Role of the Basic C-Terminal Half of Caldesmon in Its Regulation of F-Actin: Comparison between Caldesmon and Calponin
Author:
Publisher
Oxford University Press (OUP)
Subject
Molecular Biology,Biochemistry,General Medicine
Link
http://academic.oup.com/jb/article-pdf/138/6/805/2472140/mvi181.pdf
Reference56 articles.
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2. Yamashiro, S., Yamakita, Y., Yoshida, K., Takiguchi, K., and Matsumura, F. (1995) Characterization of the COOH terminus of non-muscle caldesmon mutants lacking mitosis-specific phosphorylation sites. J. Biol. Chem.270, 4023–4030
3. Sobue, K., Muramoto, Y., Fujita, M., and Kakiuchi, S. (1981) Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin. Proc. Natl. Acad. Sci. USA78, 5652–5655
4. Lash, J.A., Sellers, J.R., and Hathaway, D.R. (1986) The effects of caldesmon on smooth muscle heavy actomeromyosin ATPase activity and binding of heavy meromyosin to actin. J. Biol. Chem.261, 16155–16160
5. Velaz, L., Hemric, M.E., Benson, C.E., and Chalovich, J.M. (1989) The binding of caldesmon to actin and its effect on the ATPase activity of soluble myosin subfragments in the presence and absence of tropomyosin. J. Biol. Chem.264, 9602–9610
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