Structural and functional studies on a mesophilic stationary phase survival protein (Sur E) from Salmonella typhimurium
Author:
Publisher
Wiley
Subject
Cell Biology,Molecular Biology,Biochemistry
Link
http://onlinelibrary.wiley.com/wol1/doi/10.1111/j.1742-4658.2008.06715.x/fullpdf
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4. General enzymatic screens identify three new nucleotidases in Escherichia coli. Biochemical characterization of SurE, YfbR, and YjjG;Proudfoot;J Biol Chem,2004
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1. Molecular dynamics studies on the domain swapped Salmonella typhimurium survival protein SurE: insights on the possible reasons for catalytic cooperativity;Journal of Biomolecular Structure and Dynamics;2017-08-10
2. Conformational variability of the stationary phase survival protein E from Xylella fastidiosa revealed by X-ray crystallography, small-angle X-ray scattering studies, and normal mode analysis;Proteins: Structure, Function, and Bioinformatics;2017-07-24
3. Seeing but not believing: the structure of glycerol dehydrogenase initially assumed to be the structure of a survival protein fromSalmonella typhimurium;Acta Crystallographica Section D Structural Biology;2017-06-28
4. Structural and functional insights into the stationary-phase survival protein SurE, an important virulence factor ofBrucella abortus;Acta Crystallographica Section F Structural Biology Communications;2016-04-22
5. Insights into stabilizing interactions in the distorted domain-swapped dimer ofSalmonella typhimuriumsurvival protein;Acta Crystallographica Section D Biological Crystallography;2015-08-25
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