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CA2 — CCNG1

Text-mined interactions from Literome

Homsher et al., J Physiol 2000 : These results suggest that [Ca2+ ] primarily affects the number of attached and cycling crossbridges
Reed et al., Environ Health Perspect 1990 : The absence of extracellular Ca2+ may cause mitochondrial Ca2+ cycling that contributes to the observed oxidative stress, resultant loss of cell viability, and protein thiol homeostasis
Sirenko et al., Science signaling 2013 : Ca2+ dependent phosphorylation of Ca2+ cycling proteins generates robust rhythmic local Ca2+ releases in cardiac pacemaker cells
Ohnishi et al., Biochim Biophys Acta 1986 (Anemia, Sickle Cell) : When dehydrated cells were formed in deoxygenation-reoxygenation cycling in the presence of Ca2+ , 40-50 % of K+ was lost in 4 h
Walsh et al., Can J Physiol Pharmacol 1995 : M.P. Walsh opened the symposium with an overview emphasizing the central role of myosin phosphorylation-dephosphorylation in the regulation of vascular tone and identifying recent developments concerning regulation of [Ca2+ ] i, Ca2+ sensitization and desensitization of the contractile response, Ca ( 2+ ) -independent protein kinase C induced contraction, and direct regulation of cross-bridge cycling by the thin filament associated proteins caldesmon and calponin
Walsh et al., Mol Cell Biochem 1994 : The principal function of calmodulin in smooth muscle is to activate crossbridge cycling and the development of force in response to a [Ca2+ ] i transient via the activation of myosin light-chain kinase and phosphorylation of myosin
Netticadan et al., Arch Biochem Biophys 1996 : In this study, we investigated the effects of the SR Ca ( 2+ ) -release inhibitor, ruthenium red ( RR ), and the SR Ca ( 2+ ) -release activator, ryanodine ( at submicromolar concentrations ), on CaM kinase mediated phosphorylation of the Ca ( 2+ ) -cycling proteins in rabbit cardiac SR. Incubation of SR with RR ( 5-30 microM ) for 3 min at 37 degrees C resulted in marked ( up to 85 % ) inhibition of Ca2+ channel phosphorylation ( 50 % inhibition with 15 +/- 2 microM RR ) by the endogenous membrane associated CaM kinase
Butters et al., J Biol Chem 1997 : The myosin subfragment 1 ( S1 ) MgATPase rate was measured using thin filaments with known extents of Ca2+ binding controlled by varying the ratio of native cardiac troponin versus an inhibitory troponin with a mutation in the sole regulatory Ca2+ binding site of troponin C. Fractional MgATPase activation was less than the fraction of troponins that bound Ca2+, implying a cooperative effect of bound Ca2+ on cross-bridge cycling