Absence of phosphorylation of retinoid-binding proteins by protein kinase C in vitro
- 1 July 1986
- journal article
- research article
- Published by Elsevier in Biochemical and Biophysical Research Communications
- Vol. 138 (1) , 330-334
- https://doi.org/10.1016/0006-291x(86)90284-6
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- A high-performance liquid chromatographic technique that separates cellular retinol binding protein from cellular retinoic acid binding proteinAnalytical Biochemistry, 1985
- Protein kinase C phosphorylation of the EGF receptor at a threonine residue close to the cytoplasmic face of the plasma membraneNature, 1984
- The role of protein kinase C in cell surface signal transduction and tumour promotionNature, 1984
- Activation of calcium-activated, phospholipid-dependent protein kinase (protein kinase C) by new classes of tumor promoters: Teleocidin and debromoaplysiatoxinBiochemical and Biophysical Research Communications, 1984
- Retinoid-binding proteins are phosphorylated invitro by soluble Ca+2- and phosphatidylserine-dependent protein kinase from mouse brainBiochemical and Biophysical Research Communications, 1984
- Cellular Retinol-Binding Protein and Retinoic Acid-Binding Protein in Rat Testes: Effect of Retinol DepletionJournal of Nutrition, 1976
- Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4Nature, 1970