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Journal Abstract Search

194 related items for PubMed ID: 1967829

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  • 2. Reaction energetics of a mutant triosephosphate isomerase in which the active-site glutamate has been changed to aspartate.
    Raines RT, Sutton EL, Straus DR, Gilbert W, Knowles JR.
    Biochemistry; 1986 Nov 04; 25(22):7142-54. PubMed ID: 2879556
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  • 6. Subunit interface of triosephosphate isomerase: site-directed mutagenesis and characterization of the altered enzyme.
    Casal JI, Ahern TJ, Davenport RC, Petsko GA, Klibanov AM.
    Biochemistry; 1987 Mar 10; 26(5):1258-64. PubMed ID: 3552044
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  • 7. Nucleotide sequence of the triose phosphate isomerase gene of Escherichia coli.
    Pichersky E, Gottlieb LD, Hess JF.
    Mol Gen Genet; 1984 Mar 10; 195(1-2):314-20. PubMed ID: 6092857
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  • 8. Human triose-phosphate isomerase deficiency: a single amino acid substitution results in a thermolabile enzyme.
    Daar IO, Artymiuk PJ, Phillips DC, Maquat LE.
    Proc Natl Acad Sci U S A; 1986 Oct 10; 83(20):7903-7. PubMed ID: 2876430
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  • 9. Crystallography and site-directed mutagenesis of yeast triosephosphate isomerase: what can we learn about catalysis from a "simple" enzyme?
    Alber TC, Davenport RC, Giammona DA, Lolis E, Petsko GA, Ringe D.
    Cold Spring Harb Symp Quant Biol; 1987 Oct 10; 52():603-13. PubMed ID: 3331346
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  • 13. How can a catalytic lesion be offset? The energetics of two pseudorevertant triosephosphate isomerases.
    Blacklow SC, Knowles JR.
    Biochemistry; 1990 May 01; 29(17):4099-108. PubMed ID: 2361134
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  • 14. Crystal structure of the mutant yeast triosephosphate isomerase in which the catalytic base glutamic acid 165 is changed to aspartic acid.
    Joseph-McCarthy D, Rost LE, Komives EA, Petsko GA.
    Biochemistry; 1994 Mar 15; 33(10):2824-9. PubMed ID: 7907502
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  • 18. Simple model for the effect of Glu165----Asp165 mutation on the rate of catalysis in triose phosphate isomerase.
    Alagona G, Ghio C, Kollman PA.
    J Mol Biol; 1986 Sep 05; 191(1):23-7. PubMed ID: 3025454
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  • 19. The importance of hinge sequence for loop function and catalytic activity in the reaction catalyzed by triosephosphate isomerase.
    Xiang J, Sun J, Sampson NS.
    J Mol Biol; 2001 Apr 06; 307(4):1103-12. PubMed ID: 11286559
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  • 20. Triosephosphate isomerase: energetics of the reaction catalyzed by the yeast enzyme expressed in Escherichia coli.
    Nickbarg EB, Knowles JR.
    Biochemistry; 1988 Aug 09; 27(16):5939-47. PubMed ID: 3056516
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