TPI1/YDR050C Literature Guide Help

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

TPI1 - Protein/Nucleic Acid Structure (21)

ReferenceOther Genes Addressed
Hernandez-Santoyo A, et al.  (2012) Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability. Int J Mol Sci 13(8):10010-21
Cruces-Angeles ME, et al.  (2011) Thermodynamic and kinetic destabilization of triosephosphate isomerase resulting from the mutation of conserved and non-conserved cysteines. Protein Pept Lett 18(12):1290-8
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
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
Patel B and Finke JM  (2007) Folding and Unfolding of {gamma}TIM Monomers and Dimers. Biophys J 93(7):2457-71
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
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
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
Silverman JA and Harbury PB  (2002) The equilibrium unfolding pathway of a (beta/alpha)8 barrel. J Mol Biol 324(5):1031-40
Aqvist J and Fothergill M  (1996) Computer simulation of the triosephosphate isomerase catalyzed reaction. J Biol Chem 271(17):10010-6
Joseph-McCarthy D, et al.  (1994) Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid. Biochemistry 33(10):2824-9
Lodi PJ and Knowles JR  (1993) Direct evidence for the exploitation of an alpha-helix in the catalytic mechanism of triosephosphate isomerase. Biochemistry 32(16):4338-43
Sampson NS and Knowles JR  (1992) Segmental motion in catalysis: investigation of a hydrogen bond critical for loop closure in the reaction of triosephosphate isomerase. Biochemistry 31(36):8488-94
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
Alber TC, et al.  (1987) Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme? Cold Spring Harb Symp Quant Biol 52:603-13
Alber T, et al.  (1981) Crystallization of yeast triose phosphate isomerase from polyethylene glycol. Protein crystal formation following phase separation. J Biol Chem 256(3):1356-61
Hawkinson SW, et al.  (1972) Triose phosphate isomerase from Bakers' yeast. Preliminary crystallographic data. J Biol Chem 247(10):3361-2