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488 related items for PubMed ID: 18650089

  • 1. Allosteric FBPase inhibitors gain 10(5) times in potency when simultaneously binding two neighboring AMP sites.
    Hebeisen P, Kuhn B, Kohler P, Gubler M, Huber W, Kitas E, Schott B, Benz J, Joseph C, Ruf A.
    Bioorg Med Chem Lett; 2008 Aug 15; 18(16):4708-12. PubMed ID: 18650089
    [Abstract] [Full Text] [Related]

  • 2. [Recent advance in the discovery of allosteric inhibitors binding to the AMP site of fructose-1,6-bisphosphatase].
    Li ZM, Bie JB, Song HR, Xu BL.
    Yao Xue Xue Bao; 2011 Nov 15; 46(11):1291-300. PubMed ID: 22260018
    [Abstract] [Full Text] [Related]

  • 3. Structure-guided design of AMP mimics that inhibit fructose-1,6-bisphosphatase with high affinity and specificity.
    Erion MD, Dang Q, Reddy MR, Kasibhatla SR, Huang J, Lipscomb WN, van Poelje PD.
    J Am Chem Soc; 2007 Dec 19; 129(50):15480-90. PubMed ID: 18041833
    [Abstract] [Full Text] [Related]

  • 4. Structure of inhibited fructose-1,6-bisphosphatase from Escherichia coli: distinct allosteric inhibition sites for AMP and glucose 6-phosphate and the characterization of a gluconeogenic switch.
    Hines JK, Kruesel CE, Fromm HJ, Honzatko RB.
    J Biol Chem; 2007 Aug 24; 282(34):24697-706. PubMed ID: 17567577
    [Abstract] [Full Text] [Related]

  • 5. Characterization of the allosteric binding pocket of human liver fructose-1,6-bisphosphatase by protein crystallography and inhibitor activity studies.
    Iversen LF, Brzozowski M, Hastrup S, Hubbard R, Kastrup JS, Larsen IK, Naerum L, Nørskov-Lauridsen L, Rasmussen PB, Thim L, Wiberg FC, Lundgren K.
    Protein Sci; 1997 May 24; 6(5):971-82. PubMed ID: 9144768
    [Abstract] [Full Text] [Related]

  • 6. Fructose-1,6-bisphosphatase inhibitors. 1. Purine phosphonic acids as novel AMP mimics.
    Dang Q, Brown BS, Liu Y, Rydzewski RM, Robinson ED, van Poelje PD, Reddy MR, Erion MD.
    J Med Chem; 2009 May 14; 52(9):2880-98. PubMed ID: 19348494
    [Abstract] [Full Text] [Related]

  • 7. Discovery of potent and specific fructose-1,6-bisphosphatase inhibitors and a series of orally-bioavailable phosphoramidase-sensitive prodrugs for the treatment of type 2 diabetes.
    Dang Q, Kasibhatla SR, Reddy KR, Jiang T, Reddy MR, Potter SC, Fujitaki JM, van Poelje PD, Huang J, Lipscomb WN, Erion MD.
    J Am Chem Soc; 2007 Dec 19; 129(50):15491-502. PubMed ID: 18041834
    [Abstract] [Full Text] [Related]

  • 8. Fructose-1,6-bisphosphatase Inhibitors. 2. Design, synthesis, and structure-activity relationship of a series of phosphonic acid containing benzimidazoles that function as 5'-adenosinemonophosphate (AMP) mimics.
    Dang Q, Kasibhatla SR, Xiao W, Liu Y, Dare J, Taplin F, Reddy KR, Scarlato GR, Gibson T, van Poelje PD, Potter SC, Erion MD.
    J Med Chem; 2010 Jan 14; 53(1):441-51. PubMed ID: 20055427
    [Abstract] [Full Text] [Related]

  • 9. Calculation of relative binding affinities of fructose 1,6-bisphosphatase mutants with adenosine monophosphate using free energy perturbation method.
    Mutyala R, Reddy RN, Sumakanth M, Reddanna P, Reddy MR.
    J Comput Chem; 2007 Apr 15; 28(5):932-7. PubMed ID: 17253638
    [Abstract] [Full Text] [Related]

  • 10. Crystal structures of the active site mutant (Arg-243-->Ala) in the T and R allosteric states of pig kidney fructose-1,6-bisphosphatase expressed in Escherichia coli.
    Stec B, Abraham R, Giroux E, Kantrowitz ER.
    Protein Sci; 1996 Aug 15; 5(8):1541-53. PubMed ID: 8844845
    [Abstract] [Full Text] [Related]

  • 11. Different sensitivities of mutants and chimeric forms of human muscle and liver fructose-1,6-bisphosphatases towards AMP.
    Rakus D, Tillmann H, Wysocki R, Ulaszewski S, Eschrich K, Dzugaj A.
    Biol Chem; 2003 Jan 15; 384(1):51-8. PubMed ID: 12674499
    [Abstract] [Full Text] [Related]

  • 12. The regulation of the interaction between F-actin and muscle fructose 1,6-bisphosphatase.
    Rakus D, Gizak A, Dzugaj A.
    Int J Biol Macromol; 2005 Mar 15; 35(1-2):33-8. PubMed ID: 15769513
    [Abstract] [Full Text] [Related]

  • 13. Orally active aminopyridines as inhibitors of tetrameric fructose-1,6-bisphosphatase.
    Hebeisen P, Haap W, Kuhn B, Mohr P, Wessel HP, Zutter U, Kirchner S, Ruf A, Benz J, Joseph C, Alvarez-Sánchez R, Gubler M, Schott B, Benardeau A, Tozzo E, Kitas E.
    Bioorg Med Chem Lett; 2011 Jun 01; 21(11):3237-42. PubMed ID: 21550236
    [Abstract] [Full Text] [Related]

  • 14. New insight into the binding modes of TNP-AMP to human liver fructose-1,6-bisphosphatase.
    Han X, Huang Y, Zhang R, Xiao S, Zhu S, Qin N, Hong Z, Wei L, Feng J, Ren Y, Feng L, Wan J.
    Spectrochim Acta A Mol Biomol Spectrosc; 2016 Aug 05; 165():155-160. PubMed ID: 27137358
    [Abstract] [Full Text] [Related]

  • 15. The origin of the high sensitivity of muscle fructose 1,6-bisphosphatase towards AMP.
    Rakus D, Maciaszczyk E, Wawrzycka D, Ułaszewski S, Eschrich K, Dzugaj A.
    FEBS Lett; 2005 Oct 24; 579(25):5577-81. PubMed ID: 16213487
    [Abstract] [Full Text] [Related]

  • 16. Structures of mammalian and bacterial fructose-1,6-bisphosphatase reveal the basis for synergism in AMP/fructose 2,6-bisphosphate inhibition.
    Hines JK, Chen X, Nix JC, Fromm HJ, Honzatko RB.
    J Biol Chem; 2007 Dec 07; 282(49):36121-31. PubMed ID: 17933867
    [Abstract] [Full Text] [Related]

  • 17. In silico screening of a novel scaffold for fructose-1,6-bisphosatase (FBPase) inhibitors.
    Huang Y, Chi B, Xu Y, Song R, Wei L, Rao L, Feng L, Ren Y, Wan J.
    J Mol Graph Model; 2019 Jan 07; 86():142-148. PubMed ID: 30366190
    [Abstract] [Full Text] [Related]

  • 18. Interaction between muscle aldolase and muscle fructose 1,6-bisphosphatase results in the substrate channeling.
    Rakus D, Pasek M, Krotkiewski H, Dzugaj A.
    Biochemistry; 2004 Nov 30; 43(47):14948-57. PubMed ID: 15554702
    [Abstract] [Full Text] [Related]

  • 19. AMP inhibition of pig kidney fructose-1,6-bisphosphatase.
    Kelley-Loughnane N, Kantrowitz ER.
    Biochim Biophys Acta; 2001 Jul 09; 1548(1):66-71. PubMed ID: 11451439
    [Abstract] [Full Text] [Related]

  • 20. Evidence for an active T-state pig kidney fructose 1,6-bisphosphatase: interface residue Lys-42 is important for allosteric inhibition and AMP cooperativity.
    Lu G, Stec B, Giroux EL, Kantrowitz ER.
    Protein Sci; 1996 Nov 09; 5(11):2333-42. PubMed ID: 8931152
    [Abstract] [Full Text] [Related]

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