Competition between nucleoside diphosphates and triphosphates at the catalytic and allosteric sites of phosphorylase kinase.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference33 articles.
1. Adenosine 5'-diphosphate as an allosteric effector of phosphorylase kinase from rabbit skeletal muscle.
2. Allosteric nucleotide specificity of phosphorylase kinase: correlation of binding, conformational transitions, and activation. Utilization of lin-benzo-ADP to measure the binding of other nucleoside diphosphates, including the phosphorothioates of ADP.
3. Improved method of resolving nucleotides by reversed-phase high-performance liquid chromatography
4. Synergistic activation by Ca2+ and Mg2+ as the primary cause for hysteresis in the phosphorylase kinase reactions.
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Studies on interaction of phosphorylase kinase from rabbit skeletal muscle with glycogen in the presence of ATP and ADP;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;2001-10
2. Proximal regions of the catalytic γ and regulatory β subunits on the interior lobe face of phosphorylase kinase are structurally coupled to each other and with enzyme activation;Journal of Molecular Biology;1997-01
3. Molecular basis of signal integration in phosphorylase kinase;Biochimica et Biophysica Acta (BBA) - Molecular Cell Research;1991-09
4. The ATPase activity of phosphorylase kinase is regulated in parallel with its protein kinase activity.;Journal of Biological Chemistry;1991-09
5. The interference of EDTA in searching for heat-stable low-Mr inhibitors of protein kinases;European Journal of Biochemistry;1990-02
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