Other names published for PDC1: indolepyruvate decarboxylase 1, YLR044C
PDC1 LITERATURE TOPICS
- Curated Literature
- Genetics/Cell Biology
- Nucleic Acid Information
- Gene Product Information
- Protein Physical Properties
- Protein Processing/Modification/Regulation
- Protein Sequence Features
- Protein-protein Interactions
- Protein/Nucleic Acid Structure
- Substrates/Ligands/Cofactors
- Related Genes/Proteins
- Research Aids
- Genome-wide Analysis
- Proteome-wide Analysis
- Other Topics
- Additional Information
PDC1 - Protein Processing/Modification/Regulation (39)
| Reference | Other Genes Addressed |
|---|---|
| Tylicki A, et al. (2005) Modification of thiamine pyrophosphate dependent enzyme activity by oxythiamine in Saccharomyces cerevisiae cells. Can J Microbiol 51(10):833-839 | |
| Reverter-Branchat G, et al. (2004) Oxidative damage to specific proteins in replicative and chronological-aged Saccharomyces cerevisiae: common targets and prevention by calorie restriction. J Biol Chem 279(30):31983-9 | |
| Shanmuganathan A, et al. (2004) Copper-induced oxidative stress in Saccharomyces cerevisiae targets enzymes of the glycolytic pathway. FEBS Lett 556(1-3):253-9 | |
| Gao J, et al. (2003) Changes in the protein expression of yeast as a function of carbon source. J Proteome Res 2(6):643-9 | |
| Salusjarvi L, et al. (2003) Proteome analysis of recombinant xylose-fermenting Saccharomyces cerevisiae. Yeast 20(4):295-314 | |
| Nilsson A, et al. (2001) The catabolic capacity of Saccharomyces cerevisiae is preserved to a higher extent during carbon compared to nitrogen starvation. Yeast 18(15):1371-81 | |
| Sergienko EA and Jordan F (2001) Catalytic acid-base groups in yeast pyruvate decarboxylase. 3. A steady-state kinetic model consistent with the behavior of both wild-type and variant enzymes at all relevant pH values. Biochemistry 40(25):7382-403 | |
| Arnold RJ, et al. (1999) The action of N-terminal acetyltransferases on yeast ribosomal proteins. J Biol Chem 274(52):37035-40 | |
| Morey AV and Juni E (1968) Studies on the nature of the binding of thiamine pyrophosphate to enzymes. J Biol Chem 243(11):3009-19 | |



