Evidence map›Paper›PMID 18456819›Full record

ArticleBiophysical journal2008

sNASP, a histone H1-specific eukaryotic chaperone dimer that facilitates chromatin assembly.

Ron M Finn, Kristen Browne, Kim C Hodgson, Juan Ausió

Erratum issuedOpen access · bronzeAbstract read
In one paragraph

Article in Biophysical journal, 2008. The graph could read no effect estimate from its abstract, so it casts no vote on the map. An erratum has been issued. Cited by 43 papers.

0numbers the graph read from it
0cells of the map it votes in
43citing papers in PubMed
2.6field-weighted citation impact, top 10% of its field
1 · What the graph read from it

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.

2 · The registry

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.

3 · Its place in the literature

Who cites it

43 citing papers in PubMed, 78 citations in OpenAlex.

  1. Article
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  3. Altered memory CCR6EBioMedicine · 2024
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  14. Article
  15. Article
  16. Article
  17. Maintenance of Epigenetic Information.Cold Spring Harbor perspectives in biology · 2016
    Review
  18. Article
  19. Article
  20. Chaperone-mediated chromatin assembly and transcriptional regulation in Xenopus laevis.The International journal of developmental biology · 2016
    Review
4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

4 authors at 1 institution in 1 country.

Ron M FinnDepartment of Biochemistry and Microbiology, University of Victoria, Petch Building, Victoria, BC V8W 3P6, Canada.
Kristen Browne
Kim C Hodgson
Juan Ausió
University of Victoria · CA

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

NASP has been described as a histone H1 chaperone in mammals. However, the molecular mechanisms involved have not yet been characterized. Here, we show that this protein is not only present in mammals but is widely distributed throughout eukaryotes both in its somatic and testicular forms. The secondary structure of the human somatic version consists mainly of clusters of alpha-helices and exists as a homodimer in solution. The protein binds nonspecifically to core histone H2A-H2B dimers and H3-H4 tetramers but only forms specific complexes with histone H1. The formation of the NASP-H1 complexes is mediated by the N- and C-terminal domains of histone H1 and does not involve the winged helix domain that is characteristic of linker histones. In vitro chromatin reconstitution experiments show that this protein facilitates the incorporation of linker histones onto nucleosome arrays and hence is a bona fide linker histone chaperone.

Indexed as

Chromatin Assembly and DisassemblyAnimalsAutoantigensBinding SitesChromatinComputer SimulationCross-Linking ReagentsDimerizationEukaryotic CellsHistonesHumansModels, ChemicalModels, MolecularMolecular ChaperonesNuclear ProteinsProtein BindingAutoantigensChromatinCross-Linking ReagentsHistonesMolecular ChaperonesNASP protein, humanNuclear Proteins

Identifiers

PMID18456819
PMCPMC2479616
OpenAlexW2095516078

What OpenQuestion holds

Textmetadata
Read underepoch 390

Registered trials

None linked

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.