Structural interactions between actin, tropomyosin, caldesmon and calcium binding protein and the regulation of smooth muscle thin filaments

Author:

MARSTON S.,BURTON D.,COPELAND O.,FRASER I.,GAO Y.,HODGKINSON J.,HUBER P.,LEVINE B.,EL-MEZGUELDI M.,NOTARIANNI G.

Publisher

Wiley

Subject

Physiology

Reference63 articles.

1. Characterisation of the carboxyl-terminal 10-kDa cyanogen bromide fragment of caldesmon as an actincalmodulin-binding region;Bartegi;J Biol Chem,1990

2. Comparison of the effects of calponin and the 38kDa Caldesmon fragment on formation of the ‘strong binding’ state in ghost muscle fibres;Borovikov;Biochem Biophys Res Comm,1996

3. Cloning and expression of a smooth muscle caldesmon;Bryan;J Biol Chem,1989

4. *Regulation of smooth muscle cell contraction by a C-terminal fragment of caldesmon;Burton;J Mol Cell Cardiol,1998

5. Caldesmon inhibits skeletal actomyosin subfragment-1 ATPase activity and the binding of myosin subfragment-1 to actin;Chalovich;J Biol Chem,1987

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