TPI1/YDR050C Literature Guide Help

Other names published for TPI1: triose-phosphate isomerase TPI1, YDR050C

TPI1 - Protein Physical Properties (42)

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
Gruning NM, et al.  (2011) Pyruvate Kinase Triggers a Metabolic Feedback Loop that Controls Redox Metabolism in Respiring Cells. Cell Metab 14(3):415-27
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
Go MK, et al.  (2010) Rescue of K12G Triosephosphate Isomerase by Ammonium Cations: The Reaction of an Enzyme in Pieces. J Am Chem Soc 132(38):13525-32
Go MK, et al.  (2010) Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach. Biochemistry 49(25):5377-89
Marino SM, et al.  (2010) Characterization of Surface-Exposed Reactive Cysteine Residues in Saccharomyces cerevisiae. Biochemistry 49(35):7709-21
Xu Y, et al.  (2010) Triosephosphate Isomerase: (15)N and (13)C Chemical Shift Assignments and Conformational Change upon Ligand Binding by Magic-Angle Spinning Solid-State NMR Spectroscopy. J Mol Biol 397(1):233-248
van Eunen K, et al.  (2010) Measuring enzyme activities under standardized in vivo-like conditions for systems biology. FEBS J 277(3):749-60
Cheng JS, et al.  (2009) Inoculation-density-dependent responses and pathway shifts in Saccharomyces cerevisiae. Proteomics 9(20):4704-13
Cheng JS, et al.  (2009) Proteomic insights into adaptive responses of Saccharomyces cerevisiae to the repeated vacuum fermentation. Appl Microbiol Biotechnol 83(5):909-23
Peimbert M, et al.  (2008) Hydrophobic repacking of the dimer interface of triosephosphate isomerase by in silico design and directed evolution. Biochemistry 47(20):5556-64
Reyes-Lopez CA, et al.  (2008) The conserved salt bridge linking two C-terminal beta/alpha units in homodimeric triosephosphate isomerase determines the folding rate of the monomer. Proteins 72(3):972-9
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
Gonzalez-Mondragon E, et al.  (2007) Effect of a specific inhibitor on the unfolding and refolding kinetics of dimeric triosephosphate isomerase: establishing the dimeric and similarly structured nature of the main transition states on the forward and backward reactions. Biophys Chem 125(1):172-8
Gulotta M, et al.  (2007) Effects of cell volume regulating osmolytes on glycerol 3-phosphate binding to triosephosphate isomerase. Biochemistry 46(35):10055-62
Najera H, et al.  (2007) Thermodynamic and kinetic characterization of the association of triosephosphate isomerase: The role of diffusion. Biochim Biophys Acta 1774(8):985-94
Rozovsky S and McDermott AE  (2007) Substrate product equilibrium on a reversible enzyme, triosephosphate isomerase. Proc Natl Acad Sci U S A 104(7):2080-5
Vazquez-Perez AR and Fernandez-Velasco DA  (2007) Pressure and Denaturants in the Unfolding of Triosephosphate Isomerase: The Monomeric Intermediates of the Enzymes from Saccharomyces cerevisiae and Entamoeba histolytica. Biochemistry 46(29):8624-33
Massi F, et al.  (2006) Solution NMR and computer simulation studies of active site loop motion in triosephosphate isomerase. Biochemistry 45(36):10787-94
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
Shi Y, et al.  (2005) Genetic perturbation of glycolysis results in inhibition of de novo inositol biosynthesis. J Biol Chem 280(51):41805-10
Gonzalez-Mondragon E, et al.  (2004) Conserved cysteine 126 in triosephosphate isomerase is required not for enzymatic activity but for proper folding and stability. Biochemistry 43(11):3255-63
Jones DL, et al.  (2004) Genome-Wide Analysis of the Effects of Heat Shock on a Saccharomyces cerevisiae Mutant With a Constitutively Activated cAMP-Dependent Pathway. Comp Funct Genomics 5(5):419-31
Desamero R, et al.  (2003) Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation. Biochemistry 42(10):2941-51
Fraenkel DG  (2003) The top genes: on the distance from transcript to function in yeast glycolysis. Curr Opin Microbiol 6(2):198-201
Jogl G, et al.  (2003) Optimal alignment for enzymatic proton transfer: structure of the Michaelis complex of triosephosphate isomerase at 1.2-A resolution. Proc Natl Acad Sci U S A 100(1):50-5
Najera H, et al.  (2003) Thermodynamic characterization of yeast triosephosphate isomerase refolding: insights into the interplay between function and stability as reasons for the oligomeric nature of the enzyme. Biochem J 370(Pt 3):785-92
Ngondi-Ekome J, et al.  (2003) Study on agglutinating factors from flocculent Saccharomyces cerevisiae strains. Biochimie 85(1-2):133-43