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Unphosphorylated calponin enhances the binding force of unphosphorylated myosin to actin

  • Published:2013-10 Issue:10 Volume:1830 Page:4634-4641
  • ISSN:0304-4165
  • Container-title:Biochimica et Biophysica Acta (BBA) - General Subjects
  • language:en
  • Short-container-title:Biochimica et Biophysica Acta (BBA) - General Subjects

Author:

Roman Horia Nicolae,Zitouni Nedjma B.,Kachmar Linda,IJpma Gijs,Hilbert Lennart,Matusovsky Oleg,Benedetti Andrea,Sobieszek Apolinary,Lauzon Anne-Marie

Funder

Natural Sciences and Engineering Research Council of Canada (NSERC)

National Heart, Lung, and Blood Institute

Costello Fund

Le Fonds de la Recherche en Santé du Québec (FRSQ)

Publisher

Elsevier BV

Subject

Molecular Biology,Biochemistry,Biophysics

Reference41 articles.

1. Myosin phosphorylation and the cross-bridge cycle in arterial smooth muscle;Dillon;Science,1981

2. Mapping of the functional domains in the amino-terminal region of calponin;Mezgueldi;J. Biol. Chem.,1992

3. Interaction of calponin with actin and its functional implications;Kolakowski;Biochem. J.,1995

4. Isolation and characterization of a 34,000-dalton calmodulin- and F-actin-binding protein from chicken gizzard smooth muscle;Takahashi;Biochem. Biophys. Res. Commun.,1986

5. Slow cycling of unphosphorylated myosin is inhibited by calponin, thus keeping smooth muscle relaxed;Malmqvist;Proc. Natl. Acad. Sci. U. S. A.,1997

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