Gene Review:
TPI1 - triosephosphate isomerase 1
Gallus gallus
- Chicken triosephosphate isomerase complements an Escherichia coli deficiency. Straus, D., Gilbert, W. Proc. Natl. Acad. Sci. U.S.A. (1985)
- Cloning and overexpression of the triosephosphate isomerase genes from psychrophilic and thermophilic bacteria. Structural comparison of the predicted protein sequences. Rentier-Delrue, F., Mande, S.C., Moyens, S., Terpstra, P., Mainfroid, V., Goraj, K., Lion, M., Hol, W.G., Martial, J.A. J. Mol. Biol. (1993)
- Cellular models and tissue equivalent systems for evaluating the structures and significance of age-modified proteins. Gracy, R.W., Yüksel, K.U., Jacobson, T.M., Chapman, M.L., Hevelone, J.C., Wise, G.E., Dimitrijevich, S.D. Gerontology. (1991)
- The triosephosphate isomerase gene from maize: introns antedate the plant-animal divergence. Marchionni, M., Gilbert, W. Cell (1986)
- Structure of chicken muscle triose phosphate isomerase determined crystallographically at 2.5 angstrom resolution using amino acid sequence data. Banner, D.W., Bloomer, A.C., Petsko, G.A., Phillips, D.C., Pogson, C.I., Wilson, I.A., Corran, P.H., Furth, A.J., Milman, J.D., Offord, R.E., Priddle, J.D., Waley, S.G. Nature (1975)
- Simulations of the folding pathway of triose phosphate isomerase-type alpha/beta barrel proteins. Godzik, A., Skolnick, J., Kolinski, A. Proc. Natl. Acad. Sci. U.S.A. (1992)
- Active site of triosephosphate isomerase: in vitro mutagenesis and characterization of an altered enzyme. Straus, D., Raines, R., Kawashima, E., Knowles, J.R., Gilbert, W. Proc. Natl. Acad. Sci. U.S.A. (1985)
- A conservative amino acid substitution, arginine for lysine, abolishes export of a hybrid protein in Escherichia coli. Implications for the mechanism of protein secretion. Summers, R.G., Harris, C.R., Knowles, J.R. J. Biol. Chem. (1989)
- Structure determination of the glycosomal triosephosphate isomerase from Trypanosoma brucei brucei at 2.4 A resolution. Wierenga, R.K., Kalk, K.H., Hol, W.G. J. Mol. Biol. (1987)
- Entropy effects on protein hinges: the reaction catalyzed by triosephosphate isomerase. Xiang, J., Jung, J.Y., Sampson, N.S. Biochemistry (2004)
- Crystal structure of recombinant chicken triosephosphate isomerase-phosphoglycolohydroxamate complex at 1.8-A resolution. Zhang, Z., Sugio, S., Komives, E.A., Liu, K.D., Knowles, J.R., Petsko, G.A., Ringe, D. Biochemistry (1994)
- Studies of the histidine residues of triose phosphate isomerase by proton magnetic resonance and x-ray crystallography. Browne, C.A., Campbell, I.D., Kiener, P.A., Phillips, D.C., Waley, S.G., Wilson, I.A. J. Mol. Biol. (1976)
- Direct observation of substrate distortion by triosephosphate isomerase using Fourier transform infrared spectroscopy. Belasco, J.G., Knowles, J.R. Biochemistry (1980)
- Nucleotide cofactor-binding-domain-specific antibodies show immunologic relatedness among unrelated proteins that bind phosphoryl compounds. Tucker, M.M., Worsham, L.M., Ernst-Fonberg, M.L. Biochim. Biophys. Acta (1993)
- Genetic engineering in the Precambrian: structure of the chicken triosephosphate isomerase gene. Straus, D., Gilbert, W. Mol. Cell. Biol. (1985)
- Rapid isolation of triosephosphate isomerase utilizing high-performance liquid chromatography. Jacobson, T.M., Yüksel, K.U., Grant, S.R., Gracy, R.W. Protein Expr. Purif. (1990)