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The DOI matches its Crossref record; 50 of the 50 references it cites were found in a registry or an index.

Typical 2‐Cys peroxiredoxins – structures, mechanisms and functions

Open access
Hall, Andrea, Karplus, P. A., Poole, Leslie B.·2009·The FEBS Journal

Abstract

Peroxiredoxins are abundant cellular antioxidant proteins that help to control intracellular peroxide levels. These proteins may also function, in part, through an evolved sensitivity of some peroxiredoxins towards peroxide‐mediated inactivation in hydrogen peroxide signaling in eukaryotes. This review summarizes recent progress in our understanding of the catalytic and regulatory mechanisms of ‘typical 2‐Cys’ peroxiredoxins and of the biological roles played by these important enzymes in oxidative stress and nonstress‐related cellular signaling. New evidence suggests localized peroxide buildup plays a role in nonstress‐related signaling.

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Crossref · 10.1111/j.1742-4658.2009.06985.x

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Metadata

Authors
Hall, A., Karplus, P. A., & Poole, L. B.
Venue
The FEBS Journal
Publisher
Wiley
Published
2009-04-02
Volume
276
Issue
9
Pages
2469-2477
ISSN
  • 1742-464X (ISSN-L)
  • 1742-4658
OpenAlex
W2026225426
Cited by
465
References
50
FWCI
14.28
Type
journal article
Language
en
Open access
green

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CoChat. (2026). Citation check: Typical 2‐Cys peroxiredoxins – structures, mechanisms and functions. https://app.cochat.ai/papers/10.1111/j.1742-4658.2009.06985.x
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Hall, A., Karplus, P. A., & Poole, L. B. (2009). Typical 2‐Cys peroxiredoxins – structures, mechanisms and functions. The FEBS Journal. https://doi.org/10.1111/j.1742-4658.2009.06985.x

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Bibliographic data: Semantic Scholar, OpenAlex, Crossref.

Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).

Semantic Scholar’s data is described in: Kinney, R., et al. (2023). The Semantic Scholar Open Data Platform. arXiv:2301.10140.