TPI1/YDR050C Literature Guide Help

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

TPI1 - Function/Process (21)

ReferenceOther Genes Addressed
Go MK, et al.  (2010) Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach. Biochemistry 49(25):5377-89
Ma M and Liu LZ  (2010) Quantitative transcription dynamic analysis reveals candidate genes and key regulators for ethanol tolerance in Saccharomyces cerevisiae. BMC Microbiol 10():169
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
Rossignol T, et al.  (2009) The proteome of a wine yeast strain during fermentation, correlation with the transcriptome. J Appl Microbiol 107(1):47-55
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
Vazquez A, et al.  (2008) Impact of limited solvent capacity on metabolic rate, enzyme activities, and metabolite concentrations of S. cerevisiae glycolysis. PLoS Comput Biol 4(10):e1000195
Magherini F, et al.  (2007) Protein expression profiles in Saccharomyces cerevisiae during apoptosis induced by H(2)O(2). Proteomics 7(9):1434-45
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
Desamero R, et al.  (2003) Active site loop motion in triosephosphate isomerase: T-jump relaxation spectroscopy of thermal activation. Biochemistry 42(10):2941-51
Shenton D and Grant CM  (2003) Protein S-thiolation targets glycolysis and protein synthesis in response to oxidative stress in the yeast Saccharomyces cerevisiae. Biochem J 374(Pt 2):513-9
Capitanio D, et al.  (2002) Effects of the loss of triose phosphate isomerase activity on carbon metabolism in Kluyveromyces lactis. Res Microbiol 153(9):593-8
Overkamp KM, et al.  (2002) Metabolic engineering of glycerol production in Saccharomyces cerevisiae. Appl Environ Microbiol 68(6):2814-21
Rodriguez-Vargas S, et al.  (2002) Gene expression analysis of cold and freeze stress in Baker's yeast. Appl Environ Microbiol 68(6):3024-30
Compagno C, et al.  (2001) Alterations of the glucose metabolism in a triose phosphate isomerase-negative Saccharomyces cerevisiae mutant. Yeast 18(7):663-70
Nilsson A, et al.  (2001) Fermentative capacity after cold storage of baker's yeast is dependent on the initial physiological state but not correlated to the levels of glycolytic enzymes. Int J Food Microbiol 71(2-3):111-24
Rozovsky S and McDermott AE  (2001) The time scale of the catalytic loop motion in triosephosphate isomerase. J Mol Biol 310(1):259-70
Aqvist J and Fothergill M  (1996) Computer simulation of the triosephosphate isomerase catalyzed reaction. J Biol Chem 271(17):10010-6
Garza-Ramos G, et al.  (1996) Species-specific inhibition of homologous enzymes by modification of nonconserved amino acids residues. The cysteine residues of triosephosphate isomerase. Eur J Biochem 241(1):114-20
McKnight GL, et al.  (1986) Nucleotide sequence of the triosephosphate isomerase gene from Aspergillus nidulans: implications for a differential loss of introns. Cell 46(1):143-7
Alber T and Kawasaki G  (1982) Nucleotide sequence of the triose phosphate isomerase gene of Saccharomyces cerevisiae. J Mol Appl Genet 1(5):419-34
Krietsch WK  (1975) Triosephosphate isomerase from yeast. Methods Enzymol 41:434-8