PHAS/4E-BPs as regulators of mRNA translation and cell proliferation.

No abstract is available for this paper.

• Publication year

  1997

• Venue

  TIBS -Trends in Biochemical Sciences. Regular ed

• Publication date

  1997-09-01

• Fields of study

  Biology, Medicine

• Identifiers
  DOI 10.1016/S0968-0004(97)01101-8PMID 9301335
• External record

  Open on Semantic Scholar

• Source metadata

  Semantic Scholar, PubMed

• No claims are published for this paper.

• No concepts are published for this paper.

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  1997cited by this paper
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• Both rapamycin-sensitive and -insensitive pathways are involved in the phosphorylation of the initiation factor-4E-binding protein (4E-BP1) in response to insulin in rat epididymal fat-cells.

  1996cited by this paper
• Stimulation of protein synthesis, eukaryotic translation initiation factor 4E phosphorylation, and PHAS-I phosphorylation by insulin requires insulin receptor substrate 1 and phosphatidylinositol 3-kinase

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• A Reevaluation of the Cap-binding Protein, eIF4E, as a Rate-limiting Factor for Initiation of Translation in Reticulocyte Lysate (*)

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• Phosphorylation of eIF-4E on Serine 209 by Protein Kinase C Is Inhibited by the Translational Repressors, 4E-binding Proteins (*)

  1996cited by this paper
• 4E-BP1 phosphorylation is mediated by the FRAP-p70s6k pathway and is independent of mitogen-activated protein kinase.

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