The activation of rabbit skeletal muscle phosphorylase kinase requires the binding of 3 Ca2+ per δ subunit
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry,Biophysics
Reference24 articles.
1. The Role of Calmodulin in the Structure and Regulation of Phosphorylase Kinase from Rabbit Skeletal Muscle
2. The Regulation of Skeletal Muscle Phosphorylase Kinase by Ca2+
3. The Amino Acid Sequence of the delta Subunit (Calmodulin) of Rabbit Skeletal Muscle Phosphorylase Kinase
4. The Role of Calcium Ions, Calmodulin and Troponin in the Regulation of Phosphorylase Kinase from Rabbit Skeletal Muscle
5. The Effect of Mg2+ on the Ca2+-Binding Properties of Non-activated Phosphorylase Kinase
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2. A model for activation of the hexadecameric phosphorylase kinase complex deduced from zero-length oxidative crosslinking;Protein Science;2015-09-24
3. Mass Spectrometry Reveals Differences in Stability and Subunit Interactions between Activated and Nonactivated Conformers of the (αβγδ)4 Phosphorylase Kinase Complex;Molecular & Cellular Proteomics;2012-12
4. A Review of Methods Used for Identifying Structural Changes in a Large Protein Complex;Methods in Molecular Biology;2011-09-18
5. Expressed Phosphorylase b Kinase and Its αγδ Subcomplex as Regulatory Models for the Rabbit Skeletal Muscle Holoenzyme;Biochemistry;2009-09-28
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