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Volumn 125, Issue 3, 2005, Pages 249-252

Commentary: Modulation of cardiac function: Titin springs into action

Author keywords

[No Author keywords available]

Indexed keywords

CONNECTIN; ISOPROTEIN; MUSCLE PROTEIN; PROTEIN KINASE;

EID: 15244358176     PISSN: 00221295     EISSN: None     Source Type: Journal    
DOI: 10.1085/jgp.200509268     Document Type: Note
Times cited : (15)

References (19)
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    • Bers, D.M. 2002. Cardiac excitation-contraction coupling. Nature. 415:198-205.
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    • Bers, D.M.1
  • 5
    • 15244348075 scopus 로고    scopus 로고
    • Phosphorylation of titin modulates passive stiffness cardiac muscle in a titin isoform-dependent manner
    • Fukuda, N., P. Nair, Y. Wu, and H. Granzier. 2005. Phosphorylation of titin modulates passive stiffness cardiac muscle in a titin isoform-dependent manner. J. Gen. Physiol. 125:257-271.
    • (2005) J. Gen. Physiol. , vol.125 , pp. 257-271
    • Fukuda, N.1    Nair, P.2    Wu, Y.3    Granzier, H.4
  • 6
    • 1242342244 scopus 로고    scopus 로고
    • The giant protein titin: A major player in myocardial mechanics, signaling, and disease
    • Granzier, H.L., and S. Labeit. 2004. The giant protein titin: a major player in myocardial mechanics, signaling, and disease. Circ. Res. 94:284-295.
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    • Granzier, H.L.1    Labeit, S.2
  • 7
    • 0033546073 scopus 로고    scopus 로고
    • Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: Titin is an adjustable spring
    • Helmes, M., K. Trombitas, T. Centner, M. Kellermayer, S. Labeit, W.A. Linke, and H. Granzier. 1999. Mechanically driven contour-length adjustment in rat cardiac titin's unique N2B sequence: titin is an adjustable spring. Circ. Res. 84:1339-1352.
    • (1999) Circ. Res. , vol.84 , pp. 1339-1352
    • Helmes, M.1    Trombitas, K.2    Centner, T.3    Kellermayer, M.4    Labeit, S.5    Linke, W.A.6    Granzier, H.7
  • 10
    • 1242281665 scopus 로고    scopus 로고
    • Developmental control of titin isoform expression and passive stiffness in fetal and neonatal myocardium
    • Lahmers, S., Y. Wu, D.R. Call, S. Labeit, and H. Granzier. 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
  • 11
    • 3142673477 scopus 로고    scopus 로고
    • Titin isoforms in heart failure: Are there benefits to supersizing?
    • LeWinter, M.M. 2004. Titin isoforms in heart failure: are there benefits to supersizing? Circulation. 110:109-111.
    • (2004) Circulation , vol.110 , pp. 109-111
    • LeWinter, M.M.1
  • 15
    • 1842830381 scopus 로고    scopus 로고
    • Developmentally regulated switching of titin size alters myofibrillar stiffness in the perinatal heart
    • Opitz, C.A., M.C. Leake, I. Makarenko, V. Benes, and W.A. Linke. 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
  • 17
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    • Changes in titin isoform expression in pacing-induced cardiac failure give rise to increased passive muscle stiffness
    • Wu, Y., S.P. Bell, K. Trombitas, C.C. Witt, S. Labeit, M.M. LeWinter, and H. Granzier. 2002. Changes in titin isoform expression in pacing-induced cardiac failure give rise to increased passive muscle stiffness. Circulation. 106:1384-1389.
    • (2002) Circulation , vol.106 , pp. 1384-1389
    • Wu, Y.1    Bell, S.P.2    Trombitas, K.3    Witt, C.C.4    Labeit, S.5    Lewinter, M.M.6    Granzier, H.7
  • 19
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    • Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes
    • Yamasaki, R., Y. Wu, M. McNabb, M. Greaser, S. Labeit, and H. Granzier. 2002. Protein kinase A phosphorylates titin's cardiac-specific N2B domain and reduces passive tension in rat cardiac myocytes. Circ. Res. 90:1181-1188.
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* 이 정보는 Elsevier사의 SCOPUS DB에서 KISTI가 분석하여 추출한 것입니다.