167 related articles for article (PubMed ID: 28882541)
1. Structures of Leishmania Fructose-1,6-Bisphosphatase Reveal Species-Specific Differences in the Mechanism of Allosteric Inhibition.
Yuan M; Vásquez-Valdivieso MG; McNae IW; Michels PAM; Fothergill-Gilmore LA; Walkinshaw MD
J Mol Biol; 2017 Oct; 429(20):3075-3089. PubMed ID: 28882541
[TBL] [Abstract][Full Text] [Related]
2. 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; 278(51):51176-83. PubMed ID: 14530289
[TBL] [Abstract][Full Text] [Related]
3. T-to-R switch of muscle fructose-1,6-bisphosphatase involves fundamental changes of secondary and quaternary structure.
Barciszewski J; Wisniewski J; Kolodziejczyk R; Jaskolski M; Rakus D; Dzugaj A
Acta Crystallogr D Struct Biol; 2016 Apr; 72(Pt 4):536-50. PubMed ID: 27050133
[TBL] [Abstract][Full Text] [Related]
4. Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase.
Hines JK; Fromm HJ; Honzatko RB
J Biol Chem; 2006 Jul; 281(27):18386-93. PubMed ID: 16670087
[TBL] [Abstract][Full Text] [Related]
5. 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; 282(34):24697-706. PubMed ID: 17567577
[TBL] [Abstract][Full Text] [Related]
6. R-state AMP complex reveals initial steps of the quaternary transition of fructose-1,6-bisphosphatase.
Iancu CV; Mukund S; Fromm HJ; Honzatko RB
J Biol Chem; 2005 May; 280(20):19737-45. PubMed ID: 15767255
[TBL] [Abstract][Full Text] [Related]
7. The allosteric site of human liver fructose-1,6-bisphosphatase. Analysis of six AMP site mutants based on the crystal structure.
Gidh-Jain M; Zhang Y; van Poelje PD; Liang JY; Huang S; Kim J; Elliott JT; Erion MD; Pilkis SJ; Raafat el-Maghrabi M
J Biol Chem; 1994 Nov; 269(44):27732-8. PubMed ID: 7961695
[TBL] [Abstract][Full Text] [Related]
8. 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; 244(5):609-24. PubMed ID: 7990142
[TBL] [Abstract][Full Text] [Related]
9. 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; 5(11):2333-42. PubMed ID: 8931152
[TBL] [Abstract][Full Text] [Related]
10. Structural aspects of the allosteric inhibition of fructose-1,6-bisphosphatase by AMP: the binding of both the substrate analogue 2,5-anhydro-D-glucitol 1,6-bisphosphate and catalytic metal ions monitored by X-ray crystallography.
Villeret V; Huang S; Zhang Y; Lipscomb WN
Biochemistry; 1995 Apr; 34(13):4307-15. PubMed ID: 7703244
[TBL] [Abstract][Full Text] [Related]
11. Structural and biochemical characterization of fructose-1,6/sedoheptulose-1,7-bisphosphatase from the cyanobacterium Synechocystis strain 6803.
Feng L; Sun Y; Deng H; Li D; Wan J; Wang X; Wang W; Liao X; Ren Y; Hu X
FEBS J; 2014 Feb; 281(3):916-26. PubMed ID: 24286336
[TBL] [Abstract][Full Text] [Related]
12. Crystal structures of human muscle fructose-1,6-bisphosphatase: novel quaternary states, enhanced AMP affinity, and allosteric signal transmission pathway.
Shi R; Chen ZY; Zhu DW; Li C; Shan Y; Xu G; Lin SX
PLoS One; 2013; 8(9):e71242. PubMed ID: 24086250
[TBL] [Abstract][Full Text] [Related]
13. Structures of the Mycobacterium tuberculosis GlpX protein (class II fructose-1,6-bisphosphatase): implications for the active oligomeric state, catalytic mechanism and citrate inhibition.
Wolf NM; Gutka HJ; Movahedzadeh F; Abad-Zapatero C
Acta Crystallogr D Struct Biol; 2018 Apr; 74(Pt 4):321-331. PubMed ID: 29652259
[TBL] [Abstract][Full Text] [Related]
14. 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; 5(8):1541-53. PubMed ID: 8844845
[TBL] [Abstract][Full Text] [Related]
15. 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; 6(5):971-82. PubMed ID: 9144768
[TBL] [Abstract][Full Text] [Related]
16. Crystal structures of fructose 1,6-bisphosphatase: mechanism of catalysis and allosteric inhibition revealed in product complexes.
Choe JY; Fromm HJ; Honzatko RB
Biochemistry; 2000 Jul; 39(29):8565-74. PubMed ID: 10913263
[TBL] [Abstract][Full Text] [Related]
17. Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 2,6-bisphosphate, AMP, and Zn2+ at 2.0-A resolution: aspects of synergism between inhibitors.
Xue Y; Huang S; Liang JY; Zhang Y; Lipscomb WN
Proc Natl Acad Sci U S A; 1994 Dec; 91(26):12482-6. PubMed ID: 7809062
[TBL] [Abstract][Full Text] [Related]
18. 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; 34(41):13272-7. PubMed ID: 7577911
[TBL] [Abstract][Full Text] [Related]
19. 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; 282(49):36121-31. PubMed ID: 17933867
[TBL] [Abstract][Full Text] [Related]
20. Crystal structure of spinach chloroplast fructose-1,6-bisphosphatase at 2.8 A resolution.
Villeret V; Huang S; Zhang Y; Xue Y; Lipscomb WN
Biochemistry; 1995 Apr; 34(13):4299-306. PubMed ID: 7703243
[TBL] [Abstract][Full Text] [Related]
[Next] [New Search]