Other names published for EUG1: protein disulfide isomerase EUG1, YDR518W
EUG1 LITERATURE TOPICS
- Curated Literature
- Additional Literature
- All Curated References
- Primary Literature
- Reviews
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
EUG1 - Primary Literature (12)
| Reference | Other Genes Addressed |
|---|---|
| Grubb S, et al. (2012) Protein disulfide isomerases contribute differentially to the endoplasmic reticulum-associated degradation of apolipoprotein B and other substrates. Mol Biol Cell 23(4):520-32 | |
| Hacioglu E, et al. (2010) The roles of thiol oxidoreductases in yeast replicative aging. Mech Ageing Dev 131(11-12):692-9 | |
| Byrne KP and Wolfe KH (2005) The Yeast Gene Order Browser: combining curated homology and syntenic context reveals gene fate in polyploid species. Genome Res 15(10):1456-61 | |
| Kimura T, et al. (2005) Interactions among Yeast Protein-Disulfide Isomerase Proteins and Endoplasmic Reticulum Chaperone Proteins Influence Their Activities. J Biol Chem 280(36):31438-41 | |
| Kimura T, et al. (2004) Functional differences between human and yeast protein disulfide isomerase family proteins. Biochem Biophys Res Commun 320(2):359-65 | |
| Xiao R, et al. (2004) The contributions of protein disulfide isomerase and its homologues to oxidative protein folding in the yeast endoplasmic reticulum. J Biol Chem 279(48):49780-6 | |
| Norgaard P and Winther JR (2001) Mutation of yeast Eug1p CXXS active sites to CXXC results in a dramatic increase in protein disulphide isomerase activity. Biochem J 358(Pt 1):269-74 | |
| Norgaard P, et al. (2001) Functional differences in yeast protein disulfide isomerases. J Cell Biol 152(3):553-62 | |
| Frand AR and Kaiser CA (1999) Ero1p oxidizes protein disulfide isomerase in a pathway for disulfide bond formation in the endoplasmic reticulum. Mol Cell 4(4):469-77 | |
| Mori K, et al. (1998) Palindrome with spacer of one nucleotide is characteristic of the cis-acting unfolded protein response element in Saccharomyces cerevisiae. J Biol Chem 273(16):9912-20 | |
| Holst B, et al. (1997) Active site mutations in yeast protein disulfide isomerase cause dithiothreitol sensitivity and a reduced rate of protein folding in the endoplasmic reticulum. J Cell Biol 138(6):1229-38 | |
| Tachibana C and Stevens TH (1992) The yeast EUG1 gene encodes an endoplasmic reticulum protein that is functionally related to protein disulfide isomerase. Mol Cell Biol 12(10):4601-11 |



