ArticleNucleic acids research1998
Overlapping RNA and DNA binding domains of the wt1 tumor suppressor gene product.
Article in Nucleic acids research, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 24 papers.
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Who cites it
24 citing papers in PubMed, 86 citations in OpenAlex.
- Article
- Whole exome sequencing identified a rare WT1 loss-of-function variant in a non-syndromic POI patient.Molecular genetics & genomic medicine · 2022Article
- A NovelBiology · 2021Article
- Every Beat You Take-The Wilms' Tumor Suppressor WT1 and the Heart.International journal of molecular sciences · 2021Review
- Truncated WT1 Protein Isoform Expression Is Increased in MCF-7 Cells with Long-Term Estrogen Depletion.International journal of breast cancer · 2021Article
- Recent advances in understanding oligonucleotide aptamers and their applications as therapeutic agents.3 Biotech · 2020Review
- Article
- H3.3K27M mutant proteins reprogram epigenome by sequestering the PRC2 complex to poised enhancers.eLife · 2018Article
- Beyond Transcription: Roles of Transcription Factors in Pre-mRNA Splicing.Chemical reviews · 2018Review
- Transcription factor Wilms' tumor 1 regulates developmental RNAs through 3' UTR interaction.Genes & development · 2017Article
- Ligand-targeted theranostic nanomedicines against cancer.Journal of controlled release : official journal of the Controlled Release Society · 2016Review
- Identification of a Novel C-Terminal Truncated WT1 Isoform with Antagonistic Effects against Major WT1 Isoforms.PloS one · 2015Article
- Classification of a frameshift/extended and a stop mutation in WT1 as gain-of-function mutations that activate cell cycle genes and promote Wilms tumour cell proliferation.Human molecular genetics · 2014Article
- Nucleic acid aptamers: research tools in disease diagnostics and therapeutics.BioMed research international · 2014Review
- RNA aptamers and their therapeutic and diagnostic applications.International journal of biochemistry and molecular biology · 2013Article
- High-throughput binding analysis determines the binding specificity of ASF/SF2 on alternatively spliced human pre-mRNAs.Combinatorial chemistry & high throughput screening · 2010Article
- Bioimaging of nucleolin aptamer-containing 5-(N-benzylcarboxyamide)-2'-deoxyuridine more capable of specific binding to targets in cancer cells.Journal of biomedicine & biotechnology · 2010Article
- Induction of Wilms' tumor protein (WT1)-specific antitumor immunity using a truncated WT1-expressing adenovirus vaccine.Clinical cancer research : an official journal of the American Association for Cancer Research · 2009Article
- The Wilms' tumor 1 (WT1) gene (+KTS isoform) functions with a CTE to enhance translation from an unspliced RNA with a retained intron.Genes & development · 2006Article
- Vascular endothelial growth factor (VEGF) is suppressed in WT1-transfected LNCaP cells.Gene expression · 2006Article
Corrections and comments
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The Wilms' tumour suppressor gene (wt1) is mutated in a subset of patients with Wilms' tumour and has a critical role in urogenital development. wt1 encodes a zinc finger transcription factor which regulates expression of several genes involved in cellular proliferation and differentiation. Although a number of studies have characterized the DNA binding properties of the WT1 protein, recent evidence has suggested that WT1 may also have a role in RNA metabolism. We have used an RNA selection method to identify WT1 binding ligands from a random RNA pool. Three groups of RNA ligands specifically recognized by WT1 were identified. Mutational analysis pinpointed ribonucleotide sequences critical for binding. Analysis of truncated WT1 proteins demonstrated that three of four zinc fingers were necessary for RNA-protein interaction. The naturally occurring WT1 isoforms with insertion of lysine, threonine and serine between zinc fingers three and four were unable to bind the selected RNAs. The selected RNA ligands competed with the cognate WT1 DNA binding site for complex formation with WT1. Our findings suggest potential cellular RNA target sequences for WT1 and provide tools for studying the structural and functional properties of this tumour suppressor protein.
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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.