Results 301 to 310 of about 149,215 (350)
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[Glycogen synthase gene-glycogen synthase gene in Japanese patients with NIDDM].
Nihon rinsho. Japanese journal of clinical medicine, 1995As glycogen synthase is a key enzyme of the non-oxidative pathway of glucose metabolism in the skeletal muscle, and reduced activity of this enzyme is related to insulin resistance, it seems likely that this enzyme is a candidate gene for contributing to the pathogenesis of NIDDM.
H, Kuroyama, T, Sanke, K, Nanjo
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2003
The chapter provides a short summary of the structure, substrate specificity, functions, and regulation of glycogen synthase kinase 3 protein. Glycogen synthase kinase 3 (GSK3) is a protein that phosphorylates and inhibits glycogen synthase, the enzyme that catalyzes the transfer of glucose from UDPG to glycogen.
Cohen, Philip, Frame, Sheelagh
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The chapter provides a short summary of the structure, substrate specificity, functions, and regulation of glycogen synthase kinase 3 protein. Glycogen synthase kinase 3 (GSK3) is a protein that phosphorylates and inhibits glycogen synthase, the enzyme that catalyzes the transfer of glucose from UDPG to glycogen.
Cohen, Philip, Frame, Sheelagh
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Electron microscope studies of glycogen synthase
Molecular and Cellular Biochemistry, 1973Glycogen synthase from rabbit muscle was examined with the electron microscope. In preparations of the completely converted glucose-6-phosphate dependent form (GSD) and the independent form (GSI) three structures were observed: toroids, hexagons and stacks of four elements which appear to be aggregates of four toroids.
L I, Rebhun, C, Smith, J, Larner
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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.
S, Dickey-Dunkirk, S D, Killilea
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Action pattern of muscle glycogen synthase
Molecular and Cellular Biochemistry, 1975The action pattern of muscle glycogen synthaseI form was investigated by means of a study of the distribution of radioactive glucosyl units in the glycogen synthesized under variable concentrations of the substrates UDP-glucose and glycogen. A multiple chain mechanism was found to be operative.
E, Salsas, J, Larner
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Thyroid Hormones Regulate Hepatic Glycogen Synthase*
Endocrinology, 1984Short term (48 h) in vivo administration of either T3 or T4 was associated with an increase in hepatic glycogen synthase activity in the rat. Administration of 0.25 mg T3/kg BW 48, 24, and 2 h before enzyme preparation increased the total glycogen synthase activity by approximately 50% and increased the percentage of synthase in the I or active form ...
C C, Malbon, R, Campbell
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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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Inhibition of Glycogen Synthase Kinase-3
2008There are two homologous forms of glycogen synthase kinase (GSK)-3, GSK-3alpha and GSK-3beta, which play overlapping roles in the regulation of Wnt, Hedgehog, and insulin pathways, as well as the activation of nuclear factor (NF)-kappaB-mediated gene transcription.
Andrei V, Ougolkov, Daniel D, Billadeau
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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 +1 more source