Identification of L-type pyruvate kinase as a major phosphorylation site of endogenous cyclic AMP-dependent protein kinase in rat liver soluble fraction-Reference-Cited by-同舟云学术

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Identification of L-type pyruvate kinase as a major phosphorylation site of endogenous cyclic AMP-dependent protein kinase in rat liver soluble fraction

Published:1979-05-15 Issue:2 Volume:101 Page:289-294
ISSN:0014-5793
Container-title:FEBS Letters
language:en
Short-container-title:

Author:

Van den Berg Gerard B.,Van Berkel Theo J.C.,Koster Johan F.

Publisher

Wiley

Subject

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

Link

http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(79)81028-5/fullpdf

Reference20 articles.

1. Activation and inactivation of rat liver phosphofructokinase by phosphorylation-dephosphorylation

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1. A critical review of the role of M2PYK in the Warburg effect;Biochimica et Biophysica Acta (BBA) - Reviews on Cancer;2019-04

2. Biological roles of cAMP: variations on a theme in the different kingdoms of life;Biological Reviews;2013-01-29

3. The Role of Ca2+ and Cyclic AMP in the Phosphorylation of Rat-Liver Soluble Proteins by Endogenous Protein Kinases;European Journal of Biochemistry;2005-03-03

4. Saccharomyces cerevisiaepyruvate kinase Pyk1 is PKA phosphorylation substrate in vitro;FEMS Microbiology Letters;2001-09

5. Effect of tolbutamide and glyburide on cAMP-dependent protein kinase activity in rat liver cytosol;Diabetes;1988-07-01

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