(Q28143665)

2

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L P McMahon

3

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C T Capaldo

4

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R T Abraham

5

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J C Lawrence

Journal of Biological Chemistry

6

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language of work or name

English

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publication date

27 October 2000

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published in

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volume

275

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issue

43

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page(s)

33836-43

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cites work

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Signal transduction pathways that regulate eukaryotic protein synthesis

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Cap binding complexes and cellular growth control

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Multiple mechanisms control phosphorylation of PHAS-I in five (S/T)P sites that govern translational repression

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Mutational analysis of sites in the translational regulator, PHAS-I, that are selectively phosphorylated by mTOR

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Regulation of 4E-BP1 phosphorylation: a novel two-step mechanism

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When is a lipid kinase not a lipid kinase? When it is a protein kinase

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Mammalian target of rapamycin: immunosuppressive drugs uncover a novel pathway of cytokine receptor signaling

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PHAS proteins as mediators of the actions of insulin, growth factors and cAMP on protein synthesis and cell proliferation

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Molecular cloning and tissue distribution of PHAS-I, an intracellular target for insulin and growth factors

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Isolation of a protein target of the FKBP12-rapamycin complex in mammalian cells

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Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4

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The Translation Initiation Factor eIF-4E Binds to a Common Motif Shared by the Translation Factor eIF-4γ and the Translational Repressors 4E-Binding Proteins

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Control of p70 s6 kinase by kinase activity of FRAP in vivo

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Evidence of insulin-stimulated phosphorylation and activation of the mammalian target of rapamycin mediated by a protein kinase B signaling pathway

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Mammalian target of rapamycin is a direct target for protein kinase B: identification of a convergence point for opposing effects of insulin and amino-acid deficiency on protein translation.

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Mammalian TOR controls one of two kinase pathways acting upon nPKCdelta and nPKCepsilon

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