Other names published for URE2: [URE3], YNL229C
URE2 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
URE2 - Substrates/Ligands/Cofactors (10)
| Reference | Other Genes Addressed |
|---|---|
| Zhang ZR and Perrett S (2009) Novel Glutaredoxin Activity of the Yeast Prion Protein Ure2 Reveals a Native-like Dimer within Fibrils. J Biol Chem 284(21):14058-67 | |
| Zhang ZR, et al. (2008) "Restoration" of glutathione transferase activity by single-site mutation of the yeast prion protein Ure2. J Mol Biol 384(3):641-51 | |
| Feller A, et al. (2006) Transduction of the nitrogen signal activating Gln3-mediated transcription is independent of Npr1 kinase and Rsp5-Bul1/2 ubiquitin ligase in Saccharomyces cerevisiae. J Biol Chem 281(39):28546-54 | |
| Bai M, et al. (2004) The yeast prion protein Ure2 shows glutathione peroxidase activity in both native and fibrillar forms. J Biol Chem 279(48):50025-30 | |
| Bach S, et al. (2003) Isolation of drugs active against mammalian prions using a yeast-based screening assay. Nat Biotechnol 21(9):1075-81 | |
| Bousset L, et al. (2003) The native-like conformation of Ure2p in fibrils assembled under physiologically relevant conditions switches to an amyloid-like conformation upon heat-treatment of the fibrils. J Struct Biol 141(2):132-42 | |
| Rai R, et al. (2003) Ure2, a prion precursor with homology to glutathione S-transferase, protects Saccharomyces cerevisiae cells from heavy metal ion and oxidant toxicity. J Biol Chem 278(15):12826-33 | |
| Bousset L, et al. (2002) The yeast prion Ure2p retains its native alpha-helical conformation upon assembly into protein fibrils in vitro. EMBO J 21(12):2903-11 | |
| Bousset L, et al. (2001) Crystal structures of the yeast prion Ure2p functional region in complex with glutathione and related compounds. Biochemistry 40(45):13564-73 | |
| Garcia SC, et al. (2000) Constitutive expression of the UGA4 gene in Saccharomyces cerevisiae depends on two positive-acting proteins, Uga3p and Uga35p. FEMS Microbiol Lett 184(2):219-24 |



