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Antifungal activity of the ribosome-inactivating protein BE27 from sugar beet (Beta vulgaris L.) against the green mould Penicillium digitatum
(Wiley-Blackwell, 2016-02)
The ribosome-inactivating protein BE27 from sugar beet (Betavulgaris L.) leaves is an apoplastic protein induced by signallingcompounds, such as hydrogen peroxide and salicylic acid, whichhas been reported to be involved ...
eIF5A binds to translational machinery components and affects translation in yeast
(Elsevier B.V., 2006-10-06)
The putative translation factor eIF5A is essential for cell viability and is highly conserved from archebacteria to mammals. Although this protein was originally identified as a translation initiation factor, subsequent ...
EVOLUTION OF ADENINE CLUSTERING IN 5S RIBOSOMAL-RNA
(Tubingen Univ Press Attempto Verlag, 2014)
Evidence for a negative cooperativity between eIF5A and eEF2 on binding to the ribosome
(2016-04-01)
eIF5A is the only protein known to contain the essential and unique amino acid residue hypusine. eIF5A functions in both translation initiation due to its stimulation of methionyl-puromycin synthesis and translation ...
Is there a role for eIF5A in translation?
(Springer, 2007-08-01)
The putative translation factor eIF5A is essential for cell viability and is highly conserved from archaebacteria to mammals. This factor is the only cellular protein that undergoes an essential posttranslational modification ...
Structure And Function Of The Yeast Listerin (ltn1) Conserved N-terminal Domain In Binding To Stalled 60s Ribosomal Subunits
(Natl Acad SciencesWashington, 2016)
EIF5A dimerizes not only in vitro but also in vivo and its molecular envelope is similar to the EF-P monomer
(2013-02-01)
The protein eukaryotic initiation factor 5A (eIF5A) is highly conserved among archaea and eukaryotes, but not in bacteria. Bacteria have the elongation factor P (EF-P), which is structurally and functionally related to ...
EIF5A dimerizes not only in vitro but also in vivo and its molecular envelope is similar to the EF-P monomer
(2013-02-01)
The protein eukaryotic initiation factor 5A (eIF5A) is highly conserved among archaea and eukaryotes, but not in bacteria. Bacteria have the elongation factor P (EF-P), which is structurally and functionally related to ...