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Items: 1 to 20 of 109

1.

Rational engineering of enzyme allosteric regulation through sequence evolution analysis.

Yang JS, Seo SW, Jang S, Jung GY, Kim S.

PLoS Comput Biol. 2012;8(7):e1002612. doi: 10.1371/journal.pcbi.1002612. Epub 2012 Jul 12.

2.

Novel allosteric activation site in Escherichia coli fructose-1,6-bisphosphatase.

Hines JK, Fromm HJ, Honzatko RB.

J Biol Chem. 2006 Jul 7;281(27):18386-93. Epub 2006 May 2.

4.

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.

PMID:
7577911
5.

Purification, kinetic studies, and homology model of Escherichia coli fructose-1,6-bisphosphatase.

Kelley-Loughnane N, Biolsi SA, Gibson KM, Lu G, Hehir MJ, Phelan P, Kantrowitz ER.

Biochim Biophys Acta. 2002 Jan 31;1594(1):6-16.

PMID:
11825604
6.

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. doi: 10.1111/febs.12657. Epub 2013 Dec 23.

7.

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.

PMID:
17253638
8.

Structural and biochemical characterization of the type II fructose-1,6-bisphosphatase GlpX from Escherichia coli.

Brown G, Singer A, Lunin VV, Proudfoot M, Skarina T, Flick R, Kochinyan S, Sanishvili R, Joachimiak A, Edwards AM, Savchenko A, Yakunin AF.

J Biol Chem. 2009 Feb 6;284(6):3784-92. doi: 10.1074/jbc.M808186200. Epub 2008 Dec 10.

9.

AMP inhibition of pig kidney fructose-1,6-bisphosphatase.

Kelley-Loughnane N, Kantrowitz ER.

Biochim Biophys Acta. 2001 Jul 9;1548(1):66-71.

PMID:
11451439
10.
11.

[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;46(11):1291-300. Review. Chinese.

PMID:
22260018
12.

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. Epub 2003 Oct 6.

13.
14.

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. Epub 2007 Nov 28.

PMID:
18041833
17.

Structure of E69Q mutant of human muscle fructose-1,6-bisphosphatase.

Zarzycki M, Kołodziejczyk R, Maciaszczyk-Dziubinska E, Wysocki R, Jaskolski M, Dzugaj A.

Acta Crystallogr D Biol Crystallogr. 2011 Dec;67(Pt 12):1028-34. doi: 10.1107/S090744491104385X. Epub 2011 Nov 18.

PMID:
22120740
18.

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. doi: 10.1016/j.bmcl.2008.06.103. Epub 2008 Jul 5.

PMID:
18650089

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