ArticleMolecular and cellular biochemistry2002
HnRNP-A1 binds directly to double-stranded DNA in vitro within a 36 bp sequence.
Article in Molecular and cellular biochemistry, 2002. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 6 papers.
What it found
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Who cites it
6 citing papers in PubMed, 16 citations in OpenAlex.
- Dysregulation of miR-212 Promotes Castration Resistance through hnRNPH1-Mediated Regulation of AR and AR-V7: Implications for Racial Disparity of Prostate Cancer.Clinical cancer research : an official journal of the American Association for Cancer Research · 2016Article
- HNRNPA1 interacts with a 5'-flanking distal element of interleukin-6 and upregulates its basal transcription.Genes and immunity · 2013Article
- Heterogeneous nuclear ribonucleoprotein A/B and G inhibits the transcription of gonadotropin-releasing-hormone 1.Molecular and cellular neurosciences · 2008Article
- A role for SC35 and hnRNPA1 in the determination of amyloid precursor protein isoforms.Molecular psychiatry · 2007Article
- In-silico prediction and observations of nuclear matrix attachment.Cellular & molecular biology letters · 2006Article
- Heterogeneous nuclear ribonucleoprotein (hnRNP) binding to hormone response elements: a cause of vitamin D resistance.Proceedings of the National Academy of Sciences of the United States of America · 2003Article
Corrections and comments
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
The heterogeneous nuclear ribonucleoprotein A1 (hnRNP-A1) is known as an RNA- and single-stranded DNA-binding protein involved in alternative splicing of mRNA, RNA transport and maintenance of chromosome telomere length. In this study we tested whether this protein could bind directly to double-stranded DNA (dsDNA). Using PCR amplification of target DNA-sequences from human chromosome 11q13 followed by their incubation with hnRNP-A1 and atomic force microscopy (AFM) of the DNA/protein complexes, we found that this protein bound to DNA within a 36 bp sequence. These results were confirmed by electrophoretic mobility shift assay (EMSA). This sequence was found widely dispersed throughout the genome. There is no overlap between the 36 bp sequence and known target sequences in RNA for binding binRNP-A1.
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Registered trials
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