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Biochemistry|December 22, 1981
Modification of the allosteric activator site of Escherichia coli ADP-glucose synthetase by trinitrobenzenesulfonateC A Carlson, J PreissPlant Physiology|December 1, 1983
ATP-Dependent Proteolytic Activity from Spinach LeavesJ B Hammond, J PreissPlant Physiology|August 1, 1985
Partial purification and characterization of granule-bound starch synthases from normal and waxy maizeF D Macdonald, J PreissPlant Physiology|December 1, 1979
Properties of Citrate-stimulated Starch Synthesis Catalyzed by Starch Synthase I of Developing Maize KernelsC D Boyer, J PreissPlant Physiology|January 1, 1987
Purification and Properties of Nonproteolytic Degraded ADPglucose Pyrophosphorylase from Maize EndospermW C Plaxton, J PreissPlant Physiology|September 1, 1983
Solubilization of the starch-granule-bound starch synthase of normal maize kernelsF D Macdonald, J PreissBiochemistry|April 13, 1982
Involvement of arginine residues in the allosteric activation of Escherichia coli ADP-glucose synthetaseC A Carlson, J PreissJournal of Bacteriology|September 1, 1987
Biosynthesis of bacterial glycogen: primary structure of Salmonella typhimurium ADPglucose synthetase as deduced from the nucleotide sequence of the glgC geneP S Leung, J PreissBiochemical and Biophysical Research Communications|March 26, 1998
Functional analysis of conserved histidines in ADP-glucose pyrophosphorylase from Escherichia coliM A Hill, J PreissArchives of Biochemistry and Biophysics|September 29, 1998
The N-terminal region is important for the allosteric activation and inhibition of the Escherichia coli ADP-glucose pyrophosphorylaseM X Wu, J PreissPageof 30