ArticleNucleic acids research2012
The structural basis for the oligomerization of the N-terminal domain of SATB1.
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 22 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
22 citing papers in PubMed, 44 citations in OpenAlex.
- Clinical and Molecular Characterization of Five Additional Individuals With SATB2-Associated Syndrome in Guangxi.Biochemical genetics · 2026Article
- A MTA2-SATB2 chromatin complex restrains colonic plasticity toward small intestine by retaining HNF4A at colonic chromatin.Nature communications · 2024Article
- A dual function for the chromatin organizer Special A-T rich Binding Protein 1 in B-lineage cells.Cellular & molecular immunology · 2023Article
- A novel SATB1 protein isoform with different biophysical properties.Frontiers in cell and developmental biology · 2023Article
- The 3D enhancer network of the developing T cell genome is shaped by SATB1.Nature communications · 2022Article
- A novel mutation of SATB2 inhibits odontogenesis of human dental pulp stem cells through Wnt/β-catenin signaling pathway.Stem cell research & therapy · 2021Article
- Satb2 acts as a gatekeeper for major developmental transitions during early vertebrate embryogenesis.Nature communications · 2021Article
- Article
- Mutation-specific pathophysiological mechanisms define different neurodevelopmental disorders associated with SATB1 dysfunction.American journal of human genetics · 2021Article
- SATB2-LEMD2 interaction links nuclear shape plasticity to regulation of cognition-related genes.The EMBO journal · 2021Article
- SATB1-mediated chromatin landscape in T cells.Nucleus (Austin, Tex.) · 2020Review
- Satb1 integrates DNA binding site geometry and torsional stress to differentially target nucleosome-dense regions.Nature communications · 2019Article
- Tetramerization of SATB1 is essential for regulating of gene expression.Molecular and cellular biochemistry · 2017Article
- Special AT-rich DNA-binding protein-1 expression is associated with liver cancer metastasis.Oncology letters · 2016Article
- Satb2 determines miRNA expression and long-term memory in the adult central nervous system.eLife · 2016Article
- Article
- Homeodomain proteins: an update.Chromosoma · 2016Review
- YvoA and CcpA Repress the Expression of chiB in Bacillus thuringiensis.Applied and environmental microbiology · 2015Article
- Functional analysis of the sporulation-specific diadenylate cyclase CdaS in Bacillus thuringiensis.Frontiers in microbiology · 2015Article
- Crystal structure of the ubiquitin-like domain-CUT repeat-like tandem of special AT-rich sequence binding protein 1 (SATB1) reveals a coordinating DNA-binding mechanism.The Journal of biological chemistry · 2014Article
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
Special AT-rich sequence-binding protein 1 (SATB1) is a global chromatin organizer and gene expression regulator essential for T-cell development and breast cancer tumor growth and metastasis. The oligomerization of the N-terminal domain of SATB1 is critical for its biological function. We determined the crystal structure of the N-terminal domain of SATB1. Surprisingly, this domain resembles a ubiquitin domain instead of the previously proposed PDZ domain. Our results also reveal that SATB1 can form a tetramer through its N-terminal domain. The tetramerization of SATB1 plays an essential role in its binding to highly specialized DNA sequences. Furthermore, isothermal titration calorimetry results indicate that the SATB1 tetramer can bind simultaneously to two DNA targets. Based on these results, we propose a molecular model whereby SATB1 regulates the expression of multiple genes both locally and at a distance.
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.