Reductive Mobilization of Iron from Intact Ferritin: Mechanisms and Physiological Implication (Q58611874)

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2 May 2020

title

Reductive Mobilization of Iron from Intact Ferritin: Mechanisms and Physiological Implication (English)

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2 May 2020

1

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2 May 2020

author name string

John J Paliakkara

series ordinal

2

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30400623 AND SRC:MED&resulttype=core&format=json

2 May 2020

Galina Melman

series ordinal

3

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30400623 AND SRC:MED&resulttype=core&format=json

2 May 2020

Artem Melman

series ordinal

4

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2 May 2020

language of work or name

English

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publication date

5 November 2018

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2 May 2020

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2 May 2020

volume

11

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2 May 2020

issue

4

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Creative Commons Attribution 4.0 International

2 May 2020

copyright license

start time

5 November 2018

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April 2022 Public Data File from Crossref

copyright status

copyrighted

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cites work

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Multiple Pathways for Mineral Core Formation in Mammalian Apoferritin. The Role of Hydrogen Peroxide†

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Opening protein pores with chaotropes enhances Fe reduction and chelation of Fe from the ferritin biomineral

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Ascorbate-mediated iron release from ferritin in the presence of alloxan

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Peptides selected for the protein nanocage pores change the rate of iron recovery from the ferritin mineral

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A cytosolic iron chaperone that delivers iron to ferritin.

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12 December 2020

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Facilitated diffusion of iron(II) and dioxygen substrates into human H-chain ferritin. A fluorescence and absorbance study employing the ferroxidase center substitution Y34W.

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GATED PORES IN THE FERRITIN PROTEIN NANOCAGE

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Binding of Pseudomonas aeruginosa apobacterioferritin-associated ferredoxin to bacterioferritin B promotes heme mediation of electron delivery and mobilization of core mineral iron

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Oxido-reduction is not the only mechanism allowing ions to traverse the ferritin protein shell

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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)

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Encapsulation of β-carotene within ferritin nanocages greatly increases its water-solubility and thermal stability

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Unity in the biochemistry of the iron-storage proteins ferritin and bacterioferritin.

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Three Aromatic Residues are Required for Electron Transfer during Iron Mineralization in Bacterioferritin.

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Cisplatin encapsulation within a ferritin nanocage: a high-resolution crystallographic study

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Solving Biology's Iron Chemistry Problem with Ferritin Protein Nanocages.

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Bacterioferritin: Structure, Dynamics, and Protein-Protein Interactions at Play in Iron Storage and Mobilization

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Inhibiting the BfrB:Bfd interaction in Pseudomonas aeruginosa causes irreversible iron accumulation in bacterioferritin and iron deficiency in the bacterial cytosol

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12 December 2020

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12 December 2020

Tyr25, Tyr58 and Trp133 of Escherichia coli bacterioferritin transfer electrons between iron in the central cavity and the ferroxidase centre

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12 December 2020

Effect of chaotropes on the kinetics of iron release from ferritin by flavin nucleotides

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12 December 2020

Mobilization of iron from ferritin: new steps and details

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12 December 2020

Releasing iron from ferritin protein nanocage by reductive method: The role of electron transfer mediator.

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12 December 2020

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12 December 2020

Identifiers

DOI

10.3390/PH11040120

1 reference

https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30400623 AND SRC:MED&resulttype=core&format=json

2 May 2020

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https://www.ebi.ac.uk/europepmc/webservices/rest/search?query=EXT_ID:30400623 AND SRC:MED&resulttype=core&format=json

2 May 2020

PubMed publication ID

30400623

1 reference