Published in J Bacteriol on February 01, 2006
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Proline modulates the intracellular redox environment and protects mammalian cells against oxidative stress. Free Radic Biol Med (2007) 1.54
Structure and kinetics of monofunctional proline dehydrogenase from Thermus thermophilus. J Biol Chem (2007) 1.44
Structures of the Escherichia coli PutA proline dehydrogenase domain in complex with competitive inhibitors. Biochemistry (2004) 1.41
Flavin redox state triggers conformational changes in the PutA protein from Escherichia coli. Biochemistry (2003) 1.28
Identification and characterization of the DNA-binding domain of the multifunctional PutA flavoenzyme. J Biol Chem (2004) 1.25
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Crystal structures of the DNA-binding domain of Escherichia coli proline utilization A flavoprotein and analysis of the role of Lys9 in DNA recognition. Protein Sci (2006) 1.08
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Direct linking of metabolism and gene expression in the proline utilization A protein from Escherichia coli. Amino Acids (2008) 0.98
Characterization of a Helicobacter hepaticus putA mutant strain in host colonization and oxidative stress. Infect Immun (2008) 0.98
The three-dimensional structural basis of type II hyperprolinemia. J Mol Biol (2012) 0.96
Rapid reaction kinetics of proline dehydrogenase in the multifunctional proline utilization A protein. Biochemistry (2011) 0.95
Exploring the proline-dependent conformational change in the multifunctional PutA flavoprotein by tryptophan fluorescence spectroscopy. Biochemistry (2005) 0.95
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Substrate channeling in proline metabolism. Front Biosci (Landmark Ed) (2012) 0.94
Structures of the PutA peripheral membrane flavoenzyme reveal a dynamic substrate-channeling tunnel and the quinone-binding site. Proc Natl Acad Sci U S A (2014) 0.92
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Pseudomonas syringae Catalases Are Collectively Required for Plant Pathogenesis. J Bacteriol (2012) 0.88
Crystal structures and kinetics of monofunctional proline dehydrogenase provide insight into substrate recognition and conformational changes associated with flavin reduction and product release. Biochemistry (2012) 0.87
Structural studies of yeast Δ(1)-pyrroline-5-carboxylate dehydrogenase (ALDH4A1): active site flexibility and oligomeric state. Biochemistry (2014) 0.85
Solution structure of the Pseudomonas putida protein PpPutA45 and its DNA complex. Proteins (2009) 0.84
Evidence for hysteretic substrate channeling in the proline dehydrogenase and Δ1-pyrroline-5-carboxylate dehydrogenase coupled reaction of proline utilization A (PutA). J Biol Chem (2013) 0.84
Involvement of the β3-α3 loop of the proline dehydrogenase domain in allosteric regulation of membrane association of proline utilization A. Biochemistry (2013) 0.83
Small-angle X-ray scattering studies of the oligomeric state and quaternary structure of the trifunctional proline utilization A (PutA) flavoprotein from Escherichia coli. J Biol Chem (2011) 0.82
Kinetic and thermodynamic analysis of Bradyrhizobium japonicum PutA-membrane associations. Arch Biochem Biophys (2005) 0.82
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Kinetic and structural characterization of tunnel-perturbing mutants in Bradyrhizobium japonicum proline utilization A. Biochemistry (2014) 0.78
Cautionary tale of using tris(alkyl)phosphine reducing agents with NAD-dependent enzymes. Biochemistry (2020) 0.75