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Volumn 36, Issue 1, 2015, Pages 25-36

Emerging importance of oxidative stress in regulating striated muscle elasticity

Author keywords

Diastolic stiffness; Myofilaments; Oxidative modification; Passive tension; Sarcomere proteins; Titin

Indexed keywords

CONNECTIN; GLUTATHIONE; TTN PROTEIN, HUMAN;

EID: 84925519376     PISSN: 01424319     EISSN: 15732657     Source Type: Journal    
DOI: 10.1007/s10974-014-9392-y     Document Type: Review
Times cited : (62)

References (110)
  • 2
    • 78549277458 scopus 로고    scopus 로고
    • Titin is a target of matrix metalloproteinase-2: implications in myocardial ischemia/reperfusion injury
    • COI: 1:CAS:528:DC%2BC3cXhsVagtb3L, PID: 21041693
    • Ali MA, Cho WJ, Hudson B, Kassiri Z, Granzier H, Schulz R (2010) Titin is a target of matrix metalloproteinase-2: implications in myocardial ischemia/reperfusion injury. Circulation 122:2039–2047
    • (2010) Circulation , vol.122 , pp. 2039-2047
    • Ali, M.A.1    Cho, W.J.2    Hudson, B.3    Kassiri, Z.4    Granzier, H.5    Schulz, R.6
  • 3
    • 38349048508 scopus 로고    scopus 로고
    • Skeletal muscle fatigue: cellular mechanisms
    • COI: 1:CAS:528:DC%2BD1cXitVKgtrg%3D, PID: 18195089
    • Allen DG, Lamb GD, Westerblad H (2008) Skeletal muscle fatigue: cellular mechanisms. Physiol Rev 88:287–332
    • (2008) Physiol Rev , vol.88 , pp. 287-332
    • Allen, D.G.1    Lamb, G.D.2    Westerblad, H.3
  • 4
    • 0035256776 scopus 로고    scopus 로고
    • Contractile response of skeletal muscle to low peroxide concentrations: myofibrillar calcium sensitivity as a likely target for redox-modulation
    • COI: 1:CAS:528:DC%2BD3MXhsFenu74%3D, PID: 11156946
    • Andrade FH, Reid MB, Westerblad H (2001) Contractile response of skeletal muscle to low peroxide concentrations: myofibrillar calcium sensitivity as a likely target for redox-modulation. FASEB J 15:309–311
    • (2001) FASEB J , vol.15 , pp. 309-311
    • Andrade, F.H.1    Reid, M.B.2    Westerblad, H.3
  • 5
    • 84906053204 scopus 로고    scopus 로고
    • Nitroxyl (HNO) for treatment of acute heart failure
    • COI: 1:CAS:528:DC%2BC2cXhtVOisbbJ, PID: 24980211
    • Arcaro A, Lembo G, Tocchetti CG (2014) Nitroxyl (HNO) for treatment of acute heart failure. Curr Heart Fail Rep 11:227–235
    • (2014) Curr Heart Fail Rep , vol.11 , pp. 227-235
    • Arcaro, A.1    Lembo, G.2    Tocchetti, C.G.3
  • 7
    • 33749071170 scopus 로고    scopus 로고
    • Inhibition of xanthine oxidase improves myocardial contractility in patients with ischemic cardiomyopathy
    • COI: 1:CAS:528:DC%2BD28XhtVagtLjO, PID: 17015175
    • Baldus S, Müllerleile K, Chumley P et al (2006) Inhibition of xanthine oxidase improves myocardial contractility in patients with ischemic cardiomyopathy. Free Radic Biol Med 41:1282–1288
    • (2006) Free Radic Biol Med , vol.41 , pp. 1282-1288
    • Baldus, S.1    Müllerleile, K.2    Chumley, P.3
  • 8
    • 84891357982 scopus 로고    scopus 로고
    • Myofilament protein carbonylation contributes to the contractile dysfunction in the infarcted LV region of mouse hearts
    • COI: 1:CAS:528:DC%2BC3sXhvF2ktLjM, PID: 24127233
    • Balogh A, Santer D, Pásztor ET et al (2014) Myofilament protein carbonylation contributes to the contractile dysfunction in the infarcted LV region of mouse hearts. Cardiovasc Res 101:108–119
    • (2014) Cardiovasc Res , vol.101 , pp. 108-119
    • Balogh, A.1    Santer, D.2    Pásztor, E.T.3
  • 9
    • 0035941407 scopus 로고    scopus 로고
    • The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system
    • COI: 1:CAS:528:DC%2BD3MXovFGhsLs%3D, PID: 11717165
    • Bang ML, Centner T, Fornoff F et al (2001) The complete gene sequence of titin, expression of an unusual approximately 700-kDa titin isoform, and its interaction with obscurin identify a novel Z-line to I-band linking system. Circ Res 89:1065–1072
    • (2001) Circ Res , vol.89 , pp. 1065-1072
    • Bang, M.L.1    Centner, T.2    Fornoff, F.3
  • 10
    • 26444489672 scopus 로고    scopus 로고
    • Calpain-1-sensitive myofibrillar proteins of the human myocardium
    • COI: 1:CAS:528:DC%2BD2MXhtVentrbP, PID: 16180082
    • Barta J, Tóth A, Edes I, Vaszily M, Papp JG, Varró A, Papp Z (2005) Calpain-1-sensitive myofibrillar proteins of the human myocardium. Mol Cell Biochem 278:1–8
    • (2005) Mol Cell Biochem , vol.278 , pp. 1-8
    • Barta, J.1    Tóth, A.2    Edes, I.3    Vaszily, M.4    Papp, J.G.5    Varró, A.6    Papp, Z.7
  • 11
    • 84155163078 scopus 로고    scopus 로고
    • Sildenafil and B-type natriuretic peptide acutely phosphorylate titin and improve diastolic distensibility in vivo
    • COI: 1:CAS:528:DC%2BC3MXhs1GlsbrE, PID: 22144574
    • Bishu K, Hamdani N, Mohammed SF et al (2011) Sildenafil and B-type natriuretic peptide acutely phosphorylate titin and improve diastolic distensibility in vivo. Circulation 124:2882–2891
    • (2011) Circulation , vol.124 , pp. 2882-2891
    • Bishu, K.1    Hamdani, N.2    Mohammed, S.F.3
  • 13
    • 33644669954 scopus 로고    scopus 로고
    • The utility of N, N-biotinyl glutathione disulfide in the study of protein S-glutathiolation
    • COI: 1:CAS:528:DC%2BD28XitVagsL4%3D, PID: 16223748
    • Brennan JP, Miller JI, Fuller W, Wait R, Begum S, Dunn MJ, Eaton P (2006) The utility of N, N-biotinyl glutathione disulfide in the study of protein S-glutathiolation. Mol Cell Proteomics 5:215–225
    • (2006) Mol Cell Proteomics , vol.5 , pp. 215-225
    • Brennan, J.P.1    Miller, J.I.2    Fuller, W.3    Wait, R.4    Begum, S.5    Dunn, M.J.6    Eaton, P.7
  • 14
    • 1542349941 scopus 로고    scopus 로고
    • Association of the chaperone αB-crystallin with titin in heart muscle
    • COI: 1:CAS:528:DC%2BD2cXhsFejt7g%3D, PID: 14676215
    • Bullard B, Ferguson C, Minajeva A et al (2004) Association of the chaperone αB-crystallin with titin in heart muscle. J Biol Chem 279:7917–7924
    • (2004) J Biol Chem , vol.279 , pp. 7917-7924
    • Bullard, B.1    Ferguson, C.2    Minajeva, A.3
  • 15
    • 1342304174 scopus 로고    scopus 로고
    • Evidence of myofibrillar protein oxidation induced by postischemic reperfusion in isolated rat hearts
    • Canton M, Neverova I, Menabò R, Van Eyk J, Di Lisa F (2004) Evidence of myofibrillar protein oxidation induced by postischemic reperfusion in isolated rat hearts. Am J Physiol Heart Circ Physiol 286:870–877
    • (2004) Am J Physiol Heart Circ Physiol , vol.286 , pp. 870-877
    • Canton, M.1    Neverova, I.2    Menabò, R.3    Van Eyk, J.4    Di Lisa, F.5
  • 18
    • 84899490852 scopus 로고    scopus 로고
    • Oxidative stress in muscular dystrophy: from generic evidence to specific sources and targets
    • COI: 1:CAS:528:DC%2BC2cXmsFagu7w%3D, PID: 24619215
    • Canton M, Menazza S, Di Lisa F (2014) Oxidative stress in muscular dystrophy: from generic evidence to specific sources and targets. J Muscle Res Cell Motil 35:23–36
    • (2014) J Muscle Res Cell Motil , vol.35 , pp. 23-36
    • Canton, M.1    Menazza, S.2    Di Lisa, F.3
  • 19
    • 33645456962 scopus 로고    scopus 로고
    • Decline of contractility during ischemia–reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin
    • Chen FC, Ogut O (2006) Decline of contractility during ischemia–reperfusion injury: actin glutathionylation and its effect on allosteric interaction with tropomyosin. Am J Physiol Cell Physiol 290:719–727
    • (2006) Am J Physiol Cell Physiol , vol.290 , pp. 719-727
    • Chen, F.C.1    Ogut, O.2
  • 20
    • 50849095774 scopus 로고    scopus 로고
    • Calpain 1 binding capacities of the N1-line region of titin are significantly enhanced by physiological concentrations of calcium
    • COI: 1:CAS:528:DC%2BD1cXps1Kms7k%3D, PID: 18690715
    • Coulis G, Becila S, Herrera-Mendez CH, Sentandreu MA, Raynaud F, Richard I, Benyamin Y, Ouali A (2008) Calpain 1 binding capacities of the N1-line region of titin are significantly enhanced by physiological concentrations of calcium. Biochemistry 47:9174–9183
    • (2008) Biochemistry , vol.47 , pp. 9174-9183
    • Coulis, G.1    Becila, S.2    Herrera-Mendez, C.H.3    Sentandreu, M.A.4    Raynaud, F.5    Richard, I.6    Benyamin, Y.7    Ouali, A.8
  • 21
    • 0035500775 scopus 로고    scopus 로고
    • Actin carbonylation: from a simple marker of protein oxidation to relevant signs of severe functional impairment
    • COI: 1:CAS:528:DC%2BD3MXnslWqu74%3D, PID: 11677040
    • Dalle-Donne I, Rossi R, Giustarini D, Gagliano N, Lusini L, Milzani A, Di Simplicio P, Colombo R (2001) Actin carbonylation: from a simple marker of protein oxidation to relevant signs of severe functional impairment. Free Radic Biol Med 31:1075–1083
    • (2001) Free Radic Biol Med , vol.31 , pp. 1075-1083
    • Dalle-Donne, I.1    Rossi, R.2    Giustarini, D.3    Gagliano, N.4    Lusini, L.5    Milzani, A.6    Di Simplicio, P.7    Colombo, R.8
  • 23
    • 84902190893 scopus 로고    scopus 로고
    • Hypoxia and reoxygenation induce endothelial nitric oxide synthase uncoupling in endothelial cells through tetrahydrobiopterin depletion and S-glutathionylation
    • PID: 24758136
    • De Pascali F, Hemann C, Samons K, Chen CA, Zweier JL (2014) Hypoxia and reoxygenation induce endothelial nitric oxide synthase uncoupling in endothelial cells through tetrahydrobiopterin depletion and S-glutathionylation. Biochemistry 53:3679–3688
    • (2014) Biochemistry , vol.53 , pp. 3679-3688
    • De Pascali, F.1    Hemann, C.2    Samons, K.3    Chen, C.A.4    Zweier, J.L.5
  • 24
    • 62249115660 scopus 로고    scopus 로고
    • Mitochondrial pathways for ROS formation and myocardial injury: the relevance of p66(Shc) and monoamine oxidase
    • PID: 19242637
    • Di Lisa F, Kaludercic N, Carpi A, Menabò R, Giorgio M (2009) Mitochondrial pathways for ROS formation and myocardial injury: the relevance of p66(Shc) and monoamine oxidase. Basic Res Cardiol 104:131–139
    • (2009) Basic Res Cardiol , vol.104 , pp. 131-139
    • Di Lisa, F.1    Kaludercic, N.2    Carpi, A.3    Menabò, R.4    Giorgio, M.5
  • 25
    • 51349110109 scopus 로고    scopus 로고
    • Enhanced nitrosative stress during Trypanosoma cruzi infection causes nitrotyrosine modification of host proteins: implications in Chagas’ disease
    • Dihman M, Nakayasu ES, Madaiah YH, Reynolds BK, Wen JJ, Almeida IC, Garg NJ (2008) Enhanced nitrosative stress during Trypanosoma cruzi infection causes nitrotyrosine modification of host proteins: implications in Chagas’ disease. Am J Pathol 173:728–740
    • (2008) Am J Pathol , vol.173 , pp. 728-740
    • Dihman, M.1    Nakayasu, E.S.2    Madaiah, Y.H.3    Reynolds, B.K.4    Wen, J.J.5    Almeida, I.C.6    Garg, N.J.7
  • 26
    • 84855391247 scopus 로고    scopus 로고
    • Cardiac-oxidized antigens are targets of immune recognition by antibodies and potential molecular determinants in Chagas disease pathogenesis
    • Dihman M, Zago MP, Nunez S, Amoroso A, Rementeria H, Dousset P, Nunez Burgos F, Garg NJ (2012) Cardiac-oxidized antigens are targets of immune recognition by antibodies and potential molecular determinants in Chagas disease pathogenesis. PLoS One 7:e28449
    • (2012) PLoS One , vol.7 , pp. 28449
    • Dihman, M.1    Zago, M.P.2    Nunez, S.3    Amoroso, A.4    Rementeria, H.5    Dousset, P.6    Nunez Burgos, F.7    Garg, N.J.8
  • 27
    • 0032569827 scopus 로고    scopus 로고
    • Evidence of oxidative stress in mdx mouse muscle: studies of the pre-necrotic state
    • COI: 1:CAS:528:DyaK1cXnsFais7o%3D, PID: 9879685
    • Disatnik MH, Dhawan J, Yu Y, Beal MF, Whirl MM, Franco AA, Rando TA (1998) Evidence of oxidative stress in mdx mouse muscle: studies of the pre-necrotic state. J Neurol Sci 161:77–84
    • (1998) J Neurol Sci , vol.161 , pp. 77-84
    • Disatnik, M.H.1    Dhawan, J.2    Yu, Y.3    Beal, M.F.4    Whirl, M.M.5    Franco, A.A.6    Rando, T.A.7
  • 28
    • 78649631500 scopus 로고    scopus 로고
    • Neonatal asphyxia induces the nitration of cardiac myosin light chain 2 that is associated with cardiac systolic dysfunction
    • COI: 1:CAS:528:DC%2BC3cXhsVahur%2FK, PID: 20386496
    • Doroszko A, Polewicz D, Cadete VJ, Sawicka J, Jones M, Szczesna-Cordary D, Cheung PY, Sawicki G (2010) Neonatal asphyxia induces the nitration of cardiac myosin light chain 2 that is associated with cardiac systolic dysfunction. Shock 34:592–600
    • (2010) Shock , vol.34 , pp. 592-600
    • Doroszko, A.1    Polewicz, D.2    Cadete, V.J.3    Sawicka, J.4    Jones, M.5    Szczesna-Cordary, D.6    Cheung, P.Y.7    Sawicki, G.8
  • 29
    • 0037155862 scopus 로고    scopus 로고
    • Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion
    • COI: 1:CAS:528:DC%2BD38XisVyls7c%3D, PID: 11777920
    • Eaton P, Byers HL, Leeds N, Ward MA, Shattock MJ (2002) Detection, quantitation, purification, and identification of cardiac proteins S-thiolated during ischemia and reperfusion. J Biol Chem 277:9806–9811
    • (2002) J Biol Chem , vol.277 , pp. 9806-9811
    • Eaton, P.1    Byers, H.L.2    Leeds, N.3    Ward, M.A.4    Shattock, M.J.5
  • 30
    • 79961149543 scopus 로고    scopus 로고
    • Screening for increased protein thiol oxidation in oxidatively stressed muscle tissue
    • COI: 1:CAS:528:DC%2BC3MXpvVWltrg%3D, PID: 21696323
    • El-Shafey AF, Armstrong AE, Terrill JR, Grounds MD, Arthur PG (2011) Screening for increased protein thiol oxidation in oxidatively stressed muscle tissue. Free Radic Res 45:991–999
    • (2011) Free Radic Res , vol.45 , pp. 991-999
    • El-Shafey, A.F.1    Armstrong, A.E.2    Terrill, J.R.3    Grounds, M.D.4    Arthur, P.G.5
  • 31
    • 33745698398 scopus 로고    scopus 로고
    • Titin/connectin-based modulation of the Frank-Starling mechanism of the heart
    • COI: 1:CAS:528:DC%2BD28Xmtl2qu7k%3D, PID: 16453158
    • Fukuda N, Granzier HL (2005) Titin/connectin-based modulation of the Frank-Starling mechanism of the heart. J Muscle Res Cell Motil 26:319–323
    • (2005) J Muscle Res Cell Motil , vol.26 , pp. 319-323
    • Fukuda, N.1    Granzier, H.L.2
  • 32
    • 84866990581 scopus 로고    scopus 로고
    • Nitroxyl-mediated disulfide bond formation between cardiac myofilament cysteines enhances contractile function
    • COI: 1:CAS:528:DC%2BC38XhsVWmt77P, PID: 22851540
    • Gao WD, Murray CI, Tian Y et al (2012) Nitroxyl-mediated disulfide bond formation between cardiac myofilament cysteines enhances contractile function. Circ Res 111:1002–1011
    • (2012) Circ Res , vol.111 , pp. 1002-1011
    • Gao, W.D.1    Murray, C.I.2    Tian, Y.3
  • 33
    • 84901916949 scopus 로고    scopus 로고
    • Heart failure with preserved ejection fraction
    • COI: 1:CAS:528:DC%2BC2cXksleltLY%3D
    • Gladden JD, Linke WA, Redfield MM (2014) Heart failure with preserved ejection fraction. Pflüg Arch 466:1037–1053
    • (2014) Pflüg Arch , vol.466 , pp. 1037-1053
    • Gladden, J.D.1    Linke, W.A.2    Redfield, M.M.3
  • 34
    • 68849089514 scopus 로고    scopus 로고
    • Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2B-unique sequence
    • PID: 19651040
    • Grützner A, Garcia-Manyes S, Kötter S, Badilla CL, Fernandez JL, Linke WA (2009) Modulation of titin-based stiffness by disulfide bonding in the cardiac titin N2B-unique sequence. Biophys J 97:825–834
    • (2009) Biophys J , vol.97 , pp. 825-834
    • Grützner, A.1    Garcia-Manyes, S.2    Kötter, S.3    Badilla, C.L.4    Fernandez, J.L.5    Linke, W.A.6
  • 35
    • 84874264782 scopus 로고    scopus 로고
    • Deranged myofilament phosphorylation and function in experimental heart failure with preserved ejection fraction
    • COI: 1:CAS:528:DC%2BC3sXis1Cqsrg%3D, PID: 23213108
    • Hamdani N, Bishu KG, Frieling-Salewsky M, Redfield MM, Linke WA (2013a) Deranged myofilament phosphorylation and function in experimental heart failure with preserved ejection fraction. Cardiovasc Res 97:464–471
    • (2013) Cardiovasc Res , vol.97 , pp. 464-471
    • Hamdani, N.1    Bishu, K.G.2    Frieling-Salewsky, M.3    Redfield, M.M.4    Linke, W.A.5
  • 36
    • 84892633453 scopus 로고    scopus 로고
    • Myocardial titin hypophosphorylation importantly contributes to heart failure with preserved ejection fraction in a rat metabolic risk model
    • COI: 1:CAS:528:DC%2BC3sXhvVahtbfL, PID: 24014826
    • Hamdani N, Franssen C, Lourenço A et al (2013b) Myocardial titin hypophosphorylation importantly contributes to heart failure with preserved ejection fraction in a rat metabolic risk model. Circ Heart Fail 6:1239–1249
    • (2013) Circ Heart Fail , vol.6 , pp. 1239-1249
    • Hamdani, N.1    Franssen, C.2    Lourenço, A.3
  • 38
    • 84922027882 scopus 로고    scopus 로고
    • Discovery of serum protein biomarkers in the mdx mouse model and cross-species comparison to Duchenne muscular dystrophy patients. Hum Mol Genet
    • Hathout Y, Marathi RL, Rayavarapu S et al (2014) Discovery of serum protein biomarkers in the mdx mouse model and cross-species comparison to Duchenne muscular dystrophy patients. Hum Mol Genet. doi:10.1093/hmg/ddu366 [15 July 2014; Epub ahead of print]
    • (2014) doi:10.1093/hmg/ddu366 [15 July 2014; Epub ahead of print]
    • Hathout, Y.1    Marathi, R.L.2    Rayavarapu, S.3
  • 39
    • 0030890145 scopus 로고    scopus 로고
    • Oxidative damage to muscle protein in Duchenne muscular dystrophy
    • COI: 1:CAS:528:DyaK2sXhvFeks7c%3D, PID: 9051810
    • Haycock JW, MacNeil S, Jones P, Harris JB, Mamtle D (1996) Oxidative damage to muscle protein in Duchenne muscular dystrophy. NeuroReport 8:357–361
    • (1996) NeuroReport , vol.8 , pp. 357-361
    • Haycock, J.W.1    MacNeil, S.2    Jones, P.3    Harris, J.B.4    Mamtle, D.5
  • 40
    • 9044252721 scopus 로고    scopus 로고
    • Expression of inducible nitric oxide synthase in human heart failure
    • COI: 1:STN:280:DyaK283itVWitA%3D%3D, PID: 8653828
    • Haywood GA, Tsao PS, von der Leyen HE et al (1996) Expression of inducible nitric oxide synthase in human heart failure. Circulation 93:1087–1094
    • (1996) Circulation , vol.93 , pp. 1087-1094
    • Haywood, G.A.1    Tsao, P.S.2    von der Leyen, H.E.3
  • 41
    • 0028036491 scopus 로고
    • Altered expression of titin and contractile proteins in failing human myocardium
    • COI: 1:CAS:528:DyaK2cXmslOqsbo%3D, PID: 7869390
    • Hein S, Scholz D, Fujitani N, Rennollet H, Brand T, Friedl A, Schaper J (1994) Altered expression of titin and contractile proteins in failing human myocardium. J Mol Cell Cardiol 26:1291–1306
    • (1994) J Mol Cell Cardiol , vol.26 , pp. 1291-1306
    • Hein, S.1    Scholz, D.2    Fujitani, N.3    Rennollet, H.4    Brand, T.5    Friedl, A.6    Schaper, J.7
  • 43
    • 77954080841 scopus 로고    scopus 로고
    • The contribution of reactive oxygen species and p38 mitogen-activated protein kinase to myofilament oxidation and progression of heart failure in rabbits
    • COI: 1:CAS:528:DC%2BC3cXht1Oit7rO, PID: 20590631
    • Heusch P, Canton M, Aker S et al (2010) The contribution of reactive oxygen species and p38 mitogen-activated protein kinase to myofilament oxidation and progression of heart failure in rabbits. Br J Pharmacol 160:1408–1416
    • (2010) Br J Pharmacol , vol.160 , pp. 1408-1416
    • Heusch, P.1    Canton, M.2    Aker, S.3
  • 45
    • 70349668973 scopus 로고    scopus 로고
    • PKC phosphorylation of titin’s PEVK element: a novel and conserved pathway for modulating myocardial stiffness
    • COI: 1:CAS:528:DC%2BD1MXhtFelsrzE, PID: 19679839
    • Hidalgo CG, Hudson B, Bogomolovas J, Zhu Y, Anderson B, Greaser M, Labeit S, Granzier H (2009) PKC phosphorylation of titin’s PEVK element: a novel and conserved pathway for modulating myocardial stiffness. Circ Res 105:631–638
    • (2009) Circ Res , vol.105 , pp. 631-638
    • Hidalgo, C.G.1    Hudson, B.2    Bogomolovas, J.3    Zhu, Y.4    Anderson, B.5    Greaser, M.6    Labeit, S.7    Granzier, H.8
  • 46
    • 34248592556 scopus 로고    scopus 로고
    • Proteomic analysis of age dependent nitration of rat cardiac proteins by solution isoelectric focusing coupled to nanoHPLC tandem mass spectrometry
    • COI: 1:CAS:528:DC%2BD2sXlsF2ht74%3D, PID: 17481840
    • Hong SJ, Gokulrangan G, Schöneich C (2007) Proteomic analysis of age dependent nitration of rat cardiac proteins by solution isoelectric focusing coupled to nanoHPLC tandem mass spectrometry. Exp Gerontol 42:639–651
    • (2007) Exp Gerontol , vol.42 , pp. 639-651
    • Hong, S.J.1    Gokulrangan, G.2    Schöneich, C.3
  • 47
    • 0023047016 scopus 로고
    • A physiological role for titin and nebulin in skeletal muscle
    • COI: 1:CAS:528:DyaL28Xls12ksb0%3D, PID: 3755803
    • Horowits R, Kempner ES, Bisher ME, Podolsky RJ (1986) A physiological role for titin and nebulin in skeletal muscle. Nature 323:160–164
    • (1986) Nature , vol.323 , pp. 160-164
    • Horowits, R.1    Kempner, E.S.2    Bisher, M.E.3    Podolsky, R.J.4
  • 48
    • 84866645505 scopus 로고    scopus 로고
    • Contribution of calpains to myocardial ischaemia/reperfusion injury
    • COI: 1:CAS:528:DC%2BC38XhsVSnt7%2FL, PID: 22787134
    • Inserte J, Hernando V, Garcia-Dorado D (2012) Contribution of calpains to myocardial ischaemia/reperfusion injury. Cardiovasc Res 96:23–31
    • (2012) Cardiovasc Res , vol.96 , pp. 23-31
    • Inserte, J.1    Hernando, V.2    Garcia-Dorado, D.3
  • 49
    • 74249098410 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 and myocardial oxidative stress injury: beyond the matrix
    • COI: 1:CAS:528:DC%2BC3cXkt1emsA%3D%3D, PID: 19656780
    • Kandasamy AD, Chow AK, Ali MA, Schulz R (2010) Matrix metalloproteinase-2 and myocardial oxidative stress injury: beyond the matrix. Cardiovasc Res 85:413–423
    • (2010) Cardiovasc Res , vol.85 , pp. 413-423
    • Kandasamy, A.D.1    Chow, A.K.2    Ali, M.A.3    Schulz, R.4
  • 50
    • 11144318614 scopus 로고    scopus 로고
    • Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging
    • Kanski J, Behring A, Pelling J, Schöneich C (2005a) Proteomic identification of 3-nitrotyrosine-containing rat cardiac proteins: effects of biological aging. Am J Physiol Heart Circ Physiol 288:371–381
    • (2005) Am J Physiol Heart Circ Physiol , vol.288 , pp. 371-381
    • Kanski, J.1    Behring, A.2    Pelling, J.3    Schöneich, C.4
  • 51
    • 21244457292 scopus 로고    scopus 로고
    • Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine-containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry
    • COI: 1:CAS:528:DC%2BD2MXltlKgs7Y%3D, PID: 15851474
    • Kanski J, Hong SJ, Schöneich C (2005b) Proteomic analysis of protein nitration in aging skeletal muscle and identification of nitrotyrosine-containing sequences in vivo by nanoelectrospray ionization tandem mass spectrometry. J Biol Chem 280:24261–24266
    • (2005) J Biol Chem , vol.280 , pp. 24261-24266
    • Kanski, J.1    Hong, S.J.2    Schöneich, C.3
  • 52
    • 84872858018 scopus 로고    scopus 로고
    • Contribution of oxidative stress to pathology in diaphragm and limb muscles with Duchenne muscular dystrophy
    • COI: 1:CAS:528:DC%2BC3sXhtlGgu78%3D, PID: 23104273
    • Kim JH, Kwak HB, Thompson LV, Lawler JM (2013) Contribution of oxidative stress to pathology in diaphragm and limb muscles with Duchenne muscular dystrophy. J Muscle Res Cell Motil 34:1–13
    • (2013) J Muscle Res Cell Motil , vol.34 , pp. 1-13
    • Kim, J.H.1    Kwak, H.B.2    Thompson, L.V.3    Lawler, J.M.4
  • 54
    • 84892863880 scopus 로고    scopus 로고
    • Human myocytes are protected from titin aggregation-induced stiffening by small heat shock proteins
    • PID: 24421331
    • Kötter S, Unger A, Hamdani N, Lang P, Vorgerd M, Nagel-Steger L, Linke WA (2014) Human myocytes are protected from titin aggregation-induced stiffening by small heat shock proteins. J Cell Biol 204:187–202
    • (2014) J Cell Biol , vol.204 , pp. 187-202
    • Kötter, S.1    Unger, A.2    Hamdani, N.3    Lang, P.4    Vorgerd, M.5    Nagel-Steger, L.6    Linke, W.A.7
  • 55
    • 33748329623 scopus 로고    scopus 로고
    • Protein kinase-A phosphorylates titin in human heart muscle and reduces myofibrillar passive tension
    • PID: 16897574
    • Krüger M, Linke WA (2006) Protein kinase-A phosphorylates titin in human heart muscle and reduces myofibrillar passive tension. J Muscle Res Cell Motil 27:435–444
    • (2006) J Muscle Res Cell Motil , vol.27 , pp. 435-444
    • Krüger, M.1    Linke, W.A.2
  • 56
    • 79953178205 scopus 로고    scopus 로고
    • The giant protein titin: a regulatory node that integrates myocyte signaling pathways
    • PID: 21257761
    • Krüger M, Linke WA (2011) The giant protein titin: a regulatory node that integrates myocyte signaling pathways. J Biol Chem 286:9905–9912
    • (2011) J Biol Chem , vol.286 , pp. 9905-9912
    • Krüger, M.1    Linke, W.A.2
  • 58
    • 1242281665 scopus 로고    scopus 로고
    • Developmental control of titin isoform expression and passive stiffness in fetal and neonatal myocardium
    • COI: 1:CAS:528:DC%2BD2cXhsFOgur0%3D, PID: 14707027
    • Lahmers S, Wu Y, Call DR, Labeit S, Granzier H (2004) Developmental control of titin isoform expression and passive stiffness in fetal and neonatal myocardium. Circ Res 94:505–513
    • (2004) Circ Res , vol.94 , pp. 505-513
    • Lahmers, S.1    Wu, Y.2    Call, D.R.3    Labeit, S.4    Granzier, H.5
  • 59
    • 79955415655 scopus 로고    scopus 로고
    • Acute effects of reactive oxygen and nitrogen species on the contractile function of skeletal muscle
    • COI: 1:CAS:528:DC%2BC3MXmslOhtLo%3D, PID: 21041533
    • Lamb GD, Westerblad H (2011) Acute effects of reactive oxygen and nitrogen species on the contractile function of skeletal muscle. J Physiol 589:2119–2127
    • (2011) J Physiol , vol.589 , pp. 2119-2127
    • Lamb, G.D.1    Westerblad, H.2
  • 60
    • 0037115642 scopus 로고    scopus 로고
    • Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2
    • COI: 1:CAS:528:DC%2BD3sXis1KqtQ%3D%3D, PID: 12432079
    • Lange S, Auerbach D, McLoughlin P, Perriard E, Schäfer BW, Perriard JC, Ehler E (2002) Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2. J Cell Sci 115:4925–4936
    • (2002) J Cell Sci , vol.115 , pp. 4925-4936
    • Lange, S.1    Auerbach, D.2    McLoughlin, P.3    Perriard, E.4    Schäfer, B.W.5    Perriard, J.C.6    Ehler, E.7
  • 61
    • 84866425540 scopus 로고    scopus 로고
    • Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers
    • COI: 1:CAS:528:DC%2BC38XhsFGmu7jJ, PID: 22763123
    • Larkins NT, Murphy RM, Lamb GD (2012) Influences of temperature, oxidative stress, and phosphorylation on binding of heat shock proteins in skeletal muscle fibers. Am J Physiol Cell Physiol 303:C654–C665
    • (2012) Am J Physiol Cell Physiol , vol.303 , pp. 654-665
    • Larkins, N.T.1    Murphy, R.M.2    Lamb, G.D.3
  • 64
    • 0033928461 scopus 로고    scopus 로고
    • Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle
    • COI: 1:CAS:528:DC%2BD3cXmsFOmt7w%3D, PID: 10963124
    • Linke WA (2000) Stretching molecular springs: elasticity of titin filaments in vertebrate striated muscle. Histol Histopathol 15:799–811
    • (2000) Histol Histopathol , vol.15 , pp. 799-811
    • Linke, W.A.1
  • 65
    • 78549251018 scopus 로고    scopus 로고
    • Molecular giant vulnerable to oxidative damage: titin joins the club of proteins degraded by matrix metalloproteinase-2
    • PID: 21041688
    • Linke WA (2010) Molecular giant vulnerable to oxidative damage: titin joins the club of proteins degraded by matrix metalloproteinase-2. Circulation 122:2002–2004
    • (2010) Circulation , vol.122 , pp. 2002-2004
    • Linke, W.A.1
  • 66
    • 0037569697 scopus 로고    scopus 로고
    • Cardiac titin: molecular basis of elasticity and cellular contribution to elastic and viscous stiffness components in myocardium
    • PID: 12785099
    • Linke WA, Fernandez JM (2002) Cardiac titin: molecular basis of elasticity and cellular contribution to elastic and viscous stiffness components in myocardium. J Muscle Res Cell Motil 23:483–497
    • (2002) J Muscle Res Cell Motil , vol.23 , pp. 483-497
    • Linke, W.A.1    Fernandez, J.M.2
  • 67
    • 84897874678 scopus 로고    scopus 로고
    • Gigantic business: titin properties and function through thick and thin
    • COI: 1:CAS:528:DC%2BC2cXktF2lu7o%3D, PID: 24625729
    • Linke WA, Hamdani N (2014) Gigantic business: titin properties and function through thick and thin. Circ Res 114:1052–1068
    • (2014) Circ Res , vol.114 , pp. 1052-1068
    • Linke, W.A.1    Hamdani, N.2
  • 68
    • 0033538859 scopus 로고    scopus 로고
    • I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure
    • COI: 1:CAS:528:DyaK1MXlt1erurs%3D, PID: 10444071
    • Linke WA, Rudy DE, Centner T, Gautel M, Witt C, Labeit S, Gregorio CC (1999) I-band titin in cardiac muscle is a three-element molecular spring and is critical for maintaining thin filament structure. J Cell Biol 146:631–644
    • (1999) J Cell Biol , vol.146 , pp. 631-644
    • Linke, W.A.1    Rudy, D.E.2    Centner, T.3    Gautel, M.4    Witt, C.5    Labeit, S.6    Gregorio, C.C.7
  • 69
    • 84862776882 scopus 로고    scopus 로고
    • Ranolazine improves cardiac diastolic dysfunction through modulation of myofilament calcium sensitivity
    • COI: 1:CAS:528:DC%2BC38XjslKntrY%3D, PID: 22343711
    • Lovelock JD, Monasky MM, Jeong EM, Lardin HA, Liu H, Patel BG et al (2012) Ranolazine improves cardiac diastolic dysfunction through modulation of myofilament calcium sensitivity. Circ Res 110:841–850
    • (2012) Circ Res , vol.110 , pp. 841-850
    • Lovelock, J.D.1    Monasky, M.M.2    Jeong, E.M.3    Lardin, H.A.4    Liu, H.5    Patel, B.G.6
  • 70
    • 4944235675 scopus 로고    scopus 로고
    • Passive stiffness changes caused by upregulation of compliant titin isoforms in human dilated cardiomyopathy hearts
    • COI: 1:CAS:528:DC%2BD2cXnvVekurs%3D, PID: 15345656
    • Makarenko I, Opitz CA, Leake MC, Neagoe C, Kulke M, Gwathmey JK, del Monte F, Hajjar RJ, Linke WA (2004) Passive stiffness changes caused by upregulation of compliant titin isoforms in human dilated cardiomyopathy hearts. Circ Res 95:708–716
    • (2004) Circ Res , vol.95 , pp. 708-716
    • Makarenko, I.1    Opitz, C.A.2    Leake, M.C.3    Neagoe, C.4    Kulke, M.5    Gwathmey, J.K.6    del Monte, F.7    Hajjar, R.J.8    Linke, W.A.9
  • 71
    • 84875060926 scopus 로고    scopus 로고
    • Impact of titin isoform on length dependent activation and cross-bridge cycling kinetics in rat skeletal muscle
    • COI: 1:CAS:528:DC%2BC38Xhtlamtb7N, PID: 22951219
    • Mateja RD, Greaser ML, de Tombe PP (2013) Impact of titin isoform on length dependent activation and cross-bridge cycling kinetics in rat skeletal muscle. Biochim Biophys Acta 1833:804–811
    • (2013) Biochim Biophys Acta , vol.1833 , pp. 804-811
    • Mateja, R.D.1    Greaser, M.L.2    de Tombe, P.P.3
  • 72
    • 84911806842 scopus 로고    scopus 로고
    • Stiff muscle fibers in calf muscles of patients with cerebral palsy lead to high passive muscle stiffness
    • Mathewson MA, Chambers HG, Girard PJ, Tenenhaus M, Schwartz AK, Lieber RL (2014) Stiff muscle fibers in calf muscles of patients with cerebral palsy lead to high passive muscle stiffness. J Orthop Res 32:1667–1674
    • (2014) J Orthop Res , vol.32 , pp. 1667-1674
    • Mathewson, M.A.1    Chambers, H.G.2    Girard, P.J.3    Tenenhaus, M.4    Schwartz, A.K.5    Lieber, R.L.6
  • 73
    • 0034886351 scopus 로고    scopus 로고
    • Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin
    • COI: 1:CAS:528:DC%2BD3MXjsValsrg%3D, PID: 11525170
    • Mayans O, Wuerges J, Canela S, Gautel M, Wilmanns M (2001) Structural evidence for a possible role of reversible disulphide bridge formation in the elasticity of the muscle protein titin. Structure 9:331–340
    • (2001) Structure , vol.9 , pp. 331-340
    • Mayans, O.1    Wuerges, J.2    Canela, S.3    Gautel, M.4    Wilmanns, M.5
  • 75
    • 0038422171 scopus 로고    scopus 로고
    • Effects of peroxynitrite on isolated cardiac trabeculae: selective impact on myofibrillar energetic controllers
    • COI: 1:CAS:528:DC%2BD3sXks1Wmu7Y%3D
    • Mihm MJ, Yu F, Reiser PJ, Bauer JA (2003) Effects of peroxynitrite on isolated cardiac trabeculae: selective impact on myofibrillar energetic controllers. Biochemistry 85:587–596
    • (2003) Biochemistry , vol.85 , pp. 587-596
    • Mihm, M.J.1    Yu, F.2    Reiser, P.J.3    Bauer, J.A.4
  • 76
    • 11844279035 scopus 로고    scopus 로고
    • The chemistry of nitroxyl (HNO) and implications in biology
    • COI: 1:CAS:528:DC%2BD2MXksVCqtg%3D%3D
    • Miranda KM (2005) The chemistry of nitroxyl (HNO) and implications in biology. Coord Chem Rev 249:433–455
    • (2005) Coord Chem Rev , vol.249 , pp. 433-455
    • Miranda, K.M.1
  • 79
    • 33749344685 scopus 로고    scopus 로고
    • 2+ activation of diffusible and bound pools of mu-calpain in rat skeletal muscle
    • COI: 1:CAS:528:DC%2BD28XhtFGqt7rJ, PID: 16857710
    • 2+ activation of diffusible and bound pools of mu-calpain in rat skeletal muscle. J Physiol 576:595–612
    • (2006) J Physiol , vol.576 , pp. 595-612
    • Murphy, R.M.1    Verburg, E.2    Lamb, G.D.3
  • 80
    • 80054747192 scopus 로고    scopus 로고
    • Large potentials of small heat shock proteins
    • COI: 1:CAS:528:DC%2BC3MXhsVOjsb3F, PID: 22013208
    • Mymrikov EV, Seit-Nebi AS, Gusev NB (2011) Large potentials of small heat shock proteins. Physiol Rev 91:1123–1159
    • (2011) Physiol Rev , vol.91 , pp. 1123-1159
    • Mymrikov, E.V.1    Seit-Nebi, A.S.2    Gusev, N.B.3
  • 82
    • 33750728870 scopus 로고    scopus 로고
    • Fibre type-specific increase in passive muscle tension in spinal cord-injured subjects with spasticity
    • COI: 1:CAS:528:DC%2BD28Xht1yqsL3J, PID: 16931550
    • Olsson MC, Krüger M, Meyer LH, Ahnlund L, Gransberg L, Linke WA, Larsson L (2006) Fibre type-specific increase in passive muscle tension in spinal cord-injured subjects with spasticity. J Physiol 577:339–352
    • (2006) J Physiol , vol.577 , pp. 339-352
    • Olsson, M.C.1    Krüger, M.2    Meyer, L.H.3    Ahnlund, L.4    Gransberg, L.5    Linke, W.A.6    Larsson, L.7
  • 83
    • 1842830381 scopus 로고    scopus 로고
    • Developmentally regulated switching of titin size alters myofibrillar stiffness in the perinatal heart
    • COI: 1:CAS:528:DC%2BD2cXivVKqsL8%3D, PID: 14988228
    • Opitz CA, Leake MC, Makarenko I, Benes V, Linke WA (2004) Developmentally regulated switching of titin size alters myofibrillar stiffness in the perinatal heart. Circ Res 94:967–975
    • (2004) Circ Res , vol.94 , pp. 967-975
    • Opitz, C.A.1    Leake, M.C.2    Makarenko, I.3    Benes, V.4    Linke, W.A.5
  • 84
    • 77951887774 scopus 로고    scopus 로고
    • Susceptibility of isolated myofibrils to in vitro glutathionylation: potential relevance to muscle functions
    • COI: 1:CAS:528:DC%2BC3cXjtFCksL4%3D
    • Passarelli C, Di Venere A, Piroddi N et al (2010) Susceptibility of isolated myofibrils to in vitro glutathionylation: potential relevance to muscle functions. Cytoskeleton (Hoboken) 67:81–89
    • (2010) Cytoskeleton (Hoboken) , vol.67 , pp. 81-89
    • Passarelli, C.1    Di Venere, A.2    Piroddi, N.3
  • 85
    • 84889645206 scopus 로고    scopus 로고
    • Novel control of cardiac myofilament response to calcium by S-glutathionylation at specific sites of myosin binding protein C
    • PID: 24312057
    • Patel BG, Wilder T, Solaro RJ (2013) Novel control of cardiac myofilament response to calcium by S-glutathionylation at specific sites of myosin binding protein C. Front Physiol 4:336
    • (2013) Front Physiol , vol.4 , pp. 336
    • Patel, B.G.1    Wilder, T.2    Solaro, R.J.3
  • 86
    • 84879748718 scopus 로고    scopus 로고
    • A novel paradigm for heart failure with preserved ejection fraction: comorbidities drive myocardial dysfunction and remodeling through coronary microvascular endothelial inflammation
    • PID: 23684677
    • Paulus WJ, Tschöpe C (2013) A novel paradigm for heart failure with preserved ejection fraction: comorbidities drive myocardial dysfunction and remodeling through coronary microvascular endothelial inflammation. J Am Coll Cardiol 62:263–271
    • (2013) J Am Coll Cardiol , vol.62 , pp. 263-271
    • Paulus, W.J.1    Tschöpe, C.2
  • 87
    • 68249096218 scopus 로고    scopus 로고
    • Impact of actin glutathionylation on the actomyosin-S1 ATPase
    • COI: 1:CAS:528:DC%2BD1MXosVOgsbc%3D, PID: 19580330
    • Pizarro GO, Ogut O (2009) Impact of actin glutathionylation on the actomyosin-S1 ATPase. Biochemistry 48:7533–7538
    • (2009) Biochemistry , vol.48 , pp. 7533-7538
    • Pizarro, G.O.1    Ogut, O.2
  • 88
    • 79957598460 scopus 로고    scopus 로고
    • Ischemia induced peroxynitrite dependent modifications of cardiomyocyte MLC1 increases its degradation by MMP-2 leading to contractile dysfunction
    • COI: 1:CAS:528:DC%2BC3MXnvFelsLo%3D, PID: 20518849
    • Polewicz D, Cadete VJ, Doroszko A, Hunter BE, Sawicka J, Szczesna-Cordary D, Light PE, Sawicki G (2011) Ischemia induced peroxynitrite dependent modifications of cardiomyocyte MLC1 increases its degradation by MMP-2 leading to contractile dysfunction. J Cell Mol Med 15:1136–1147
    • (2011) J Cell Mol Med , vol.15 , pp. 1136-1147
    • Polewicz, D.1    Cadete, V.J.2    Doroszko, A.3    Hunter, B.E.4    Sawicka, J.5    Szczesna-Cordary, D.6    Light, P.E.7    Sawicki, G.8
  • 91
    • 23044497564 scopus 로고    scopus 로고
    • Degradation of myosin light chain in isolated rat hearts subjected to ischemia–reperfusion injury: a new intracellular target for matrix metalloproteinase-2
    • COI: 1:CAS:528:DC%2BD2MXmt1yht7g%3D, PID: 16027249
    • Sawicki G, Leon H, Sawicka J, Sariahmetoglu M, Schulze CJ, Scott PG, Szczesna-Cordary D, Schulz R (2005) Degradation of myosin light chain in isolated rat hearts subjected to ischemia–reperfusion injury: a new intracellular target for matrix metalloproteinase-2. Circulation 112:544–552
    • (2005) Circulation , vol.112 , pp. 544-552
    • Sawicki, G.1    Leon, H.2    Sawicka, J.3    Sariahmetoglu, M.4    Schulze, C.J.5    Scott, P.G.6    Szczesna-Cordary, D.7    Schulz, R.8
  • 93
    • 0029938767 scopus 로고    scopus 로고
    • Characterization of 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one as a heme-site inhibitor of nitric oxide-sensitive guanylyl cyclase
    • COI: 1:CAS:528:DyaK28XksVymu7Y%3D, PID: 8700100
    • Schrammel A, Behrends S, Schmidt K, Koesling D, Mayer B (1996) Characterization of 1H-[1,2,4]oxadiazolo[4,3-a]quinoxalin-1-one as a heme-site inhibitor of nitric oxide-sensitive guanylyl cyclase. Mol Pharmacol 50:1–5
    • (1996) Mol Pharmacol , vol.50 , pp. 1-5
    • Schrammel, A.1    Behrends, S.2    Schmidt, K.3    Koesling, D.4    Mayer, B.5
  • 94
    • 0034069386 scopus 로고    scopus 로고
    • Paracrine and autocrine effects of nitric oxide on myocardial function
    • COI: 1:CAS:528:DC%2BD3cXit1WmsLs%3D, PID: 10760546
    • Shah AM, MacCarthy PA (2000) Paracrine and autocrine effects of nitric oxide on myocardial function. Pharmacol Ther 86:49–86
    • (2000) Pharmacol Ther , vol.86 , pp. 49-86
    • Shah, A.M.1    MacCarthy, P.A.2
  • 95
    • 57449117141 scopus 로고    scopus 로고
    • An FHL1-containing complex within the cardiomyocyte sarcomere mediates hypertrophic biomechanical stress responses in mice
    • COI: 1:CAS:528:DC%2BD1cXhsVKgu73F, PID: 19033658
    • Sheikh F, Raskin A, Chu PH et al (2008) An FHL1-containing complex within the cardiomyocyte sarcomere mediates hypertrophic biomechanical stress responses in mice. J Clin Investig 118:3870–3880
    • (2008) J Clin Investig , vol.118 , pp. 3870-3880
    • Sheikh, F.1    Raskin, A.2    Chu, P.H.3
  • 96
    • 33645969578 scopus 로고    scopus 로고
    • Redox modulation of contractile function in respiratory and limb skeletal muscle
    • COI: 1:CAS:528:DC%2BD28XjsFOgsb4%3D, PID: 16481226
    • Smith MA, Reid MB (2006) Redox modulation of contractile function in respiratory and limb skeletal muscle. Respir Physiol Neurobiol 151:229–241
    • (2006) Respir Physiol Neurobiol , vol.151 , pp. 229-241
    • Smith, M.A.1    Reid, M.B.2
  • 97
    • 84872865639 scopus 로고    scopus 로고
    • Oxidative stress and sarcomeric proteins
    • COI: 1:CAS:528:DC%2BC3sXhtFynsLw%3D, PID: 23329794
    • Steinberg SF (2013) Oxidative stress and sarcomeric proteins. Circ Res 112:393–405
    • (2013) Circ Res , vol.112 , pp. 393-405
    • Steinberg, S.F.1
  • 98
    • 0037160091 scopus 로고    scopus 로고
    • Topology of superoxide production from different sites in the mitochondrial electron transport chain
    • COI: 1:CAS:528:DC%2BD38Xosl2msro%3D, PID: 12237311
    • St-Pierre J, Buckingham JA, Roebuck SJ, Brand MD (2002) Topology of superoxide production from different sites in the mitochondrial electron transport chain. J Biol Chem 277:44784–44790
    • (2002) J Biol Chem , vol.277 , pp. 44784-44790
    • St-Pierre, J.1    Buckingham, J.A.2    Roebuck, S.J.3    Brand, M.D.4
  • 99
    • 34548820960 scopus 로고    scopus 로고
    • Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-actinin in peroxynitrite mediated myocardial injury
    • COI: 1:CAS:528:DC%2BD2sXhtFWit7fF, PID: 17854826
    • Sung MM, Schulz CG, Wang W, Sawicki G, Bautista-López NL, Schulz R (2007) Matrix metalloproteinase-2 degrades the cytoskeletal protein alpha-actinin in peroxynitrite mediated myocardial injury. J Mol Cell Cardiol 43:429–436
    • (2007) J Mol Cell Cardiol , vol.43 , pp. 429-436
    • Sung, M.M.1    Schulz, C.G.2    Wang, W.3    Sawicki, G.4    Bautista-López, N.L.5    Schulz, R.6
  • 100
    • 84882600223 scopus 로고    scopus 로고
    • Oxidative stress and pathology in muscular dystrophies: focus on protein thiol oxidation and dysferlinopathies
    • COI: 1:CAS:528:DC%2BC3sXht1ylsrzN, PID: 23332128
    • Terrill JR, Radley-Crabb HG, Iwasaki T, Lemckert FA, Arthur PG, Grounds MD (2013) Oxidative stress and pathology in muscular dystrophies: focus on protein thiol oxidation and dysferlinopathies. FEBS J 280:4149–4164
    • (2013) FEBS J , vol.280 , pp. 4149-4164
    • Terrill, J.R.1    Radley-Crabb, H.G.2    Iwasaki, T.3    Lemckert, F.A.4    Arthur, P.G.5    Grounds, M.D.6
  • 102
  • 103
    • 84865209443 scopus 로고    scopus 로고
    • Low myocardial protein kinase G activity in heart failure with preserved ejection fraction
    • PID: 22806632
    • van Heerebeek L, Hamdani N, Falcão-Pires I et al (2012) Low myocardial protein kinase G activity in heart failure with preserved ejection fraction. Circulation 126:830–839
    • (2012) Circulation , vol.126 , pp. 830-839
    • van Heerebeek, L.1    Hamdani, N.2    Falcão-Pires, I.3
  • 104
    • 0037126045 scopus 로고    scopus 로고
    • Intracellular action of matrix metalloproteinase-2 accounts for acute myocardial ischemia and reperfusion injury
    • COI: 1:CAS:528:DC%2BD38XntVKktr8%3D, PID: 12234962
    • Wang W, Schulze CJ, Suarez-Pinzon WL, Dyck JR, Sawicki G, Schulz R (2002) Intracellular action of matrix metalloproteinase-2 accounts for acute myocardial ischemia and reperfusion injury. Circulation 106:1543–1549
    • (2002) Circulation , vol.106 , pp. 1543-1549
    • Wang, W.1    Schulze, C.J.2    Suarez-Pinzon, W.L.3    Dyck, J.R.4    Sawicki, G.5    Schulz, R.6
  • 105
    • 0035164934 scopus 로고    scopus 로고
    • Additional PKA phosphorylation sites in human cardiac troponin I
    • COI: 1:CAS:528:DC%2BD3MXktVOitw%3D%3D, PID: 11121119
    • Ward DG, Ashton PR, Trayer HR, Trayer IP (2001) Additional PKA phosphorylation sites in human cardiac troponin I. Eur J Biochem 268:179–185
    • (2001) Eur J Biochem , vol.268 , pp. 179-185
    • Ward, D.G.1    Ashton, P.R.2    Trayer, H.R.3    Trayer, I.P.4
  • 106
    • 5344277512 scopus 로고    scopus 로고
    • Titin isoform changes in rat myocardium during development
    • COI: 1:CAS:528:DC%2BD2cXnvV2kt7k%3D, PID: 15454261
    • Warren CM, Krzesinski PR, Campbell KS, Moss RL, Greaser ML (2004) Titin isoform changes in rat myocardium during development. Mech Dev 121:1301–1312
    • (2004) Mech Dev , vol.121 , pp. 1301-1312
    • Warren, C.M.1    Krzesinski, P.R.2    Campbell, K.S.3    Moss, R.L.4    Greaser, M.L.5
  • 107
    • 71249163851 scopus 로고    scopus 로고
    • Redox modulation of global phosphatase activity and protein phosphorylation in intact skeletal muscle
    • COI: 1:CAS:528:DC%2BD1MXhsFGqt77O, PID: 19841000
    • Wright VP, Reiser PJ, Clanton TL (2009) Redox modulation of global phosphatase activity and protein phosphorylation in intact skeletal muscle. J Physiol 587:5767–5781
    • (2009) J Physiol , vol.587 , pp. 5767-5781
    • Wright, V.P.1    Reiser, P.J.2    Clanton, T.L.3
  • 108
    • 0032475865 scopus 로고    scopus 로고
    • 2+/calmodulin-dependent and tetrahydrobiopterin regulatory process
    • COI: 1:CAS:528:DyaK1cXms1egtro%3D, PID: 9748253
    • 2+/calmodulin-dependent and tetrahydrobiopterin regulatory process. J Biol Chem 273:25804–25808
    • (1998) J Biol Chem , vol.273 , pp. 25804-25808
    • Xia, Y.1    Tsai, A.L.2    Berka, V.3    Zweier, J.L.4
  • 109
    • 0037076791 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates titin’s cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes
    • COI: 1:CAS:528:DC%2BD38XkvV2gsLY%3D, PID: 12065321
    • Yamasaki R, Wu Y, McNabb M, Greaser M, Labeit S, Granzier H (2002) Protein kinase A phosphorylates titin’s cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes. Circ Res 90:1181–1188
    • (2002) Circ Res , vol.90 , pp. 1181-1188
    • Yamasaki, R.1    Wu, Y.2    McNabb, M.3    Greaser, M.4    Labeit, S.5    Granzier, H.6
  • 110
    • 84905179504 scopus 로고    scopus 로고
    • Molecular mechanisms of neuronal nitric oxide synthase in cardiac function and pathophysiology
    • COI: 1:CAS:528:DC%2BC2cXht1GitL%2FK, PID: 24756636
    • Zhang YH, Jin CZ, Jang JH, Wang Y (2014) Molecular mechanisms of neuronal nitric oxide synthase in cardiac function and pathophysiology. J Physiol 592:3189–3200
    • (2014) J Physiol , vol.592 , pp. 3189-3200
    • Zhang, Y.H.1    Jin, C.Z.2    Jang, J.H.3    Wang, Y.4


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