Other names published for TDH2: GLD2, GAPDH, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) TDH2, YJR009C
TDH2 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
TDH2 - Protein/Nucleic Acid Structure (6)
| Reference | Other Genes Addressed |
|---|---|
| Waingeh VF, et al. (2006) Glycolytic enzyme interactions with yeast and skeletal muscle F-actin. Biophys J 90(4):1371-84 | |
| Davis JM and Maki AH (1984) Comparative phosphorescence and optically detected magnetic resonance studies of pig and yeast glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 23(25):6249-56 | |
| Nakano M, et al. (1976) Relationship between structure and chemical reactivity in D-glyceraldehyde 3-phosphate dehydrogenase. Trinitrophenylation of the lysine residues in yeast, sturgeon and rabbit muscle enzyme. J Mol Biol 105(2):275-91 | |
| Byers LD and Koshland DE Jr (1975) The specificity of induced conformational changes. The case of yeast glyceraldehyde-3-phosphate dehydrogenase. Biochemistry 14(16):3661-9 | |
| Heilmann H-D and Pfleiderer G (1975) On the role of tryptophan residues in the mechanism of action of glyceraldehyde-3phosphate dehydrogenase as tested by specific modification. Biochim Biophys Acta 384(2):331-41 | |
| Sloan DL, et al. (1973) Protein hydration changes in the formation of the nicotinamide adenine dinucleotide complexes of glyceraldehyde 3-phosphate dehydrogenase of yeast. II. The spin lattice relaxation of solvent water protons. J Biol Chem 248(15):5424-7 |



