Biophysics of Titin in Cardiac Health and Disease
Author:
Publisher
Springer New York
Link
http://link.springer.com/content/pdf/10.1007/978-1-4614-7678-8_10
Reference110 articles.
1. Furst, D. O., Osborn, M., Nave, R., & Weber, K. (1988). 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. The Journal of Cell Biology, 106(5), 1563–1572.
2. Labeit, S., & Kolmerer, B. (1995). Titins: Giant proteins in charge of muscle ultrastructure and elasticity. Science, 270(5234), 293–296.
3. Bang, M. L., 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. Circulation Research, 89(11), 1065–1072.
4. Helmes, M., et al. (1999). Mechanically driven contour-length adjustment in rat cardiac titin’s unique N2B sequence: Titin is an adjustable spring. Circulation Research, 84(11), 1339–1352.
5. Horowits, R., & Podolsky, R. J. (1987). The positional stability of thick filaments in activated skeletal muscle depends on sarcomere length: Evidence for the role of titin filaments. The Journal of Cell Biology, 105(5), 2217–2223.
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