Nanopublications LDF server

Matches in Nanopublications for { ?s ?p "Akt phosphorylates and inactivates GSK-3, decreasing the rate of phosphorylation of glycogen synthase, thus increasing its activity state59. Insulin does not activate PP1 globally, but rather specifically targets discrete pools of the phosphatase, primarily increasing PP1 activity localized at the glycogen particle. The compartmentalized activation of PP1 by insulin is due to glycogen-targeting subunits, which serve as 'molecular scaffolds', bringing together the enzyme directly with its substrates glycogen synthase and phosphorylase in a macromolecular complex," ?g. }

• _6 value "Akt phosphorylates and inactivates GSK-3, decreasing the rate of phosphorylation of glycogen synthase, thus increasing its activity state59. Insulin does not activate PP1 globally, but rather specifically targets discrete pools of the phosphatase, primarily increasing PP1 activity localized at the glycogen particle. The compartmentalized activation of PP1 by insulin is due to glycogen-targeting subunits, which serve as 'molecular scaffolds', bringing together the enzyme directly with its substrates glycogen synthase and phosphorylase in a macromolecular complex," provenance.
• _6 value "Akt phosphorylates and inactivates GSK-3, decreasing the rate of phosphorylation of glycogen synthase, thus increasing its activity state59. Insulin does not activate PP1 globally, but rather specifically targets discrete pools of the phosphatase, primarily increasing PP1 activity localized at the glycogen particle. The compartmentalized activation of PP1 by insulin is due to glycogen-targeting subunits, which serve as 'molecular scaffolds', bringing together the enzyme directly with its substrates glycogen synthase and phosphorylase in a macromolecular complex," provenance.
• _6 value "Akt phosphorylates and inactivates GSK-3, decreasing the rate of phosphorylation of glycogen synthase, thus increasing its activity state59. Insulin does not activate PP1 globally, but rather specifically targets discrete pools of the phosphatase, primarily increasing PP1 activity localized at the glycogen particle. The compartmentalized activation of PP1 by insulin is due to glycogen-targeting subunits, which serve as 'molecular scaffolds', bringing together the enzyme directly with its substrates glycogen synthase and phosphorylase in a macromolecular complex," provenance.
• _6 value "Akt phosphorylates and inactivates GSK-3, decreasing the rate of phosphorylation of glycogen synthase, thus increasing its activity state59. Insulin does not activate PP1 globally, but rather specifically targets discrete pools of the phosphatase, primarily increasing PP1 activity localized at the glycogen particle. The compartmentalized activation of PP1 by insulin is due to glycogen-targeting subunits, which serve as 'molecular scaffolds', bringing together the enzyme directly with its substrates glycogen synthase and phosphorylase in a macromolecular complex," provenance.
• _6 value "Akt phosphorylates and inactivates GSK-3, decreasing the rate of phosphorylation of glycogen synthase, thus increasing its activity state59. Insulin does not activate PP1 globally, but rather specifically targets discrete pools of the phosphatase, primarily increasing PP1 activity localized at the glycogen particle. The compartmentalized activation of PP1 by insulin is due to glycogen-targeting subunits, which serve as 'molecular scaffolds', bringing together the enzyme directly with its substrates glycogen synthase and phosphorylase in a macromolecular complex," provenance.
• _6 value "Akt phosphorylates and inactivates GSK-3, decreasing the rate of phosphorylation of glycogen synthase, thus increasing its activity state59. Insulin does not activate PP1 globally, but rather specifically targets discrete pools of the phosphatase, primarily increasing PP1 activity localized at the glycogen particle. The compartmentalized activation of PP1 by insulin is due to glycogen-targeting subunits, which serve as 'molecular scaffolds', bringing together the enzyme directly with its substrates glycogen synthase and phosphorylase in a macromolecular complex," provenance.