Importance of the Dimer-Dimer Interface for Allosteric Signal Transduction and AMP Cooperativity of Pig Kidney Fructose-1,6-Bisphosphatase
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference29 articles.
1. Hepatic Gluconeogenesis/Glycolysis: Regulation and Structure/Function Relationships of Substrate Cycle Enzymes
2. Isolation and sequence analysis of the cDNA for pig kidney fructose 1,6-bisphosphatase.
3. Crystal structure of fructose-1,6-bisphosphatase complexed with fructose 6-phosphate, AMP, and magnesium.
4. Crystal structure of the neutral form of fructose-1,6-bisphosphatase complexed with the product fructose 6-phosphate at 2.1-A resolution.
5. Crystal structure of the neutral form of fructose 1,6-bisphosphatase complexed with regulatory inhibitor fructose 2,6-bisphosphate at 2.6-A resolution.
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1. Mechanism of Displacement of a Catalytically Essential Loop from the Active Site of Mammalian Fructose-1,6-bisphosphatase;Biochemistry;2013-07-24
2. Contact rearrangements form coupled networks from local motions in allosteric proteins;Proteins: Structure, Function, and Bioinformatics;2008-04
3. Structures of Activated Fructose-1,6-bisphosphatase from Escherichia coli;Journal of Biological Chemistry;2007-04
4. R-State AMP Complex Reveals Initial Steps of the Quaternary Transition of Fructose-1,6-bisphosphatase;Journal of Biological Chemistry;2005-05
5. Inhibition of Fructose-1,6-bisphosphatase by a New Class of Allosteric Effectors;Journal of Biological Chemistry;2003-12
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