ArticleThe Journal of biological chemistry2018
Dimerization site 2 of the bacterial DNA-binding protein H-NS is required for gene silencing and stiffened nucleoprotein filament formation.
Article in The Journal of biological chemistry, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 17 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
17 citing papers in PubMed, 26 citations in OpenAlex.
- Abundant bacterial nucleoid-associated protein H-NS limits plasmid transfer through mechanical modification of DNA.Nucleic acids research · 2025Article
- Propionylation of Fis K32 inFuture microbiology · 2025Article
- Article
- Post-translational modifications of the nucleoid protein H-NS: sites, mechanisms, and regulatory cues.FEMS microbiology reviews · 2025Review
- Macromolecular Crowding and DNA: Bridging the Gap between In Vitro and In Vivo.International journal of molecular sciences · 2023Review
- Review
- The Xenogeneic Silencer Histone-Like Nucleoid-Structuring Protein Mediates the Temperature and Salinity-Dependent Regulation of the Type III Secretion System 2 in Vibrio parahaemolyticus.Journal of bacteriology · 2023Article
- TheJournal of bacteriology · 2022Article
- Histone-like nucleoid structuring (H-NS) protein silences the beta-glucoside (Computational and structural biotechnology journal · 2022Article
- Molecular Basis for Environment Sensing by a Nucleoid-Structuring Bacterial Protein Filament.The journal of physical chemistry letters · 2021Article
- Xenogeneic silencing relies on temperature-dependent phosphorylation of the host H-NS protein in Shewanella.Nucleic acids research · 2021Article
- Impact of Self-Association on the Architectural Properties of Bacterial Nucleoid Proteins.Biophysical journal · 2021Article
- Regulation of gene expression by protein lysine acetylation in Salmonella.Journal of microbiology (Seoul, Korea) · 2020Review
- Redefining the H-NS protein family: a diversity of specialized core and accessory forms exhibit hierarchical transcriptional network integration.Nucleic acids research · 2020Article
- Epistatic Effect of Regulators to the Adaptive Growth of Escherichia coli.Scientific reports · 2020Article
- Measurement of the Promoter Activity inBio-protocol · 2020Article
- Impact of Chromosomal Architecture on the Function and Evolution of Bacterial Genomes.Frontiers in microbiology · 2018Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 2 institutions in 3 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
The bacterial nucleoid-associated protein H-NS is a DNA-binding protein, playing a major role in gene regulation. To regulate transcription, H-NS silences genes, including horizontally acquired foreign genes.
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.