Evidence map›Paper›PMID 26455956›Full record

ReviewBiochimica et biophysica acta2016

Linker histone H1 and protein-protein interactions.

Anna A Kalashnikova, Ryan A Rogge, Jeffrey C Hansen

Abstract readReview
In one paragraph

Review in Biochimica et biophysica acta, 2016. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 35 papers.

0numbers the graph read from it
0cells of the map it votes in
35citing papers in PubMed
–field-weighted citation impact
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

35 citing papers in PubMed.

  1. Article
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  4. Article
  5. Review
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  8. Review
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  15. Article
  16. Article
  17. The role of the DFF40/CAD endonuclease in genomic stability.Apoptosis : an international journal on programmed cell death · 2021
    Review
  18. Silencing the genome with linker histones.Proceedings of the National Academy of Sciences of the United States of America · 2020
    Article
  19. Article
  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

3 authors.

Anna A KalashnikovaDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA.
Ryan A RoggeDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA.
Jeffrey C HansenDepartment of Biochemistry and Molecular Biology, Colorado State University, Fort Collins, CO 80523-1870, USA. Electronic address: Jeffrey.C.Hansen@colostate.edu.

Funding

CHROMATIN STRUCTURE AND STABILITY IN THE SOLUTION STATER01GM045916 · NIGMS · UNIVERSITY OF TEXAS HLTH SCI CTR SAN ANT · PI HANSEN, JEFFREY C · 1996 to 2012
$3.3M
NIGMS NIH HHS R01 GM045916
6 · The paper itself

Abstract

Linker histones H1 are ubiquitous chromatin proteins that play important roles in chromatin compaction, transcription regulation, nucleosome spacing and chromosome spacing. H1 function in DNA and chromatin structure stabilization is well studied and established. The current paradigm of linker histone mode of function considers all other cellular roles of linker histones to be a consequence from H1 chromatin compaction and repression. Here we review the multiple processes regulated by linker histones and the emerging importance of protein interactions in H1 functioning. We propose a new paradigm which explains the multi functionality of linker histones through linker histones protein interactions as a way to directly regulate recruitment of proteins to chromatin.

Indexed as

AmyloidAnimalsHistonesHumansPhosphorylationProtein FoldingProtein Structure, SecondaryProtein Structure, TertiaryAmyloidHistonesChromatinGenomeIntrinsic disordermRNA splicingNucleolusNucleosomeTranscription

Identifiers

PMID26455956
PMCPMC4775371

What OpenQuestion holds

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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.