The DOI matches its Crossref record; 286 of the 286 references it cites were found in a registry or an index.
Thioredoxin and Related Molecules–From Biology to Health and Disease
Abstract
Thioredoxin and glutaredoxin systems in mammalian cells utilize thiol and selenol groups to maintain a reducing intracellular redox state acting as antioxidants and reducing agents in redox signaling with oxidizing reactive oxygen species. During the last decade, the functional roles of thioredoxin in particular have continued to expand, also including novel functions such as a secreted growth factor or a chemokine for immune cells. The role of thioredoxin and glutaredoxin in antioxidant defense and the role of thioredoxin in controlling recruitment of inflammatory cells offer potential use in clinical therapy. The fundamental differences between bacterial and mammalian thioredoxin reductases offer new principles for treatment of infections. Clinical drugs already in use target the active site selenol in thioredoxin reductases, inducing cell death in tumor cells. Thioredoxin and binding proteins (ASK1 and TBP2) appear to control apoptosis or metabolic states such as carbohydrate and lipid metabolism related to diseases such as diabetes and atherosclerosis.
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“The thioredoxin (Trx) and glutaredoxin (Grx) systems are important as antioxidants for maintaining cellular redox balance and providing electrons for thiol-dependent reactions like those catalyzed by ribonucleotide reductase and peroxiredoxins (Prxs).”
From Inhibition of the glutaredoxin and thioredoxin systems and ribonucleotide reductase by mutant p53-targeting compound APR-246 (2018) · cites this paper as [19]
In the citing paper
“The Trx system also reduces peroxiredoxins which control reactive oxygen species (ROS) and hydrogen peroxide levels19.”
From Inhibition of the glutaredoxin and thioredoxin systems and ribonucleotide reductase by mutant p53-targeting compound APR-246 (2018) · cites this paper as [19]
In the citing paper
“These systems are present in all mammalian cells19,20, and are required for the activity of ribonucleotide reductase (RNR) which provides deoxyribonucleotides for DNA replication and repair.”
From Inhibition of the glutaredoxin and thioredoxin systems and ribonucleotide reductase by mutant p53-targeting compound APR-246 (2018) · cites this paper as [19]
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Metadata
- Authors
- Lillig, C. H., & Holmgren, A.
- Affiliations
- Karolinska Institutet (SE)
- Venue
- Antioxidants & Redox Signaling
- Publisher
- SAGE Publications
- Published
- 2007-01
- Volume
- 9
- Issue
- 1
- Pages
- 25-47
- ISSN
- 1523-0864 (ISSN-L)
- 1557-7716
- OpenAlex
- W2050083026
- Cited by
- 724
- References
- 286
- Citations by year
- 2026: 16 · 2025: 14 · 2024: 27 · 2023: 17 · 2022: 33 · 2021: 36 · 2020: 34 · 2019: 33 · 2018: 29 · 2017: 45 · 2016: 17 · 2015: 33 · 2014: 45 · 2013: 52 · 2012: 59
- FWCI
- 3.27
- Type
- journal article
- Language
- en
- Open access
- closed
- Locations
- Antioxidants and Redox Signaling (publishedVersion)
- PubMed (publishedVersion)
- Topics
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Redox biology and oxidative stress
- Health Sciences › Nursing › Nutrition and Dietetics › Selenium in Biological Systems
- Life Sciences › Biochemistry, Genetics and Molecular Biology › Molecular Biology › Genomics, phytochemicals, and oxidative stress
- Keywords
- thioredoxin, glutaredoxin, thioredoxin reductase, selenols, thiols, cellular redox state, antioxidant defense, redox signaling, reactive oxygen species, secreted growth factors, chemokines, immune cell recruitment, inflammation, infection treatment, apoptosis, ASK1, carbohydrate metabolism, lipid metabolism, diabetes mellitus, atherosclerosis, cancer cell death
- MeSH terms
- Amino Acid Sequence, Animals, Diabetes Mellitus, Humans, Models, Biological, Molecular Sequence Data, Oxidoreductases, Thioredoxins, Tissue Distribution, Signal Transduction, Protein Structure, Secondary, Protein Structure, Tertiary, Protein Folding, Atherosclerosis, Glutaredoxins
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