Results 181 to 190 of about 76,168 (194)
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Purification of bovine heart glycogen synthase
Analytical Biochemistry, 1985Glycogen synthase was purified to apparent homogeneity from bovine heart muscle by a procedure involving precipitation of the enzyme in the presence of added glycogen by polyethylene glycol, chromatography on DEAE-Sephacel, and high-speed centrifugation through a sucrose-containing buffer.
Dickey-Dunkirk S, Killilea Sd
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Characterization of human endometrial glycogen synthase
Fertility and Sterility, 1994To characterize and compare human endometrial glycogen synthase complementary DNA (cDNA) to the published rat liver and human skeletal muscle glycogen synthase transcripts and then to determine whether P-induced glycogen accumulation in endometrium is accompanied by a rise in glycogen synthase transcripts.We performed bidirectional sequencing of ...
Gayla S. Harris+2 more
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Trehalose synthase converts glycogen to trehalose
The FEBS Journal, 2008Trehalose (α,α‐1,1‐glucosyl‐glucose) is essential for the growth of mycobacteria, and these organisms have three different pathways that can produce trehalose. One pathway involves the enzyme described in the present study, trehalose synthase (TreS), which interconverts trehalose and maltose.
Alan D. Elbein+5 more
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Journal of Medicinal Chemistry, 2012
The glycogen synthase kinase-3 (GSK-3) has been linked to the pathogenesis of colorectal cancer, diabetes, cardiovascular disease, acute myeloid leukemia (AML), and Alzheimer's disease (AD). The debate on the respective contributions of GSK-3α and GSK-3β to AD pathology and AML is ongoing. Thus, the identification of potent GSK-3α-selective inhibitors,
Lo Monte F.+14 more
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The glycogen synthase kinase-3 (GSK-3) has been linked to the pathogenesis of colorectal cancer, diabetes, cardiovascular disease, acute myeloid leukemia (AML), and Alzheimer's disease (AD). The debate on the respective contributions of GSK-3α and GSK-3β to AD pathology and AML is ongoing. Thus, the identification of potent GSK-3α-selective inhibitors,
Lo Monte F.+14 more
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Multisite phosphorylation of glycogen synthase
Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1984Glycogen synthase kinase-3 was isolated from rabbit skeletal muscle by an improved procedure. The purification was estimated to be 67000-fold and 0.2 mg of enzyme was isolated from 5000 g muscle, corresponding to an overall yield of 7%. The preparation was homogeneous by ultracentrifugal and electrophoretic criteria. The enzyme had a relative molecular
Woodgett, James R., Cohen, Philip
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1986
Publisher Summary This chapter reviews knowledge of mammalian liver glycogen synthase and its short-term regulation by covalent phosphorylation mechanisms. Elevated concentrations of insulin and glucose promote glycogen synthesis and the activation of glycogen synthase.
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Publisher Summary This chapter reviews knowledge of mammalian liver glycogen synthase and its short-term regulation by covalent phosphorylation mechanisms. Elevated concentrations of insulin and glucose promote glycogen synthesis and the activation of glycogen synthase.
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Glycogen synthase in prenatal rat liver
Biochemical and Biophysical Research Communications, 1985Glycogen synthase first appears in significant levels in fetal rat liver on day 18 of gestation (22 day term), but in a mostly inactive, phospho- form. This was reflected in a decreased affinity for its allosteric activator (increased A0.5 for glucose-6-phosphate), and with limited glycogen synthesis and accumulation.
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Structure and Regulation of Glycogen Synthase in the Brain
2019Brain glycogen synthesis is a regulated, multi-step process that begins with glucose transport across the blood brain barrier and culminates with the actions of glycogen synthase and the glycogen branching enzyme to elongate glucose chains and introduce branch points in a growing glycogen molecule.
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1986
Publisher Summary This chapter discusses the structure and activity of muscle glycogen synthase. Glycogen synthase is regulated by a phosphorylation–dephosphorylation mechanism. Following the discovery that glycogen phosphorylase and phosphorylase kinase were activated by phosphorylation, Larner and co-workers found that glycogen synthase could exist
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Publisher Summary This chapter discusses the structure and activity of muscle glycogen synthase. Glycogen synthase is regulated by a phosphorylation–dephosphorylation mechanism. Following the discovery that glycogen phosphorylase and phosphorylase kinase were activated by phosphorylation, Larner and co-workers found that glycogen synthase could exist
openaire +2 more sources