TDH2/YJR009C Literature Guide Help

Other names published for TDH2: GLD2, GAPDH, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) TDH2, YJR009C

TDH2 - Non-Fungal Related Genes/Proteins (16)

ReferenceOther Genes Addressed
Kovalev N, et al.  (2012) A Co-Opted DEAD-Box RNA Helicase Enhances Tombusvirus Plus-Strand Synthesis. PLoS Pathog 8(2):e1002537
Waingeh VF, et al.  (2006) Glycolytic enzyme interactions with yeast and skeletal muscle F-actin. Biophys J 90(4):1371-84
Tanaka T, et al.  (2005) Evolution of vitamin B6 (pyridoxine) metabolism by gain and loss of genes. Mol Biol Evol 22(2):243-50
Bakker BM, et al.  (2000) Compartmentation protects trypanosomes from the dangerous design of glycolysis. Proc Natl Acad Sci U S A 97(5):2087-92
Karlberg O, et al.  (2000) The dual origin of the yeast mitochondrial proteome. Yeast 17(3):170-87
Carmona P, et al.  (1999) Conformational structure and binding mode of glyceraldehyde-3-phosphate dehydrogenase to tRNA studied by Raman and CD spectroscopy. Biochim Biophys Acta 1432(2):222-33
Lambeir AM, et al.  (1991) The cytosolic and glycosomal glyceraldehyde-3-phosphate dehydrogenase from Trypanosoma brucei. Kinetic properties and comparison with homologous enzymes. Eur J Biochem 198(2):429-35
Asryants RA, et al.  (1989) An examination of the role of arginine residues in the functioning of D-glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 997(3):159-66
Klichko VI, et al.  (1986) [Comparative study of glyceraldehyde-3-phosphate dehydrogenases isolated from rabbit skeletal muscles and baker's yeast using cationic fluorescent probes] Biokhimiia 51(9):1465-75
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
Musti AM, et al.  (1983) Transcriptional mapping of two yeast genes coding for glyceraldehyde 3-phosphate dehydrogenase isolated by sequence homology with the chicken gene. Gene 25(1):133-43
Foucault G, et al.  (1981) Structure and reactivity relationship in glyceraldehyde-3-phosphate dehydrogenase. Dinitrophenylation of cysteine residues of yeast and rabbit muscle enzymes. Eur J Biochem 119(3):625-32
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
Herzfeld J and Schlesinger PA  (1975) Analysis of the allosteric basis for positive and negative co-operativity and half-of-the-sites reactivity in yeast and rabbit muscle glyceraldehyde 3-phosphate dehydrogenase. J Mol Biol 97(4):483-517
Fensleau A  (1972) Structure-function studies on glyceraldehyde 3-phosphate dehydrogenase. IV. Subunit interactions of the rabbit muscle and yeast enzymes. J Biol Chem 247(4):1074-9
TAYLOR EL, et al.  (1963) The hydrolysis of p-nitrophenyl acetate catalyzed by 3-phosphoglyceraldehyde dehydrogenase crystallized from yeast. J Biol Chem 238:734-40