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217 related items for PubMed ID: 17253638

  • 1. 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]

  • 2. 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
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  • 4. Calculation of relative binding free energy differences for fructose 1,6-bisphosphatase inhibitors using the thermodynamic cycle perturbation approach.
    Reddy MR, Erion MD.
    J Am Chem Soc; 2001 Jul 04; 123(26):6246-52. PubMed ID: 11427047
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  • 5. Relative binding affinities of fructose-1,6-bisphosphatase inhibitors calculated using a quantum mechanics-based free energy perturbation method.
    Reddy MR, Erion MD.
    J Am Chem Soc; 2007 Aug 01; 129(30):9296-7. PubMed ID: 17616196
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  • 7. 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
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  • 8. Absolute and relative binding free energy calculations of the interaction of biotin and its analogs with streptavidin using molecular dynamics/free energy perturbation approaches.
    Miyamoto S, Kollman PA.
    Proteins; 1993 Jul 15; 16(3):226-45. PubMed ID: 8346190
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  • 11. Free energy simulations and MM-PBSA analyses on the affinity and specificity of steroid binding to antiestradiol antibody.
    Laitinen T, Kankare JA, Peräkylä M.
    Proteins; 2004 Apr 01; 55(1):34-43. PubMed ID: 14997538
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  • 13. Calculation of the relative binding free energy of 2'GMP and 2'AMP to ribonuclease T1 using molecular dynamics/free energy perturbation approaches.
    Hirono S, Kollman PA.
    J Mol Biol; 1990 Mar 05; 212(1):197-209. PubMed ID: 2157020
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  • 14. Minimum MD simulation length required to achieve reliable results in free energy perturbation calculations: case study of relative binding free energies of fructose-1,6-bisphosphatase inhibitors.
    Rathore RS, Aparoy P, Reddanna P, Kondapi AK, Reddy MR.
    J Comput Chem; 2011 Jul 30; 32(10):2097-103. PubMed ID: 21503928
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  • 15. 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 30; 5(11):2333-42. PubMed ID: 8931152
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  • 16. 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
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  • 17. 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
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  • 18. 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 24; 384(1):51-8. PubMed ID: 12674499
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  • 19. Performance Evaluation of Docking Programs- Glide, GOLD, AutoDock & SurflexDock, Using Free Energy Perturbation Reference Data: A Case Study of Fructose-1, 6-bisphosphatase-AMP Analogs.
    Reddy KK, Rathore RS, Srujana P, Burri RR, Reddy CR, Sumakanth M, Reddanna P, Reddy MR.
    Mini Rev Med Chem; 2020 Jan 24; 20(12):1179-1187. PubMed ID: 32459606
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  • 20. Toward a mechanism for the allosteric transition of pig kidney fructose-1,6-bisphosphatase.
    Zhang Y, Liang JY, Huang S, Lipscomb WN.
    J Mol Biol; 1994 Dec 16; 244(5):609-24. PubMed ID: 7990142
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