The calmodulin and F-actin binding sites of smooth muscle caldesmon lie in the carboxyl-terminal domain whereas the molecular weight heterogeneity lies in the middle of the molecule-Reference-Cited by-同舟云学术

The calmodulin and F-actin binding sites of smooth muscle caldesmon lie in the carboxyl-terminal domain whereas the molecular weight heterogeneity lies in the middle of the molecule

Published:1989-02 Issue:5 Volume:264 Page:2869-2875
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Riseman V M,Lynch W P,Nefsky B,Bretscher A

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference30 articles.

1. Caldesmon: Thin filament regulatory proteins of smooth- and non-muscle cells

2. The thin filaments of smooth muscles

3. Purification of a calmodulin-binding protein from chicken gizzard that interacts with F-actin.

4. Caldesmon is a Ca2+-regulatory component of native smooth-muscle thin filaments

5. Inhibition of smooth muscle actin-activated myosin Mg2+-ATPase activity by caldesmon.

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