Evidence map›Paper›PMID 32101746›Full record

ArticleCell reports2020

Mechanism of Crosstalk between the LSD1 Demethylase and HDAC1 Deacetylase in the CoREST Complex.

Yun Song, Lisbeth Dagil, Louise Fairall, Naomi Robertson, Mingxuan Wu, T J Ragan, Christos G Savva, Almutasem Saleh, Nobuhiro Morone, Micha B A Kunze and 4 more

Open access · goldAbstract read
In one paragraph

Article in Cell reports, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 92 papers.

0numbers the graph read from it
0cells of the map it votes in
92citing papers in PubMed
6.6field-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

92 citing papers in PubMed, 135 citations in OpenAlex.

  1. Review
  2. Article
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  6. Review
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  8. Article
  9. Review
  10. [Potential Mechanisms and Research Advances of HDAC1 in Lung Cancer].Zhongguo fei ai za zhi = Chinese journal of lung cancer · 2026
    Review
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
  16. Complex-specific HDAC1/2 regulation in the heart: insights from MiDAC disruption.American journal of physiology. Heart and circulatory physiology · 2026
    Article
  17. Article
  18. Article
  19. Article
  20. Article

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

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

14 authors at 6 institutions in 2 countries.

Yun SongLeicester Institute of Chemical and Molecular Biology, Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7RH, UK.
Lisbeth DagilInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower Street, London WC1E 6BT, UK.
Louise FairallLeicester Institute of Chemical and Molecular Biology, Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7RH, UK.
Naomi RobertsonDepartment of Chemistry, University of Leicester, University Road, Leicester LE1 7RH, UK.
Mingxuan WuDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
T J RaganLeicester Institute of Chemical and Molecular Biology, Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7RH, UK.
Christos G SavvaLeicester Institute of Chemical and Molecular Biology, Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7RH, UK.
Almutasem SalehLeicester Institute of Chemical and Molecular Biology, Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7RH, UK.
Nobuhiro MoroneMRC-Toxicology Unit, University of Cambridge, University Road, Leicester LE1 7RH, UK.
Micha B A KunzeInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower Street, London WC1E 6BT, UK.
Andrew G JamiesonDepartment of Chemistry, University of Leicester, University Road, Leicester LE1 7RH, UK.
Philip A ColeDivision of Genetics, Department of Medicine, Brigham and Women's Hospital and Department of Biological Chemistry and Molecular Pharmacology, Harvard Medical School, Boston, MA 02115, USA.
D Flemming HansenInstitute of Structural and Molecular Biology, Division of Biosciences, University College London, Gower Street, London WC1E 6BT, UK. Electronic address: d.hansen@ucl.ac.uk.
John W R SchwabeLeicester Institute of Chemical and Molecular Biology, Department of Molecular and Cell Biology, University of Leicester, Lancaster Road, Leicester LE1 7RH, UK. Electronic address: john.schwabe@le.ac.uk.
University of Leicester · GBInstitute of Structural and Molecular Biology · GBBrigham and Women's Hospital · USHarvard University · USMRC Toxicology Unit · GBUniversity College London · GB

Funding

Protein Acylation and Methylation Mechanisms_Administrative SupplementR37GM062437 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2013 to 2022
$4.1M
Mechanisms &Inhibition of Histone AcetyltransferasesR01GM062437 · NIGMS · JOHNS HOPKINS UNIVERSITY · PI COLE, PHILIP A · 2001 to 2012
$3.8M
Medical Research Council MC_PC_17136NIGMS NIH HHS R01 GM062437NIGMS NIH HHS R37 GM062437Wellcome Trust 055663/Z/98/ZWellcome Trust 100237Wellcome Trust 100237/Z/12/ZWellcome Trust 101569/Z/13/Z
6 · The paper itself

Abstract

The transcriptional corepressor complex CoREST is one of seven histone deacetylase complexes that regulate the genome through controlling chromatin acetylation. The CoREST complex is unique in containing both histone demethylase and deacetylase enzymes, LSD1 and HDAC1, held together by the RCOR1 scaffold protein. To date, it has been assumed that the enzymes function independently within the complex. Now, we report the assembly of the ternary complex. Using both structural and functional studies, we show that the activity of the two enzymes is closely coupled and that the complex can exist in at least two distinct states with different kinetics. Electron microscopy of the complex reveals a bi-lobed structure with LSD1 and HDAC1 enzymes at opposite ends of the complex. The structure of CoREST in complex with a nucleosome reveals a mode of chromatin engagement that contrasts with previous models.

Indexed as

AcetylationAmino Acid SequenceAnimalsCo-Repressor ProteinsCryoelectron MicroscopyDemethylationHEK293 CellsHistone Deacetylase 1Histone DemethylasesHumansKineticsModels, MolecularNerve Tissue ProteinsNucleosomesXenopusCo-Repressor ProteinsHDAC1 protein, humanHistone Deacetylase 1Histone DemethylasesKDM1A protein, humanNerve Tissue ProteinsNucleosomesRCOR1 protein, humanCoREST complexHDAC1histone deacetylaseKDM1ALSD1lysine demethylasenucleosomeRCOR1

Identifiers

PMID32101746
PMCPMC7043024
OpenAlexW3008324499

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.