ArticleThe Journal of cell biology2010
Histone H1 phosphorylation is associated with transcription by RNA polymerases I and II.
Article in The Journal of cell biology, 2010. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 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.
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Who cites it
57 citing papers in PubMed, 107 citations in OpenAlex.
- Linker histone H1.5 contributes to centromere integrity.Nucleic acids research · 2026Article
- Histone modifications and metabolic reprogramming in tumor-associated macrophages: a potential target of tumor immunotherapy.Frontiers in immunology · 2025Review
- Article
- Proteomics and Phosphoproteomic Analysis to Identify Spleen of Takifugu rubripes Infected Cryptocaryon irritans.Marine biotechnology (New York, N.Y.) · 2023Article
- Histone variant-specific post-translational modifications.Seminars in cell & developmental biology · 2023Review
- Post-Translation Modifications and Mutations of Human Linker Histone Subtypes: Their Manifestation in Disease.International journal of molecular sciences · 2023Review
- Structural basis of RNA polymerase II transcription on the chromatosome containing linker histone H1.Nature communications · 2022Article
- Chromatin transitions triggered by LH density as epigenetic regulators of the genome.Nucleic acids research · 2022Article
- Phosphorylation-dependent association of human chromatin protein PC4 to linker histone H1 regulates genome organization and transcription.Nucleic acids research · 2022Article
- The Highest Density of Phosphorylated Histone H1 Appeared in Prophase and Prometaphase in Parallel with Reduced H3K9me3, and HDAC1 Depletion Increased H1.2/H1.3 and H1.4 Serine 38 Phosphorylation.Life (Basel, Switzerland) · 2022Article
- Single-stranded nucleic acid binding and coacervation by linker histone H1.Nature structural & molecular biology · 2022Article
- H1.0 C Terminal Domain Is Integral for Altering Transcription Factor Binding within Nucleosomes.Biochemistry · 2022Article
- Epigenetic Modifications in Tumor-Associated Macrophages: A New Perspective for an Old Foe.Frontiers in immunology · 2022Review
- Antagonising Chromatin Remodelling Activities in the Regulation of Mammalian Ribosomal Transcription.Genes · 2021Review
- Review
- Histone variants in skeletal myogenesis.Epigenetics · 2021Review
- Molecular and Cellular Functions of the Linker Histone H1.2.Frontiers in cell and developmental biology · 2021Review
- The missing linkGenes & development · 2021Review
- Site-Specific Phosphorylation of Histone H1.4 Is Associated with Transcription Activation.International journal of molecular sciences · 2020Article
- Histone H1 Post-Translational Modifications: Update and Future Perspectives.International journal of molecular sciences · 2020Review
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
10 authors at 5 institutions in 2 countries.
Funding
Abstract
Histone H1 phosphorylation affects chromatin condensation and function, but little is known about how specific phosphorylations impact the function of H1 variants in higher eukaryotes. In this study, we show that specific sites in H1.2 and H1.4 of human cells are phosphorylated only during mitosis or during both mitosis and interphase. Antisera generated to individual H1.2/H1.4 interphase phosphorylations reveal that they are distributed throughout nuclei and enriched in nucleoli. Moreover, interphase phosphorylated H1.4 is enriched at active 45S preribosomal RNA gene promoters and is rapidly induced at steroid hormone response elements by hormone treatment. Our results imply that site-specific interphase H1 phosphorylation facilitates transcription by RNA polymerases I and II and has an unanticipated function in ribosome biogenesis and control of cell growth. Differences in the numbers, structure, and locations of interphase phosphorylation sites may contribute to the functional diversity of H1 variants.
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.