Results 1 to 10 of about 454,859 (358)
Mechanism of glycogen synthase inactivation and interaction with glycogenin [PDF]
Nature Communications, 2021 Glycogen is the major glucose reserve in eukaryotes, and defects in glycogen metabolism and structure lead to disease. Glycogenesis involves interaction of glycogenin (GN) with glycogen synthase (GS), where GS is activated by glucose-6-phosphate (G6P ...
L. Marr +13 more
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The Hysteretic Properties of Glycogen Synthase I [PDF]
European Journal of Biochemistry, 1977 Glycogen‐free synthase I from human polymorphonuclear leukocytes is activated by its own substrate, glycogen, in a slow, time‐dependent proces (hysteretic activation). This lag in response to addition of glycogen depends on the concentration of glycogen, pH and temperature.
Henrik Sølling, Viggo Esmann
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Structural basis for 2′-phosphate incorporation into glycogen by glycogen synthase [PDF]
Proceedings of the National Academy of Sciences, 2013 Significance Glycogen is a branched glucose polymer found in most animals, fungi, bacteria, and archaea as an osmotically neutral means of energy storage. Glycogen also contains minor amounts of phosphate which can be removed by a dual specificity phosphatase, laforin.
V. Chikwana +7 more
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The inactivation of glycogen phosphorylase is not a prerequisite for the activation of liver glycogen synthase [PDF]
FEBS Letters, 1979 Carlos J. Ciudad +2 more
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In vivo regulation of muscle glycogen synthase and the control of glycogen synthesis. [PDF]
Proceedings of the National Academy of Sciences, 1995 The activity of glycogen synthase (GSase; EC 2.4.1.11) is regulated by covalent phosphorylation. Because of this regulation, GSase has generally been considered to control the rate of glycogen synthesis. This hypothesis is examined in light of recent in vivo NMR experiments on rat and human muscle and is found to be quantitatively inconsistent with the
Robert G. Shulman +2 more
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Isozymes of glycogen synthase [PDF]
FEBS Letters, 1984 Antisera to rat skeletal muscle glycogen synthase failed to recognize liver glycogen synthase by electroblot analysis. The antisera recognized the enzyme in skeletal muscle, heart, fat, kidney, and brain. The results support the hypothesis that there are at least two isozymes of glycogen synthase, and that most tissues contain a form similar or ...
Harvey R. Kaslow, David D. Lesikar
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Incorporation of phosphate into glycogen by glycogen synthase [PDF]
Archives of Biochemistry and Biophysics, 2016 The storage polymer glycogen normally contains small amounts of covalently attached phosphate as phosphomonoesters at C2, C3 and C6 atoms of glucose residues. In the absence of the laforin phosphatase, as in the rare childhood epilepsy Lafora disease, the phosphorylation level is elevated and is associated with abnormal glycogen structure that ...
Christopher J. Contreras +7 more
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Liver Glycogen Synthase in Rats with a Glycogen‐Storage Disorder [PDF]
European Journal of Biochemistry, 1980 1. A strain of rats with a genetically‐determined liver glycogen‐storage disorder (gsd/gsd) caused by a deficiency of liver phosphorylase kinase has a very high concentration of glycogen in the liver with a total glycogen synthase activity higher than in liver of fed normal animals, but only a small amount of the enzyme in the active form.
Colin Watts, Rex S. Malthus
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Glycogen Synthase Kinase‐3 [PDF]
International Journal of Alzheimer’s Disease, 2011 Glycogen synthase kinase-3 (GSK3) is a ubiquitous and promiscuous kinase that has been studied extensively for over four decades. Initial reports beginning in the 1970s described its role in cellular metabolic pathways fundamental to glucose metabolism, but in more recent years the number of reports describing aberrant GSK3 activity in pathological ...
Crouch, P +4 more
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Glycogen Synthase Kinase 3β in Cancer Biology and Treatment
Cells, 2020 Glycogen synthase kinase (GSK)3β is a multifunctional serine/threonine protein kinase with more than 100 substrates and interacting molecules. GSK3β is normally active in cells and negative regulation of GSK3β activity via phosphorylation of its serine 9
Takahiro Domoto +3 more
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