ArticleRNA (New York, N.Y.)2013
The Runt domain of AML1 (RUNX1) binds a sequence-conserved RNA motif that mimics a DNA element.
Article in RNA (New York, N.Y.), 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.
What it found
Each row is one number read from the abstract, on the scale the paper reported it, with its interval. Left of the dashed line favours the treatment, right favours the comparator. Under each row is the sentence it came from. New to these charts? A ten-minute tutorial.
The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
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.
Neither the registry nor the abstract names a trial number. If this is a trial report, that itself is worth knowing.
Who cites it
15 citing papers in PubMed, 30 citations in OpenAlex.
- From Selection to Use: Aptamers as Targeting Reagents in Hematology.Biomedicines · 2026Review
- Mapping rat lncRNA Bdnf-as.Molecular biology reports · 2025Article
- Interface-guided phenotyping of coding variants in the transcription factor RUNX1.Cell reports · 2024Article
- USP10 deubiquitinates RUNX1 and promotes proneural-to-mesenchymal transition in glioblastoma.Cell death & disease · 2023Article
- RUNX1 deficiency cooperates with SRSF2 mutation to induce multilineage hematopoietic defects characteristic of MDS.Blood advances · 2022Article
- Nucleic Acid Aptamer: A Novel Potential Diagnostic and Therapeutic Tool for Leukemia.OncoTargets and therapy · 2019Review
- [Research advances in the role of aptamers in the diagnosis and targeted therapy of pediatric cancer].Zhongguo dang dai er ke za zhi = Chinese journal of contemporary pediatrics · 2018Review
- Characterisation of an aptamer against the Runt domain of AML1 (RUNX1) by NMR and mutational analyses.FEBS open bio · 2018Article
- Preleukemic and second-hit mutational events in an acute myeloid leukemia patient with a novel germlineBiomarker research · 2018Article
- Osteogenic Programming of Human Mesenchymal Stem Cells with Highly Efficient Intracellular Delivery of RUNX2.Stem cells translational medicine · 2017Article
- The SMAD3 transcription factor binds complex RNA structures with high affinity.Nucleic acids research · 2017Article
- NMR monitoring of the SELEX process to confirm enrichment of structured RNA.Scientific reports · 2017Article
- Anti-Transcription Factor RNA Aptamers as Potential Therapeutics.Nucleic acid therapeutics · 2016Review
- RNA aptamer inhibitors of a restriction endonuclease.Nucleic acids research · 2015Article
- The structure, function and evolution of proteins that bind DNA and RNA.Nature reviews. Molecular cell biology · 2014Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
AML1 (RUNX1) is a key transcription factor for hematopoiesis that binds to the Runt-binding double-stranded DNA element (RDE) of target genes through its N-terminal Runt domain. Aberrations in the AML1 gene are frequently found in human leukemia. To better understand AML1 and its potential utility for diagnosis and therapy, we obtained RNA aptamers that bind specifically to the AML1 Runt domain. Enzymatic probing and NMR analyses revealed that Apt1-S, which is a truncated variant of one of the aptamers, has a CACG tetraloop and two stem regions separated by an internal loop. All the isolated aptamers were found to contain the conserved sequence motif 5'-NNCCAC-3' and 5'-GCGMGN'N'-3' (M:A or C; N and N' form Watson-Crick base pairs). The motif contains one AC mismatch and one base bulged out. Mutational analysis of Apt1-S showed that three guanines of the motif are important for Runt binding as are the three guanines of RDE, which are directly recognized by three arginine residues of the Runt domain. Mutational analyses of the Runt domain revealed that the amino acid residues used for Apt1-S binding were similar to those used for RDE binding. Furthermore, the aptamer competed with RDE for binding to the Runt domain in vitro. These results demonstrated that the Runt domain of the AML1 protein binds to the motif of the aptamer that mimics DNA. Our findings should provide new insights into RNA function and utility in both basic and applied sciences.
Indexed as
Identifiers
What OpenQuestion holds
Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.