Phosphorylation and inactivation of HMG-CoA reductase at the AMP-activated protein kinase site in response to fructose treatment of isolated rat hepatocytes-Reference-Cited by-同舟云学术

Phosphorylation and inactivation of HMG-CoA reductase at the AMP-activated protein kinase site in response to fructose treatment of isolated rat hepatocytes

Published:1992-07-13 Issue:1 Volume:306 Page:59-62
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Gillespie John G.,Hardie D.Grahame

Publisher

Wiley

Subject

Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(92)80837-7/fullpdf

Reference17 articles.

1. Regulation of the mevalonate pathway

2. Regulation of fatty acid and cholesterol metabolism by the AMP-activated protein kinase

3. A common bicyclic protein kinase cascade inactivates the regulatory enzymes of fatty acid and cholesterol biosynthesis

4. Purification and characterization of the AMP-activated protein kinase. Copurification of acetyl-CoA carboxylase kinase and 3-hydroxy-3-methylglutaryl-CoA reductase kinase activities

5. Phosphorylation of hepatic 3-hydroxy-3-methylglutaryl coenzyme A reductase and modulation of its enzymic activity by calcium-activated and phospholipid-dependent protein kinase.

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