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Phosphorylase b

Known as: Phosphorylase b [Chemical/Ingredient], b phosphorylase 
The inactive form of GLYCOGEN PHOSPHORYLASE that is converted to the active form PHOSPHORYLASE A via phosphorylation by PHOSPHORYLASE KINASE and ATP.
National Institutes of Health

Related topics

Related topics

9 relations

Broader (2)

Glycogen PhosphorylasePhosphorylases
In BloodProcess of secretionantagonists & inhibitorsaspects of radiation effects

Papers overview

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Highly Cited
1990
Highly Cited
1990
Refined crystal structure of the phosphorylase-heptulose 2-phosphate-oligosaccharide-AMP complex.
Highly Cited
1984
Highly Cited
1984
Phosphorylation and inactivation of liver glycogen synthase by liver protein kinases.
Highly Cited
1980
Highly Cited
1980
ATP x Mg-dependent protein phosphatase from rabbit skeletal muscle. I. Purification of the enzyme and its regulation by the interaction with an activating protein factor.
Highly Cited
1978
Highly Cited
1978
Crystallographic studies on the activity of glycogen phosphorylase b
High resolution studies on the crystal structure of glycogen phosphorylase b have identified the catalytic site to which the… 
Highly Cited
1977
Highly Cited
1977
On the role of calcium as second messenger in liver for the hormonally induced activation of glycogen phosphorylase.
Highly Cited
1977
Highly Cited
1977
Complete amino acid sequence of rabbit muscle glycogen phosphorylase.
The sequence of the 841 amino acid residues in each subunit (molecular weight 97,412) of rabbit muscle glycogen phosphorylase b… 
Highly Cited
1975
Highly Cited
1975
Effect of denaturation on the susceptibility of proteins to enzymic phosphorylation.
Highly Cited
1971
Highly Cited
1971
The control of liver glycogen synthetase phosphatase by phosphorylase.
The activation of glycogen synthetase in a liver gel filtrate and the latency by which it is normally preceded have been studied… 
Highly Cited
1964
Highly Cited
1964
ENZYMIC DEGRADATION AND MICRODETERMINATION OF GLYCOGEN.
Highly Cited
1956
Highly Cited
1956
The effect of epinephrine and other glycogenolytic agents on the phosphorylase A content of muscle.
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