TDH2/YJR009C Literature Guide Help

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

TDH2 - Protein Sequence Features (17)

ReferenceOther Genes Addressed
Brandes N, et al.  (2011) Using quantitative redox proteomics to dissect the yeast redoxome. J Biol Chem 286(48):41893-903
Carroll KM, et al.  (2011) Absolute quantification of the glycolytic pathway in yeast: deployment of a complete QconCAT approach. Mol Cell Proteomics 10(12):M111.007633
Lee PY, et al.  (2011) The S-nitrosylation of glyceraldehyde-3-phosphate dehydrogenase 2 is reduced by interaction with glutathione peroxidase 3 in Saccharomyces cerevisiae. Mol Cells 31(3):255-9
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Norbeck J and Blomberg A  (1995) Gene linkage of two-dimensional polyacrylamide gel electrophoresis resolved proteins from isogene families in Saccharomyces cerevisiae by microsequencing of in-gel trypsin generated peptides. Electrophoresis 16(1):149-56
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
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
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
Holland MJ and Holland JP  (1979) Isolation and characterization of a gene coding for glyceraldehyde-3-phosphate dehydrogenase from Saccharomyces cerevisiae. J Biol Chem 254(12):5466-74
Muronetz VI, et al.  (1979) Half-of-the-sites reactivity in immobilized hybrids of glyceraldehyde-3-phosphate dehydrogenase. FEBS Lett 107(2):277-80
Rudolph R, et al.  (1977) Mechanism of reactivation and refolding of glyceraldehyde-3-phosphate dehydrogenase from yeast after denaturation and dissociation. Eur J Biochem 81(3):563-70
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
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
Nagradova NK and Asryants RA  (1975) Essential arginine residues in D-glyceraldehyde-3-phosphate dehydrogenase. Biochim Biophys Acta 386(1):365-8
HALSEY YD  (1955) The reaction of methyl mercury nitrate with the sulfhydryl groups of yeast glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 214(2):589-93