Iron(II) triggered conformational changes in Escherichia coli fur upon DNA binding: a study using molecular modeling
Author:
Publisher
Elsevier BV
Subject
Materials Chemistry,Computer Graphics and Computer-Aided Design,Physical and Theoretical Chemistry,Spectroscopy
Reference47 articles.
1. Ferric uptake regulation protein acts as a repressor, employing iron(II) as a cofactor to bind the operator of an iron transport operon in Escherichia coli
2. Binding of the Fur (ferric uptake regulator) repressor of Escherichia coli to arrays of the GATAAT sequence
3. An electron spin resonance study of the Mn(II) and Cu(II) complexes of the Fur repressor protein
4. Binding of the ferric uptake regulation repressor protein (Fur) to Mn(II), Fe(II), Co(II), and Cu(II) ions as co-repressors: Electronic absorption, equilibrium, and 57Fe Mössbauer studies
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3. Two Amino Acids Mutation of Ferric Uptake Regulator DeterminesHelicobacter pyloriResistance to Metronidazole;Antioxidants & Redox Signaling;2011-01
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5. Cys-92, Cys-95, and the C-terminal 12 residues of the Vibrio harveyi ferric uptake regulator (Fur) are functionally inessential;The Journal of Microbiology;2008-12
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