Other names published for DUG1: metallodipeptidase, YFR044C
DUG1 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
- Additional Information
DUG1 - Primary Literature (7)
| Reference | Other Genes Addressed |
|---|---|
| Baudouin-Cornu P, et al. (2012) Glutathione degradation is a key determinant of glutathione homeostasis. J Biol Chem 287(7):4552-61 | |
| Kaur H, et al. (2012) Glutathione degradation by the alternative pathway (DUG pathway) in Saccharomyces cerevisiae is initiated by (Dug2p-Dug3p)2 complex, a novel glutamine amidotransferase (GATase) enzyme acting on glutathione. J Biol Chem 287(12):8920-31 | |
| Kaur H, et al. (2011) Cys-Gly specific dipeptidase Dug1p from S. cerevisiae binds promiscuously to di-, tri-, and tetra-peptides: Peptide-protein interaction, homology modeling, and activity studies reveal a latent promiscuity in substrate recognition. Biochimie 93(2):175-86 | |
| Pandya V, et al. (2011) Mass spectrometry assay for studying kinetic properties of dipeptidases: characterization of human and yeast dipeptidases. Anal Biochem 418(1):134-42 | |
| Kaur H, et al. (2009) Dug1p Is a Cys-Gly Peptidase of the {gamma}-Glutamyl Cycle of Saccharomyces cerevisiae and Represents a Novel Family of Cys-Gly Peptidases. J Biol Chem 284(21):14493-502 | |
| Ganguli D, et al. (2007) The Alternative Pathway of Glutathione Degradation Is Mediated by a Novel Protein Complex Involving Three New Genes in Saccharomyces cerevisiae. Genetics 175(3):1137-51 | |
| Cai H, et al. (2006) Genomewide Screen Reveals a Wide Regulatory Network for Di/Tripeptide Utilization in Saccharomyces cerevisiae. Genetics 172(3):1459-76 |



