ArticleThe Journal of biological chemistry2008
A thermodynamic model for Nap1-histone interactions.
Article in The Journal of biological chemistry, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 62 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
62 citing papers in PubMed, 95 citations in OpenAlex.
- Nucleosome Assembly Protein 1 in Dinoflagellate Cells Without Architectural Nucleosomes.International journal of molecular sciences · 2026Article
- Structural basis for HIV-1 Rev recognition by the histone chaperone human Nap1.The Journal of biological chemistry · 2026Article
- Roles of histone chaperone Nap1 and histone acetylation in regulating phase-separation of nucleosome arrays.Nature communications · 2025Article
- Stepwise order in protein complex assembly: approaches and emerging themes.Open biology · 2025Review
- Glutamylation of Npm2 and Nap1 acidic disordered regions increases DNA mimicry and histone chaperone efficiency.iScience · 2024Article
- Histone chaperone Nap1 dismantles an H2A/H2B dimer from a partially unwrapped nucleosome.Nucleic acids research · 2023Article
- Histone variants and chromatin structure, update of advances.Computational and structural biotechnology journal · 2023Review
- Dynamic structures of intrinsically disordered proteins related to the general transcription factor TFIIH, nucleosomes, and histone chaperones.Biophysical reviews · 2022Review
- Nucleus size and its effect on nucleosome stability in living cells.Biophysical journal · 2022Article
- Nucleosome Assembly Protein 1, Nap1, Is Required for the Growth, Development, and Pathogenicity ofInternational journal of molecular sciences · 2022Article
- Structural comparisons reveal diverse binding modes between nucleosome assembly proteins and histones.Epigenetics & chromatin · 2022Review
- Histone chaperone-mediated co-expression assembly of tetrasomes and nucleosomes.FEBS open bio · 2021Article
- Nucleosome Dynamics during Transcription Elongation.ACS chemical biology · 2020Article
- Comprehensive analysis of histone-binding proteins with multi-angle light scattering.Methods (San Diego, Calif.) · 2020Article
- Tsr4 and Nap1, two novel members of the ribosomal protein chaperOME.Nucleic acids research · 2019Article
- Structural insights into the ability of nucleoplasmin to assemble and chaperone histone octamers for DNA deposition.Scientific reports · 2019Article
- Importin-9 wraps around the H2A-H2B core to act as nuclear importer and histone chaperone.eLife · 2019Article
- Article
- DNA repair factor APLF acts as a H2A-H2B histone chaperone through binding its DNA interaction surface.Nucleic acids research · 2018Article
- A Screen for Epstein-Barr Virus Proteins That Inhibit the DNA Damage Response Reveals a Novel Histone Binding Protein.Journal of virology · 2018Article
2 more citing papers are in PubMed but not listed here.
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 2 institutions in 1 country.
Funding
Abstract
The yeast nucleosome assembly protein 1 (yNap1) plays a role in chromatin maintenance by facilitating histone exchange as well as nucleosome assembly and disassembly. It has been suggested that yNap1 carries out these functions by regulating the concentration of free histones. Therefore, a quantitative understanding of yNap1-histone interactions also provides information on the thermodynamics of chromatin. We have developed quantitative methods to study the affinity of yNap1 for histones. We show that yNap1 binds H2A/H2B and H3/H4 histone complexes with low nm affinity, and that each yNap1 dimer binds two histone fold dimers. The yNap1 tails contribute synergistically to histone binding while the histone tails have a slightly repressive effect on binding. The (H3/H4)(2) tetramer binds DNA with higher affinity than it binds yNap1.
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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.