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Cited by 582

The DOI matches its Crossref record; 3 of the 3 references it cites were found in a registry or an index.

Peroxiredoxins

Hofmann, B., Hecht, H.-J., Flohé, L.·2002·Biological Chemistry
DOI 10.1515/bc.2002.040
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Abstract

Present knowledge on peroxiredoxins is reviewed with special emphasis on catalytic principles, specificities and biological function. Peroxiredoxins are low efficiency peroxidases using thiols as reductants. They appear to be fairly promiscuous with respect to the hydroperoxide substrate; the specificities for the donor substrate vary considerably between the subfamilies, comprising GSH, thioredoxin, tryparedoxin and the analogous CXXC motifs in bacterial AhpF proteins. Peroxiredoxins are definitely responsible for antioxidant defense in bacteria (AhpC), yeast (thioredoxin peroxidase) and trypanosomatids (tryparedoxin peroxidase). They are considered to determine virulence of mycobacteria and trypanosomatids. In higher plants they are involved in balancing hydroperoxide production during photosynthesis. In higher animals peroxiredoxins appear to be involved in the redox-regulation of cellular signaling and differentiation, displaying in part opposite effects.

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Metadata

Authors
Hofmann, B., Hecht, H.-J., & Flohé, L.
Venue
Biological Chemistry
Publisher
Walter de Gruyter GmbH
Published
2002-01-12
Volume
383
Issue
3-4
Pages
347-64
ISSN
1431-6730 (ISSN-L)
DOI
10.1515/bc.2002.040
OpenAlex
W4249820148
Cited by
582
References
3
FWCI
12.31
Type
journal article
Language
en
Open access
closed

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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.