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Post translational modification of eif 4d by spermidine






Journal of Cell Biology 103(5 PART 2): 327A

Post translational modification of eif 4d by spermidine



Accession: 028935683



Related references

Gerner, E.W.; Mamont, P.S.; Bernhardt, A.; Siat, M., 1986: Post-translational modification of the protein-synthesis initiation factor eIF-4D by spermidine in rat hepatoma cells. The rates of synthesis and turnover of the rare amino acid hypusine [N6-(4-amino-2-hydroxybutyl)-2,6-diaminohexanoic acid] in protein were studied in relationship to polyamine metabolism and growth rates in rat hepatoma tissue-culture (HTC) cells....

Mehta, A.M.; Saftner, R.A.; Schaeffer, G.W.; Mattoo, A.K., 1991: Translational modification of an 18 kilodalton polypeptide by spermidine in rice cell suspension cultures. When rice (Oryza sativa) cell suspension cultures are grown in the presence of [terminal methylenes-(3)H]spermidine, label is incorporated in a single polypeptide with a molecular mass of 18 kilodaltons on sodium dodecyl sulfate-polyacrylamide gel...

Eisenberg-Lerner, A.; Ciechanover, A.; Merbl, Y., 2016: Post-translational modification profiling - A novel tool for mapping the protein modification landscape in cancer. The ubiquitin system plays an important role in essentially every cellular process, regulating numerous pathways ranging from development, transcription, DNA damage response, cell cycle, and signal transduction. Its best studied role involves remo...

Wold, F., 1981: In vivo chemical modification of proteins (post-translational modification). Annual Review of Biochemistry 50: 783-814

Garner, B.; Shaw, D.C.; Lindner, R.A.; Carver, J.A.; Truscott, R.J., 2000: Non-oxidative modification of lens crystallins by kynurenine: a novel post-translational protein modification with possible relevance to ageing and cataract. In humans, the crystallin proteins of the ocular lens become yellow-coloured and fluorescent with ageing. With the development of senile nuclear cataract, the crystallins become brown and additional fluorophores are formed. The mechanism underlyin...

Suiko, M.; Fernando, P.H.; Sakakibara, Y.; Nakajima, H.; Liu, M.C.; Abe, S.; Nakatsu, S., 1992: Post-translational modification of protein by tyrosine sulfation: active sulfate PAPS is the essential substrate for this modification. In vitro tyrosine sulfation of recombinant proteins would be a valuable tool in converting those proteins expressed in prokaryotic vectors to their natural form. For this purpose tyrosylprotein sulfotransferase (TPST), the enzyme responsible for t...

Serra I.; Kamiyama M.; Hashim G.A.; Ragonese P.; Giuffrida A.M., 1983: Post translational modification of nuclear proteins in rat cerebral hemispheres during post natal development. The processes of acetylation, phosphorylation and methylation of nuclear proteins in cerebral hemispheres of 10- and 30-day-old rats were investigated. The experiments were carried out in vitro by measuring the incorporation of labeled precursors...

Benayoun, Bérénice.A.; Auer, J.; Caburet, S.; Veitia, R.A., 2008: The post-translational modification profile of the forkhead transcription factor FOXL2 suggests the existence of parallel processive/concerted modification pathways. The transcription factor Forkhead box L subfamily member 2 (FOXL2) is involved in craniofacial development and ovarian function. Using 2-DE and immunoblotting, we show that it is highly modified post-translationally. The most outstanding feature...

Kumar, P.; Van Patten, S.M.; Walsh, D.A., 1997: Multiplicity of the b form of the cAMP-dependent protein kinase inhibitor protein generated by post-translational modification and alternate translational initiation. The Journal of Biological Chemistry 272: 011-20

Bachmair, A.; Novatchkova, M.; Potuschak, T.; Eisenhaber, F., 2001: Ubiquitylation in plants: a post-genomic look at a post-translational modification. In this article, we summarize Arabidopsis genes encoding ubiquitin, ubiquitin-activating enzyme (E1), ubiquitin-conjugating enzymes (E2s) and an additional selected set of proteins related to ubiquitylation. We emphasize comparisons to components...