Other names published for TDH3: GLD1, HSP35, HSP36, SSS2, GPD, GAPDH, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) TDH3, YGR192C
TDH3 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
TDH3 - Cellular Location (11)
| Reference | Other Genes Addressed |
|---|---|
| Miura N, et al. (2012) Tracing putative trafficking of the glycolytic enzyme enolase via SNARE-driven unconventional secretion. Eukaryot Cell 11(8):1075-82 | |
| Morisaka H, et al. (2012) Two-dimensional protein separation by the HPLC system with a monolithic column. Biosci Biotechnol Biochem 76(3):585-8 | |
| Braconi D, et al. (2011) Surfome analysis of a wild-type wine Saccharomyces cerevisiae strain. Food Microbiol 28(6):1220-30 | |
| Kim KH, et al. (2011) Effect of Saccharomyces cerevisiae ret1-1 mutation on glycosylation and localization of the secretome. Mol Cells 31(2):151-8 | |
| Almeida B, et al. (2007) NO-mediated apoptosis in yeast. J Cell Sci 120(Pt 18):3279-88 | |
| Sarry JE, et al. (2007) Analysis of the vacuolar luminal proteome of Saccharomyces cerevisiae. FEBS J 274(16):4287-305 | |
| Brandina I, et al. (2006) Enolase takes part in a macromolecular complex associated to mitochondria in yeast. Biochim Biophys Acta 1757(9-10):1217-1228 | |
| Reinders J, et al. (2006) Toward the complete yeast mitochondrial proteome: multidimensional separation techniques for mitochondrial proteomics. J Proteome Res 5(7):1543-54 | |
| Delgado ML, et al. (2001) The glyceraldehyde-3-phosphate dehydrogenase polypeptides encoded by the Saccharomyces cerevisiae TDH1, TDH2 and TDH3 genes are also cell wall proteins. Microbiology 147(Pt 2):411-7 | |
| Ashmarina LI, et al. (1981) Immobilized D-glyceraldehyde-3-phosphate dehydrogenase can exist as a trimer. FEBS Lett 128(1):22-6 | |
| Nagradova NK, et al. (1980) Glyceraldehyde-3-phosphate dehydrogenase: the role of subunit interactions in enzyme functioning. Adv Enzyme Regul 19:171-204 |




