1. This article is from 1978. It is a rather old article but it looks at the regulation of gluconeogenesis by fructose 1,6-bisphosphatase and other enzymes in the kidney. This paper basically talks about the process of glucose regulation. They looked at the affects of phosphorylation on several of enzymes and determined that phosphorylation did not affect the activity of fructose 1,6-bisphosphatase. They found that it had no allosteric effects of phosphorylation on this enzyme. It is interesting to see how they discovered the affects of phosphorylation on enzymes back in the late 70's and how the basic principles still are in practice today.

Joseph Mendicino,* Fredrich Leibach, and Sesha Reddy, 1978 "Role of Enzyme Interactions in the Regulation of Gluconeogenesis: Phosphorylation of Fructose 1,6-Bisphosphataseand Phosphofructokinase by Kidney Protein Kinase?"

http://pubs.acs.org.lib-proxy.calvin.edu/doi/pdf/10.1021/bi00615a012

2. The inhibition of Fructose 1,6-bisphosphatase is maybe a form of controlling diabetes. Fructose 1,6-bisphosphatase is one of the enzymes used in the synthesis of glucose. They looked at three possible inhibitor points: 1. the active site for 1,6-bisphosphatase, 2. An allosteric binding site for AMP, and 3. A tetrameric binding site at the dimer interface. The leading compounds for inhibiting fructose 1,6-bisphosphates is organofluorines. Through this  research they found three inhibitors. It is a really interesting that  an inhibitor of this protein can help treat diseases like diabetes. 

Aleksandra Rudnitskaya, Ken Huynh, Be ́la To ̈ro ̈k,* and Kimberly Stieglitz*

Novel Heteroaromatic Organofluorine Inhibitors of Fructose-1,6-bisphosphatase

http://pubs.acs.org.lib-proxy.calvin.edu/doi/pdf/10.1021/jm800720a

3. Fructose 1,6-bisphosphatase has multiple subunits that allows it to change from R state to T state. This paper looks at the conformational change of the protein. The dimers shift 17 degrees from each other. This change the Arg-22 residue to go from interacting with Glu-108 and Arg-110 to Thr-27 and Glu-29. To see if the arginine was important part of the protein functionality, they converted it to an alanine. They looked at the differences in the catalytic ability of R-state vs. T state. Through their research they found that the Arg22 to Ala has no effect on the enzyme and the R-state enhances catalytic potential. This research shows that the arginine is only part of the catalytic properties of the enzyme. 

Guqiang Lu, Mark K. Williams, Eugene L. Giroux, and Evan R. Kantrowitz"

Fructose-1,6-bisphosphatase: Arginine-22 Is Involved in Stabilization of the T Allosteric State?

http://pubs.acs.org.lib-proxy.calvin.edu/doi/pdf/10.1021/bi00041a002