Cited by 297Iron Metabolism and DisordersMetalloenzymes and iron-sulfur proteinsHemoglobin structure and function

Unity in the Biochemistry of the Iron-Storage Proteins Ferritin and Bacterioferritin

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Honarmand Ebrahimi, Kourosh, Hagedoorn, Peter-Leon, Hagen, Wilfred R.·2015·Chemical Reviews

Abstract

ADVERTISEMENT RETURN TO ISSUEPREVReviewNEXTUnity in the Biochemistry of the Iron-Storage Proteins Ferritin and BacterioferritinKourosh Honarmand Ebrahimi*, Peter-Leon Hagedoorn, and Wilfred R. Hagen*View Author Information Department of Biotechnology, Delft University of Technology, Julianalaan 67, 2628 BC Delft, The Netherlands*Phone: 0031(0)152782347. E-mail: [email protected]*Phone: 0031(0)152785051. E-mail: [email protected]Cite this: Chem. Rev. 2015, 115, 1, 295–326Publication Date (Web):November 24, 2014Publication History Received2 September 2014Published online24 November 2014Published inissue 14 January 2015https://doi.org/10.1021/cr5004908Copyright © 2014 American Chemical SocietyRIGHTS & PERMISSIONSACS AuthorChoiceArticle Views10814Altmetric-Citations175LEARN ABOUT THESE METRICSArticle Views are the COUNTER-compliant sum of full text article downloads since November 2008 (both PDF and HTML) across all institutions and individuals. These metrics are regularly updated to reflect usage leading up to the last few days.Citations are the number of other articles citing this article, calculated by Crossref and updated daily. Find more information about Crossref citation counts.The Altmetric Attention Score is a quantitative measure of the attention that a research article has received online. Clicking on the donut icon will load a page at altmetric.com with additional details about the score and the social media presence for the given article. Find more information on the…

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  • When grown with an abundance of iron, the cell may sequester iron in hollow multimeric proteins (ferritin, mini-ferritins, and bacterioferritins).

    “When grown with an abundance of iron, the cell may sequester iron in hollow multimeric proteins (ferritin,126,127 mini-ferritins,128 and bacterioferritins129) (Figure 5).”
  • Mobilization of stored iron pools often requires reduction, or in some cases proteolysis, and occurs on a time-scale of minutes.

    “Mobilization of these stored iron pools often requires reduction,132 or in some cases proteolysis,127,133 and occurs on a time-scale of minutes.”

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Authors
Honarmand Ebrahimi, K., Hagedoorn, P.-L., & Hagen, W. R.
Affiliations
  • Delft University of Technology , , Julianalaan 67 , ,
  • Delft University of Technology (NL)
Venue
Chemical Reviews
Published
2014-11-24
Volume
115
Issue
1
Pages
295-326
ISSN
  • 0009-2665 (ISSN-L)
  • 1520-6890
OpenAlex
W2029703359
Cited by
297
References
11
Citations by year
2026: 25 · 2025: 31 · 2024: 33 · 2023: 29 · 2022: 30 · 2021: 24 · 2020: 17 · 2019: 24 · 2018: 14 · 2017: 27 · 2016: 33 · 2015: 10
FWCI
3.54
Type
journal article
Language
en
Open access
Locations
  • Chemical Reviews (publishedVersion, other-oa)
  • PubMed (publishedVersion)
Topics
  • Health Sciences › Medicine › Hematology › Iron Metabolism and Disorders
  • Physical Sciences › Energy › Renewable Energy, Sustainability and the Environment › Metalloenzymes and iron-sulfur proteins
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cell Biology › Hemoglobin structure and function
Keywords
ferritin, bacterioferritin, iron storage protein, iron-binding proteins, protein structure, protein oligomerization, iron oxidation
MeSH terms
Bacterial Proteins, Biochemical Phenomena, Cytochrome b Group, Ferritins, Models, Molecular

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