YEF3/YLR249W Literature Guide Help

Other names published for YEF3: TEF3, eEF3, EF-3, eEF1Bgamma, YLR249W

YEF3 - Protein Sequence Features (20)

ReferenceOther Genes Addressed
Visweswaraiah J, et al.  (2012) Overexpression of eukaryotic translation elongation factor 3 impairs Gcn2 protein activation. J Biol Chem 287(45):37757-68
Kovalchuk A and Driessen AJ  (2010) Phylogenetic analysis of fungal ABC transporters. BMC Genomics 11():177
Anand M, et al.  (2006) Domain and nucleotide dependence of the interaction between Saccharomyces cerevisiae translation elongation factors 3 and 1A. J Biol Chem 281(43):32318-26
Anand M, et al.  (2003) Functional interactions between yeast translation eukaryotic elongation factor (eEF) 1A and eEF3. J Biol Chem 278(9):6985-91
Jeppesen MG, et al.  (2003) The crystal structure of the glutathione S-transferase-like domain of elongation factor 1Bgamma from Saccharomyces cerevisiae. J Biol Chem 278(47):47190-8
Kambampati R, et al.  (2000) Limited proteolysis of yeast elongation factor 3. Sequence and location of the subdomains. J Biol Chem 275(22):16963-8
Chakraburtty K and Triana-Alonso FJ  (1998) Yeast elongation factor 3: structure and function. Biol Chem 379(7):831-40
Gontarek RR, et al.  (1998) The N terminus of eukaryotic translation elongation factor 3 interacts with 18 S rRNA and 80 S ribosomes. J Biol Chem 273(17):10249-52
Sarthy AV, et al.  (1998) Identification and kinetic analysis of a functional homolog of elongation factor 3, YEF3 in Saccharomyces cerevisiae. Yeast 14(3):239-53
Marton MJ, et al.  (1997) Evidence that GCN1 and GCN20, translational regulators of GCN4, function on elongating ribosomes in activation of eIF2alpha kinase GCN2. Mol Cell Biol 17(8):4474-89
Masahiro U, et al.  (1996) A monoclonal antibody specific for carboxy-terminal region of yeast translation elongation factor-3 inhibits ribosome-activated ATPase activity but not intrinsic ATPase activity. Biochem Mol Biol Int 39(2):227-34
Yang H, et al.  (1996) A point mutation within each of two ATP-binding motifs inactivates the functions of elongation factor 3. Biochim Biophys Acta 1310(3):303-8
Belfield GP, et al.  (1995) Translation elongation factor-3 (EF-3): an evolving eukaryotic ribosomal protein? J Mol Evol 41(3):376-87
Kovalchuke O, et al.  (1995) Comparative analysis of ATPase of yeast elongation factor 3 and ATPase associated with Tetrahymena ribosomes. Biochimie 77(9):713-18
Kovalchuke O and Chakraburtty K  (1994) Comparative analysis of ribosome-associated adenosinetriphosphatase (ATPase) from pig liver and the ATPase of elongation factor 3 from Saccharomyces cerevisiae. Eur J Biochem 226(1):133-40
Qin SL, et al.  (1990) Sequence analysis of the translational elongation factor 3 from Saccharomyces cerevisiae. J Biol Chem 265(4):1903-12
Sandbaken M, et al.  (1990) Isolation and characterization of the structural gene encoding elongation factor 3. Biochim Biophys Acta 1050(1-3):230-4
Sandbaken MG, et al.  (1990) Protein synthesis in yeast. Structural and functional analysis of the gene encoding elongation factor 3. J Biol Chem 265(26):15838-44
Miyazaki M, et al.  (1988) The yeast peptide elongation factor 3 (EF-3) carries an active site for ATP hydrolysis which can interact with various nucleoside triphosphates in the absence of ribosomes. J Biochem 104(3):445-50
Dasmahapatra B and Chakraburtty K  (1981) Protein synthesis in yeast. I. Purification and properties of elongation factor 3 from Saccharomyces cerevisiae. J Biol Chem 256(19):9999-10004