1
|
A whole genome view of prokaryotic haem biosynthesis.
|
Microbiology
|
2002
|
1.92
|
2
|
Interaction between the bacterial iron response regulator and ferrochelatase mediates genetic control of heme biosynthesis.
|
Mol Cell
|
2002
|
1.53
|
3
|
Bradyrhizobium japonicum senses iron through the status of haem to regulate iron homeostasis and metabolism.
|
Mol Microbiol
|
2006
|
1.45
|
4
|
Two heme binding sites are involved in the regulated degradation of the bacterial iron response regulator (Irr) protein.
|
J Biol Chem
|
2004
|
1.29
|
5
|
Oxidative stress promotes degradation of the Irr protein to regulate haem biosynthesis in Bradyrhizobium japonicum.
|
Mol Microbiol
|
2006
|
1.29
|
6
|
The hmuQ and hmuD genes from Bradyrhizobium japonicum encode heme-degrading enzymes.
|
J Bacteriol
|
2006
|
1.21
|
7
|
A novel DNA-binding site for the ferric uptake regulator (Fur) protein from Bradyrhizobium japonicum.
|
J Biol Chem
|
2003
|
1.19
|
8
|
Fur is involved in manganese-dependent regulation of mntA (sitA) expression in Sinorhizobium meliloti.
|
Appl Environ Microbiol
|
2004
|
1.12
|
9
|
Identification of a soybean protein that interacts with GAGA element dinucleotide repeat DNA.
|
Plant Physiol
|
2002
|
1.12
|
10
|
The mntH gene encodes the major Mn(2+) transporter in Bradyrhizobium japonicum and is regulated by manganese via the Fur protein.
|
Mol Microbiol
|
2009
|
1.10
|
11
|
Control of bacterial iron homeostasis by manganese.
|
Proc Natl Acad Sci U S A
|
2010
|
1.07
|
12
|
The ferric uptake regulator (Fur) protein from Bradyrhizobium japonicum is an iron-responsive transcriptional repressor in vitro.
|
J Biol Chem
|
2004
|
1.07
|
13
|
KatG is the primary detoxifier of hydrogen peroxide produced by aerobic metabolism in Bradyrhizobium japonicum.
|
J Bacteriol
|
2004
|
1.02
|
14
|
The Bradyrhizobium japonicum Irr protein is a transcriptional repressor with high-affinity DNA-binding activity.
|
J Bacteriol
|
2008
|
1.02
|
15
|
Positive control of ferric siderophore receptor gene expression by the Irr protein in Bradyrhizobium japonicum.
|
J Bacteriol
|
2008
|
1.01
|
16
|
Heme-dependent metalloregulation by the iron response regulator (Irr) protein in Rhizobium and other Alpha-proteobacteria.
|
Biometals
|
2008
|
0.99
|
17
|
Bacterial outer membrane channel for divalent metal ion acquisition.
|
Proc Natl Acad Sci U S A
|
2011
|
0.95
|
18
|
Transcriptional control of the Bradyrhizobium japonicum irr gene requires repression by fur and Antirepression by Irr.
|
J Biol Chem
|
2010
|
0.93
|
19
|
Control of DegP-dependent degradation of c-type cytochromes by heme and the cytochrome c maturation system in Escherichia coli.
|
J Bacteriol
|
2007
|
0.87
|
20
|
Manganese is required for oxidative metabolism in unstressed Bradyrhizobium japonicum cells.
|
Mol Microbiol
|
2012
|
0.86
|
21
|
Unusual heme binding in the bacterial iron response regulator protein: spectral characterization of heme binding to the heme regulatory motif.
|
Biochemistry
|
2011
|
0.85
|
22
|
The Bradyrhizobium japonicum frcB gene encodes a diheme ferric reductase.
|
J Bacteriol
|
2011
|
0.85
|
23
|
Differential control of Bradyrhizobium japonicum iron stimulon genes through variable affinity of the iron response regulator (Irr) for target gene promoters and selective loss of activator function.
|
Mol Microbiol
|
2014
|
0.85
|
24
|
HmuP is a coactivator of Irr-dependent expression of heme utilization genes in Bradyrhizobium japonicum.
|
J Bacteriol
|
2012
|
0.83
|
25
|
A new small regulatory protein, HmuP, modulates haemin acquisition in Sinorhizobium meliloti.
|
Microbiology
|
2010
|
0.83
|
26
|
Iron-dependent cytochrome c1 expression is mediated by the status of heme in Bradyrhizobium japonicum.
|
J Bacteriol
|
2005
|
0.81
|
27
|
Legume biology: sequence to seeds.
|
Plant Physiol
|
2007
|
0.80
|
28
|
ShmR is essential for utilization of heme as a nutritional iron source in Sinorhizobium meliloti.
|
Appl Environ Microbiol
|
2008
|
0.79
|
29
|
Magnesium-dependent processes are targets of bacterial manganese toxicity.
|
Mol Microbiol
|
2014
|
0.77
|
30
|
Legume focus: model species sequenced, mutagenesis approaches extended, and debut of a new model.
|
Plant Physiol
|
2009
|
0.75
|