Ser-64 and Ser-111 in PHAS-I Are Dispensable for Insulin-stimulated Dissociation from eIF4E

This publication has 30 references indexed in Scilit:

• Two Motifs in the Translational Repressor PHAS-I Required for Efficient Phosphorylation by Mammalian Target of Rapamycin and for Recognition by Raptor
  Journal of Biological Chemistry, 2003
• The C Terminus of Initiation Factor 4E-Binding Protein 1 Contains Multiple Regulatory Features That Influence Its Function and Phosphorylation
  Molecular and Cellular Biology, 2003
• mTOR Interacts with Raptor to Form a Nutrient-Sensitive Complex that Signals to the Cell Growth Machinery
  Cell, 2002
• Caspase Cleavage of Initiation Factor 4E-Binding Protein 1 Yields a Dominant Inhibitor of Cap-Dependent Translation and Reveals a Novel Regulatory Motif
  Molecular and Cellular Biology, 2002
• Cloning of a Novel Phosphatidylinositol Kinase-related Kinase
  Journal of Biological Chemistry, 2001
• A Quantitative Molecular Model for Modulation of Mammalian Translation by the eIF4E-binding Protein 1
  Journal of Biological Chemistry, 2001
• Mammalian Target of Rapamycin-dependent Phosphorylation of PHAS-I in Four (S/T)P Sites Detected by Phospho-specific Antibodies
  Journal of Biological Chemistry, 2000
• Multiple Mechanisms Control Phosphorylation of PHAS-I in Five (S/T)P Sites That Govern Translational Repression
  Molecular and Cellular Biology, 2000
• Control of the Translational Regulators PHAS-I and PHAS-II by Insulin and cAMP in 3T3-L1 Adipocytes
  Published by Elsevier ,1996
• Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4
  Nature, 1970