TPI1/YDR050C Literature Guide Help

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

TPI1 - Non-Fungal Related Genes/Proteins (19)

ReferenceOther Genes Addressed
Dengjel J, et al.  (2012) Identification of autophagosome-associated proteins and regulators by quantitative proteomic analysis and genetic screens. Mol Cell Proteomics 11(3):M111.014035
Sharma S, et al.  (2012) Characterization of stress and methylglyoxal inducible triose phosphate isomerase (OscTPI) from rice. Plant Signal Behav 7(10):1337-45
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
Samanta M, et al.  (2011) Probing the role of the fully conserved Cys126 in triosephosphate isomerase by site-specific mutagenesis--distal effects on dimer stability. FEBS J 278(11):1932-43
Go MK, et al.  (2010) Role of Lys-12 in catalysis by triosephosphate isomerase: a two-part substrate approach. Biochemistry 49(25):5377-89
Rodriguez-Almazan C, et al.  (2008) Structural basis of human triosephosphate isomerase deficiency: mutation E104D is related to alterations of a conserved water network at the dimer interface. J Biol Chem 283(34):23254-63
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
Olivares-Illana V, et al.  (2006) Structural differences in triosephosphate isomerase from different species and discovery of a multitrypanosomatid inhibitor. Biochemistry 45(8):2556-60
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
Olah J, et al.  (2002) Triosephosphate isomerase deficiency: a neurodegenerative misfolding disease. Biochem Soc Trans 30(2):30-8
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
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
Sun AQ, et al.  (1992) Interactions between the catalytic centers and subunit interface of triosephosphate isomerase probed by refolding, active site modification, and subunit exchange. J Biol Chem 267(28):20168-74
Wierenga RK, et al.  (1992) Comparison of the refined crystal structures of liganded and unliganded chicken, yeast and trypanosomal triosephosphate isomerase. J Mol Biol 224(4):1115-26
Lolis E, et al.  (1990) Structure of yeast triosephosphate isomerase at 1.9-A resolution. Biochemistry 29(28):6609-18
Lambeir AM, et al.  (1987) Kinetic properties of triose-phosphate isomerase from Trypanosoma brucei brucei. A comparison with the rabbit muscle and yeast enzymes. Eur J Biochem 168(1):69-74
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