , Issue.15 , pp. 4637-4642
    • Golitsina, N.1    An, Y.2    Greenfield, N.J.3    Thierfelder, L.4    Iizuka, K.5    Seidman, J.G.6    Seidman, C.E.7    Lehrer, S.S.8    Hitchcock-Degregori, S.E.9
  • 19
    • 0034059761 scopus 로고    scopus 로고
    • Regulation of contraction in striated muscle
    • 10747208 1:CAS:528:DC%2BD3cXisFSgsr8%3D
    • Gordon AM, Homsher E, Regnier M (2000) Regulation of contraction in striated muscle. Physiol Rev 80(2):853-924
    • (2000) Physiol Rev , vol.80 , Issue.2 , pp. 853-924
    • Gordon, A.M.1    Homsher, E.2    Regnier, M.3
  • 20
    • 33748323383 scopus 로고    scopus 로고
    • Regulation of cardiac hypertrophy by intracellular signalling pathways
    • 10.1038/nrm1983 16936699 10.1038/nrm1983 1:CAS:528:DC%2BD28Xot1Cqu78%3D
    • Heineke J, Molkentin JD (2006) Regulation of cardiac hypertrophy by intracellular signalling pathways. Nat Rev Mol Cell Biol 7(8):589-600. doi: 10.1038/nrm1983
    • (2006) Nat Rev Mol Cell Biol , vol.7 , Issue.8 , pp. 589-600
    • Heineke, J.1    Molkentin, J.D.2
  • 21
    • 0142149180 scopus 로고    scopus 로고
    • 2+ sensitivity and tropomyosin N-domain flexibility
    • 10.1074/jbc.M303408200 12900417 10.1074/jbc.M303408200 1:CAS:528:DC%2BD3sXot1amsL8%3D
    • 2+ sensitivity and tropomyosin N-domain flexibility. J Biol Chem 278(43):41742-41748. doi: 10.1074/jbc.M303408200
    • (2003) J Biol Chem , vol.278 , Issue.43 , pp. 41742-41748
    • Heller, M.J.1    Nili, M.2    Homsher, E.3    Tobacman, L.S.4
  • 22
    • 77953023261 scopus 로고    scopus 로고
    • Coding sequence rare variants identified in MYBPC3, MYH6, TPM1, TNNC1, and TNNI3 from 312 patients with familial or idiopathic dilated cardiomyopathy
    • 10.1161/CIRCGENETICS.109.912345 20215591 10.1161/CIRCGENETICS.109.912345 1:CAS:528:DC%2BC3cXmvF2murY%3D
    • Hershberger RE, Norton N, Morales A, Li D, Siegfried JD, Gonzalez-Quintana J (2010) Coding sequence rare variants identified in MYBPC3, MYH6, TPM1, TNNC1, and TNNI3 from 312 patients with familial or idiopathic dilated cardiomyopathy. Circ Cardiovasc Genet 3(2):155-161. doi: 10.1161/CIRCGENETICS.109.912345
    • (2010) Circ Cardiovasc Genet , vol.3 , Issue.2 , pp. 155-161
    • Hershberger, R.E.1    Norton, N.2    Morales, A.3    Li, D.4    Siegfried, J.D.5    Gonzalez-Quintana, J.6
  • 24
    • 2442419136 scopus 로고    scopus 로고
    • 2+-induced rolling of tropomyosin in muscle thin filaments: The alpha- and beta-band hypothesis revisited
    • 10.1074/jbc.M308904200 14724287 10.1074/jbc.M308904200 1:CAS:528:DC%2BD2cXivVKgs7k%3D
    • 2+-induced rolling of tropomyosin in muscle thin filaments: the alpha- and beta-band hypothesis revisited. J Biol Chem 279(15):15204-15213. doi: 10.1074/jbc.M308904200
    • (2004) J Biol Chem , vol.279 , Issue.15 , pp. 15204-15213
    • Holthauzen, L.M.1    Correa, F.2    Farah, C.S.3
  • 26
    • 84870918869 scopus 로고    scopus 로고
    • Alpha-tropomyosin with a D175N or E180G mutation in only one chain differs from tropomyosin with mutations in both chains
    • 10.1021/bi301323n 23170982 10.1021/bi301323n 1:CAS:528:DC%2BC38XhslWksbfM
    • Janco M, Kalyva A, Scellini B, Piroddi N, Tesi C, Poggesi C, Geeves MA (2012) Alpha-tropomyosin with a D175N or E180G mutation in only one chain differs from tropomyosin with mutations in both chains. Biochemistry 51(49):9880-9890. doi: 10.1021/bi301323n
    • (2012) Biochemistry , vol.51 , Issue.49 , pp. 9880-9890
    • Janco, M.1    Kalyva, A.2    Scellini, B.3    Piroddi, N.4    Tesi, C.5    Poggesi, C.6    Geeves, M.A.7
  • 27
    • 78650832959 scopus 로고    scopus 로고
    • Targeted amino-terminal acetylation of recombinant proteins in E. Coli
    • 10.1371/journal.pone.0015801 21203426 10.1371/journal.pone.0015801 1:CAS:528:DC%2BC3MXjvVSqsw%3D%3D
    • Johnson M, Coulton AT, Geeves MA, Mulvihill DP (2010) Targeted amino-terminal acetylation of recombinant proteins in E. coli. PLoS One 5(12):e15801. doi: 10.1371/journal.pone.0015801
    • (2010) PLoS One , vol.5 , Issue.12 , pp. 15801
    • Johnson, M.1    Coulton, A.T.2    Geeves, M.A.3    Mulvihill, D.P.4
  • 28
    • 0037454157 scopus 로고    scopus 로고
    • Variable clinical manifestation of a novel missense mutation in the alpha-tropomyosin (TPM1) gene in familial hypertrophic cardiomyopathy
    • 12651045 10.1016/S0735-1097(02)03005-X 1:CAS:528:DC%2BD3sXislejsLg%3D
    • Jongbloed RJ, Marcelis CL, Doevendans PA, Schmeitz-Mulkens JM, Van Dockum WG, Geraedts JP, Smeets HJ (2003) Variable clinical manifestation of a novel missense mutation in the alpha-tropomyosin (TPM1) gene in familial hypertrophic cardiomyopathy. J Am Coll Cardiol 41(6):981-986
    • (2003) J Am Coll Cardiol , vol.41 , Issue.6 , pp. 981-986
    • Jongbloed, R.J.1    Marcelis, C.L.2    Doevendans, P.A.3    Schmeitz-Mulkens, J.M.4    Van Dockum, W.G.5    Geraedts, J.P.6    Smeets, H.J.7
  • 29
    • 0035830394 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy caused by a novel alpha-tropomyosin mutation (V95A) is associated with mild cardiac phenotype, abnormal calcium binding to troponin, abnormal myosin cycling, and poor prognosis
    • 11136687 10.1161/01.CIR.103.1.65 1:CAS:528:DC%2BD3MXhtFant7w%3D
    • Karibe A, Tobacman LS, Strand J, Butters C, Back N, Bachinski LL, Arai AE, Ortiz A, Roberts R, Homsher E, Fananapazir L (2001) Hypertrophic cardiomyopathy caused by a novel alpha-tropomyosin mutation (V95A) is associated with mild cardiac phenotype, abnormal calcium binding to troponin, abnormal myosin cycling, and poor prognosis. Circulation 103(1):65-71
    • (2001) Circulation , vol.103 , Issue.1 , pp. 65-71
    • Karibe, A.1    Tobacman, L.S.2    Strand, J.3    Butters, C.4    Back, N.5    Bachinski, L.L.6    Arai, A.E.7    Ortiz, A.8    Roberts, R.9    Homsher, E.10    Fananapazir, L.11
  • 30
    • 33748291631 scopus 로고    scopus 로고
    • Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation
    • 10.1007/s10974-006-9075-4 16909198 10.1007/s10974-006-9075-4
    • Kawai M, Ishiwata S (2006) Use of thin filament reconstituted muscle fibres to probe the mechanism of force generation. J Muscle Res Cell Motil 27(5-7):455-468. doi: 10.1007/s10974-006-9075-4
    • (2006) J Muscle Res Cell Motil , vol.27 , Issue.5-7 , pp. 455-468
    • Kawai, M.1    Ishiwata, S.2
  • 32
    • 10044280728 scopus 로고    scopus 로고
    • Effects of two familial hypertrophic cardiomyopathy mutations in alpha-tropomyosin, Asp175Asn and Glu180Gly, on the thermal unfolding of actin-bound tropomyosin
    • 10.1529/biophysj.104.048793 15454401 10.1529/biophysj.104.048793 1:CAS:528:DC%2BD2cXhtVOmtbnK
    • Kremneva E, Boussouf S, Nikolaeva O, Maytum R, Geeves MA, Levitsky DI (2004) Effects of two familial hypertrophic cardiomyopathy mutations in alpha-tropomyosin, Asp175Asn and Glu180Gly, on the thermal unfolding of actin-bound tropomyosin. Biophys J 87(6):3922-3933. doi: 10.1529/biophysj.104. 048793
    • (2004) Biophys J , vol.87 , Issue.6 , pp. 3922-3933
    • Kremneva, E.1    Boussouf, S.2    Nikolaeva, O.3    Maytum, R.4    Geeves, M.A.5    Levitsky, D.I.6
  • 35
    • 79951834827 scopus 로고    scopus 로고
    • Tropomyosin position on F-actin revealed by em reconstruction and computational chemistry
    • 10.1016/j.bpj.2010.12.3697 21320445 10.1016/j.bpj.2010.12.3697 1:CAS:528:DC%2BC3MXhvFKgtbs%3D
    • Li XE, Tobacman LS, Mun JY, Craig R, Fischer S, Lehman W (2011) Tropomyosin position on F-actin revealed by EM reconstruction and computational chemistry. Biophys J 100(4):1005-1013. doi: 10.1016/j.bpj.2010.12.3697
    • (2011) Biophys J , vol.100 , Issue.4 , pp. 1005-1013
    • Li, X.E.1    Tobacman, L.S.2    Mun, J.Y.3    Craig, R.4    Fischer, S.5    Lehman, W.6
  • 36
    • 84864767294 scopus 로고    scopus 로고
    • The flexibility of two tropomyosin mutants, D175N and E180G, that cause hypertrophic cardiomyopathy
    • 10.1016/j.bbrc.2012.06.141 22789852 10.1016/j.bbrc.2012.06.141 1:CAS:528:DC%2BC38XhtVOqu7%2FF
    • Li XE, Suphamungmee W, Janco M, Geeves MA, Marston SB, Fischer S, Lehman W (2012) The flexibility of two tropomyosin mutants, D175N and E180G, that cause hypertrophic cardiomyopathy. Biochem Biophys Res Commun 424(3):493-496. doi: 10.1016/j.bbrc.2012.06.141
    • (2012) Biochem Biophys Res Commun , vol.424 , Issue.3 , pp. 493-496
    • Li, X.E.1    Suphamungmee, W.2    Janco, M.3    Geeves, M.A.4    Marston, S.B.5    Fischer, S.6    Lehman, W.7
  • 37
    • 84866607365 scopus 로고    scopus 로고
    • Familial hypertrophic cardiomyopathy related E180G mutation increases flexibility of human cardiac alpha-tropomyosin
    • 10.1016/j.febslet.2012.08.005 22958892 10.1016/j.febslet.2012.08.005 1:CAS:528:DC%2BC38Xht1OjsLnF
    • Loong CK, Zhou HX, Chase PB (2012) Familial hypertrophic cardiomyopathy related E180G mutation increases flexibility of human cardiac alpha-tropomyosin. FEBS Lett 586(19):3503-3507. doi: 10.1016/j.febslet.2012.08.005
    • (2012) FEBS Lett , vol.586 , Issue.19 , pp. 3503-3507
    • Loong, C.K.1    Zhou, H.X.2    Chase, P.B.3
  • 38
    • 84865119925 scopus 로고    scopus 로고
    • Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin
    • 10.1021/bi3006835 22794249 10.1021/bi3006835 1:CAS:528:DC%2BC38XhtVWhtLjP
    • Ly S, Lehrer SS (2012) Long-range effects of familial hypertrophic cardiomyopathy mutations E180G and D175N on the properties of tropomyosin. Biochemistry 51(32):6413-6420. doi: 10.1021/bi3006835
    • (2012) Biochemistry , vol.51 , Issue.32 , pp. 6413-6420
    • Ly, S.1    Lehrer, S.S.2
  • 39
    • 0037070514 scopus 로고    scopus 로고
    • Hypertrophic cardiomyopathy: A systematic review
    • 11886323 10.1001/jama.287.10.1308
    • Maron BJ (2002) Hypertrophic cardiomyopathy: a systematic review. JAMA 287(10):1308-1320
    • (2002) JAMA , vol.287 , Issue.10 , pp. 1308-1320
    • Maron, B.J.1
  • 40
    • 79960564849 scopus 로고    scopus 로고
    • How do mutations in contractile proteins cause the primary familial cardiomyopathies?
    • 10.1007/s12265-011-9266-2 21424860 10.1007/s12265-011-9266-2
    • Marston SB (2011) How do mutations in contractile proteins cause the primary familial cardiomyopathies? J Cardiovasc Transl Res 4(3):245-255. doi: 10.1007/s12265-011-9266-2
    • (2011) J Cardiovasc Transl Res , vol.4 , Issue.3 , pp. 245-255
    • Marston, S.B.1
  • 41
    • 0017136639 scopus 로고
    • The 14-fold periodicity in alpha-tropomyosin and the interaction with actin
    • 950663 10.1016/0022-2836(76)90313-2 1:CAS:528:DyaE28XktFGkur0%3D
    • McLachlan AD, Stewart M (1976) The 14-fold periodicity in alpha-tropomyosin and the interaction with actin. J Mol Biol 103(2):271-298
    • (1976) J Mol Biol , vol.103 , Issue.2 , pp. 271-298
    • McLachlan, A.D.1    Stewart, M.2
  • 42
    • 0016747961 scopus 로고
    • Sequence repeats in alpha-tropomyosin
    • 1195388 10.1016/S0022-2836(75)80118-5 1:CAS:528:DyaE28XhtlOhug%3D%3D
    • McLachlan AD, Stewart M, Smillie LB (1975) Sequence repeats in alpha-tropomyosin. J Mol Biol 98(2):281-291
    • (1975) J Mol Biol , vol.98 , Issue.2 , pp. 281-291
    • McLachlan, A.D.1    Stewart, M.2    Smillie, L.B.3
  • 43
    • 84873855851 scopus 로고    scopus 로고
    • Genetic mutations and mechanisms in dilated cardiomyopathy
    • 10.1172/JCI62862 23281406 10.1172/JCI62862 1:CAS:528: DC%2BC3sXnsFGhsA%3D%3D
    • McNally EM, Golbus JR, Puckelwartz MJ (2013) Genetic mutations and mechanisms in dilated cardiomyopathy. J Clin Invest 123(1):19-26. doi: 10.1172/JCI62862
    • (2013) J Clin Invest , vol.123 , Issue.1 , pp. 19-26
    • McNally, E.M.1    Golbus, J.R.2    Puckelwartz, M.J.3
  • 45
    • 0034470169 scopus 로고    scopus 로고
    • Contractile dysfunction in hypertrophic cardiomyopathy: Elucidating primary defects of mutant contractile proteins by gene transfer
    • 11239799 10.1016/S1050-1738(00)00067-0 1:CAS:528:DC%2BD3MXhs1ejurs%3D
    • Michele DE, Metzger JM (2000) Contractile dysfunction in hypertrophic cardiomyopathy: elucidating primary defects of mutant contractile proteins by gene transfer. Trends Cardiovasc Med 10(4):177-182
    • (2000) Trends Cardiovasc Med , vol.10 , Issue.4 , pp. 177-182
    • Michele, D.E.1    Metzger, J.M.2
  • 46
    • 0032751723 scopus 로고    scopus 로고
    • Direct, convergent hypersensitivity of calcium-activated force generation produced by hypertrophic cardiomyopathy mutant alpha-tropomyosins in adult cardiac myocytes
    • 10.1038/70990 10581085 10.1038/70990 1:CAS:528:DyaK1MXnvFGju74%3D
    • Michele DE, Albayya FP, Metzger JM (1999) Direct, convergent hypersensitivity of calcium-activated force generation produced by hypertrophic cardiomyopathy mutant alpha-tropomyosins in adult cardiac myocytes. Nat Med 5(12):1413-1417. doi: 10.1038/70990
    • (1999) Nat Med , vol.5 , Issue.12 , pp. 1413-1417
    • Michele, D.E.1    Albayya, F.P.2    Metzger, J.M.3
  • 47
    • 0036370089 scopus 로고    scopus 로고
    • Divergent abnormal muscle relaxation by hypertrophic cardiomyopathy and nemaline myopathy mutant tropomyosins
    • 10.1152/physiolgenomics.00099.2001 12006676 1:CAS:528: DC%2BD38XkslOnsLc%3D
    • Michele DE, Coutu P, Metzger JM (2002a) Divergent abnormal muscle relaxation by hypertrophic cardiomyopathy and nemaline myopathy mutant tropomyosins. Physiol Genomics 9(2):103-111. doi: 10.1152/physiolgenomics.00099. 2001
    • (2002) Physiol Genomics , vol.9 , Issue.2 , pp. 103-111
    • Michele, D.E.1    Coutu, P.2    Metzger, J.M.3
  • 48
    • 0037047648 scopus 로고    scopus 로고
    • Cardiac dysfunction in hypertrophic cardiomyopathy mutant tropomyosin mice is transgene-dependent, hypertrophy-independent, and improved by beta-blockade
    • 12169652 10.1161/01.RES.0000027530.58419.82 1:CAS:528: DC%2BD38Xmt12jtbs%3D
    • Michele DE, Gomez CA, Hong KE, Westfall MV, Metzger JM (2002b) Cardiac dysfunction in hypertrophic cardiomyopathy mutant tropomyosin mice is transgene-dependent, hypertrophy-independent, and improved by beta-blockade. Circ Res 91(3):255-262
    • (2002) Circ Res , vol.91 , Issue.3 , pp. 255-262
    • Michele, D.E.1    Gomez, C.A.2    Hong, K.E.3    Westfall, M.V.4    Metzger, J.M.5
  • 49
    • 23344452467 scopus 로고    scopus 로고
    • Dilated cardiomyopathy mutations in three thin filament regulatory proteins result in a common functional phenotype
    • 10.1074/jbc.M412281200 15923195 10.1074/jbc.M412281200 1:CAS:528:DC%2BD2MXmvFSnsLo%3D
    • Mirza M, Marston S, Willott R, Ashley C, Mogensen J, McKenna W, Robinson P, Redwood C, Watkins H (2005) Dilated cardiomyopathy mutations in three thin filament regulatory proteins result in a common functional phenotype. J Biol Chem 280(31):28498-28506. doi: 10.1074/jbc.M412281200
    • (2005) J Biol Chem , vol.280 , Issue.31 , pp. 28498-28506
    • Mirza, M.1    Marston, S.2    Willott, R.3    Ashley, C.4    Mogensen, J.5    McKenna, W.6    Robinson, P.7    Redwood, C.8    Watkins, H.9
  • 50
    • 34250322240 scopus 로고    scopus 로고
    • The effect of mutations in alpha-tropomyosin (E40K and E54K) that cause familial dilated cardiomyopathy on the regulatory mechanism of cardiac muscle thin filaments
    • 10.1074/jbc.M701071200 17360712 10.1074/jbc.M701071200 1:CAS:528:DC%2BD2sXks1Ggt70%3D
    • Mirza M, Robinson P, Kremneva E, Copeland O, Nikolaeva O, Watkins H, Levitsky D, Redwood C, El-Mezgueldi M, Marston S (2007) The effect of mutations in alpha-tropomyosin (E40K and E54K) that cause familial dilated cardiomyopathy on the regulatory mechanism of cardiac muscle thin filaments. J Biol Chem 282(18):13487-13497. doi: 10.1074/jbc.M701071200
    • (2007) J Biol Chem , vol.282 , Issue.18 , pp. 13487-13497
    • Mirza, M.1    Robinson, P.2    Kremneva, E.3    Copeland, O.4    Nikolaeva, O.5    Watkins, H.6    Levitsky, D.7    Redwood, C.8    El-Mezgueldi, M.9    Marston, S.10
  • 51
    • 8144224216 scopus 로고    scopus 로고
    • Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy
    • 10.1016/j.jacc.2004.08.027 15542288 10.1016/j.jacc.2004.08.027 1:CAS:528:DC%2BD2cXpslGnsrs%3D
    • Mogensen J, Murphy RT, Shaw T, Bahl A, Redwood C, Watkins H, Burke M, Elliott PM, McKenna WJ (2004) Severe disease expression of cardiac troponin C and T mutations in patients with idiopathic dilated cardiomyopathy. J Am Coll Cardiol 44(10):2033-2040. doi: 10.1016/j.jacc.2004.08.027
    • (2004) J Am Coll Cardiol , vol.44 , Issue.10 , pp. 2033-2040
    • Mogensen, J.1    Murphy, R.T.2    Shaw, T.3    Bahl, A.4    Redwood, C.5    Watkins, H.6    Burke, M.7    Elliott, P.M.8    McKenna, W.J.9
  • 52
    • 0028177556 scopus 로고
    • Functional alpha-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group
    • 8144630 1:CAS:528:DyaK2cXkt12ntLk%3D
    • Monteiro PB, Lataro RC, Ferro JA, Reinach Fde C (1994) Functional alpha-tropomyosin produced in Escherichia coli. A dipeptide extension can substitute the amino-terminal acetyl group. J Biol Chem 269(14):10461-10466
    • (1994) J Biol Chem , vol.269 , Issue.14 , pp. 10461-10466
    • Monteiro, P.B.1    Lataro, R.C.2    Ferro, J.A.3    Reinach Fde, C.4
  • 54
    • 44449160070 scopus 로고    scopus 로고
    • Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-T
    • 10.1073/pnas.0801950105 18483193 10.1073/pnas.0801950105 1:CAS:528:DC%2BD1cXmsFCrsbo%3D
    • Murakami K, Stewart M, Nozawa K, Tomii K, Kudou N, Igarashi N, Shirakihara Y, Wakatsuki S, Yasunaga T, Wakabayashi T (2008) Structural basis for tropomyosin overlap in thin (actin) filaments and the generation of a molecular swivel by troponin-T. Proc Natl Acad Sci USA 105(20):7200-7205. doi: 10.1073/pnas.0801950105
    • (2008) Proc Natl Acad Sci USA , vol.105 , Issue.20 , pp. 7200-7205
    • Murakami, K.1    Stewart, M.2    Nozawa, K.3    Tomii, K.4    Kudou, N.5    Igarashi, N.6    Shirakihara, Y.7    Wakatsuki, S.8    Yasunaga, T.9    Wakabayashi, T.10
  • 56
    • 0029164976 scopus 로고
    • Novel missense mutation in alpha-tropomyosin gene found in Japanese patients with hypertrophic cardiomyopathy
    • 8523464 10.1016/0022-2828(95)90026-8 1:STN:280:DyaK28%2FptF2isQ%3D%3D
    • Nakajima-Taniguchi C, Matsui H, Nagata S, Kishimoto T, Yamauchi-Takihara K (1995) Novel missense mutation in alpha-tropomyosin gene found in Japanese patients with hypertrophic cardiomyopathy. J Mol Cell Cardiol 27(9):2053-2058
    • (1995) J Mol Cell Cardiol , vol.27 , Issue.9 , pp. 2053-2058
    • Nakajima-Taniguchi, C.1    Matsui, H.2    Nagata, S.3    Kishimoto, T.4    Yamauchi-Takihara, K.5
  • 57
    • 79959422575 scopus 로고    scopus 로고
    • Left ventricular non-compaction revisited: A distinct phenotype with genetic heterogeneity?
    • 10.1093/eurheartj/ehq508 21285074 10.1093/eurheartj/ehq508
    • Oechslin E, Jenni R (2011) Left ventricular non-compaction revisited: a distinct phenotype with genetic heterogeneity? Eur Heart J 32(12):1446-1456. doi: 10.1093/eurheartj/ehq508
    • (2011) Eur Heart J , vol.32 , Issue.12 , pp. 1446-1456
    • Oechslin, E.1    Jenni, R.2
  • 59
    • 0034971165 scopus 로고    scopus 로고
    • Mutations that alter the surface charge of alpha-tropomyosin are associated with dilated cardiomyopathy
    • 10.1006/jmcc.2000.1339 11273725 10.1006/jmcc.2000.1339 1:CAS:528:DC%2BD3MXitFylsrg%3D
    • Olson TM, Kishimoto NY, Whitby FG, Michels VV (2001) Mutations that alter the surface charge of alpha-tropomyosin are associated with dilated cardiomyopathy. J Mol Cell Cardiol 33(4):723-732. doi: 10.1006/jmcc.2000.1339
    • (2001) J Mol Cell Cardiol , vol.33 , Issue.4 , pp. 723-732
    • Olson, T.M.1    Kishimoto, N.Y.2    Whitby, F.G.3    Michels, V.V.4
  • 61
    • 0032555166 scopus 로고    scopus 로고
    • Mechanism of acute mechanical benefit from VDD pacing in hypertrophied heart: Similarity of responses in hypertrophic cardiomyopathy and hypertensive heart disease
    • 9697824 10.1161/01.CIR.98.3.242 1:STN:280:DyaK1czmtFaruw%3D%3D
    • Pak PH, Maughan WL, Baughman KL, Kieval RS, Kass DA (1998) Mechanism of acute mechanical benefit from VDD pacing in hypertrophied heart: similarity of responses in hypertrophic cardiomyopathy and hypertensive heart disease. Circulation 98(3):242-248
    • (1998) Circulation , vol.98 , Issue.3 , pp. 242-248
    • Pak, P.H.1    Maughan, W.L.2    Baughman, K.L.3    Kieval, R.S.4    Kass, D.A.5
  • 62
    • 0034841005 scopus 로고    scopus 로고
    • Vertebrate tropomyosin: Distribution, properties and function
    • 11563548 10.1023/A:1010303732441 1:CAS:528:DC%2BD3MXntFGqsrk%3D
    • Perry SV (2001) Vertebrate tropomyosin: distribution, properties and function. J Muscle Res Cell Motil 22(1):5-49
    • (2001) J Muscle Res Cell Motil , vol.22 , Issue.1 , pp. 5-49
    • Perry, S.V.1
  • 63
    • 0742289174 scopus 로고    scopus 로고
    • What is the role of tropomyosin in the regulation of muscle contraction?
    • 14870975 10.1023/B:JURE.0000009811.95652.68 1:CAS:528:DC%2BD3sXhtVSjs7rK
    • Perry SV (2003) What is the role of tropomyosin in the regulation of muscle contraction? J Muscle Res Cell Motil 24(8):593-596
    • (2003) J Muscle Res Cell Motil , vol.24 , Issue.8 , pp. 593-596
    • Perry, S.V.1
  • 64
    • 0034781383 scopus 로고    scopus 로고
    • A familial hypertrophic cardiomyopathy alpha-tropomyosin mutation causes severe cardiac hypertrophy and death in mice
    • 10.1006/jmcc.2001.1445 11603924 10.1006/jmcc.2001.1445 1:CAS:528:DC%2BD3MXnsFOjtrw%3D
    • Prabhakar R, Boivin GP, Grupp IL, Hoit B, Arteaga G, Solaro RJ, Wieczorek DF (2001) A familial hypertrophic cardiomyopathy alpha-tropomyosin mutation causes severe cardiac hypertrophy and death in mice. J Mol Cell Cardiol 33(10):1815-1828. doi: 10.1006/jmcc.2001.1445
    • (2001) J Mol Cell Cardiol , vol.33 , Issue.10 , pp. 1815-1828
    • Prabhakar, R.1    Boivin, G.P.2    Grupp, I.L.3    Hoit, B.4    Arteaga, G.5    Solaro, R.J.6    Wieczorek, D.F.7
  • 65
    • 80052752591 scopus 로고    scopus 로고
    • Sarcomere gene mutations in isolated left ventricular noncompaction cardiomyopathy do not predict clinical phenotype
    • 10.1161/CIRCGENETICS.110.959270 21551322 10.1161/CIRCGENETICS.110.959270 1:CAS:528:DC%2BC3MXhtF2itbbI
    • Probst S, Oechslin E, Schuler P, Greutmann M, Boye P, Knirsch W, Berger F, Thierfelder L, Jenni R, Klaassen S (2011) Sarcomere gene mutations in isolated left ventricular noncompaction cardiomyopathy do not predict clinical phenotype. Circ Cardiovasc Genet 4(4):367-374. doi: 10.1161/CIRCGENETICS.110. 959270
    • (2011) Circ Cardiovasc Genet , vol.4 , Issue.4 , pp. 367-374
    • Probst, S.1    Oechslin, E.2    Schuler, P.3    Greutmann, M.4    Boye, P.5    Knirsch, W.6    Berger, F.7    Thierfelder, L.8    Jenni, R.9    Klaassen, S.10
  • 66
    • 34547605959 scopus 로고    scopus 로고
    • Dilated cardiomyopathy mutant tropomyosin mice develop cardiac dysfunction with significantly decreased fractional shortening and myofilament calcium sensitivity
    • 10.1161/CIRCRESAHA.107.148379 17556658 10.1161/CIRCRESAHA.107.148379 1:CAS:528:DC%2BD2sXns1Cmsb8%3D
    • Rajan S, Ahmed RP, Jagatheesan G, Petrashevskaya N, Boivin GP, Urboniene D, Arteaga GM, Wolska BM, Solaro RJ, Liggett SB, Wieczorek DF (2007) Dilated cardiomyopathy mutant tropomyosin mice develop cardiac dysfunction with significantly decreased fractional shortening and myofilament calcium sensitivity. Circ Res 101(2):205-214. doi: 10.1161/CIRCRESAHA.107.148379
    • (2007) Circ Res , vol.101 , Issue.2 , pp. 205-214
    • Rajan, S.1    Ahmed, R.P.2    Jagatheesan, G.3    Petrashevskaya, N.4    Boivin, G.P.5    Urboniene, D.6    Arteaga, G.M.7    Wolska, B.M.8    Solaro, R.J.9    Liggett, S.B.10    Wieczorek, D.F.11
  • 67
    • 0034710851 scopus 로고    scopus 로고
    • Novel mutation in the alpha-tropomyosin gene and transition from hypertrophic to hypocontractile dilated cardiomyopathy
    • 11044437 10.1161/01.CIR.102.17.e112 1:STN:280:DC%2BD3crgt1eltg%3D%3D
    • Regitz-Zagrosek V, Erdmann J, Wellnhofer E, Raible J, Fleck E (2000) Novel mutation in the alpha-tropomyosin gene and transition from hypertrophic to hypocontractile dilated cardiomyopathy. Circulation 102(17):E112-E116
    • (2000) Circulation , vol.102 , Issue.17
    • Regitz-Zagrosek, V.1    Erdmann, J.2    Wellnhofer, E.3    Raible, J.4    Fleck, E.5
  • 68
    • 0017618863 scopus 로고
    • Phosphorylation of tropomyosin in live frog muscle
    • 851366 10.1016/0003-9861(77)90162-X 1:CAS:528:DyaE2sXhtVegt7c%3D
    • Ribolow H, Barany M (1977) Phosphorylation of tropomyosin in live frog muscle. Arch Biochem Biophys 179(2):718-720
    • (1977) Arch Biochem Biophys , vol.179 , Issue.2 , pp. 718-720
    • Ribolow, H.1    Barany, M.2
  • 70
    • 37349042936 scopus 로고    scopus 로고
    • Dilated and hypertrophic cardiomyopathy mutations in troponin and alpha-tropomyosin have opposing effects on the calcium affinity of cardiac thin filaments
    • 10.1161/CIRCRESAHA.107.156380 17932326 10.1161/CIRCRESAHA.107.156380 1:CAS:528:DC%2BD2sXhtlOjsLzK
    • Robinson P, Griffiths PJ, Watkins H, Redwood CS (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. doi: 10.1161/CIRCRESAHA.107.156380
    • (2007) Circ Res , vol.101 , Issue.12 , pp. 1266-1273
    • Robinson, P.1    Griffiths, P.J.2    Watkins, H.3    Redwood, C.S.4
  • 71
    • 84055187642 scopus 로고    scopus 로고
    • The effect of the Asp175Asn and Glu180Gly TPM1 mutations on actin-myosin interaction during the ATPase cycle
    • 10.1016/j.bbapap.2011.11.004 22155441 10.1016/j.bbapap.2011.11.004 1:CAS:528:DC%2BC38XkslGgsA%3D%3D
    • Rysev NA, Karpicheva OE, Redwood CS, Borovikov YS (2012) The effect of the Asp175Asn and Glu180Gly TPM1 mutations on actin-myosin interaction during the ATPase cycle. Biochim Biophys Acta 1824(2):366-373. doi: 10.1016/j.bbapap.2011.11.004
    • (2012) Biochim Biophys Acta , vol.1824 , Issue.2 , pp. 366-373
    • Rysev, N.A.1    Karpicheva, O.E.2    Redwood, C.S.3    Borovikov, Y.S.4
  • 72
    • 84863723103 scopus 로고    scopus 로고
    • Myofilament Ca sensitization increases cytosolic Ca binding affinity, alters intracellular Ca homeostasis, and causes pause-dependent Ca-triggered arrhythmia
    • 10.1161/CIRCRESAHA.112.270041 22647877 10.1161/CIRCRESAHA.112.270041 1:CAS:528:DC%2BC38XpvVejsL8%3D
    • Schober T, Huke S, Venkataraman R, Gryshchenko O, Kryshtal D, Hwang HS, Baudenbacher FJ, Knollmann BC (2012) Myofilament Ca sensitization increases cytosolic Ca binding affinity, alters intracellular Ca homeostasis, and causes pause-dependent Ca-triggered arrhythmia. Circ Res 111(2):170-179. doi: 10.1161/CIRCRESAHA.112.270041
    • (2012) Circ Res , vol.111 , Issue.2 , pp. 170-179
    • Schober, T.1    Huke, S.2    Venkataraman, R.3    Gryshchenko, O.4    Kryshtal, D.5    Hwang, H.S.6    Baudenbacher, F.J.7    Knollmann, B.C.8
  • 73
    • 84890115115 scopus 로고    scopus 로고
    • Tropomyosin de-phosphorylation in the heart: What are the consequences?
    • 10.1007/s10974-013-9348-7 23793376
    • Schulz EM, Wieczorek DF (2013) Tropomyosin de-phosphorylation in the heart: what are the consequences? J Muscle Res Cell Motil. doi: 10.1007/s10974-013-9348-7
    • (2013) J Muscle Res Cell Motil
    • Schulz, E.M.1    Wieczorek, D.F.2
  • 79
    • 0028178083 scopus 로고
    • Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: A disease of the sarcomere
    • 8205619 10.1016/0092-8674(94)90054-X
    • Thierfelder L, Watkins H, MacRae C, Lamas R, McKenna W, Vosberg HP, Seidman JG, Seidman CE (1994) Alpha-tropomyosin and cardiac troponin T mutations cause familial hypertrophic cardiomyopathy: a disease of the sarcomere. Cell 77(5):701-712
    • (1994) Cell , vol.77 , Issue.5 , pp. 701-712
    • Thierfelder, L.1    Watkins, H.2    Macrae, C.3    Lamas, R.4    McKenna, W.5    Vosberg, H.P.6    Seidman, J.G.7    Seidman, C.E.8
  • 80
    • 0030004861 scopus 로고    scopus 로고
    • Thin filament-mediated regulation of cardiac contraction
    • 10.1146/annurev.ph.58.030196.002311 8815803 10.1146/annurev.ph.58.030196. 002311 1:CAS:528:DyaK28XhvVahtrg%3D
    • Tobacman LS (1996) Thin filament-mediated regulation of cardiac contraction. Annu Rev Physiol 58:447-481. doi: 10.1146/annurev.ph.58.030196. 002311
    • (1996) Annu Rev Physiol , vol.58 , pp. 447-481
    • Tobacman, L.S.1
  • 82
    • 0037111937 scopus 로고    scopus 로고
    • A novel TPM1 mutation in a family with hypertrophic cardiomyopathy and sudden cardiac death in childhood
    • 12423715 10.1016/S0002-9149(02)02780-7
    • Van Driest SL, Will ML, Atkins DL, Ackerman MJ (2002) A novel TPM1 mutation in a family with hypertrophic cardiomyopathy and sudden cardiac death in childhood. Am J Cardiol 90(10):1123-1127
    • (2002) Am J Cardiol , vol.90 , Issue.10 , pp. 1123-1127
    • Van Driest, S.L.1    Will, M.L.2    Atkins, D.L.3    Ackerman, M.J.4
  • 83
    • 0041663609 scopus 로고    scopus 로고
    • Prevalence and spectrum of thin filament mutations in an outpatient referral population with hypertrophic cardiomyopathy
    • 10.1161/01.CIR.0000080896.52003.DF 12860912 10.1161/01.CIR.0000080896. 52003.DF
    • Van Driest SL, Ellsworth EG, Ommen SR, Tajik AJ, Gersh BJ, Ackerman MJ (2003) Prevalence and spectrum of thin filament mutations in an outpatient referral population with hypertrophic cardiomyopathy. Circulation 108(4):445-451. doi: 10.1161/01.CIR.0000080896.52003.DF
    • (2003) Circulation , vol.108 , Issue.4 , pp. 445-451
    • Van Driest, S.L.1    Ellsworth, E.G.2    Ommen, S.R.3    Tajik, A.J.4    Gersh, B.J.5    Ackerman, M.J.6
  • 85
    • 0028902929 scopus 로고
    • Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy
    • 10.1056/NEJM199504203321603 7898523 10.1056/NEJM199504203321603 1:CAS:528:DyaK2MXlslCnsrw%3D
    • Watkins H, McKenna WJ, Thierfelder L, Suk HJ, Anan R, O'Donoghue A, Spirito P, Matsumori A, Moravec CS, Seidman JG et al (1995) Mutations in the genes for cardiac troponin T and alpha-tropomyosin in hypertrophic cardiomyopathy. N Engl J Med 332(16):1058-1064. doi: 10.1056/NEJM199504203321603
    • (1995) N Engl J Med , vol.332 , Issue.16 , pp. 1058-1064
    • Watkins, H.1    McKenna, W.J.2    Thierfelder, L.3    Suk, H.J.4    Anan, R.5    O'Donoghue, A.6    Spirito, P.7    Matsumori, A.8    Moravec, C.S.9    Seidman, J.G.10
  • 86
    • 79955519460 scopus 로고    scopus 로고
    • Inherited cardiomyopathies
    • 10.1056/NEJMra0902923 21524215 10.1056/NEJMra0902923 1:CAS:528: DC%2BC3MXlsFeltLk%3D
    • Watkins H, Ashrafian H, Redwood C (2011) Inherited cardiomyopathies. N Engl J Med 364(17):1643-1656. doi: 10.1056/NEJMra0902923
    • (2011) N Engl J Med , vol.364 , Issue.17 , pp. 1643-1656
    • Watkins, H.1    Ashrafian, H.2    Redwood, C.3
  • 88
    • 0029794498 scopus 로고    scopus 로고
    • Clinical implications of hypertrophic cardiomyopathy associated with mutations in the alpha-tropomyosin gene
    • 8774330 10.1136/hrt.76.1.63 1:STN:280:DyaK28zntVCgtg%3D%3D
    • Yamauchi-Takihara K, Nakajima-Taniguchi C, Matsui H, Fujio Y, Kunisada K, Nagata S, Kishimoto T (1996) Clinical implications of hypertrophic cardiomyopathy associated with mutations in the alpha-tropomyosin gene. Heart 76(1):63-65
    • (1996) Heart , vol.76 , Issue.1 , pp. 63-65
    • Yamauchi-Takihara, K.1    Nakajima-Taniguchi, C.2    Matsui, H.3    Fujio, Y.4    Kunisada, K.5    Nagata, S.6    Kishimoto, T.7


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