Association of initiation factor eIF-4E in a cap binding protein complex (eIF-4F) is critical for and enhances phosphorylation by protein kinase C.
Open Access
- 1 June 1990
- journal article
- research article
- Published by Elsevier in Journal of Biological Chemistry
- Vol. 265 (18), 10617-10621
- https://doi.org/10.1016/s0021-9258(18)86991-5
Abstract
No abstract availableThis publication has 40 references indexed in Scilit:
- Identification of a protein kinase activity in rabbit reticulocytes that phosphorylates the mRNA cap binding proteinBiochemical and Biophysical Research Communications, 1988
- Cap recognition and the entry of mRNA into the protein synthesis initiation cycleTrends in Biochemical Sciences, 1988
- A three-step purification procedure for protein kinase C: Characterization of the purified enzymeAnalytical Biochemistry, 1987
- Translational control of mRNA expression during the early mitogenic response in Swiss mouse 3T3 cells: identification of specific proteins.The Journal of cell biology, 1986
- Preferential stimulation of rabbit α globin mRNA translation by a cap-binding protein complexBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1984
- Purification of the messenger RNA cap-binding protein using a new affinity mediumBiochemistry, 1984
- [11] Purification and characterization of seven initiation factors for mammalian protein synthesisMethods in Enzymology, 1979
- [3] Protein synthesis initiation factors from rabbit raticulocytes: Purification, characterization, and radiochemical labelingMethods in Enzymology, 1979
- Initiation of mammalian protein synthesisJournal of Molecular Biology, 1977
- Dissociation of eukaryotic ribosomes by purified initiation factor EIF-3Biochemical and Biophysical Research Communications, 1973