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.-Reference-Cited by-同舟云学术

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.

Published:1988-04 Issue:12 Volume:263 Page:5534-5542
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Cheng A,Fitzgerald T J,Bhatnagar D,Roskoski R,Carlson G M

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference37 articles.

1. Activation of Skeletal Muscle Phosphorylase Kinase by Adenosine Triphosphate and Adenosine 3′,5′-Monophosphate

2. Reversible Stimulation of Muscle Phosphorylase b Kinase by Low Concentrations of Calcium Ions

3. Properties of phosphorylase kinase and its control in skeletal muscle

4. Synergistic activation by Ca2+ and Mg2+ as the primary cause for hysteresis in the phosphorylase kinase reactions.

5. Adenosine 5'-diphosphate as an allosteric effector of phosphorylase kinase from rabbit skeletal muscle.

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