Dephospho-[reductase kinase] kinase
Author:
Publisher
Springer Berlin Heidelberg
Link
http://link.springer.com/content/pdf/10.1007/978-3-540-85699-3_3.pdf
Reference9 articles.
1. Ingebritsen, T.S.; Parker, R.A.; Gibson, D.M.: Regulation of liver hydroxymethylglutaryl-CoA reductase by a bicyclic phosphorylation system. J. Biol. Chem., 256, 1138–1144 (1981)
2. Ingebritsen, T.S.; Lee, H.-S.; Parker, R.A.; Gibson, D.M.: Reversible modulation of the activities of both liver microsomal hydroxymethylglutaryl coenzyme A reductase and its inactivating enzyme. Evidence for regulation by phosphorylation-dephosphorylation. Biochem. Biophys. Res. Commun., 81, 1268–1277 (1978)
3. Beg, Z.H.; Stonik, J.A.; Brewer, B.: Characterization and regulation of reductase kinase, a protein kinase that modulates the enzymic activity of 3-hydroxy-3-methylglutaryl-coenzyme A reductase. Proc. Natl. Acad. Sci. USA, 76, 4375–4379 (1979)
4. Weekes, J.; Hawley, S.A.; Corton, J.; Shugar, D.; Hardie, D.G.: Activation of rat liver AMP-activated protein kinase by kinase kinase in a purified, reconstituted system. Effects of AMP and AMP analogues. Eur. J. Biochem., 219, 751–757 (1994)
5. Beg, Z.H.; Stonik, J.A.; Brewer, B.: In vivo modulation of rat liver 3-hydroxy-3-methylglutaryl-coenzyme A reductase, reductase kinase, and reductase kinase kinase by mevalonolactone. Proc. Natl. Acad. Sci. USA, 81, 7293–7297 (1984)
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