ArticleBiochemistry2010
DNA bending by the mammalian high-mobility group protein AT hook 2.
Article in Biochemistry, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 19 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
19 citing papers in PubMed, 34 citations in OpenAlex.
- Exploring the Conformational and Binding Dynamics of HMGA2·DNA Complexes Using Trapped Ion Mobility Spectrometry-Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- Exploring the Conformations and Binding Location of HMGA2·DNA Complexes Using Ion Mobility Spectrometry and 193 nm Ultraviolet Photodissociation Mass Spectrometry.Journal of the American Society for Mass Spectrometry · 2022Article
- AT-hook peptides bind the major and minor groove of AT-rich DNA duplexes.Nucleic acids research · 2022Article
- Structural insights into the functional divergence of WhiB-like proteins in Mycobacterium tuberculosis.Molecular cell · 2021Article
- Identification of HMGA2 inhibitors by AlphaScreen-based ultra-high-throughput screening assays.Scientific reports · 2020Article
- The Mammalian High Mobility Group Protein AT-Hook 2 (HMGA2): Biochemical and Biophysical Properties, and Its Association with Adipogenesis.International journal of molecular sciences · 2020Review
- Impact of high-mobility-group A2 overexpression on epithelial-mesenchymal transition in pancreatic cancer.Cancer management and research · 2019Article
- NOTCH-mediated non-cell autonomous regulation of chromatin structure during senescence.Nature communications · 2018Article
- Oncofetal HMGA2 effectively curbs unconstrained (+) and (-) DNA supercoiling.Scientific reports · 2017Article
- Protein-induced DNA linking number change by sequence-specific DNA binding proteins and its biological effects.Biophysical reviews · 2016Review
- Protein-induced DNA linking number change by sequence-specific DNA binding proteins and its biological effects.Biophysical reviews · 2016Review
- The Dimerization State of the Mammalian High Mobility Group Protein AT-Hook 2 (HMGA2).PloS one · 2015Article
- HMGA proteins as modulators of chromatin structure during transcriptional activation.Frontiers in cell and developmental biology · 2014Review
- Molecular basis for sequence-dependent induced DNA bending.Chembiochem : a European journal of chemical biology · 2013Article
- Genome-wide analysis of HMGA2 transcription factor binding sites by ChIP on chip in gastric carcinoma cells.Molecular and cellular biochemistry · 2012Article
- Mechanisms of unphosphorylated STAT3 transcription factor binding to DNA.The Journal of biological chemistry · 2012Article
- Article
- Tip60-mediated acetylation activates transcription independent apoptotic activity of Abl.Molecular cancer · 2011Article
- 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
3 authors at 1 institution in 1 country.
Funding
Abstract
The mammalian high-mobility group protein AT hook 2 (HMGA2) is a DNA binding protein that specifically recognizes the minor groove of AT-rich DNA sequences. Disruption of its expression pattern is directly linked to oncogenesis and obesity. In this paper, we constructed a new plasmid pBendAT to study HMGA2-induced DNA bending. pBendAT carries a 230 bp DNA segment containing five pairs of restriction enzyme sites, which can be used to produce a set of DNA fragments of identical length to study protein-induced DNA bending. The DNA fragments of identical length can also be generated using PCR amplification. Since pBendAT does not contain more than three consecutive AT base pairs, it is suitable for the assessment of DNA bending induced by proteins recognizing AT-rich DNA sequences. Indeed, using pBendAT, we demonstrated that HMGA2 is a DNA bending protein and bends all three tested DNA binding sequences of HMGA2, SELEX1, SELEX2, and PRDII. The DNA bending angles were estimated to be 34.2 degrees , 33.5 degrees , and 35.4 degrees , respectively.
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.