The DOI matches its Crossref record; 188 of the 188 references it cites were found in a registry or an index.
Properties and Biological Activities of Thioredoxins
Abstract
The mammalian thioredoxins are a family of small (approximately 12 kDa) redox proteins that undergo NADPH-dependent reduction by thioredoxin reductase and in turn reduce oxidized cysteine groups on proteins. The two main thioredoxins are thioredoxin-1, a cytosolic and nuclear form, and thioredoxin-2, a mitochondrial form. Thioredoxin-1 has been studied more. It performs many biological actions including the supply of reducing equivalents to thioredoxin peroxidases and ribonucleotide reductase, the regulation of transcription factor activity, and the regulation of enzyme activity by heterodimer formation. Thioredoxin-1 stimulates cell growth and is an inhibitor of apoptosis. Thioredoxins may play a role in a variety of human diseases including cancer. An increased level of thioredoxin-1 is found in many human tumors, where it is associated with aggressive tumor growth. Drugs are being developed that inhibit thioredoxin and that have antitumor activity.
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Cites
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Cited by
Shen, S., Li, X.-F., Cullen, W. R., Weinfeld, M., & Le, X. C. (2013) · Chemical Reviews · doi:10.1021/cr300015c · Cited by 818
Thioredoxin and Related Molecules–From Biology to Health and Disease
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Mechanism of arsenic carcinogenesis: an integrated approach
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Metadata
- Authors
- Powis, G., & Montfort, W. R.
- Venue
- Annual Review of Pharmacology and Toxicology
- Publisher
- Annual Reviews
- Published
- 2001-04
- Volume
- 41
- Issue
- 1
- Pages
- 261-295
- ISSN
- 0362-1642 (ISSN-L)
- 1545-4304
- OpenAlex
- W2141874177
- Cited by
- 451
- References
- 188
- FWCI
- 1.82
- Type
- journal article
- Language
- en
- Open access
- closed
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Contains information from the Semantic Scholar Academic Graph Datasets, made available under the ODC Attribution License (ODC-BY 1.0).
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