Evidence map›Paper›PMID 28177778›Full record

ReviewBiochemistry and cell biology = Biochimie et biologie cellulaire2017

Linker histones: novel insights into structure-specific recognition of the nucleosome.

Amber R Cutter, Jeffrey J Hayes

Open access · greenAbstract readReview
In one paragraph

Review in Biochemistry and cell biology = Biochimie et biologie cellulaire, 2017. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 20 papers.

0numbers the graph read from it
0cells of the map it votes in
20citing papers in PubMed
1.7field-weighted citation impact, top 15% 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

20 citing papers in PubMed, 26 citations in OpenAlex.

  1. Article
  2. Article
  3. Article
  4. Review
  5. Review
  6. Review
  7. Article
  8. Identification and characterization of histones inNAR genomics and bioinformatics · 2021
    Article
  9. Unraveling linker histone interactions in nucleosomes.Current opinion in structural biology · 2021
    Review
  10. Review
  11. Article
  12. Article
  13. Article
  14. Article
  15. Article
  16. Targeting Chromatin Remodeling for Cancer Therapy.Current molecular pharmacology · 2019
    Review
  17. Article
  18. Review
  19. Review
  20. Article
4 · The record

Corrections and comments

PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.

5 · Who and what money

Authors and funding

2 authors at 1 institution in 1 country.

Amber R CutterDepartment of Biochemistry & Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USA.
Jeffrey J HayesDepartment of Biochemistry & Biophysics, University of Rochester Medical Center, Rochester, NY 14642, USA.
University of Rochester Medical Center · US

Funding

Histone Tall Interactions and Functions in ChromatinR01GM052426 · NIGMS · UNIVERSITY OF ROCHESTER · PI HAYES, JEFFREY J · 1995 to 2021
$6.2M
Training in Cellular, Biochemical and Molecular SciencesT32GM068411 · NIGMS · UNIVERSITY OF ROCHESTER · PI MAQUAT, LYNNE E · 2005 to 2019
$3.9M
NIGMS NIH HHS R01 GM052426NIGMS NIH HHS T32 GM068411
6 · The paper itself

Abstract

Linker histones (H1s) are a primary component of metazoan chromatin, fulfilling numerous functions, both in vitro and in vivo, including stabilizing the wrapping of DNA around the nucleosome, promoting folding and assembly of higher order chromatin structures, influencing nucleosome spacing on DNA, and regulating specific gene expression. However, many molecular details of how H1 binds to nucleosomes and recognizes unique structural features on the nucleosome surface remain undefined. Numerous, confounding studies are complicated not only by experimental limitations, but the use of different linker histone isoforms and nucleosome constructions. This review summarizes the decades of research that has resulted in several models of H1 association with nucleosomes, with a focus on recent advances that suggest multiple modes of H1 interaction in chromatin, while highlighting the remaining questions.

Indexed as

Chromatin Assembly and DisassemblyAmino Acid SequenceAnimalsCaenorhabditis elegansChickensDNAGene Expression RegulationHistonesHumansMiceModels, MolecularNucleosomesPhylogenyProtein BindingProtein IsoformsProtein Structure, SecondaryDNAHistonesNucleosomesProtein IsoformsADNDNAhistone de liaisonlinker histonenucleosomenucléosome

Identifiers

PMID28177778
PMCPMC5654525
OpenAlexW2473503437

What OpenQuestion holds

Textmetadata
LicenceTDM
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.