Evidence map›Paper›PMID 26305776›Full record

ArticleNature communications2015

Generation of a synthetic GlcNAcylated nucleosome reveals regulation of stability by H2A-Thr101 GlcNAcylation.

Lukas Lercher, Ritu Raj, Nisha A Patel, Joshua Price, Shabaz Mohammed, Carol V Robinson, Christopher J Schofield, Benjamin G Davis

Open access · goldAbstract read
In one paragraph

Article in Nature communications, 2015. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 31 papers.

0numbers the graph read from it
0cells of the map it votes in
31citing papers in PubMed
3.9field-weighted citation impact, top 6% 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

31 citing papers in PubMed, 59 citations in OpenAlex.

  1. Review
  2. Maternal O-GlcNAc Transferase Is Required for the Asymmetry of Epigenetic Modifications in Mouse Zygotes.FASEB journal : official publication of the Federation of American Societies for Experimental Biology · 2026
    Article
  3. Review
  4. Article
  5. Review
  6. Review
  7. Writing and erasing O-GlcNAc from target proteins in cells.Biochemical Society transactions · 2021
    Article
  8. Review
  9. Review
  10. Review
  11. Advances in chemical probing of proteinChemical Society reviews · 2021
    Review
  12. Review
  13. Article
  14. Article
  15. Review
  16. Frontiers in genetics · 2020
    Review
  17. Review
  18. Article
  19. 'Molecules (Basel, Switzerland) · 2018
    Review
  20. Review
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

8 authors at 1 institution in 1 country.

Lukas LercherDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK.
Ritu RajDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK.
Nisha A PatelDepartment of Chemistry, University of Oxford, Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ, UK.
Joshua PriceDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK.
Shabaz MohammedDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK.
Carol V RobinsonDepartment of Chemistry, University of Oxford, Physical and Theoretical Chemistry Laboratory, South Parks Road, Oxford OX1 3QZ, UK.
Christopher J SchofieldDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK.
Benjamin G DavisDepartment of Chemistry, University of Oxford, Chemistry Research Laboratory, Mansfield Road, Oxford OX1 3TA, UK.
University of Oxford · GB

Funding

Biotechnology and Biological Sciences Research Council BB/E004350/1Biotechnology and Biological Sciences Research Council EGA17763Cancer Research UK 18245Wellcome TrustWellcome Trust 088150/B/09/Z
6 · The paper itself

Abstract

O-GlcNAcylation is a newly discovered histone modification implicated in transcriptional regulation, but no structural information on the physical effect of GlcNAcylation on chromatin exists. Here, we generate synthetic, pure GlcNAcylated histones and nucleosomes and reveal that GlcNAcylation can modulate structure through direct destabilization of H2A/H2B dimers in the nucleosome, thus promoting an 'open' chromatin state. The results suggest that a plausible molecular basis for one role of histone O-GlcNAcylation in epigenetic regulation is to lower the barrier for RNA polymerase passage and hence increase transcription.

Indexed as

Gene Expression RegulationHistone CodeAcetylglucosamineAnimalsChromatinChromatin ImmunoprecipitationChromatography, LiquidCircular DichroismDimerizationDNA-Directed RNA PolymerasesElectrophoresisEpigenesis, GeneticHistonesMass SpectrometryN-AcetylglucosaminyltransferasesNucleosomesAcetylglucosamineChromatinDNA-Directed RNA PolymerasesHistonesN-AcetylglucosaminyltransferasesNucleosomesThreonine

Identifiers

PMID26305776
PMCPMC4560749
OpenAlexW1925680595

What OpenQuestion holds

Textmetadata
LicenceCC BY
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.