Other names published for HEF3: ZRG7, translation elongation factor EF-3, YNL014W
HEF3 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
HEF3 - Substrates/Ligands/Cofactors (13)
| Reference | Other Genes Addressed |
|---|---|
| Andersen CB, et al. (2006) Structure of eEF3 and the mechanism of transfer RNA release from the E-site. Nature 443(7112):663-8 | |
| 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 | |
| Kambampati R and Chakraburtty K (1997) Functional subdomains of yeast elongation factor 3. Localization of ribosome-binding domain. J Biol Chem 272(10):6377-81 | |
| 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 | |
| El'skaya EV, et al. (1995) Stimulation of yeast EF-3 factor by mammalian ribosomes. Ukr Biokhim Zh 67(6):28-32 | |
| 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 | |
| Triana-Alonso FJ, et al. (1995) The elongation factor 3 unique in higher fungi and essential for protein biosynthesis is an E site factor. J Biol Chem 270(35):20473-8 | |
| 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 | |
| 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 | |
| Miyazaki M, et al. (1986) Intrinsic ATPase activity of yeast peptide chain elongation factor 3(EF-3) and its direct interaction with various nucleotides. Nucleic Acids Symp Ser(17):171-4 | |
| Uritani M and Miyazaki M (1985) Interaction of yeast polypeptide chain elongation factor-3 (EF-3) with different nucleotides. Nucleic Acids Symp Ser(16):229-32 |



