Selective modification of fructose 1,6-bisphosphatase by periodate-oxidized AMP
Author:
Publisher
Wiley
Subject
Cell Biology,Genetics,Molecular Biology,Biochemistry,Structural Biology,Biophysics
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1016/0014-5793(79)80921-7/fullpdf
Reference13 articles.
1. Fructose 1,6-diphosphatase from rabbit liver XI. Relation between the adenosine 5′-monophosphate binding and the allosteric inhibition
2. Univalent cation activation of fructose 1,6-diphosphatase
Cited by 7 articles. 订阅此论文施引文献 订阅此论文施引文献，注册后可以免费订阅5篇论文的施引文献，订阅后可以查看论文全部施引文献
1. Affinity Labeling of the Allosteric Site of Fructose 1,6-Bisphosphatase with an AMP Analog;The Journal of Biochemistry;1987-08
2. Fructose 1,6-bisphosphatase: Dissociation of AMP cooperativity and AMP inhibition by carbamylation;Journal of Protein Chemistry;1983-12
3. Interactions between the mitochondrial adenosinetriphosphatase and periodate-oxidized adenosine 5'-triphosphate, an affinity label for adenosine 5'-triphosphate binding sites;Biochemistry;1982-08-17
4. Affinity labeling of rabbit muscle pyruvate kinase with dialdehyde-ADP;Biochimica et Biophysica Acta (BBA) - Protein Structure and Molecular Enzymology;1982-06
5. FRUCTOSE 1,6-BISPHOSPHATASE: A MODEL FOR STUDIES ON STRUCTURE-FUNCTION RELATIONSHIPS IN A REGULATORY ENZYME;Molecular Approaches to Gene Expression and Protein Structure;1981
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