ArticleJournal of biochemistry2016
Aptamers that bind specifically to human KPNA2 (importin-α1) and efficiently interfere with nuclear transport.
Article in Journal of biochemistry, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
What it found
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Who cites it
8 citing papers in PubMed, 10 citations in OpenAlex.
- KPNA2 knockdown suppresses gastric cancer progression through modulation of the β-catenin/EMT signaling axis, inducing cell cycle arrest, apoptosis, and reduced metastatic capacity.Journal of molecular histology · 2026Article
- NCBP1 promotes the malignant progression of Wilms' tumor through stabilization of KPNA2 mRNA.Cancer gene therapy · 2026Article
- Article
- MicroRNA-517c Functions as a Tumor Suppressor in Hepatocellular Carcinoma via Downregulation of KPNA2 and Inhibition of PI3K/AKT Pathway.Journal of healthcare engineering · 2022Article
- KPNA2 interaction with CBX8 contributes to the development and progression of bladder cancer by mediating the PRDM1/c-FOS pathway.Journal of translational medicine · 2021Article
- Integrative bioinformatics analysis of KPNA2 in six major human cancers.Open medicine (Warsaw, Poland) · 2021Article
- Aptamers that bind to the human complement component receptor hC5aR1 interfere with hC5aR1 interaction to its hC5a ligand.Molecular biology reports · 2018Article
- Knockdown of KPNA2 inhibits autophagy in oral squamous cell carcinoma cell lines by blocking p53 nuclear translocation.Oncology reports · 2018Article
Corrections and comments
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Authors and funding
2 authors at 2 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The importin-α family of proteins plays an important role in the eukaryotic importin/exportin nuclear transport system. These proteins recognize a nuclear localization signal (NLS) within cargo proteins and import them into the nucleus through nuclear pores, in a process mediated by importin-β. Recent studies have shown that importin-α proteins specifically recognize the NLS of several cellular factors and viral proteins, thus regulating their movement. Dysregulation of importin-α is a common hallmark of many pathologies including, multiple cancers. In this study, we isolated aptamers 76 and 72, which bind specifically and efficiently to KPNA2, a member of a subfamily of importin-α1. Both of these aptamers bind to KPNA2 with an equilibrium dissociation constant (K
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Registered trials
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