ReviewGenes2017
Proteins Recognizing DNA: Structural Uniqueness and Versatility of DNA-Binding Domains in Stem Cell Transcription Factors.
Review in Genes, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 25 papers.
What it found
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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
25 citing papers in PubMed, 55 citations in OpenAlex.
- Nanoclustering of a plant transcription factor enables strong yet specific DNA binding.Science advances · 2026Article
- Multi-omics analyses reveal the virulence differentiation underlying natural variation inApplied and environmental microbiology · 2025Article
- CAP: Commutative algebra prediction of protein-nucleic acid binding affinities.Machine learning: science and technology · 2025Article
- OptimDase: An Algorithm for Predicting DNA Binding Sites with Combined Feature Encoding.Interdisciplinary sciences, computational life sciences · 2025Article
- Zinc finger domains bind low-complexity domain polymers.Nature communications · 2025Article
- Evidence for vitellogenin DNA-binding in honey bees.Protein science : a publication of the Protein Society · 2025Article
- MORC2 is a phosphorylation-dependent DNA compaction machine.Nature communications · 2025Article
- The potential role of PAX5 and PAX8 in regulating telomerase activity: a narrative mini-review.Molecular biology reports · 2025Review
- NovelImmune network · 2025Article
- Diverse genetic conflicts mediated by molecular mimicry and computational approaches to detect them.Seminars in cell & developmental biology · 2025Review
- Putative looping factor ZNF143/ZFP143 is an essential transcriptional regulator with no looping function.Molecular cell · 2025Article
- Genome-wide identification and expression profiling of bHLH transcription factors associated with ferulic acid biosynthesis inFrontiers in plant science · 2025Article
- Advances in Language-Model-Informed Protein-Nucleic Acid Binding Site Prediction.Methods in molecular biology (Clifton, N.J.) · 2025Article
- Review
- Species-Specific Transcription Factors Associated with Long Terminal Repeat Promoters of Endogenous Retroviruses: A Comprehensive Review.Biomolecules · 2024Review
- Photo-caged 2-butene-1,4-dial as an efficient, target-specific photo-crosslinker for covalent trapping of DNA-binding proteins.Chemical science · 2023Article
- DeepDISE: DNA Binding Site Prediction Using a Deep Learning Method.International journal of molecular sciences · 2021Article
- MET Expression and Cancer Stem Cell Networks Impact Outcome in High-Grade Serous Ovarian Cancer.Genes · 2021Article
- Amino Acid Composition in Various Types of Nucleic Acid-Binding Proteins.International journal of molecular sciences · 2021Review
- A Tale of Loops and Tails: The Role of Intrinsically Disordered Protein Regions in R-Loop Recognition and Phase Separation.Frontiers in molecular biosciences · 2021Article
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
5 authors at 1 institution in 1 country.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Proteins in the form of transcription factors (TFs) bind to specific DNA sites that regulate cell growth, differentiation, and cell development. The interactions between proteins and DNA are important toward maintaining and expressing genetic information. Without knowing TFs structures and DNA-binding properties, it is difficult to completely understand the mechanisms by which genetic information is transferred between DNA and proteins. The increasing availability of structural data on protein-DNA complexes and recognition mechanisms provides deeper insights into the nature of protein-DNA interactions and therefore, allows their manipulation. TFs utilize different mechanisms to recognize their cognate DNA (direct and indirect readouts). In this review, we focus on these recognition mechanisms as well as on the analysis of the DNA-binding domains of stem cell TFs, discussing the relative role of various amino acids toward facilitating such interactions. Unveiling such mechanisms will improve our understanding of the molecular pathways through which TFs are involved in repressing and activating gene expression.
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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.