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Volumn 109, Issue 12, 2015, Pages 2592-2601

Phosphorylating Titin's Cardiac N2B Element by ERK2 or CaMKIIδ Lowers the Single Molecule and Cardiac Muscle Force

Author keywords

[No Author keywords available]

Indexed keywords

CALCIUM CALMODULIN DEPENDENT PROTEIN KINASE II; CONNECTIN; MITOGEN ACTIVATED PROTEIN KINASE 1;

EID: 84954117825     PISSN: 00063495     EISSN: 15420086     Source Type: Journal    
DOI: 10.1016/j.bpj.2015.11.002     Document Type: Article
Times cited : (29)

References (58)
  • 1
    • 30944461257 scopus 로고    scopus 로고
    • Titin: Physiological function and role in cardiomyopathy and failure
    • H. Granzier, and Y. Wu M. LeWinter Titin: physiological function and role in cardiomyopathy and failure Heart Fail. Rev. 10 2005 211 223
    • (2005) Heart Fail. Rev. , vol.10 , pp. 211-223
    • Granzier, H.1    Wu, Y.2    LeWinter, M.3
  • 2
    • 0025816649 scopus 로고
    • Regulation of skeletal muscle stiffness and elasticity by titin isoforms: A test of the segmental extension model of resting tension
    • K. Wang, and R. McCarter R. Ramirez-Mitchell Regulation of skeletal muscle stiffness and elasticity by titin isoforms: a test of the segmental extension model of resting tension Proc. Natl. Acad. Sci. USA 88 1991 7101 7105
    • (1991) Proc. Natl. Acad. Sci. USA , vol.88 , pp. 7101-7105
    • Wang, K.1    McCarter, R.2    Ramirez-Mitchell, R.3
  • 3
    • 0023924769 scopus 로고
    • The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: A map of ten nonrepetitive epitopes starting at the Z line extends close to the M line
    • D.O. Fürst, and M. Osborn K. Weber The organization of titin filaments in the half-sarcomere revealed by monoclonal antibodies in immunoelectron microscopy: a map of ten nonrepetitive epitopes starting at the Z line extends close to the M line J. Cell Biol. 106 1988 1563 1572
    • (1988) J. Cell Biol. , vol.106 , pp. 1563-1572
    • Fürst, D.O.1    Osborn, M.2    Weber, K.3
  • 4
    • 0029805084 scopus 로고    scopus 로고
    • Titin/connectin and nebulin: Giant protein rulers of muscle structure and function
    • K. Wang Titin/connectin and nebulin: giant protein rulers of muscle structure and function Adv. Biophys. 33 1996 123 134
    • (1996) Adv. Biophys. , vol.33 , pp. 123-134
    • Wang, K.1
  • 5
    • 0028957373 scopus 로고
    • Passive tension in cardiac muscle: Contribution of collagen, titin, microtubules, and intermediate filaments
    • H.L. Granzier, and T.C. Irving Passive tension in cardiac muscle: contribution of collagen, titin, microtubules, and intermediate filaments Biophys. J. 68 1995 1027 1044
    • (1995) Biophys. J. , vol.68 , pp. 1027-1044
    • Granzier, H.L.1    Irving, T.C.2
  • 6
    • 0027934071 scopus 로고
    • Passive and active tension in single cardiac myofibrils
    • W.A. Linke, V.I. Popov, and G.H. Pollack Passive and active tension in single cardiac myofibrils Biophys. J. 67 1994 782 792
    • (1994) Biophys. J. , vol.67 , pp. 782-792
    • Linke, W.A.1    Popov, V.I.2    Pollack, G.H.3
  • 7
    • 0029143981 scopus 로고
    • The mechanically active domain of titin in cardiac muscle
    • K. Trombitás, J.P. Jin, and H. Granzier The mechanically active domain of titin in cardiac muscle Circ. Res. 77 1995 856 861
    • (1995) Circ. Res. , vol.77 , pp. 856-861
    • Trombitás, K.1    Jin, J.P.2    Granzier, H.3
  • 8
    • 18544406997 scopus 로고    scopus 로고
    • Series of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity
    • A. Freiburg, and K. Trombitas S. Labeit Series of exon-skipping events in the elastic spring region of titin as the structural basis for myofibrillar elastic diversity Circ. Res. 86 2000 1114 1121
    • (2000) Circ. Res. , vol.86 , pp. 1114-1121
    • Freiburg, A.1    Trombitas, K.2    Labeit, S.3
  • 9
    • 0033962880 scopus 로고    scopus 로고
    • Differential expression of cardiac titin isoforms and modulation of cellular stiffness
    • O. Cazorla, and A. Freiburg H. Granzier Differential expression of cardiac titin isoforms and modulation of cellular stiffness Circ. Res. 86 2000 59 67
    • (2000) Circ. Res. , vol.86 , pp. 59-67
    • Cazorla, O.1    Freiburg, A.2    Granzier, H.3
  • 10
    • 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
    • M.L. Bang, and T. Centner S. Labeit 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 2001 1065 1072
    • (2001) Circ. Res. , vol.89 , pp. 1065-1072
    • Bang, M.L.1    Centner, T.2    Labeit, S.3
  • 11
    • 84878871182 scopus 로고    scopus 로고
    • Tuning the molecular giant titin through phosphorylation: Role in health and disease
    • C. Hidalgo, and H. Granzier Tuning the molecular giant titin through phosphorylation: role in health and disease Trends Cardiovasc. Med. 23 2013 165 171
    • (2013) Trends Cardiovasc. Med. , vol.23 , pp. 165-171
    • Hidalgo, C.1    Granzier, H.2
  • 12
    • 84897874678 scopus 로고    scopus 로고
    • Gigantic business: Titin properties and function through thick and thin
    • W.A. Linke, and N. Hamdani Gigantic business: titin properties and function through thick and thin Circ. Res. 114 2014 1052 1068
    • (2014) Circ. Res. , vol.114 , pp. 1052-1068
    • Linke, W.A.1    Hamdani, N.2
  • 13
    • 84929376932 scopus 로고    scopus 로고
    • Myocardial stiffness in patients with heart failure and a preserved ejection fraction: Contributions of collagen and titin
    • M.R. Zile, and C.F. Baicu M.M. LeWinter Myocardial stiffness in patients with heart failure and a preserved ejection fraction: contributions of collagen and titin Circulation 131 2015 1247 1259
    • (2015) Circulation , vol.131 , pp. 1247-1259
    • Zile, M.R.1    Baicu, C.F.2    LeWinter, M.M.3
  • 14
    • 84874264782 scopus 로고    scopus 로고
    • Deranged myofilament phosphorylation and function in experimental heart failure with preserved ejection fraction
    • N. Hamdani, and K.G. Bishu W.A. Linke Deranged myofilament phosphorylation and function in experimental heart failure with preserved ejection fraction Cardiovasc. Res. 97 2013 464 471
    • (2013) Cardiovasc. Res. , vol.97 , pp. 464-471
    • Hamdani, N.1    Bishu, K.G.2    Linke, W.A.3
  • 16
    • 84874476580 scopus 로고    scopus 로고
    • Titin is a major human disease gene
    • M.M. LeWinter, and H.L. Granzier Titin is a major human disease gene Circulation 127 2013 938 944
    • (2013) Circulation , vol.127 , pp. 938-944
    • LeWinter, M.M.1    Granzier, H.L.2
  • 17
    • 79952829685 scopus 로고    scopus 로고
    • Heart failure with preserved ejection fraction: Pathophysiology, diagnosis, and treatment
    • B.A. Borlaug, and W.J. Paulus Heart failure with preserved ejection fraction: pathophysiology, diagnosis, and treatment Eur. Heart J. 32 2011 670 679
    • (2011) Eur. Heart J. , vol.32 , pp. 670-679
    • Borlaug, B.A.1    Paulus, W.J.2
  • 18
    • 0037076791 scopus 로고    scopus 로고
    • Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes
    • R. Yamasaki, and Y. Wu H. Granzier Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes Circ. Res. 90 2002 1181 1188
    • (2002) Circ. Res. , vol.90 , pp. 1181-1188
    • Yamasaki, R.1    Wu, Y.2    Granzier, H.3
  • 19
    • 15244348075 scopus 로고    scopus 로고
    • Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner
    • N. Fukuda, and Y. Wu H.L. Granzier Phosphorylation of titin modulates passive stiffness of cardiac muscle in a titin isoform-dependent manner J. Gen. Physiol. 125 2005 257 271
    • (2005) J. Gen. Physiol. , vol.125 , pp. 257-271
    • Fukuda, N.1    Wu, Y.2    Granzier, H.L.3
  • 20
    • 59649084739 scopus 로고    scopus 로고
    • Protein kinase G modulates human myocardial passive stiffness by phosphorylation of the titin springs
    • M. Krüger, and S. Kötter W.A. Linke Protein kinase G modulates human myocardial passive stiffness by phosphorylation of the titin springs Circ. Res. 104 2009 87 94
    • (2009) Circ. Res. , vol.104 , pp. 87-94
    • Krüger, M.1    Kötter, S.2    Linke, W.A.3
  • 21
    • 84874256463 scopus 로고    scopus 로고
    • Crucial role for Ca2(+)/calmodulin-dependent protein kinase-II in regulating diastolic stress of normal and failing hearts via titin phosphorylation
    • N. Hamdani, and J. Krysiak W.A. Linke Crucial role for Ca2(+)/calmodulin-dependent protein kinase-II in regulating diastolic stress of normal and failing hearts via titin phosphorylation Circ. Res. 112 2013 664 674
    • (2013) Circ. Res. , vol.112 , pp. 664-674
    • Hamdani, N.1    Krysiak, J.2    Linke, W.A.3
  • 22
    • 84871383473 scopus 로고    scopus 로고
    • The multifunctional Ca(2+)/calmodulin-dependent protein kinase II delta (CaMKIIδ) phosphorylates cardiac titin's spring elements
    • C.G. Hidalgo, and C.S. Chung H.L. Granzier The multifunctional Ca(2+)/calmodulin-dependent protein kinase II delta (CaMKIIδ) phosphorylates cardiac titin's spring elements J. Mol. Cell. Cardiol. 54 2013 90 97
    • (2013) J. Mol. Cell. Cardiol. , vol.54 , pp. 90-97
    • Hidalgo, C.G.1    Chung, C.S.2    Granzier, H.L.3
  • 23
    • 49049108214 scopus 로고    scopus 로고
    • The role of calmodulin kinase II in myocardial physiology and disease
    • L.F. Couchonnal, and M.E. Anderson The role of calmodulin kinase II in myocardial physiology and disease Physiology (Bethesda) 23 2008 151 159
    • (2008) Physiology (Bethesda) , vol.23 , pp. 151-159
    • Couchonnal, L.F.1    Anderson, M.E.2
  • 24
    • 0034697901 scopus 로고    scopus 로고
    • Frequency-encoding Thr17 phospholamban phosphorylation is independent of Ser16 phosphorylation in cardiac myocytes
    • D. Hagemann, and M. Kuschel R.P. Xiao Frequency-encoding Thr17 phospholamban phosphorylation is independent of Ser16 phosphorylation in cardiac myocytes J. Biol. Chem. 275 2000 22532 22536
    • (2000) J. Biol. Chem. , vol.275 , pp. 22532-22536
    • Hagemann, D.1    Kuschel, M.2    Xiao, R.P.3
  • 25
    • 0035957010 scopus 로고    scopus 로고
    • Calmodulin kinase is a molecular switch for cardiac excitation-contraction coupling
    • Y. Wu, R.J. Colbran, and M.E. Anderson Calmodulin kinase is a molecular switch for cardiac excitation-contraction coupling Proc. Natl. Acad. Sci. USA 98 2001 2877 2881
    • (2001) Proc. Natl. Acad. Sci. USA , vol.98 , pp. 2877-2881
    • Wu, Y.1    Colbran, R.J.2    Anderson, M.E.3
  • 27
    • 0028908407 scopus 로고
    • A site phosphorylated in bovine cardiac troponin T by cardiac CaM kinase II
    • K. Jaquet, and K. Fukunaga H.E. Meyer A site phosphorylated in bovine cardiac troponin T by cardiac CaM kinase II Biochim. Biophys. Acta 1248 1995 193 195
    • (1995) Biochim. Biophys. Acta , vol.1248 , pp. 193-195
    • Jaquet, K.1    Fukunaga, K.2    Meyer, H.E.3
  • 28
    • 0021713707 scopus 로고
    • 2+-calmodulin-dependent protein kinases
    • 2+-calmodulin-dependent protein kinases J. Biol. Chem. 259 1984 15587 15596
    • (1984) J. Biol. Chem. , vol.259 , pp. 15587-15596
    • Hartzell, H.C.1    Glass, D.B.2
  • 29
    • 52049115619 scopus 로고    scopus 로고
    • Phospholamban phosphorylation by CaMKII under pathophysiological conditions
    • L. Vittone, C. Mundina-Weilenmann, and A. Mattiazzi Phospholamban phosphorylation by CaMKII under pathophysiological conditions Front. Biosci. 13 2008 5988 6005
    • (2008) Front. Biosci. , vol.13 , pp. 5988-6005
    • Vittone, L.1    Mundina-Weilenmann, C.2    Mattiazzi, A.3
  • 30
    • 84865495526 scopus 로고    scopus 로고
    • A novel mechanism involving four-and-a-half LIM domain protein-1 and extracellular signal-regulated kinase-2 regulates titin phosphorylation and mechanics
    • A. Raskin, and S. Lange F. Sheikh A novel mechanism involving four-and-a-half LIM domain protein-1 and extracellular signal-regulated kinase-2 regulates titin phosphorylation and mechanics J. Biol. Chem. 287 2012 29273 29284
    • (2012) J. Biol. Chem. , vol.287 , pp. 29273-29284
    • Raskin, A.1    Lange, S.2    Sheikh, F.3
  • 32
    • 80053123311 scopus 로고    scopus 로고
    • Mechanics on myocardium deficient in the N2B region of titin: The cardiac-unique spring element improves efficiency of the cardiac cycle
    • J. Nedrud, and S. Labeit H. Granzier Mechanics on myocardium deficient in the N2B region of titin: the cardiac-unique spring element improves efficiency of the cardiac cycle Biophys. J. 101 2011 1385 1392
    • (2011) Biophys. J. , vol.101 , pp. 1385-1392
    • Nedrud, J.1    Labeit, S.2    Granzier, H.3
  • 33
    • 33747751861 scopus 로고    scopus 로고
    • Mechanical properties of cardiac titin's N2B-region by single-molecule atomic force spectroscopy
    • M.C. Leake, and A. Grützner W.A. Linke Mechanical properties of cardiac titin's N2B-region by single-molecule atomic force spectroscopy J. Struct. Biol. 155 2006 263 272
    • (2006) J. Struct. Biol. , vol.155 , pp. 263-272
    • Leake, M.C.1    Grützner, A.2    Linke, W.A.3
  • 34
    • 0028071373 scopus 로고
    • Entropic elasticity of lambda-phage DNA
    • C. Bustamante, and J.F. Marko S. Smith Entropic elasticity of lambda-phage DNA Science 265 1994 1599 1600
    • (1994) Science , vol.265 , pp. 1599-1600
    • Bustamante, C.1    Marko, J.F.2    Smith, S.3
  • 35
    • 0028000456 scopus 로고
    • Fluctuations and supercoiling of DNA
    • J.F. Marko, and E.D. Siggia Fluctuations and supercoiling of DNA Science 265 1994 506 508
    • (1994) Science , vol.265 , pp. 506-508
    • Marko, J.F.1    Siggia, E.D.2
  • 36
    • 77955277122 scopus 로고    scopus 로고
    • Calcium sensitivity and the Frank-Starling mechanism of the heart are increased in titin N2B region-deficient mice
    • E.J. Lee, and J. Peng H.L. Granzier Calcium sensitivity and the Frank-Starling mechanism of the heart are increased in titin N2B region-deficient mice J. Mol. Cell. Cardiol. 49 2010 449 458
    • (2010) J. Mol. Cell. Cardiol. , vol.49 , pp. 449-458
    • Lee, E.J.1    Peng, J.2    Granzier, H.L.3
  • 37
    • 79952073647 scopus 로고    scopus 로고
    • Contribution of titin and extracellular matrix to passive pressure and measurement of sarcomere length in the mouse left ventricle
    • C.S. Chung, and H.L. Granzier Contribution of titin and extracellular matrix to passive pressure and measurement of sarcomere length in the mouse left ventricle J. Mol. Cell. Cardiol. 50 2011 731 739
    • (2011) J. Mol. Cell. Cardiol. , vol.50 , pp. 731-739
    • Chung, C.S.1    Granzier, H.L.2
  • 38
    • 0031711834 scopus 로고    scopus 로고
    • Complete unfolding of the titin molecule under external force
    • M.S. Kellermayer, and S.B. Smith H.L. Granzier Complete unfolding of the titin molecule under external force J. Struct. Biol. 122 1998 197 205
    • (1998) J. Struct. Biol. , vol.122 , pp. 197-205
    • Kellermayer, M.S.1    Smith, S.B.2    Granzier, H.L.3
  • 39
    • 0037192845 scopus 로고    scopus 로고
    • Molecular mechanics of cardiac titin's PEVK and N2B spring elements
    • K. Watanabe, and P. Nair H. Granzier Molecular mechanics of cardiac titin's PEVK and N2B spring elements J. Biol. Chem. 277 2002 11549 11558
    • (2002) J. Biol. Chem. , vol.277 , pp. 11549-11558
    • Watanabe, K.1    Nair, P.2    Granzier, H.3
  • 40
    • 67650738888 scopus 로고    scopus 로고
    • Stress-induced dilated cardiomyopathy in a knock-in mouse model mimicking human titin-based disease
    • M. Gramlich, and B. Michely B. Gerull Stress-induced dilated cardiomyopathy in a knock-in mouse model mimicking human titin-based disease J. Mol. Cell. Cardiol. 47 2009 352 358
    • (2009) J. Mol. Cell. Cardiol. , vol.47 , pp. 352-358
    • Gramlich, M.1    Michely, B.2    Gerull, B.3
  • 41
    • 0032785903 scopus 로고    scopus 로고
    • Molecular dissection of N2B cardiac titin's extensibility
    • K. Trombitás, and A. Freiburg H. Granzier Molecular dissection of N2B cardiac titin's extensibility Biophys. J. 77 1999 3189 3196
    • (1999) Biophys. J. , vol.77 , pp. 3189-3196
    • Trombitás, K.1    Freiburg, A.2    Granzier, H.3
  • 42
    • 0033637514 scopus 로고    scopus 로고
    • Extensibility of isoforms of cardiac titin: Variation in contour length of molecular subsegments provides a basis for cellular passive stiffness diversity
    • K. Trombitás, and A. Redkar H. Granzier Extensibility of isoforms of cardiac titin: variation in contour length of molecular subsegments provides a basis for cellular passive stiffness diversity Biophys. J. 79 2000 3226 3234
    • (2000) Biophys. J. , vol.79 , pp. 3226-3234
    • Trombitás, K.1    Redkar, A.2    Granzier, H.3
  • 43
    • 0035144607 scopus 로고    scopus 로고
    • Mechanical fatigue in repetitively stretched single molecules of titin
    • M.S. Kellermayer, and S.B. Smith H.L. Granzier Mechanical fatigue in repetitively stretched single molecules of titin Biophys. J. 80 2001 852 863
    • (2001) Biophys. J. , vol.80 , pp. 852-863
    • Kellermayer, M.S.1    Smith, S.B.2    Granzier, H.L.3
  • 44
    • 0033546073 scopus 로고    scopus 로고
    • Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: Titin is an adjustable spring
    • M. Helmes, and K. Trombitás H. Granzier Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring Circ. Res. 84 1999 1339 1352
    • (1999) Circ. Res. , vol.84 , pp. 1339-1352
    • Helmes, M.1    Trombitás, K.2    Granzier, H.3
  • 45
    • 77951977209 scopus 로고    scopus 로고
    • The effects of PKCalpha phosphorylation on the extensibility of titin's PEVK element
    • B.R. Anderson, and J. Bogomolovas H. Granzier The effects of PKCalpha phosphorylation on the extensibility of titin's PEVK element J. Struct. Biol. 170 2010 270 277
    • (2010) J. Struct. Biol. , vol.170 , pp. 270-277
    • Anderson, B.R.1    Bogomolovas, J.2    Granzier, H.3
  • 46
    • 70349668973 scopus 로고    scopus 로고
    • PKC phosphorylation of titin's PEVK element: A novel and conserved pathway for modulating myocardial stiffness
    • 617 p following 638
    • C. Hidalgo, and B. Hudson H. Granzier PKC phosphorylation of titin's PEVK element: a novel and conserved pathway for modulating myocardial stiffness Circ. Res. 105 2009 631 638 617 p following 638
    • (2009) Circ. Res. , vol.105 , pp. 631-638
    • Hidalgo, C.1    Hudson, B.2    Granzier, H.3
  • 48
    • 84864794549 scopus 로고    scopus 로고
    • CaMKII effects on inotropic but not lusitropic force frequency responses require phospholamban
    • Y. Wu, and E.D. Luczak M.E. Anderson CaMKII effects on inotropic but not lusitropic force frequency responses require phospholamban J. Mol. Cell. Cardiol. 53 2012 429 436
    • (2012) J. Mol. Cell. Cardiol. , vol.53 , pp. 429-436
    • Wu, Y.1    Luczak, E.D.2    Anderson, M.E.3
  • 49
    • 33644837326 scopus 로고    scopus 로고
    • Control of cardiac growth by histone acetylation/deacetylation
    • J. Backs, and E.N. Olson Control of cardiac growth by histone acetylation/deacetylation Circ. Res. 98 2006 15 24
    • (2006) Circ. Res. , vol.98 , pp. 15-24
    • Backs, J.1    Olson, E.N.2
  • 51
    • 58149351369 scopus 로고    scopus 로고
    • A new type of ERK1/2 autophosphorylation causes cardiac hypertrophy
    • K. Lorenz, and J.P. Schmitt M.J. Lohse A new type of ERK1/2 autophosphorylation causes cardiac hypertrophy Nat. Med. 15 2009 75 83
    • (2009) Nat. Med. , vol.15 , pp. 75-83
    • Lorenz, K.1    Schmitt, J.P.2    Lohse, M.J.3
  • 52
    • 0036843158 scopus 로고    scopus 로고
    • Involvement of extracellular signal-regulated kinases 1/2 in cardiac hypertrophy and cell death
    • O.F. Bueno, and J.D. Molkentin Involvement of extracellular signal-regulated kinases 1/2 in cardiac hypertrophy and cell death Circ. Res. 91 2002 776 781
    • (2002) Circ. Res. , vol.91 , pp. 776-781
    • Bueno, O.F.1    Molkentin, J.D.2
  • 53
    • 4043076222 scopus 로고    scopus 로고
    • Raf-1 kinase is required for cardiac hypertrophy and cardiomyocyte survival in response to pressure overload
    • I.S. Harris, and S. Zhang A.J. Muslin Raf-1 kinase is required for cardiac hypertrophy and cardiomyocyte survival in response to pressure overload Circulation 110 2004 718 723
    • (2004) Circulation , vol.110 , pp. 718-723
    • Harris, I.S.1    Zhang, S.2    Muslin, A.J.3
  • 54
    • 57449117141 scopus 로고    scopus 로고
    • An FHL1-containing complex within the cardiomyocyte sarcomere mediates hypertrophic biomechanical stress responses in mice
    • F. Sheikh, and A. Raskin J. Chen An FHL1-containing complex within the cardiomyocyte sarcomere mediates hypertrophic biomechanical stress responses in mice J. Clin. Invest. 118 2008 3870 3880
    • (2008) J. Clin. Invest. , vol.118 , pp. 3870-3880
    • Sheikh, F.1    Raskin, A.2    Chen, J.3
  • 55
    • 0037115642 scopus 로고    scopus 로고
    • Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2
    • S. Lange, and D. Auerbach E. Ehler Subcellular targeting of metabolic enzymes to titin in heart muscle may be mediated by DRAL/FHL-2 J. Cell Sci. 115 2002 4925 4936
    • (2002) J. Cell Sci. , vol.115 , pp. 4925-4936
    • Lange, S.1    Auerbach, D.2    Ehler, E.3
  • 56
    • 84912056762 scopus 로고    scopus 로고
    • Increased myocardial stiffness due to cardiac titin isoform switching in a mouse model of volume overload limits eccentric remodeling
    • K.R. Hutchinson, and C. Saripalli H. Granzier Increased myocardial stiffness due to cardiac titin isoform switching in a mouse model of volume overload limits eccentric remodeling J. Mol. Cell. Cardiol. 79 2015 104 114
    • (2015) J. Mol. Cell. Cardiol. , vol.79 , pp. 104-114
    • Hutchinson, K.R.1    Saripalli, C.2    Granzier, H.3
  • 57
    • 84991481602 scopus 로고    scopus 로고
    • Deleting titin's I-band/A-band junction reveals critical roles for titin in biomechanical sensing and cardiac function
    • H.L. Granzier, and K.R. Hutchinson J.E. Smith 3rd Deleting titin's I-band/A-band junction reveals critical roles for titin in biomechanical sensing and cardiac function Proc. Natl. Acad. Sci. USA 111 2014 14589 14594
    • (2014) Proc. Natl. Acad. Sci. USA , vol.111 , pp. 14589-14594
    • Granzier, H.L.1    Hutchinson, K.R.2    Smith, J.E.3
  • 58
    • 84879753113 scopus 로고    scopus 로고
    • Shortening of the elastic tandem immunoglobulin segment of titin leads to diastolic dysfunction
    • C.S. Chung, and K.R. Hutchinson H.L. Granzier Shortening of the elastic tandem immunoglobulin segment of titin leads to diastolic dysfunction Circulation 128 2013 19 28
    • (2013) Circulation , vol.128 , pp. 19-28
    • Chung, C.S.1    Hutchinson, K.R.2    Granzier, H.L.3


* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.