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Caldesmon, human

Known as: CDM, Caldesmon 
Caldesmon (793 aa, ~93 kDa) is encoded by the human CALD1 gene. This protein is involved in binding to and stabilization of filamentous actin.
National Institutes of Health

Related topics

Related topics

14 relations
Actin-Binding ProteinCALD1 geneCALD1 wt AlleleCell Movement

Broader (1)

Caldesmon

Papers overview

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Highly Cited
2012
Highly Cited
2012
Failed Mechanism: How the CDM is Subsidizing Hydro Developers and Harming the Kyoto Protocol
Five years age, International Rivers started monitoring the Kyoto Protocol’s Clean Development Mechanism (CDM), concerned that… 
Highly Cited
2000
Highly Cited
2000
Phosphorylation of Caldesmon by p21-activated Kinase
We have previously shown that p21-activated kinase, PAK, induces Ca2+-independent contraction of Triton-skinned smooth muscle… 
Highly Cited
1999
Highly Cited
1999
Mammal-specific, ERK-dependent, Caldesmon Phosphorylation in Smooth Muscle
Extracellular signal-regulated kinases (ERKs) phosphorylate the high molecular mass isoform of the actin-binding protein… 
Highly Cited
1996
Highly Cited
1996
Phenotypic Modulation of the Mesangium Reflected by Contractile Proteins in Diabetes
The phenotypic change of the mesangial cell is considered to play a pivotal role in the accumulation of extracellular matrix in… 
Highly Cited
1991
Highly Cited
1991
Localization of the calmodulin- and the actin-binding sites of caldesmon.
Review
1991
Review
1991
Regulation of the contractile element of airway smooth muscle.
Smooth muscle of the mammalian airways controls airway diameter and resistance to airflow. Smooth muscle tone is in turn… 
Highly Cited
1990
Highly Cited
1990
Dissociation of the effect of caldesmon on the ATPase activity and on the binding of smooth heavy meromyosin to actin by partial digestion of caldesmon.
Highly Cited
1988
Highly Cited
1988
Binding of caldesmon to smooth muscle myosin.
Highly Cited
1984
Highly Cited
1984
Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties.
A method for the rapid purification of caldesmon, an F-actin binding protein of smooth muscle, has been developed. Caldesmon… 
Highly Cited
1984
Highly Cited
1984
Occurrence of caldesmon (a calmodulin-binding protein) in cultured cells: comparison of normal and transformed cells.
Caldesmon is a calmodulin-binding and F-actin-binding protein originally purified from chicken gizzard smooth muscle. This… 
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