Subunit association of enzyme I of the Salmonella typhimurium phosphoenolpyruvate: glycose phosphotransferase system. Temperature dependence and thermodynamic properties.
Author:
Publisher
Elsevier BV
Subject
Cell Biology,Molecular Biology,Biochemistry
Reference12 articles.
1. The bacterial phosphoenolpyruvate: Sugar phosphotransferase system
2. Sugar transport by the bacterial phosphotransferase system. Phosphoryl transfer reactions catalyzed by enzyme I of Salmonella typhimurium.
3. beta-Adrenergic receptor regulation of N-linked protein glycosylation in rat parotid acinar cells.
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1. Stability and binding of the phosphorylated species of the N-terminal domain of enzyme I and the histidine phosphocarrier protein from the Streptomyces coelicolor phosphoenolpyruvate:sugar phosphotransferase system;Archives of Biochemistry and Biophysics;2012-10
2. Calorimetric and spectroscopic investigation of the interaction between the C-terminal domain of Enzyme I and its ligands;Protein Science;2012-09-25
3. The N-terminal domain of the enzyme I is a monomeric well-folded protein with a low conformational stability and residual structure in the unfolded state;Protein Engineering Design and Selection;2010-07-14
4. Defining the Epitope Region of a Peptide from the Streptomyces coelicolor Phosphoenolpyruvate:Sugar Phosphotransferase System Able to Bind to the Enzyme I;Biophysical Journal;2008-08
5. Structure of phosphorylated enzyme I, the phosphoenolpyruvate:sugar phosphotransferase system sugar translocation signal protein;Proceedings of the National Academy of Sciences;2006-10-19
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