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. 1969 Dec;64(4):1349–1355. doi: 10.1073/pnas.64.4.1349

CYCLIC NUCLEOTIDE-DEPENDENT PROTEIN KINASES, IV. WIDESPREAD OCCURRENCE OF ADENOSINE 3′,5′-MONOPHOSPHATE-DEPENDENT PROTEIN KINASE IN VARIOUS TISSUES AND PHYLA OF THE ANIMAL KINGDOM*

J F Kuo 1, Paul Greengard 1
PMCID: PMC223291  PMID: 4393915

Abstract

Adenosine 3′,5′-monophosphate-dependent protein kinase activity was found in about thirty sources including many mammalian tissues as well as species representative of eight different invertebrate phyla. The data support a unifying theory for the mechanism of action of adenosine 3′,5′-monophosphate, namely that its many and diverse effects are mediated through activation of tissue-specific protein kinases.

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Selected References

These references are in PubMed. This may not be the complete list of references from this article.

  1. DeLange R. J., Kemp R. G., Riley W. D., Cooper R. A., Krebs E. G. Activation of skeletal muscle phosphorylase kinase by adenosine triphosphate and adenosine 3',5'-monophosphate. J Biol Chem. 1968 May 10;243(9):2200–2208. [PubMed] [Google Scholar]
  2. Kuo J. F., Greengard P. An adenosine 3',5'-monophosphate-dependent protein kinase from Escherichia coli. J Biol Chem. 1969 Jun 25;244(12):3417–3419. [PubMed] [Google Scholar]
  3. Langan T. A. Histone phosphorylation: stimulation by adenosine 3',5'-monophosphate. Science. 1968 Nov 1;162(3853):579–580. doi: 10.1126/science.162.3853.579. [DOI] [PubMed] [Google Scholar]
  4. Miyamoto E., Kuo J. F., Greengard P. Adenosine 3',5'-monophosphate-dependent protein kinase from brain. Science. 1968 Jul 4;165(3888):63–65. [PubMed] [Google Scholar]
  5. Miyamoto E., Kuo J. F., Greengard P. Cyclic nucleotide-dependent protein kinases. 3. Purification and properties of adenosine 3',5'-monophosphate-dependent protein kinase from bovine brain. J Biol Chem. 1969 Dec 10;244(23):6395–6402. [PubMed] [Google Scholar]
  6. Perlman R. L., Pastan I. Regulation of beta-galactosidase synthesis in Escherichia coli by cyclic adenosine 3',5'-monophosphate. J Biol Chem. 1968 Oct 25;243(20):5420–5427. [PubMed] [Google Scholar]
  7. Perlman R., Pastan I. Cyclic 3'5-AMP: stimulation of beta-galactosidase and tryptophanase induction in E. coli. Biochem Biophys Res Commun. 1968 Mar 27;30(6):656–664. doi: 10.1016/0006-291x(68)90563-9. [DOI] [PubMed] [Google Scholar]
  8. RODBELL M. METABOLISM OF ISOLATED FAT CELLS. I. EFFECTS OF HORMONES ON GLUCOSE METABOLISM AND LIPOLYSIS. J Biol Chem. 1964 Feb;239:375–380. [PubMed] [Google Scholar]
  9. Robison G. A., Butcher R. W., Sutherland E. W. Cyclic AMP. Annu Rev Biochem. 1968;37:149–174. doi: 10.1146/annurev.bi.37.070168.001053. [DOI] [PubMed] [Google Scholar]
  10. Walsh D. A., Perkins J. P., Krebs E. G. An adenosine 3',5'-monophosphate-dependant protein kinase from rabbit skeletal muscle. J Biol Chem. 1968 Jul 10;243(13):3763–3765. [PubMed] [Google Scholar]

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