ArticleNucleic acids research2012
Structural analysis and dimerization profile of the SCAN domain of the pluripotency factor Zfp206.
Article in Nucleic acids research, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 16 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
16 citing papers in PubMed, 23 citations in OpenAlex.
- Mix-and-match between transposable elements and zinc finger proteins fuels genic and regulatory innovation.Current opinion in genetics & development · 2025Review
- Genes as Genome Stabilizers in Pluripotent Stem Cells.Advances in experimental medicine and biology · 2025Review
- Dimerization Activity of a Disordered N-Terminal Domain fromInternational journal of molecular sciences · 2022Article
- Structural evidence that MOAP1 and PEG10 are derived from retrovirus/retrotransposon Gag proteins.Proteins · 2022Article
- Proteome-Wide Profiling of Readers for DNA Modification.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2021Article
- Structural basis of diversity and homodimerization specificity of zinc-finger-associated domains in Drosophila.Nucleic acids research · 2021Article
- The Role and Specific Mechanism of OCT4 in Cancer Stem Cells: A Review.International journal of stem cells · 2020Review
- ZSCAN10 promotes cell proliferation, upregulates OCT4 expression, and activates Wnt/β-catenin signaling in glioma.International journal of clinical and experimental pathology · 2019Article
- NRF1 and ZSCAN10 bind to the promoter region of the SIX1 gene and their effects body measurements in Qinchuan cattle.Scientific reports · 2017Article
- The Mutational Landscape of the Oncogenic MZF1 SCAN Domain in Cancer.Frontiers in molecular biosciences · 2016Article
- SOXE transcription factors form selective dimers on non-compact DNA motifs through multifaceted interactions between dimerization and high-mobility group domains.Scientific reports · 2015Article
- Recognition Code of ZNF191(243-368) and Its Interaction with DNA.Bioinorganic chemistry and applications · 2015Article
- Pleiotropic functions for transcription factor zscan10.PloS one · 2014Article
- Review
- Article
- Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
7 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Zfp206 (also named as Zscan10) belongs to the subfamily of C(2)H(2) zinc finger transcription factors, which is characterized by the N-terminal SCAN domain. The SCAN domain mediates self-association and association between the members of SCAN family transcription factors, but the structural basis and selectivity determinants for complex formation is unknown. Zfp206 is important for maintaining the pluripotency of embryonic stem cells presumably by combinatorial assembly of itself or other SCAN family members on enhancer regions. To gain insights into the folding topology and selectivity determinants for SCAN dimerization, we solved the 1.85 Å crystal structure of the SCAN domain of Zfp206. In vitro binding studies using a panel of 20 SCAN proteins indicate that the SCAN domain Zfp206 can selectively associate with other members of SCAN family transcription factors. Deletion mutations showed that the N-terminal helix 1 is critical for heterodimerization. Double mutations and multiple mutations based on the Zfp206SCAN-Zfp110SCAN model suggested that domain swapped topology is a possible preference for Zfp206SCAN-Zfp110SCAN heterodimer. Together, we demonstrate that the Zfp206SCAN constitutes a protein module that enables C(2)H(2) transcription factor dimerization in a highly selective manner using a domain-swapped interface architecture and identify novel partners for Zfp206 during embryonal development.
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.