Mechanism of calponin stabilization of cross-linked actin networks
The actin-binding protein calponin has been previously implicated in actin cytoskeletal
regulation and is thought to act as an actin stabilizer, but the mechanism of its function is …
regulation and is thought to act as an actin stabilizer, but the mechanism of its function is …
Functional interrelationship between calponin and caldesmon
R Makuch, K Birukov, V Shirinsky… - Biochemical …, 1991 - portlandpress.com
Calponin and caldesmon, constituents of smooth-muscle thin filaments, are considered to be
potential modulators of smooth-muscle contraction. Both of them interact with actin and …
potential modulators of smooth-muscle contraction. Both of them interact with actin and …
Identification of the binding region of basic calponin on α and β tubulins
T Fujii, Y Koizumi - The journal of biochemistry, 1999 - jstage.jst.go.jp
Calponin is a basic smooth muscle protein capable of binding to actin, calmodulin,
tropomyosin, and phospholipids. We have found that the basic calponin interacted with brain …
tropomyosin, and phospholipids. We have found that the basic calponin interacted with brain …
Biochemical and functional characterization of smooth muscle calponin
SJ Winder, C Sutherland, MP Walsh - Regulation of smooth muscle …, 1991 - Springer
Calponin (cal cium-and cal modulin-binding tro ponin T-like protein) was first described by
Takahashi et al.(1986) and isolated from chicken gizzard smooth muscle taking advantage …
Takahashi et al.(1986) and isolated from chicken gizzard smooth muscle taking advantage …
A direct interaction with calponin inhibits the actin-nucleating activity of gelsolin
I Ferjani, A Fattoum, SK Maciver, C Bénistant… - Biochemical …, 2006 - portlandpress.com
Gelsolin and calponin are well-characterized cytoskeletal proteins that are abundant and
widely expressed in vertebrate tissues. It is also becoming apparent, however, that they are …
widely expressed in vertebrate tissues. It is also becoming apparent, however, that they are …
Association of calponin with desmin intermediate filaments
K Mabuchi, B Li, W Ip, T Tao - Journal of Biological Chemistry, 1997 - ASBMB
Our previous immunoelectron microscopy studies of chicken gizzard smooth muscle cells
showed that in certain areas the distribution of anti-calponin exhibits a high degree of …
showed that in certain areas the distribution of anti-calponin exhibits a high degree of …
Suppression of cancer phenotypes through a multifunctional actin‐binding protein, calponin, that attacks cancer cells and simultaneously protects the host from …
S Taniguchi - Cancer science, 2005 - Wiley Online Library
Quantitative and/or qualitative alteration of actin cytoskeletal molecules, involved in the
regulation of cellular dynamic functions, should be intimately related with cancer …
regulation of cellular dynamic functions, should be intimately related with cancer …
Interaction between calponin and smooth muscle myosin
PT Szymanski, T Tao - FEBS letters, 1993 - Wiley Online Library
Calponin is a thin filament‐associated protein in smooth muscle that has been shown to
bind actin, tropomyosin and calmodulin, and has been implicated to play a role in regulation …
bind actin, tropomyosin and calmodulin, and has been implicated to play a role in regulation …
Identification of calponin as a novel substrate of Rho-kinase
T Kaneko, M Amano, A Maeda, H Goto… - Biochemical and …, 2000 - Elsevier
Calponin, an F-actin-associated protein implicated in the regulation of smooth muscle
contraction, is known to be phosphorylated in vitro by protein kinase C (PKC) and …
contraction, is known to be phosphorylated in vitro by protein kinase C (PKC) and …
Calponin
M El-Mezgueldi - The international journal of biochemistry & cell biology, 1996 - Elsevier
Calponin is a troponin-T like protein purified from chicken gizzard smooth muscle. It binds to
actin, myosin, Ca2+-binding proteins and tropomyosin and inhibits the actomyosin ATPase …
actin, myosin, Ca2+-binding proteins and tropomyosin and inhibits the actomyosin ATPase …