ArticleInternational journal of molecular sciences2015
A Critical Role for Cysteine 57 in the Biological Functions of Selenium Binding Protein-1.
Article in International journal of molecular sciences, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
9 citing papers in PubMed, 18 citations in OpenAlex.
- Selenium nanoparticle-loaded microneedle patches promote diabetic oral ulcer healing by regulating the inflammatory microenvironment through upregulation of SELENBP1-mediated mitophagy.Journal of nanobiotechnology · 2026Article
- SELENBP1 protects against kidney fibrosis in chronic kidney disease as a methanethiol oxidase.Science China. Life sciences · 2025Article
- Protective Role of Selenium-Binding Protein 1 (SELENBP1) in Patients with Ulcerative Colitis.Metabolites · 2024Article
- SBP1 promotes tumorigenesis of thyroid cancer through TXN/NIS pathway.Molecular medicine (Cambridge, Mass.) · 2023Article
- The role of SELENBP1 and its epigenetic regulation in carcinogenic progression.Frontiers in genetics · 2022Review
- Article
- A Caenorhabditis elegans ortholog of human selenium-binding protein 1 is a pro-aging factor protecting against selenite toxicity.Redox biology · 2020Article
- Selenium-Binding Protein 1 Indicates Myocardial Stress and Risk for Adverse Outcome in Cardiac Surgery.Nutrients · 2019Article
- Selenium-Binding Protein 1 in Human Health and Disease.International journal of molecular sciences · 2018Review
Corrections and comments
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Authors and funding
4 authors at 2 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The concentration of selenium-binding protein1 (SBP1) is often lower in tumors than in the corresponding tissue and lower levels have been associated with poor clinical outcomes. SBP1 binds tightly selenium although what role selenium plays in its biological functions remains unknown. Previous studies indicated that cysteine 57 is the most likely candidate amino acid for selenium binding. In order to investigate the role of cysteine 57 in SBP1, this amino acid was altered to a glycine and the mutated protein was expressed in human cancer cells. The SBP1 half-life, as well as the cellular response to selenite cytotoxicity, was altered by this change. The ectopic expression of SBP1(GLY) also caused mitochondrial damage in HCT116 cells. Taken together, these results indicated that cysteine 57 is a critical determinant of SBP1 function and may play a significant role in mitochondrial function.
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