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Literature summary for 1.5.1.3 extracted from

  • Ghosh, P.; Cheng, J.; Chou, T.F.; Jia, Y.; Avdulov, S.; Bitterman, P.B.; Polunovsky, V.A.; Wagner, C.R.
    Expression, purification and characterization of recombinant mouse translation initiation factor eIF4E as a dihydrofolate reductase (DHFR) fusion protein (2008), Protein Expr. Purif., 60, 132-139.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
synthesis develoment of a method for bacterial expression of mouse translation factor eIF4E tagged with mutant dihydrofolate reductase. Recombinant eIF4E and DHFR-eIF4E both show to significantly enhance in vitro translation in dose dependent manner by 75% at 0.0005 mM. Increased concentrations of eIF4E and DHFR-eIF4E significantly inhibit translation in a dose dependent manner by a maximum at 0.0022 mM of 60% and 90%, respectively Mus musculus

Organism

Organism UniProt Comment Textmining
Mus musculus
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