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CA2 — PHKB

Text-mined interactions from Literome

Andreeva et al., FEBS Lett 1999 : On the other hand, the interaction of phosphorylase kinase with glycogen requires Ca2+ at both pH values
Andreeva et al., Biochemistry (Mosc) 1999 : Binding of phosphorylase kinase by glycogen occurs only in the presence of Ca2+ and Mg2+
Newsholme et al., Biochem J 1992 : In contrast, all published kinetic data to date have strongly suggested that activation of phosphorylase kinase by Ca2+ or phosphorylation is attributable solely to a change in affinity for phosphorylase, with no effect on the Vmax
Priddy et al., Protein Sci 2005 : Ca2+ induced structural changes in phosphorylase kinase detected by small-angle X-ray scattering
Carlsen et al., Can J Physiol Pharmacol 1985 (Fatigue) : We also propose that the slow Ca2+ current may contribute to the allosteric activation of phosphorylase kinase during muscle activity
Krause et al., Biomed Biochim Acta 1987 : Contrary the activity ratio of phosphorylase retains, in the presence of propranolol, its transient changes during the cardiac cycle, probably caused by a Ca2+ mediated activation of phosphorylase kinase during the contraction process
Farkas et al., FEBS Lett 1986 : Liver protein kinases ( regulatory subunit of cAMP dependent protein kinase and/or Ca2+ dependent phosphorylase kinase ) are suggested to regulate the activity of hepatic phosphorylase phosphatase ( type 1 and 2A )
Andreeva et al., Eur J Biochem 1986 : The activity of chicken phosphorylase kinase was largely dependent on Ca2+
Sørensen et al., Biochim Biophys Acta 1979 : The non activated form of phosphorylase kinase was activated by Ca2+ in the range 10 ( -7 ) -- 5
Borregaard et al., Eur J Clin Invest 1981 : However, since phosphorylase kinase was not activated, the activation of phosphorylase is believed to be secondary to non-covalent activation of phosphorylase kinase by Ca2+
Furuya et al., Proc Natl Acad Sci U S A 1982 : The enzyme is also inactivated by phosphorylase kinase in the presence of Ca2+ and calmodulin
Erdödi et al., Int J Biochem 1984 : Heparin stimulates the activity of nonactivated and activated skeletal muscle phosphorylase kinase in a Ca2+ dependent manner
Silver et al., Mol Pharmacol 1983 : The activities of phosphorylase kinase and myosin light-chain kinase are regulated by Ca2+ binding to calmodulin
King et al., J Biol Chem 1981 : A synergistic activation of phosphorylase kinase by Ca2+ plus Mg2+ was found to be the primary cause of the hysteresis, or lag, in the phosphorylase kinase reaction
Cohen et al., Ann N Y Acad Sci 1980 : The current evidence suggests that the regulation of phosphorylase kinase by Ca2+ in vivo is achieved through the interaction of this divalent cation with calmodulin ( the delta subunit ) and troponin C, and that the relative importance of these two calcium binding proteins depends on the state of phosphorylation of the enzyme [ FIGURE 1 ] ... The regulation of phosphorylase kinase by Ca2+ may therefore also provide a mechanism for achieving synchronous control of the pathways of glycogenolysis and glycogen synthesis
Gergely et al., Biochim Biophys Acta 1980 : The changing level of intracellular Ca2+ and cyclic AMP may control the activity of phosphorylase kinase , regulating the mobilization of glycogen
Khoo et al., Biochim Biophys Acta 1976 : Ca2+ dependent activation of phosphorylase by phosphorylase kinase in adipose tissue
Nadeau et al., J Biol Chem 1997 : The structural effects of endogenous and exogenous Ca2+/calmodulin on phosphorylase kinase
Shmelev et al., Biochem Mol Biol Int 1997 : The complex formation occurs in two stages : ( i ) the formation of phosphorylase-glycogen complex controlled by ATP, ( ii ) the binding of phosphorylase kinase to the previously formed phosphorylase-glycogen complex exclusively in the presence of Ca2+ and Mg2+