ArticleMethods in enzymology2010
Alteration of thioredoxin reductase 1 levels in elucidating cancer etiology.
Article in Methods in enzymology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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Who cites it
8 citing papers in PubMed, 16 citations in OpenAlex.
- Sorafenib-Loaded Silica-Containing Redox Nanoparticle Decreases Tumorigenic Potential of Lewis Lung Carcinoma.Pharmaceutics · 2025Article
- Elemental profiles in distant tissues during tumor progression.BMC cancer · 2023Article
- Chemoproteomic interrogation of selenocysteine by low-pH isoTOP-ABPP.Methods in enzymology · 2022Article
- A Quantitative Chemoproteomic Platform to Monitor Selenocysteine Reactivity within a Complex Proteome.Cell chemical biology · 2018Article
- The 15kDa selenoprotein and thioredoxin reductase 1 promote colon cancer by different pathways.PloS one · 2015Article
- The effects of di(2-ethylhexyl)phthalate on rat liver in relation to selenium status.International journal of experimental pathology · 2014Article
- CLIC4 is a tumor suppressor for cutaneous squamous cell cancer.Carcinogenesis · 2012Article
- The chemopreventive and clinically used agent curcumin sensitizes HPV (-) but not HPV (+) HNSCC to ionizing radiation, in vitro and in a mouse orthotopic model.Cancer biology & therapy · 2012Article
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Authors and funding
6 authors at 4 institutions in 1 country.
Funding
Abstract
Thioredoxin reductase 1 (TR1) is a major antioxidant and redox regulator in mammalian cells and appears to function as a double-edged sword in that it has roles in preventing and promoting/sustaining cancer. TR1 is overexpressed in many cancer cells and targeting its removal often leads to a reversal in numerous malignant characteristics which has marked this selenoenzyme as a prime target for cancer therapy. Since alterations in TR1 activity may lead to a better understanding of the etiology of cancer and new avenues for providing better therapeutic procedures, we have described herein techniques for removing and reexpressing TR1 employing RNAi technology and for assessing the catalytic activity of this enzyme.
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