Novel phosphorylation sites of eukaryotic initiation factor-4F and evidence that phosphorylation stabilizes interactions of the p25 and p220 subunits.-Reference-Cited by-同舟云学术

Novel phosphorylation sites of eukaryotic initiation factor-4F and evidence that phosphorylation stabilizes interactions of the p25 and p220 subunits.

Published:1993-03 Issue:7 Volume:268 Page:4975-4978
ISSN:0021-9258
Container-title:Journal of Biological Chemistry
language:en
Short-container-title:Journal of Biological Chemistry

Author:

Bu X.,Haas D.W.,Hagedorn C.H.

Publisher

Elsevier BV

Subject

Cell Biology,Molecular Biology,Biochemistry

Reference22 articles.

1. New initiation factor activity required for globin mRNA translation.

2. Cap recognition and the entry of mRNA into the protein synthesis initiation cycle

3. A polypeptide in eukaryotic initiation factors that crosslinks specifically to the 5'-terminal cap in mRNA.

4. Regulated phosphorylation and low abundance of HeLa cell initiation factor eIF-4F suggest a role in translational control. Heat shock effects on eIF-4F.

5. Heat shock impairs the interaction of cap-binding protein complex with 5' mRNA cap.

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