Structural Studies of Bacterioferritin B from Pseudomonas aeruginosa Suggest a Gating Mechanism for Iron Uptake via the Ferroxidase Center,
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Two Distinct Ferritin-like Molecules in Pseudomonas aeruginosa : The Product of the bfrA Gene Is a Bacterial Ferritin (FtnA) and Not a Bacterioferritin (Bfr)The Structure of the BfrB–Bfd Complex Reveals Protein–Protein Interactions Enabling Iron Release from BacterioferritinStructural Characterization of Bacterioferritin from Blastochloris viridisStructural Insights into the Ferroxidase Site of Ferritins from Higher EukaryotesFerritins: furnishing proteins with ironThe catalytic center of ferritin regulates iron storage via Fe(II)-Fe(III) displacement.Inhibition and stimulation of formation of the ferroxidase center and the iron core in Pyrococcus furiosus ferritin.Simulations of stressosome activation emphasize allosteric interactions between RsbR and RsbT.Concerted motions networking pores and distant ferroxidase centers enable bacterioferritin function and iron traffic.The FinR-regulated essential gene fprA, encoding ferredoxin NADP+ reductase: Roles in superoxide-mediated stress protection and virulence of Pseudomonas aeruginosaCharacterization of the Bacterioferritin/Bacterioferritin Associated Ferredoxin Protein-Protein Interaction in Solution and Determination of Binding Energy Hot Spots.Local packing modulates diversity of iron pathways and cooperative behavior in eukaryotic and prokaryotic ferritins.Mechanisms of iron mineralization in ferritins: one size does not fit all.The Ferritin Superfamily.The workings of ferritin: a crossroad of opinions.Protein dynamics and ion traffic in bacterioferritin.Bacterioferritin: Structure, Dynamics, and Protein-Protein Interactions at Play in Iron Storage and Mobilization.Self-assembly is prerequisite for catalysis of Fe(II) oxidation by catalytically active subunits of ferritin.Tyr25, Tyr58 and Trp133 of Escherichia coli bacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre.Benchmarking a computational design method for the incorporation of metal ion-binding sites at symmetric protein interfaces.Inhibiting the BfrB:Bfd interaction in Pseudomonas aeruginosa causes irreversible iron accumulation in bacterioferritin and iron deficiency in the bacterial cytosol.Desulfovibrio vulgaris bacterioferritin uses H(2)O(2) as a co-substrate for iron oxidation and reveals DPS-like DNA protection and binding activities.
P2860
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P2860
Structural Studies of Bacterioferritin B from Pseudomonas aeruginosa Suggest a Gating Mechanism for Iron Uptake via the Ferroxidase Center,
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2010 nî lūn-bûn
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2010 թուականի Փետրուարին հրատարակուած գիտական յօդուած
@hyw
2010 թվականի փետրվարին հրատարակված գիտական հոդված
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2010年の論文
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2010年論文
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2010年論文
@zh-hant
2010年論文
@zh-hk
2010年論文
@zh-mo
2010年論文
@zh-tw
2010年论文
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name
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@ast
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@en
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@nl
type
label
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@ast
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@en
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@nl
prefLabel
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@ast
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@en
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@nl
P2093
P2860
P356
P1433
P1476
Structural Studies of Bacterio ...... ke via the Ferroxidase Center,
@en
P2093
Casey E Gee
Christopher J Fischer
Kevin P Battaile
Mario Rivera
Saroja K Weeratunga
P2860
P304
P356
10.1021/BI9015204
P407
P577
2010-02-16T00:00:00Z