The possible significance of adenosine 3′:5′-cyclic monophosphate-stimulated protein kinase activity associated with purified microtubular protein preparations from mammalian brain
- 1 July 1972
- journal article
- Published by Portland Press Ltd. in Biochemical Journal
- Vol. 128 (3) , 95P
- https://doi.org/10.1042/bj1280095pa
Abstract
No abstract availableThis publication has 8 references indexed in Scilit:
- Turnover of protein-bound phosphorylserine in membrane preparations from ox brain catalysed by intrinsic kinase and phosphatase activityBiochemical Journal, 1971
- Morphologic Differentiation of Mouse Neuroblastoma Cells induced in vitro by Dibutyryl Adenosine 3′:5′-Cyclic MonophosphateNature New Biology, 1971
- Comparison of the Microtubule Proteins of Neuroblastoma Cells, Brain, and Chlamydomonas FlagellaProceedings of the National Academy of Sciences, 1971
- Heterogeneity of Tubulin SubunitsProceedings of the National Academy of Sciences, 1971
- Are Cytoplasmic Microtubules Heteropolymers?Proceedings of the National Academy of Sciences, 1971
- Cyclic Adenosine 3′:5′-Monophosphate-Stimulated Phosphorylation of Isolated Neurotubule SubunitsProceedings of the National Academy of Sciences, 1970
- Mechanism of Activation by Adenosine 3′:5′-Cyclic Monophosphate of a Protein Phosphokinase from Rabbit ReticulocytesProceedings of the National Academy of Sciences, 1970
- Cyclic nucleotide-dependent protein kinases. 3. Purification and properties of adenosine 3',5'-monophosphate-dependent protein kinase from bovine brain.1969