ArticleNucleic acids research2018
Role for first zinc finger of WT1 in DNA sequence specificity: Denys-Drash syndrome-associated WT1 mutant in ZF1 enhances affinity for a subset of WT1 binding sites.
Article in Nucleic acids research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 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
14 citing papers in PubMed, 29 citations in OpenAlex.
- Conformational stability and domain-specific structural features of tumor autoantigens regulate autoantibody epitope propensity.Protein science : a publication of the Protein Society · 2026Article
- RNA Sequencing Identifies WT1 Overexpression as a Predictor of Poor Outcomes in Acute Myeloid Leukemia.Cancers · 2025Article
- Desmoplastic small round cell tumor: an update of current management practices.Journal of the Egyptian National Cancer Institute · 2025Review
- Genotype-Phenotype Correlations in Denys-Drash Syndrome in Children.Kidney international reports · 2025Article
- Overexpression of WT1 in all molecular subtypes of breast cancer and its impact on survival: exploring oncogenic and tumor suppressor roles of distinct WT1 isoforms.Molecular biology reports · 2024Article
- Neural network modeling of differential binding between wild-type and mutant CTCF reveals putative binding preferences for zinc fingers 1-2.BMC genomics · 2022Article
- FBXO38 Ubiquitin Ligase Controls Centromere Integrity via ZXDA/B Stability.Frontiers in cell and developmental biology · 2022Article
- Whole exome sequencing identified a rare WT1 loss-of-function variant in a non-syndromic POI patient.Molecular genetics & genomic medicine · 2022Article
- LAHMA: structure analysis through local annotation of homology-matched amino acids.Acta crystallographica. Section D, Structural biology · 2021Article
- Influence of Disease-Causing Mutations on Protein Structural Networks.Frontiers in molecular biosciences · 2020Article
- Molecular update on biology of Wilms Tumor 1 gene and its applications in acute myeloid leukemia.American journal of blood research · 2020Review
- Disorder and cysteines in proteins: A design for orchestration of conformational see-saw and modulatory functions.Progress in molecular biology and translational science · 2020Review
- Crystal structures of REF6 and its complex with DNA reveal diverse recognition mechanisms.Cell discovery · 2020Article
- Structural basis of specific DNA binding by the transcription factor ZBTB24.Nucleic acids research · 2019Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
6 authors at 3 institutions in 1 country.
Funding
Abstract
Wilms tumor protein (WT1) is a Cys2-His2 zinc-finger transcription factor vital for embryonic development of the genitourinary system. The protein contains a C-terminal DNA binding domain with four tandem zinc-fingers (ZF1-4). An alternative splicing of Wt1 can add three additional amino acids-lysine (K), threonine (T) and serine (S)-between ZF3 and ZF4. In the -KTS isoform, ZF2-4 determine the sequence-specificity of DNA binding, whereas the function of ZF1 remains elusive. Three X-ray structures are described here for wild-type -KTS isoform ZF1-4 in complex with its cognate DNA sequence. We observed four unique ZF1 conformations. First, like ZF2-4, ZF1 can be positioned continuously in the DNA major groove forming a 'near-cognate' complex. Second, while ZF2-4 make base-specific interactions with one DNA molecule, ZF1 can interact with a second DNA molecule (or, presumably, two regions of the same DNA molecule). Third, ZF1 can intercalate at the joint of two tail-to-head DNA molecules. If such intercalation occurs on a continuous DNA molecule, it would kink the DNA at the ZF1 binding site. Fourth, two ZF1 units can dimerize. Furthermore, we examined a Denys-Drash syndrome-associated ZF1 mutation (methionine at position 342 is replaced by arginine). This mutation enhances WT1 affinity for a guanine base. X-ray crystallography of the mutant in complex with its preferred sequence revealed the interactions responsible for this affinity change. These results provide insight into the mechanisms of action of WT1, and clarify the fact that ZF1 plays a role in determining sequence specificity of this critical transcription factor.
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.