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Journal Abstract Search

209 related items for PubMed ID: 15709745

  • 1. Elucidating the specificity of binding of sulfonylurea herbicides to acetohydroxyacid synthase.
    McCourt JA, Pang SS, Guddat LW, Duggleby RG.
    Biochemistry; 2005 Feb 22; 44(7):2330-8. PubMed ID: 15709745
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  • 3. Crystal structure of yeast acetohydroxyacid synthase: a target for herbicidal inhibitors.
    Pang SS, Duggleby RG, Guddat LW.
    J Mol Biol; 2002 Mar 22; 317(2):249-62. PubMed ID: 11902841
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  • 5. Comprehensive understanding of acetohydroxyacid synthase inhibition by different herbicide families.
    Garcia MD, Nouwens A, Lonhienne TG, Guddat LW.
    Proc Natl Acad Sci U S A; 2017 Feb 14; 114(7):E1091-E1100. PubMed ID: 28137884
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  • 6. Electron transfer in acetohydroxy acid synthase as a side reaction of catalysis. Implications for the reactivity and partitioning of the carbanion/enamine form of (alpha-hydroxyethyl)thiamin diphosphate in a "nonredox" flavoenzyme.
    Tittmann K, Schröder K, Golbik R, McCourt J, Kaplun A, Duggleby RG, Barak Z, Chipman DM, Hübner G.
    Biochemistry; 2004 Jul 13; 43(27):8652-61. PubMed ID: 15236573
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  • 7. Structural insights into the mechanism of inhibition of AHAS by herbicides.
    Lonhienne T, Garcia MD, Pierens G, Mobli M, Nouwens A, Guddat LW.
    Proc Natl Acad Sci U S A; 2018 Feb 27; 115(9):E1945-E1954. PubMed ID: 29440497
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  • 9. Characterization of acetohydroxyacid synthase I from Escherichia coli K-12 and identification of its inhibitors.
    Pham NC, Moon JY, Cho JH, Lee SJ, Park JS, Kim DE, Park Y, Yoon MY.
    Biosci Biotechnol Biochem; 2010 Feb 27; 74(11):2281-6. PubMed ID: 21071847
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  • 11. Structure and mechanism of inhibition of plant acetohydroxyacid synthase.
    Duggleby RG, McCourt JA, Guddat LW.
    Plant Physiol Biochem; 2008 Mar 27; 46(3):309-24. PubMed ID: 18234503
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  • 14. Acetohydroxyacid synthase: a target for antimicrobial drug discovery.
    Pue N, Guddat LW.
    Curr Pharm Des; 2014 Mar 27; 20(5):740-53. PubMed ID: 23688082
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  • 15. The 2.0 Å X-ray structure for yeast acetohydroxyacid synthase provides new insights into its cofactor and quaternary structure requirements.
    Lonhienne T, Garcia MD, Fraser JA, Williams CM, Guddat LW.
    PLoS One; 2017 Mar 27; 12(2):e0171443. PubMed ID: 28178302
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  • 16. Many of the functional differences between acetohydroxyacid synthase (AHAS) isozyme I and other AHASs are a result of the rapid formation and breakdown of the covalent acetolactate-thiamin diphosphate adduct in AHAS I.
    Belenky I, Steinmetz A, Vyazmensky M, Barak Z, Tittmann K, Chipman DM.
    FEBS J; 2012 Jun 27; 279(11):1967-79. PubMed ID: 22443469
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  • 18. Binding and activation of thiamin diphosphate in acetohydroxyacid synthase.
    Bar-Ilan A, Balan V, Tittmann K, Golbik R, Vyazmensky M, Hübner G, Barak Z, Chipman DM.
    Biochemistry; 2001 Oct 02; 40(39):11946-54. PubMed ID: 11570896
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  • 20. Structural and functional evaluation of three well-conserved serine residues in tobacco acetohydroxyacid synthase.
    Yoon MY, Gedi V, Kim J, Park Y, Kim DE, Park EH, Choi JD.
    Biochimie; 2010 Jan 02; 92(1):65-70. PubMed ID: 19825392
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