Page last updated: 2024-08-24

ferric citrate and histidine

ferric citrate has been researched along with histidine in 2 studies

Research

Studies (2)

Timeframe	Studies, this research(%)	All Research%
pre-1990	0 (0.00)	18.7374
1990's	0 (0.00)	18.2507
2000's	2 (100.00)	29.6817
2010's	0 (0.00)	24.3611
2020's	0 (0.00)	2.80

Authors

Authors	Studies
Braun, V; Enz, S; Mahren, S; Stroeher, UH	1
deSzoeke, E; Frei, B; Hagen, TM; Suh, JH; Zhu, BZ	1

Other Studies

2 other study(ies) available for ferric citrate and histidine

Article	Year
Surface signaling in ferric citrate transport gene induction: interaction of the FecA, FecR, and FecI regulatory proteins. Journal of bacteriology, 2000, Volume: 182, Issue:3 Topics: Bacterial Proteins; Biological Transport, Active; Chromatography, Affinity; Escherichia coli; Escherichia coli Proteins; Ferric Compounds; Gene Expression Regulation, Bacterial; Histidine; Molecular Weight; Rec A Recombinases; Sigma Factor; Signal Transduction; Structure-Activity Relationship; Transcriptional Activation	2000
Dihydrolipoic acid lowers the redox activity of transition metal ions but does not remove them from the active site of enzymes. Redox report : communications in free radical research, 2004, Volume: 9, Issue:1 Topics: Aconitate Hydratase; Animals; Binding Sites; Cattle; Chelating Agents; Ditiocarb; Ferric Compounds; Histidine; Organometallic Compounds; Oxidation-Reduction; Protein Binding; Superoxide Dismutase; Thioctic Acid; Transition Elements	2004

Article

Year

Surface signaling in ferric citrate transport gene induction: interaction of the FecA, FecR, and FecI regulatory proteins.

Journal of bacteriology, 2000, Volume: 182, Issue:3

Topics: Bacterial Proteins; Biological Transport, Active; Chromatography, Affinity; Escherichia coli; Escherichia coli Proteins; Ferric Compounds; Gene Expression Regulation, Bacterial; Histidine; Molecular Weight; Rec A Recombinases; Sigma Factor; Signal Transduction; Structure-Activity Relationship; Transcriptional Activation

2000

Dihydrolipoic acid lowers the redox activity of transition metal ions but does not remove them from the active site of enzymes.

Redox report : communications in free radical research, 2004, Volume: 9, Issue:1

Topics: Aconitate Hydratase; Animals; Binding Sites; Cattle; Chelating Agents; Ditiocarb; Ferric Compounds; Histidine; Organometallic Compounds; Oxidation-Reduction; Protein Binding; Superoxide Dismutase; Thioctic Acid; Transition Elements

2004