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Eukaryotic translation initiation factor 5A

eIF-5A, eukaryotic translation initiation factor 5A, eIF-4D, ANB1
This gene encodes an elongation initiation factor, which participates in protein synthesis. The encoded protein also plays roles in mRNA metabolism, cell proliferation, and cell cycle control. This protein contains a modified lysine residue called hypusine, which appears to be necessary for its function. Alternatively spliced transcript variants have been described. Related pseudogenes exist on chromosomes 2, 5, and 19. [provided by RefSeq, Oct 2009] (from NCBI)
Top mentioned proteins: ACID, CAN, STEP, fibrillin-1, HAD
Papers using eIF-5A antibodies
The Growth Factor Granulin Interacts with Cyclin T1 and Modulates P-TEFb-Defendent Transcription
Mathews Michael B et al., In Retrovirology, 2002
... Anti-eIF5A-1 monoclonal antibody (BD) was purchased from BD Biosciences.
Papers on eIF-5A
Structural Analysis and Optimization of Context-Independent Anti-Hypusine Antibodies.
Carter et al., San Francisco, United States. In J Mol Biol, Feb 2016
Affinity maturation of these anti-hypusine antibodies improved their performance in affinity-capture of the only currently known hypusinated protein, eIF-5A.
Eukaryotic translation initiation factor 5A (eIF5A) is essential for HIF-1α activation in hypoxia.
Yoshida et al., Wako, Japan. In Biochem Biophys Res Commun, Feb 2016
UNASSIGNED: The eukaryotic initiation factor 5A (eIF5A) is an essential protein involved in translation elongation and cell proliferation.
Linker-Region Modified Derivatives of the Deoxyhypusine Synthase Inhibitor CNI-1493 Suppress HIV-1 Replication.
Meier et al., Hamburg, Germany. In Arch Pharm (weinheim), Feb 2016
The guanylhydrazone CNI-1493, a potent inhibitor of the deoxyhypusine synthase (DHS), prevents the activation of the cellular factor eIF-5A and thereby suppresses HIV replication and a number of other diseases.
Structure of the hypusinylated eukaryotic translation factor eIF-5A bound to the ribosome.
Beckmann et al., München, Germany. In Nucleic Acids Res, Jan 2016
UNASSIGNED: During protein synthesis, ribosomes become stalled on polyproline-containing sequences, unless they are rescued in archaea and eukaryotes by the initiation factor 5A (a/eIF-5A) and in bacteria by the homologous protein EF-P.
The Essential Role of Spermidine in Growth of Agrobacterium tumefaciens Is Determined by the 1,3-Diaminopropane Moiety.
Michael et al., Dallas, United States. In Acs Chem Biol, Jan 2016
A conserved vital function of spermidine across eukaryotes is conferred by its aminobutyl group that is transferred to a single lysine in translation factor eIF5A to form the essential hypusine post-translational modification required for cellular translation.
Remaining Mysteries of Molecular Biology: The Role of Polyamines in the Cell.
Ralser et al., Cambridge, United Kingdom. In J Mol Biol, Nov 2015
These include the regulation of translation via upstream open reading frames, the over-reading of stop codons via ribosomal frameshifting, the existence of an antizyme and an antizyme inhibitor, ubiquitin-independent proteasomal degradation, a complex bi-directional membrane transport system and a unique posttranslational modification-hypusination-that is believed to occur on a single protein only (eIF-5A).
The translation factor eIF5A and human cancer.
Hershey et al., Newark, United States. In Biochim Biophys Acta, Jul 2015
The eukaryotic initiation factor eIF5A is a translation factor that, unusually, has been assigned functions in both initiation and elongation.
Modulation of protein synthesis by polyamines.
Kashiwagi et al., Chiba, Japan. In Iubmb Life, Mar 2015
In addition, the role of eIF5A, containing hypusine formed from spermidine, on protein synthesis is described.
Targeting polyamine metabolism for finding new drugs against leishmaniasis: a review.
Colotti et al., Roma, Italy. In Mini Rev Med Chem, 2014
Hypusination is a posttranslational modification occurring exclusively in the eukaryotic initiation factor 5A (eIF5A), which has an important role in avoiding the ribosome stalling during the biosynthesis of protein containing polyprolines sequences.
The hypusine-containing translation factor eIF5A.
Shin et al., Bethesda, United States. In Crit Rev Biochem Mol Biol, 2014
The eukaryotic translation initiation factor 5A (eIF5A) and its bacterial ortholog elongation factor P (EF-P) were initially characterized based on their ability to stimulate methionyl-puromycin (Met-Pmn) synthesis, a model assay for protein synthesis; however, the function of these factors in cellular protein synthesis has been difficult to resolve.
EF-P is essential for rapid synthesis of proteins containing consecutive proline residues.
Rodnina et al., Göttingen, Germany. In Science, 2013
We propose that EF-P and its eukaryotic homolog, eIF5A, are essential for the synthesis of a subset of proteins containing proline stretches in all cells.
Translation elongation factor EF-P alleviates ribosome stalling at polyproline stretches.
Jung et al., München, Germany. In Science, 2013
EF-P is present in all bacteria and orthologous to archaeal and eukaryotic initiation factor 5A, yet the biological function has so far remained enigmatic.
A tumour suppressor network relying on the polyamine-hypusine axis.
Lowe et al., New York City, United States. In Nature, 2012
Among the new tumour suppressors are adenosylmethionine decarboxylase 1 (AMD1) and eukaryotic translation initiation factor 5A (eIF5A), two genes associated with hypusine, a unique amino acid produced as a product of polyamine metabolism through a highly conserved pathway.
Overexpression of EIF5A2 promotes colorectal carcinoma cell aggressiveness by upregulating MTA1 through C-myc to induce epithelial-mesenchymaltransition.
Xie et al., Guangzhou, China. In Gut, 2012
EIF5A2 promotes colorectal carcinoma cell aggressiveness by upregulating MTA1 through C-myc to induce epithelial-mesenchymaltransition.
Essential role of eIF5A-1 and deoxyhypusine synthase in mouse embryonic development.
Park et al., Bethesda, United States. In Amino Acids, 2012
knockout of either the eIF5A-1 gene (Eif5a) or of the deoxyhypusine synthase gene (Dhps) caused early embryonic lethality in mice, indicating the essential nature of both eIF5A-1 and deoxyhypusine synthase in mammalian development
Phosphorylation of maize eukaryotic translation initiation factor on Ser2 by catalytic subunit CK2.
Muszyńska et al., Warsaw, Poland. In Mol Cell Biochem, 2011
Maize ZmeIF5Awt Ser2 is exclusively phosphorylated by catalytic subunit of CK2 (CK2alpha).
Overexpression of eIF-5A2 in mice causes accelerated organismal aging by increasing chromosome instability.
Guan et al., Hong Kong, Hong Kong. In Bmc Cancer, 2010
activation of eIF-5A2 repressed p19 level and therefore destabilized p53 in transgenic mouse embryo fibroblast (MEF) cells. This subsequently allowed for the accumulation of chromosomal instability.
"Hybrid exercise" prevents muscle atrophy in association with a distinct gene expression pattern.
Nagata et al., Kurume, Japan. In Kurume Med J, 2010
hybrid exercise increases expression of eukaryotic translation initiation factor 5A (EIFSA), peroxisomal biogenesis factor 6 (PEX6) and histone cluster 1 H4 (HIST1H4), compared with electrical stimulation alone
Hypusine-containing protein eIF5A promotes translation elongation.
Dever et al., Bethesda, United States. In Nature, 2009
eIF5A promotes translation elongation
Inhibition of HIV-1 replication in lymphocytes by mutants of the Rev cofactor eIF-5A.
Hauber et al., Vienna, Austria. In Science, 1996
Eukaryotic initiation factor 5A(eIF-5A) is a cellular cofactor require d for the function of the human immunodeficiency virus type-1 (HIV-1) Rev trans-activator protein.
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