Phosphorylation-dependent translocation of glycogen synthase to a novel structure during glycogen resynthesis. [electronic resource]
Producer: 20050719Description: 23165-72 p. digitalISSN:- 0021-9258
- Actins -- metabolism
- Adenosine Monophosphate -- chemistry
- Allosteric Site
- Amino Acid Sequence
- Animals
- Centrifugation
- Cytoplasm -- metabolism
- Cytoskeleton -- metabolism
- Female
- Glycogen -- chemistry
- Glycogen Phosphorylase -- metabolism
- Glycogen Synthase -- chemistry
- Image Processing, Computer-Assisted
- Immunohistochemistry
- Microscopy, Electron, Transmission
- Microscopy, Fluorescence
- Molecular Sequence Data
- Muscle, Skeletal -- metabolism
- Muscles -- enzymology
- Peptides -- chemistry
- Phosphorylation
- Protein Conformation
- Protein Structure, Tertiary
- Protein Transport
- Rabbits
- Sarcoplasmic Reticulum -- ultrastructure
- Subcellular Fractions -- metabolism
- Tibia -- metabolism
- Time Factors
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Publication Type: Journal Article; Research Support, Non-U.S. Gov't
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