Published in Protein Sci on July 06, 2004
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Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase. J Biol Chem (2014) 0.86
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Crystal structure of the Kelch domain of human Keap1. J Biol Chem (2004) 2.04
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Crystal structure of PMM/PGM: an enzyme in the biosynthetic pathway of P. aeruginosa virulence factors. Structure (2002) 1.49
Structural basis of diverse substrate recognition by the enzyme PMM/PGM from P. aeruginosa. Structure (2004) 1.32
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Backbone flexibility, conformational change, and catalysis in a phosphohexomutase from Pseudomonas aeruginosa. Biochemistry (2008) 0.94
Optimization of fluorescently labeled Nrf2 peptide probes and the development of a fluorescence polarization assay for the discovery of inhibitors of Keap1-Nrf2 interaction. J Biomol Screen (2011) 0.91
Kinetic analyses of Keap1-Nrf2 interaction and determination of the minimal Nrf2 peptide sequence required for Keap1 binding using surface plasmon resonance. Chem Biol Drug Des (2011) 0.91
Complexes of the enzyme phosphomannomutase/phosphoglucomutase with a slow substrate and an inhibitor. Acta Crystallogr Sect F Struct Biol Cryst Commun (2006) 0.90
Domain motion and interdomain hot spots in a multidomain enzyme. Protein Sci (2010) 0.89
Solution NMR of a 463-residue phosphohexomutase: domain 4 mobility, substates, and phosphoryl transfer defect. Biochemistry (2012) 0.89
A coevolutionary residue network at the site of a functionally important conformational change in a phosphohexomutase enzyme family. PLoS One (2012) 0.88
Promotion of enzyme flexibility by dephosphorylation and coupling to the catalytic mechanism of a phosphohexomutase. J Biol Chem (2014) 0.86
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Crystal structure of Bacillus anthracis phosphoglucosamine mutase, an enzyme in the peptidoglycan biosynthetic pathway. J Bacteriol (2011) 0.83
Breaking the covalent connection: Chain connectivity and the catalytic reaction of PMM/PGM. Protein Sci (2010) 0.83
Identification of an essential active-site residue in the α-D-phosphohexomutase enzyme superfamily. FEBS J (2013) 0.82
Crystal structure of a bacterial phosphoglucomutase, an enzyme involved in the virulence of multiple human pathogens. Proteins (2011) 0.81
Quaternary structure, conformational variability and global motions of phosphoglucosamine mutase. FEBS J (2011) 0.80
Crystallization and initial crystallographic analysis of the Kelch domain from human Keap1. Acta Crystallogr D Biol Crystallogr (2004) 0.80
Conservation of functionally important global motions in an enzyme superfamily across varying quaternary structures. J Mol Biol (2012) 0.80
Crystallization and initial crystallographic analysis of phosphoglucosamine mutase from Bacillus anthracis. Acta Crystallogr Sect F Struct Biol Cryst Commun (2009) 0.77
Chemical shift assignments of domain 4 from the phosphohexomutase from Pseudomonas aeruginosa suggest that freeing perturbs its coevolved domain interface. Biomol NMR Assign (2013) 0.77