Evidence map›Paper›PMID 16462749›Full record

ArticleNature structural & molecular biology2006

Mapping the interaction surface of linker histone H1(0) with the nucleosome of native chromatin in vivo.

David T Brown, Tina Izard, Tom Misteli

Erratum issuedOpen access · greenAbstract read
In one paragraph

Article in Nature structural & molecular biology, 2006. 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 105 papers.

0numbers the graph read from it
0cells of the map it votes in
105citing papers in PubMed
7.1field-weighted citation impact, top 2% 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

105 citing papers in PubMed, 193 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Article
  5. Article
  6. Article
  7. Article
  8. Article
  9. Article
  10. Article
  11. Histone variants and chromatin structure, update of advances.Computational and structural biotechnology journal · 2023
    Review
  12. Article
  13. Review
  14. Liquid-Liquid Phase Separation in Chromatin.Cold Spring Harbor perspectives in biology · 2022
    Review
  15. Article
  16. Article
  17. Review
  18. Article
  19. Article
  20. Review

45 more citing papers are in PubMed but not listed here.

4 · The record

Corrections and comments

  • Erratum issued
5 · Who and what money

Authors and funding

3 authors at 3 institutions in 1 country.

David T BrownDepartment of Biochemistry, University of Mississippi Medical Center, Jackson, Mississippi 39216, USA.
Tina Izard
Tom Misteli
National Cancer Institute · USSt. Jude Children's Research Hospital · USUniversity of Mississippi Medical Center · US

Funding

TOUGALOO PROTEOMICSP20RR016476 · NCRR · UNIVERSITY OF SOUTHERN MISSISSIPPI · PI SHEARER, GLEN · 2001 to 2011
$30.4M
Nuclear architecture and gene expression Z01BC010309 · NCI · DIVISION OF BASIC SCIENCES - NCI · PI MISTELI, THOMAS A · 1999 to 2008
$3.6M
Intramural NIH HHSNCI NIH HHS Z01 BC010309-07NCRR NIH HHS P20 RR016476NCRR NIH HHS RR016476
6 · The paper itself

Abstract

H1 linker histones stabilize the nucleosome, limit nucleosome mobility and facilitate the condensation of metazoan chromatin. Here, we have combined systematic mutagenesis, measurement of in vivo binding by photobleaching microscopy, and structural modeling to determine the binding geometry of the globular domain of the H1(0) linker histone variant within the nucleosome in unperturbed, native chromatin in vivo. We demonstrate the existence of two distinct DNA-binding sites within the globular domain that are formed by spatial clustering of multiple residues. The globular domain is positioned via interaction of one binding site with the major groove near the nucleosome dyad. The second site interacts with linker DNA adjacent to the nucleosome core. Multiple residues bind cooperatively to form a highly specific chromatosome structure that provides a mechanism by which individual domains of linker histones interact to facilitate chromatin condensation.

Indexed as

Amino Acid SequenceAnimalsBALB 3T3 CellsBinding SitesFluorescence Recovery After PhotobleachingHistonesMiceModels, MolecularMolecular Sequence DataMutationNucleosomesProtein BindingProtein Interaction MappingRecombinant Fusion ProteinsHistonesNucleosomesRecombinant Fusion Proteins

Identifiers

PMID16462749
PMCPMC1868459
OpenAlexW2128254777

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.