ReviewBiochemistry and cell biology = Biochimie et biologie cellulaire2011
Structure of the H1 C-terminal domain and function in chromatin condensation.
Review in Biochemistry and cell biology = Biochimie et biologie cellulaire, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 56 papers.
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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.
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Who cites it
56 citing papers in PubMed.
- Linker histone H1 functions as a liquid-like glue to organize chromatin in living human cells.Science advances · 2026Article
- The linker histone chaperone Prothymosin α (PTMA) is essential for efficient DNA damage repair and the recruitment of PARP1.Epigenetics & chromatin · 2025Article
- Sperm-specific histone H1 in highly condensed sperm nucleus of Sargassum horneri.Scientific reports · 2024Article
- Development of a mouse embryonic stem cell model for investigating the functions of the linker histone H1-4.FEBS open bio · 2024Article
- Dynamic action of an intrinsically disordered protein in DNA compaction that induces mycobacterial dormancy.Nucleic acids research · 2024Article
- Single-molecule study reveals Hmo1, not Hho1, promotes chromatin assembly in budding yeast.mBio · 2023Article
- H1.0 C Terminal Domain Is Integral for Altering Transcription Factor Binding within Nucleosomes.Biochemistry · 2022Article
- Epigenetic Activation of Silent Biosynthetic Gene Clusters in Endophytic Fungi Using Small Molecular Modifiers.Frontiers in microbiology · 2022Review
- Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021Review
- DNA sequence-dependent positioning of the linker histone in a nucleosome: A single-pair FRET study.Biophysical journal · 2021Article
- Characterization of functional disordered regions within chromatin-associated proteins.iScience · 2021Review
- Distinct Structures and Dynamics of Chromatosomes with Different Human Linker Histone Isoforms.Molecular cell · 2021Article
- Mapping Influenza-Induced Posttranslational Modifications on Histones from CD8+ T Cells.Viruses · 2020Article
- Alternative linker histone permits fast paced nuclear divisions in early Drosophila embryo.Nucleic acids research · 2020Article
- White spot syndrome viral protein VP9 alters the cellular higher-order chromatin structure.FASEB bioAdvances · 2020Article
- Mesoscale modeling reveals formation of an epigenetically driven HOXC gene hub.Proceedings of the National Academy of Sciences of the United States of America · 2019Article
- Significance of avian linker histone (H1) polymorphic variation.Journal of biosciences · 2018Review
- Dynamic placement of the linker histone H1 associated with nucleosome arrangement and gene transcription in early Drosophila embryonic development.Cell death & disease · 2018Article
- Chromatin Fiber Folding Directed by Cooperative Histone Tail Acetylation and Linker Histone Binding.Biophysical journal · 2018Article
- Dependence of the Linker Histone and Chromatin Condensation on the Nucleosome Environment.The journal of physical chemistry. B · 2017Article
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2 authors.
Funding
Abstract
Linker histones are multifunctional proteins that are involved in a myriad of processes ranging from stabilizing the folding and condensation of chromatin to playing a direct role in regulating gene expression. However, how this class of enigmatic proteins binds in chromatin and accomplishes these functions remains unclear. Here we review data regarding the H1 structure and function in chromatin, with special emphasis on the C-terminal domain (CTD), which typically encompasses approximately half of the mass of the linker histone and includes a large excess of positively charged residues. Owing to its amino acid composition, the CTD was previously proposed to function in chromatin as an unstructured polycation. However, structural studies have shown that the CTD adopts detectable secondary structure when interacting with DNA and macromolecular crowding agents. We describe classic and recent experiments defining the function of this domain in chromatin folding and emerging data indicating that the function of this protein may be linked to intrinsic disorder.
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