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175 related items for PubMed ID: 10759847

  • 1. The C1-C2 interface residue lysine 50 of pig kidney fructose-1, 6-bisphosphatase has a crucial role in the cooperative signal transmission of the AMP inhibition.
    Cárcamo JG, Yañez AJ, Ludwig HC, León O, Pinto RO, Reyes AM, Slebe JC.
    Eur J Biochem; 2000 Apr; 267(8):2242-51. PubMed ID: 10759847
    [Abstract] [Full Text] [Related]

  • 2. A study of subunit interface residues of fructose-1,6-bisphosphatase by site-directed mutagenesis: effects on AMP and Mg2+ affinities.
    Shyur LF, Aleshin AE, Fromm HJ.
    Biochemistry; 1996 Jun 11; 35(23):7492-8. PubMed ID: 8652527
    [Abstract] [Full Text] [Related]

  • 3. Major changes in the kinetic mechanism of AMP inhibition and AMP cooperativity attend the mutation of Arg49 in fructose-1,6-bisphosphatase.
    Shyur LF, Poland BW, Honzatko RB, Fromm HJ.
    J Biol Chem; 1997 Oct 17; 272(42):26295-9. PubMed ID: 9334199
    [Abstract] [Full Text] [Related]

  • 4. Importance of the dimer-dimer interface for allosteric signal transduction and AMP cooperativity of pig kidney fructose-1,6-bisphosphatase. Site-specific mutagenesis studies of Glu-192 and Asp-187 residues on the 190's loop.
    Lu G, Giroux EL, Kantrowitz ER.
    J Biol Chem; 1997 Feb 21; 272(8):5076-81. PubMed ID: 9030572
    [Abstract] [Full Text] [Related]

  • 5. Mutation of arginine 276 to methionine changes Mg2+ cooperativity and the kinetic mechanism of fructose-1,6-bisphosphatase.
    Zhang R, Fromm HJ.
    Biochemistry; 1995 Jun 27; 34(25):8190-5. PubMed ID: 7794933
    [Abstract] [Full Text] [Related]

  • 6. Directed mutations in the poorly defined region of porcine liver fructose-1,6-bisphosphatase significantly affect catalysis and the mechanism of AMP inhibition.
    Kurbanov FT, Choe JY, Honzatko RB, Fromm HJ.
    J Biol Chem; 1998 Jul 10; 273(28):17511-6. PubMed ID: 9651342
    [Abstract] [Full Text] [Related]

  • 7. 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 10; 5(8):1541-53. PubMed ID: 8844845
    [Abstract] [Full Text] [Related]

  • 8. Suppression of kinetic AMP cooperativity of fructose-1,6-bisphosphatase by carbamoylation of lysine 50.
    Ludwig HC, Herrera R, Reyes AM, Hubert E, Slebe JC.
    J Protein Chem; 1999 Jul 10; 18(5):533-45. PubMed ID: 10524771
    [Abstract] [Full Text] [Related]

  • 9. Site-directed mutagenesis of the substrate binding site of porcine fructose-1,6-bisphosphatase.
    Shyur LF, Zhang R, Fromm HJ.
    Arch Biochem Biophys; 1995 May 10; 319(1):123-7. PubMed ID: 7771775
    [Abstract] [Full Text] [Related]

  • 10. 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 10; 5(11):2333-42. PubMed ID: 8931152
    [Abstract] [Full Text] [Related]

  • 11. Site-directed mutagenesis of residues at subunit interfaces of porcine fructose-1,6-bisphosphatase.
    Shyur LF, Aleshin AE, Honzatko RB, Fromm HJ.
    J Biol Chem; 1996 Feb 09; 271(6):3005-10. PubMed ID: 8621693
    [Abstract] [Full Text] [Related]

  • 12. Shared active sites of fructose-1,6-bisphosphatase. Arginine 243 mediates substrate binding and fructose 2,6-bisphosphate inhibition.
    Giroux E, Williams MK, Kantrowitz ER.
    J Biol Chem; 1994 Dec 16; 269(50):31404-9. PubMed ID: 7989306
    [Abstract] [Full Text] [Related]

  • 13. 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]

  • 14. Fructose-1,6-bisphosphatase: arginine-22 is involved in stabilization of the T allosteric state.
    Lu G, Williams MK, Giroux EL, Kantrowitz ER.
    Biochemistry; 1995 Oct 17; 34(41):13272-7. PubMed ID: 7577911
    [Abstract] [Full Text] [Related]

  • 15. The allosteric properties of rat liver fructose-1,6-bisphosphatase.
    Meek DW, Nimmo HG.
    Biochem J; 1984 Aug 15; 222(1):131-8. PubMed ID: 6089752
    [Abstract] [Full Text] [Related]

  • 16. Inhibition of fructose-1,6-bisphosphatase by a new class of allosteric effectors.
    Choe JY, Nelson SW, Arienti KL, Axe FU, Collins TL, Jones TK, Kimmich RD, Newman MJ, Norvell K, Ripka WC, Romano SJ, Short KM, Slee DH, Fromm HJ, Honzatko RB.
    J Biol Chem; 2003 Dec 19; 278(51):51176-83. PubMed ID: 14530289
    [Abstract] [Full Text] [Related]

  • 17. Replacement of glutamic acid 29 with glutamine leads to a loss of cooperativity for AMP with porcine fructose-1,6-bisphosphatase.
    Chen M, Chen L, Fromm HJ.
    J Biol Chem; 1994 Feb 25; 269(8):5554-8. PubMed ID: 7907084
    [Abstract] [Full Text] [Related]

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  • 20. 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 25; 384(1):51-8. PubMed ID: 12674499
    [Abstract] [Full Text] [Related]

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