Structures of the troponin core domain containing the cardiomyopathy-causing mutants studied by small-angle X-ray scattering
Author:
Affiliation:
1. Quantum Beam Science Center, Japan Atomic Energy Agency
2. National Cerebral and Cardiovascular Center Research Institute
3. RIKEN SPring-8 center, RIKEN Harima Institute
4. Present address: Tokai Gakuin University
Publisher
Biophysical Society of Japan
Subject
General Medicine
Link
https://www.jstage.jst.go.jp/article/biophysico/12/0/12_145/_pdf
Reference19 articles.
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2. [3] Harada, K. & Morimoto, S. Inherited cardiomyopathies as a troponin disease. Jpn. J. Physiol. 54, 307–318 (2004).
3. [5] Maeda, Y., Nitanai, Y. & Oda, T. From the crystal structure of troponin to the mechanism of calcium regulation of muscle contraction. Adv. Exp. Med. Biol. 592, 37–46 (2007).
4. [6] Takeda, S., Yamashita, A., Maeda, K. & Maéda, Y. Structure of the core domain of human cardiac troponin in the Ca2+-saturated form. Nature 424, 35–41 (2003).
5. [7] Yanaga, F., Morimoto, S. & Ohtsuki, I. Ca2+ sensitization and potentiation of the maximum level of myofibrillar ATPase activity caused by mutations of troponin T found in familial hypertrophic cardiomyopathy. J. Biol. Chem. 274, 8806–8812 (1999).
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