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CA2 — CALD1

Text-mined interactions from Literome

Mayanagi et al., Cell Adh Migr 2011 : CaD function is regulated qualitatively by Ca2+/CaM and by its phosphorylation state and quantitatively at the mRNA level, by three different transcriptional regulation of the CALD1 gene
Fujii et al., J Biochem 1990 : Caldesmon was bound to S100 protein-Sepharose in the presence of Ca2+ and released with EGTA, indicating that there is a direct interaction between caldesmon and S100 protein
Ngai et al., Biochem J 1987 : Caldesmon containing endogenous kinase activity was rapidly phosphorylated ( to approx. 1 mol of Pi/mol of caldesmon in 5 min ) when reconstituted with actin, myosin, tropomyosin, calmodulin and myosin light-chain kinase in the presence of Ca2+ and MgATP2-
Marston et al., Am J Obstet Gynecol 1989 : Caldesmon inhibition was not Ca2+ dependent , but inhibition could be reversed by further addition of Ca2+ and calmodulin
Smith et al., J Biol Chem 1987 : Caldesmon was found to bind to calmodulin in the presence of Ca2+ , with an affinity of 10 ( 6 ) M-1
Lim et al., Biochem J 1986 : Caldesmon inhibited the Ca2+-ATPase activity of skeletal-muscle myosin in the presence or absence of actin, at both low ( 0.1 M-KCl ) and high ( 0.3 M-KCl ) ionic strength