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Journal Abstract Search

152 related items for PubMed ID: 3331346

  • 1. 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; 52():603-13. PubMed ID: 3331346
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  • 2. Probing the catalytic mechanism of yeast triose phosphate isomerase by site-specific mutagenesis.
    Petsko GA, Davenport RC, Frankel D, RaiBhandary UL.
    Biochem Soc Trans; 1984 Apr; 12(2):229-32. PubMed ID: 6373437
    [No Abstract] [Full Text] [Related]

  • 3. 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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  • 4. Control of oligomeric enzyme thermostability by protein engineering.
    Ahern TJ, Casal JI, Petsko GA, Klibanov AM.
    Proc Natl Acad Sci U S A; 1987 Feb 10; 84(3):675-9. PubMed ID: 3543933
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  • 5. Crystallographic analysis of the complex between triosephosphate isomerase and 2-phosphoglycolate at 2.5-A resolution: implications for catalysis.
    Lolis E, Petsko GA.
    Biochemistry; 1990 Jul 17; 29(28):6619-25. PubMed ID: 2204418
    [Abstract] [Full Text] [Related]

  • 6. Triosephosphate isomerase: removal of a putatively electrophilic histidine residue results in a subtle change in catalytic mechanism.
    Nickbarg EB, Davenport RC, Petsko GA, Knowles JR.
    Biochemistry; 1988 Aug 09; 27(16):5948-60. PubMed ID: 2847777
    [Abstract] [Full Text] [Related]

  • 7. Effects of a buried cysteine-to-serine mutation on yeast triosephosphate isomerase structure and stability.
    Hernández-Santoyo A, Domínguez-Ramírez L, Reyes-López CA, González-Mondragón E, Hernández-Arana A, Rodríguez-Romero A.
    Int J Mol Sci; 2012 Aug 09; 13(8):10010-10021. PubMed ID: 22949845
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  • 10. Searching sequence space by definably random mutagenesis: improving the catalytic potency of an enzyme.
    Hermes JD, Blacklow SC, Knowles JR.
    Proc Natl Acad Sci U S A; 1990 Jan 09; 87(2):696-700. PubMed ID: 1967829
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  • 11. The mechanistic pathway of a mutant triosephosphate isomerase.
    Raines RT, Knowles JR.
    Ann N Y Acad Sci; 1986 Jan 09; 471():266-71. PubMed ID: 3460499
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  • 14. The time scale of the catalytic loop motion in triosephosphate isomerase.
    Rozovsky S, McDermott AE.
    J Mol Biol; 2001 Jun 29; 310(1):259-70. PubMed ID: 11419951
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  • 15. Apparent equivalence of the active-site glutamyl residue and the essential group with pKalpha 6.0 in triosephosphate isomerase.
    Hartman FC, Ratrie H.
    Biochem Biophys Res Commun; 1977 Jul 25; 77(2):746-52. PubMed ID: 20092
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  • 17. Solution-state NMR investigations of triosephosphate isomerase active site loop motion: ligand release in relation to active site loop dynamics.
    Rozovsky S, Jogl G, Tong L, McDermott AE.
    J Mol Biol; 2001 Jun 29; 310(1):271-80. PubMed ID: 11419952
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  • 19. 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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  • 20. Triosephosphate isomerase requires a positively charged active site: the role of lysine-12.
    Lodi PJ, Chang LC, Knowles JR, Komives EA.
    Biochemistry; 1994 Mar 15; 33(10):2809-14. PubMed ID: 8130193
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