Evidence map›Paper›PMID 33432055›Full record

ArticleScientific reports2021

Linker histone defines structure and self-association behaviour of the 177 bp human chromatosome.

Sai Wang, Vinod K Vogirala, Aghil Soman, Nikolay V Berezhnoy, Zhehui Barry Liu, Andrew S W Wong, Nikolay Korolev, Chun-Jen Su, Sara Sandin, Lars Nordenskiöld

Open access · goldAbstract read
In one paragraph

Article in Scientific reports, 2021. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 21 papers.

0numbers the graph read from it
0cells of the map it votes in
21citing papers in PubMed
2.7field-weighted citation impact, top 9% 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

21 citing papers in PubMed, 36 citations in OpenAlex.

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  12. The Emerging Role of Chromatin Remodeling Complexes in Ovarian Cancer.International journal of molecular sciences · 2022
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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

10 authors at 2 institutions in 2 countries.

Sai WangSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Dr., Singapore, 637551, Singapore.
Vinod K VogiralaSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Dr., Singapore, 637551, Singapore.
Aghil SomanSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Dr., Singapore, 637551, Singapore.
Nikolay V BerezhnoySchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Dr., Singapore, 637551, Singapore.
Zhehui Barry LiuNTU Institute of Structural Biology, Nanyang Technological University, Singapore, 639798, Singapore.
Andrew S W WongNTU Institute of Structural Biology, Nanyang Technological University, Singapore, 639798, Singapore.
Nikolay KorolevSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Dr., Singapore, 637551, Singapore.
Chun-Jen SuNational Synchrotron Radiation Research Center, Hsinchu Science Park, Hsinchu, 30076, Taiwan.
Sara SandinSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Dr., Singapore, 637551, Singapore.
Lars NordenskiöldSchool of Biological Sciences, Nanyang Technological University, 60 Nanyang Dr., Singapore, 637551, Singapore. LarsNor@ntu.edu.sg.
Nanyang Technological University · SGNational Synchrotron Radiation Research Center · TW

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Linker histones play essential roles in the regulation and maintenance of the dynamic chromatin structure of higher eukaryotes. The influence of human histone H1.0 on the nucleosome structure and biophysical properties of the resulting chromatosome were investigated and compared with the 177-bp nucleosome using Cryo-EM and SAXS. The 4.5 Å Cryo-EM chromatosome structure showed that the linker histone binds at the nucleosome dyad interacting with both linker DNA arms but in a tilted manner leaning towards one of the linker sides. The chromatosome is laterally compacted and rigid in the dyad and linker DNA area, in comparison with the nucleosome where linker DNA region is more flexible and displays structural variability. In solution, the chromatosomes appear slightly larger than the nucleosomes, with the volume increase compared to the bound linker histone, according to solution SAXS measurements. SAXS X-ray diffraction characterisation of Mg-precipitated samples showed that the different shapes of the 177 chromatosome enabled the formation of a highly ordered lamello-columnar phase when precipitated by Mg

Indexed as

Base SequenceChromatinDNAHistonesHumansModels, MolecularNucleic Acid ConformationNucleosomesProtein BindingProtein MultimerizationProtein Structure, QuaternaryScattering, Small AngleX-Ray DiffractionChromatinDNAHistonesnuclear protein H1(0)Nucleosomes

Identifiers

PMID33432055
PMCPMC7801413
OpenAlexW3117770785

What OpenQuestion holds

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Registered trials

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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.