Regulation of polypeptide-chain initiation in rat skeletal muscle Starvation does not alter the activity or phosphorylation state of initiation factor eIF-2
- 7 November 1988
- journal article
- Published by Wiley in FEBS Letters
- Vol. 239 (2), 333-338
- https://doi.org/10.1016/0014-5793(88)80946-3
Abstract
No abstract availableKeywords
This publication has 19 references indexed in Scilit:
- Isolation and characterisation of the guanine nucleotide exchange factor from rat liverBiochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology, 1987
- Structure and regulation of eukaryotic initiation factor eIF-2. Sequence of the site in the alpha subunit phosphorylated by the haem-controlled repressor and by the double-stranded RNA-activated inhibitorEuropean Journal of Biochemistry, 1987
- Initiation factor protein modifications and inhibition of protein synthesis.Molecular and Cellular Biology, 1987
- Eukaryotic initiation factor 2 from rat liver: no apparent function for the β-subunit in the formation of initiation complexesBiochimica et Biophysica Acta (BBA) - Gene Structure and Expression, 1986
- Guanine nucleotides, protein phosphorylation and the control of translationTrends in Biochemical Sciences, 1986
- Translational control by adenovirus: lack of virus-associated RNAI during adenovirus infection results in phosphorylation of initiation factor eIF-2 and inhibition of protein synthesis.Proceedings of the National Academy of Sciences, 1985
- Effects of starvation, diabetes and acute insulin treatment on the regulation of polypeptide-chain initiation in rat skeletal muscleBiochemical Journal, 1984
- Insulin promoted decrease in the phosphorylation of protein synthesis initiation factor eIF-2Biochemical and Biophysical Research Communications, 1984
- Purification and phosphorylation of initiation factor eIF‐2 from rabbit skeletal muscleFEBS Letters, 1982
- Role of Insulin in the Regulation of Protein SynthesisDiabetes, 1980