TDH1/YJL052W Literature Guide Help

Other names published for TDH1: GLD3, GAPDH, glyceraldehyde-3-phosphate dehydrogenase (phosphorylating) TDH1, YJL052W

TDH1 - Protein Physical Properties (30)

ReferenceOther Genes Addressed
Postmus J, et al.  (2012) Isoenzyme expression changes in response to high temperature determine the metabolic regulation of increased glycolytic flux in yeast. FEMS Yeast Res 12(5):571-81
Canelas AB, et al.  (2011) An in vivo data-driven framework for classification and quantification of enzyme kinetics and determination of apparent thermodynamic data. Metab Eng 13(3):294-306
Swainston N, et al.  (2011) A QconCAT informatics pipeline for the analysis, visualization and sharing of absolute quantitative proteomics data. Proteomics 11(2):329-33
Cyrne L, et al.  (2010) Glyceraldehyde-3-phosphate dehydrogenase is largely unresponsive to low regulatory levels of hydrogen peroxide in Saccharomyces cerevisiae. BMC Biochem 11():49
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
van Eunen K, et al.  (2010) Measuring enzyme activities under standardized in vivo-like conditions for systems biology. FEBS J 277(3):749-60
van Eunen K, et al.  (2010) Time-dependent regulation of yeast glycolysis upon nitrogen starvation depends on cell history. IET Syst Biol 4(2):157
Tong L, et al.  (2009) Hydrolase regulates NAD+ metabolites and modulates cellular redox. J Biol Chem 284(17):11256-66
van Eunen K, et al.  (2009) Time-dependent regulation analysis dissects shifts between metabolic and gene-expression regulation during nitrogen starvation in baker's yeast. FEBS J 276(19):5521-36
Rossell S, et al.  (2008) Mixed and diverse metabolic and gene-expression regulation of the glycolytic and fermentative pathways in response to a HXK2 deletion in Saccharomyces cerevisiae. FEMS Yeast Res 8(1):155-64
van den Brink J, et al.  (2008) Dynamics of glycolytic regulation during adaptation of Saccharomyces cerevisiae to fermentative metabolism. Appl Environ Microbiol 74(18):5710-23
Rossell S, et al.  (2006) Unraveling the complexity of flux regulation: a new method demonstrated for nutrient starvation in Saccharomyces cerevisiae. Proc Natl Acad Sci U S A 103(7):2166-71
Waingeh VF, et al.  (2006) Glycolytic enzyme interactions with yeast and skeletal muscle F-actin. Biophys J 90(4):1371-84
Fraenkel DG  (2003) The top genes: on the distance from transcript to function in yeast glycolysis. Curr Opin Microbiol 6(2):198-201
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
van Hoek P, et al.  (1998) Effect of specific growth rate on fermentative capacity of baker's yeast. Appl Environ Microbiol 64(11):4226-33
Barnes G, et al.  (1992) Yeast proteins associated with microtubules in vitro and in vivo. Mol Biol Cell 3(1):29-47
Watanabe Y, et al.  (1991) Identification and characterization of a thermolabile antigen (TLAb, glyceraldehyde-3-phosphate dehydrogenase) in Saccharomyces cerevisiae. Biotechnol Appl Biochem 13(2):269-76
Persson LO and Johansson G  (1990) Studies of protein-protein interaction using countercurrent distribution in aqueous two-phase systems: partition behavior of five glycolytic enzymes from crude baker's yeast extract. Arch Biochem Biophys 276(1):227-31
McAlister L and Holland MJ  (1985) Differential expression of the three yeast glyceraldehyde-3-phosphate dehydrogenase genes. J Biol Chem 260(28):15019-27
Banuelos M and Gancedo C  (1978) In situ study of the glycolytic pathway in Saccharomyces cerevisiae. Arch Microbiol 117(2):197-201
Holland MJ and Holland JP  (1978) Isolation and identification of yeast messenger ribonucleic acids coding for enolase, glyceraldehyde-3-phosphate dehydrogenase, and phosphoglycerate kinase. Biochemistry 17(23):4900-7
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
Sloan DL and Velick SF  (1973) Protein hydration changes in the formation of the nicotinamide adenine dinucleotide complexes of glyceraldehyde 3-phosphate dehydrogenase of yeast. I. Buoyant densities, preferential hydrations, and fluorescence-quenching titrations. J Biol Chem 248(15):5419-23
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
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
STOCKELL A  (1959) The binding of analogues of diphosphopyridine nucleotide by yeast glyceraldehyde-3-phosphate dehydrogenase. J Biol Chem 234(5):1293-6
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
KREBS EG  (1953) Yeast Glyceraldehyde-3-phosphate dehydrogenase. I. Electrophoresis of fractions precipitated by nucleic acid. J Biol Chem 200(2):471-8
KREBS EG, et al.  (1953) Yeast glyceraldehyde-3-phosphate dehydrogenase. II. Yeast protein 2. J Biol Chem 200(2):479-92