HYP2/YEL034W Literature Guide Help

Other names published for HYP2: TIF51A, eIF5A, eIF-5A, YEL034W

HYP2 - Non-Fungal Related Genes/Proteins (20)

ReferenceOther Genes Addressed
Dias CA, et al.  (2013) eIF5A dimerizes not only in vitro but also in vivo and its molecular envelope is similar to the EF-P monomer. Amino Acids 44(2):631-44
Armache JP, et al.  (2010) Cryo-EM structure and rRNA model of a translating eukaryotic 80S ribosome at 5.5-A resolution. Proc Natl Acad Sci U S A 107(46):19748-19753
Bailly M and de Crecy-Lagard V  (2010) Predicting the pathway involved in post-translational modification of Elongation factor P in a subset of bacterial species. Biol Direct 5():3
Lebska M, et al.  (2010) Phosphorylation of Maize Eukaryotic Translation Initiation Factor 5A (eIF5A) by Casein Kinase 2: IDENTIFICATION OF PHOSPHORYLATED RESIDUE AND INFLUENCE ON INTRACELLULAR LOCALIZATION OF eIF5A. J Biol Chem 285(9):6217-26
Gentz PM, et al.  (2009) Dimerization of the yeast eukaryotic translation initiation factor 5A requires hypusine and is RNA dependent. FEBS J 276(3):695-706
Saini P, et al.  (2009) Hypusine-containing protein eIF5A promotes translation elongation. Nature 459(7243):118-21
Dias CA, et al.  (2008) Structural modeling and mutational analysis of yeast eukaryotic translation initiation factor 5A reveal new critical residues and reinforce its involvement in protein synthesis. FEBS J 275(8):1874-88
Feng H, et al.  (2007) Functional Characterization of the Arabidopsis Eukaryotic Translation Initiation Factor 5A-2 That Plays a Crucial Role in Plant Growth and Development by Regulating Cell Division, Cell Growth, and Cell Death. Plant Physiol 144(3):1531-45
Schrader R, et al.  (2006) Temperature-sensitive eIF5A Mutant Accumulates Transcripts Targeted to the Nonsense-mediated Decay Pathway. J Biol Chem 281(46):35336-35346
Takahashi K, et al.  (2004) Cellular signaling mediated by calphoglin-induced activation of IPP and PGM. Biochem Biophys Res Commun 325(1):203-14
Kim KK, et al.  (1998) Crystal structures of eukaryotic translation initiation factor 5A from Methanococcus jannaschii at 1.8 A resolution. Proc Natl Acad Sci U S A 95(18):10419-24
Kyrpides NC and Woese CR  (1998) Universally conserved translation initiation factors. Proc Natl Acad Sci U S A 95(1):224-8
Bevec D, et al.  (1996) Inhibition of HIV-1 replication in lymphocytes by mutants of the Rev cofactor eIF-5A. Science 271(5257):1858-60
Koettnitz K, et al.  (1995) Identification of a new member of the human eIF-5A gene family. Gene 159(2):283-4
Magdolen V, et al.  (1994) The function of the hypusine-containing proteins of yeast and other eukaryotes is well conserved. Mol Gen Genet 244(6):646-52
Schwelberger HG, et al.  (1993) Translation initiation factor eIF-5A expressed from either of two yeast genes or from human cDNA. Functional identity under aerobic and anaerobic conditions. J Biol Chem 268(19):14018-25
Schnier J, et al.  (1991) Translation initiation factor 5A and its hypusine modification are essential for cell viability in the yeast Saccharomyces cerevisiae. Mol Cell Biol 11(6):3105-14
Gordon ED, et al.  (1987) Eukaryotic initiation factor 4D, the hypusine-containing protein, is conserved among eukaryotes. J Biol Chem 262(34):16585-9
Gordon ED, et al.  (1987) Hypusine formation in eukaryotic initiation factor 4D is not reversed when rates or specificity of protein synthesis is altered. J Biol Chem 262(34):16590-5
Benne R and Hershey JW  (1978) The mechanism of action of protein synthesis initiation factors from rabbit reticulocytes. J Biol Chem 253(9):3078-87