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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
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Related topics
Related topics
14 relations
Actin-Binding Protein
CALD1 gene
CALD1 wt Allele
Cell Movement
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Broader (1)
Caldesmon
Papers overview
Semantic Scholar uses AI to extract papers important to this topic.
Highly Cited
2012
Highly Cited
2012
Failed Mechanism: How the CDM is Subsidizing Hydro Developers and Harming the Kyoto Protocol
Barbara K. Haya
2012
Corpus ID: 128371926
Five years age, International Rivers started monitoring the Kyoto Protocol’s Clean Development Mechanism (CDM), concerned that…
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Highly Cited
2000
Highly Cited
2000
Phosphorylation of Caldesmon by p21-activated Kinase
D. B. Foster
,
L. Shen
,
J. Kelly
,
P. Thibault
,
J. V. Van Eyk
,
A. Mak
Journal of Biological Chemistry
2000
Corpus ID: 24197258
We have previously shown that p21-activated kinase, PAK, induces Ca2+-independent contraction of Triton-skinned smooth muscle…
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Highly Cited
1999
Highly Cited
1999
Mammal-specific, ERK-dependent, Caldesmon Phosphorylation in Smooth Muscle
G. D'Angelo
,
P. Graceffa
,
C. A. Wang
,
J. Wrangle
,
L. Adam
Journal of Biological Chemistry
1999
Corpus ID: 30202904
Extracellular signal-regulated kinases (ERKs) phosphorylate the high molecular mass isoform of the actin-binding protein…
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Highly Cited
1996
Highly Cited
1996
Phenotypic Modulation of the Mesangium Reflected by Contractile Proteins in Diabetes
H. Makino
,
N. Kashihara
,
+6 authors
R. Nagai
Diabetes
1996
Corpus ID: 20873559
The phenotypic change of the mesangial cell is considered to play a pivotal role in the accumulation of extracellular matrix in…
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Highly Cited
1991
Highly Cited
1991
Localization of the calmodulin- and the actin-binding sites of caldesmon.
C. L. Wang
,
L. W. Wang
,
S. Xu
,
R. Lu
,
V. Saavedra-Alanis
,
J. Bryan
Journal of Biological Chemistry
1991
Corpus ID: 24089954
Review
1991
Review
1991
Regulation of the contractile element of airway smooth muscle.
W. Gerthoffer
American Journal of Physiology
1991
Corpus ID: 28410641
Smooth muscle of the mammalian airways controls airway diameter and resistance to airflow. Smooth muscle tone is in turn…
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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.
L. Velaz
,
R. Ingraham
,
J. Chalovich
Journal of Biological Chemistry
1990
Corpus ID: 8952342
Highly Cited
1988
Highly Cited
1988
Binding of caldesmon to smooth muscle myosin.
M. Ikebe
,
S. Reardon
Journal of Biological Chemistry
1988
Corpus ID: 21412947
Highly Cited
1984
Highly Cited
1984
Smooth muscle caldesmon. Rapid purification and F-actin cross-linking properties.
A. Bretscher
Journal of Biological Chemistry
1984
Corpus ID: 45220897
A method for the rapid purification of caldesmon, an F-actin binding protein of smooth muscle, has been developed. Caldesmon…
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Highly Cited
1984
Highly Cited
1984
Occurrence of caldesmon (a calmodulin-binding protein) in cultured cells: comparison of normal and transformed cells.
M. Owada
,
Akira Hakura
,
Kazuko IIDAt
,
Ichiro YAHARAt
,
Kenji Sobueo
,
Shiro KAKIUCHIt
Proceedings of the National Academy of Sciences…
1984
Corpus ID: 25245472
Caldesmon is a calmodulin-binding and F-actin-binding protein originally purified from chicken gizzard smooth muscle. This…
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