ArticlePloS one2012
Solution structure of the oncogenic MIEN1 protein reveals a thioredoxin-like fold with a redox-active motif.
Article in PloS one, 2012. 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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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
8 citing papers in PubMed, 18 citations in OpenAlex.
- Research and progress of microRNA-136 in metastatic tumors.Frontiers in oncology · 2025Review
- The circular RNA circ_0030018/miR-136/migration and invasion enhancer 1 (MIEN1) axis promotes the progression of polycystic ovary syndrome.Bioengineered · 2022Article
- C-terminal Redox Domain ofAntioxidants (Basel, Switzerland) · 2019Article
- Article
- Emerging Role of Migration and Invasion Enhancer 1 (MIEN1) in Cancer Progression and Metastasis.Frontiers in oncology · 2019Review
- miR-136 targets MIEN1 and involves the metastasis of colon cancer by suppressing epithelial-to-mesenchymal transition.OncoTargets and therapy · 2018Article
- Utilizing Selenocysteine for Expressed Protein Ligation and Bioconjugations.Journal of the American Chemical Society · 2017Article
- MicroRNA-940 suppresses prostate cancer migration and invasion by regulating MIEN1.Molecular cancer · 2014Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The novel tumor biomarker MIEN1, identified by representational difference analysis, is overexpressed in breast cancer and prostate cancer. MIEN1 is considered an oncogenic protein, because MIEN1 overexpression functionally enhances migration and invasion of tumor cells via modulating the activity of AKT. However, the structure and molecular function of MIEN1 is little understood. Here, we report the solution structure of MIEN1, which adopts a thioredoxin-like fold with a redox-active motif. Comparison of backbone chemical shifts showed that most of the residues for both oxidized and reduced MIEN1 possessed the same backbone conformation, with differences limited to the active motif and regions in proximity. The redox potential of this disulfide bond was measured as -225 mV, which compares well with that of disulfides for other thioredoxin-like proteins. Overall, our results suggest that MIEN1 may have an important regulatory role in phosphorylation of AKT with its redox potential.
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Registered trials
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