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A calponin peptide enhances Ca2+ sensitivity of smooth muscle contraction without affecting myosin light chain phosphorylation.
Itoh T, Suzuki A, Watanabe Y, Mino T, Naka M, Tanaka T. Itoh T, et al. Among authors: tanaka t. J Biol Chem. 1995 Sep 1;270(35):20400-3. doi: 10.1074/jbc.270.35.20400. J Biol Chem. 1995. PMID: 7657614 Free article.
In permeabilized smooth muscle, exogenously applied calponin binds to myofibrils and reduces Ca(2+)-activated tension (Itoh, T., Suzuki, S., Suzuki, A., Nakamura, F., Naka, M., and Tanaka, T. (1994) Pflugers Arch. ...
In permeabilized smooth muscle, exogenously applied calponin binds to myofibrils and reduces Ca(2+)-activated tension (Itoh, T., Suzu …
Two distinct actin-binding sites of smooth muscle calponin.
Mino T, Yuasa U, Nakamura F, Naka M, Tanaka T. Mino T, et al. Among authors: tanaka t. Eur J Biochem. 1998 Jan 15;251(1-2):262-8. doi: 10.1046/j.1432-1327.1998.2510262.x. Eur J Biochem. 1998. PMID: 9492292 Free article.
Our previous work demonstrated that a fragment of calponin, which corresponded to the first repeated region of calponin and contained the preferred site of phosphorylation by protein kinase C [Nakamura, F., Mino, T., Yamamoto, J., Naka, M. & Tanaka, T. (1 …
Our previous work demonstrated that a fragment of calponin, which corresponded to the first repeated region of calponin and contained the pr …
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