Phosphorylative and functional modifications of nucleoplasmic RNA polymerase II by homologous adenosine 3':5'-monophosphate-dependent protein kinase from calf thymus and by heterologous phosphatase.
Open Access
- 1 October 1977
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 252 (19), 6750-6758
- https://doi.org/10.1016/s0021-9258(17)39913-1
Abstract
No abstract availableThis publication has 53 references indexed in Scilit:
- Evidence for the Identity of Nuclear and Cytoplasmic Adenosine-3':5'-Monophosphate-Dependent Protein Kinase from Porcine Ovaries and Nuclear Translocation of the Cytoplasmic EnzymeEuropean Journal of Biochemistry, 1977
- The presence of phosphorylated subunits in yeast RNA polymerases A and BFEBS Letters, 1976
- The 24,000 dalton subunit and the activity of yeast RNA polymerasesBiochemical and Biophysical Research Communications, 1976
- Stimulation of ascites tumor RNA polymerase II by protein kinaseBiochemistry, 1976
- Nuclear Protein Kinases from Murine CellsEuropean Journal of Biochemistry, 1975
- Presence of two protein kinases in highly purified rat liver nucleoliLife Sciences, 1974
- Role of 3′,5′-cyclic AMP in the control of nuclear protein kinase activityBiochemical and Biophysical Research Communications, 1973
- Enzymatic Interconversion of Active and Inactive Forms of EnzymesScience, 1973
- Animal DNA‐Dependent RNA PolymerasesEuropean Journal of Biochemistry, 1972
- Presence of multiple protein kinase activities in rat liver nucleiBiochemical and Biophysical Research Communications, 1972