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Targeting tumors that lack methylthioadenosine phosphorylase (MTAP) activity
TLDR
The frequency of MTAP-deficiency is presented and past and recent strategies to target such deficient cells are discussed, including one in which MTA is administered, followed by very high doses of a toxic purine or pyrimidine analog.
ON THE ROLE OF INTRACELLULAR POTASSIUM IN PROTEIN SYNTHESIS.
Cycloheximide: Aspects of Inhibition of Protein Synthesis in Mammalian Cells
Cycloheximide and acetoxy-cycloheximide specifically inhibit protein synthesis in L-cells growing in suspension culture. In extracts of rat liver, the drugs inhibit transfer of amino acid from
Inhibition of elongation steps of protein synthesis at reduced potassium concentrations in reticulocytes and reticulocyte lysate.
  • F. Cahn, M. Lubin
  • Chemistry, Medicine
    The Journal of biological chemistry
  • 10 November 1978
TLDR
Analysis of the kinetics of synthesis showed that lowering the K+ concentration inhibits the rate of elongation of nascent chains, but has little effect on the relative rate of initiation of chains.
Selective Killing of Tumors Deficient in Methylthioadenosine Phosphorylase: A Novel Strategy
TLDR
A selective strategy to kill tumor cells lacking MTAP is described, in which both MTA and a toxic adenine analog, such as 2,6-diaminopurine (DAP), 6-methylpurine (MeP), or 2-fluoroadenine (F-Ade), are administered.
Expression of Differentiated Functions in Mouse Neuroblastoma mediated by Dibutyryl-cyclic Adenosine Monophosphate
TLDR
It is shown that differentiated characteris-tics of neuroblastoma cells can be induced by N6,O2′-dibutyryl adenosine 3′ : 5′-monophosphate (dibutiesryl-cyclicAMP).
Intracellular Potassium and Macromolecular Synthesis in Mammalian Cells
  • M. Lubin
  • Chemistry, Medicine
    Nature
  • 4 February 1967
TLDR
The surface properties of cells may affect their ability to synthesize large molecules and the question whether the intracellular potassium concentration affects the synthesis of proteins and nucleic acids is raised.
The homeo domain of a murine protein binds 5' to its own homeo box.
TLDR
Results support the hypothesis that murine homeo boxes are DNA binding domains of proteins involved in the regulation of embryonic development.
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