Evidence map›Paper›PMID 32396821›Full record

ArticleMolecular cell2020

Crystal Structure of the LSD1/CoREST Histone Demethylase Bound to Its Nucleosome Substrate.

Sang-Ah Kim, Jiang Zhu, Neela Yennawar, Priit Eek, Song Tan

Open access · bronzeAbstract read
In one paragraph

Article in Molecular cell, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 66 papers.

0numbers the graph read from it
0cells of the map it votes in
66citing papers in PubMed
5.9field-weighted citation impact, top 3% 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

66 citing papers in PubMed, 109 citations in OpenAlex.

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  16. Histone demethylases in autophagy and inflammation.Cell communication and signaling : CCS · 2025
    Review
  17. Article
  18. Article
  19. Article
  20. Review

6 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

5 authors at 1 institution in 1 country.

Sang-Ah KimDepartment of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, The Pennsylvania State University, University Park, PA 16802, USA.
Jiang ZhuDepartment of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, The Pennsylvania State University, University Park, PA 16802, USA.
Neela YennawarHuck Institutes of the Life Sciences, The Pennsylvania State University, University Park, PA 16802, USA.
Priit EekDepartment of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, The Pennsylvania State University, University Park, PA 16802, USA.
Song TanDepartment of Biochemistry and Molecular Biology, Center for Eukaryotic Gene Regulation, The Pennsylvania State University, University Park, PA 16802, USA. Electronic address: sxt30@psu.edu.
Pennsylvania State University · US

Funding

User Training and OutreachP30GM124165 · NIGMS · CORNELL UNIVERSITY · PI MALCOLM S. CAPEL · 2018 to 2026
$34.2M
Structural studies of chromatin complexesR35GM127034 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI SONG TAN · 2018 to 2026
$4.8M
Structural Basis for RCC1 Directed Recruitment of Ran GTPase to ChromatinR01GM088236 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI TAN, SONG · 2009 to 2017
$2.5M
Pixel Array Detector for Macromolecular CrystallographyS10OD021527 · OD · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2016 to 2016
$2.0M
Pixel Array Detector for X-ray CrystallographyS10RR029205 · NCRR · CORNELL UNIVERSITY · PI EALICK, STEVEN E · 2010 to 2010
$1.8M
Molecular interactions of histone ubiquitylation enzymes with the nucleosomeR01GM111651 · NIGMS · PENNSYLVANIA STATE UNIVERSITY, THE · PI TAN, SONG · 2014 to 2017
$1.1M
NCRR NIH HHS S10 RR029205NIGMS NIH HHS P30 GM124165NIGMS NIH HHS R01 GM088236NIGMS NIH HHS R01 GM111651NIGMS NIH HHS R35 GM127034NIH HHS S10 OD021527
6 · The paper itself

Abstract

LSD1 (lysine specific demethylase; also known as KDM1A), the first histone demethylase discovered, regulates cell-fate determination and is overexpressed in multiple cancers. LSD1 demethylates histone H3 Lys4, an epigenetic mark for active genes, but requires the CoREST repressor to act on nucleosome substrates. To understand how an accessory subunit (CoREST) enables a chromatin enzyme (LSD1) to function on a nucleosome and not just histones, we have determined the crystal structure of the LSD1/CoREST complex bound to a 191-bp nucleosome. We find that the LSD1 catalytic domain binds extranucleosomal DNA and is unexpectedly positioned 100 Å away from the nucleosome core. CoREST makes critical contacts with both histone and DNA components of the nucleosome, explaining its essential function in demethylating nucleosome substrates. Our studies also show that the LSD1(K661A) frequently used as a catalytically inactive mutant in vivo (based on in vitro peptide studies) actually retains substantial H3K4 demethylase activity on nucleosome substrates.

Indexed as

Amino Acid SequenceCatalytic DomainChromatinCo-Repressor ProteinsCrystallography, X-RayDNAHistone DemethylasesHistonesHumansMethylationModels, MolecularNerve Tissue ProteinsNucleosomesPeptidesProtein BindingProtein ConformationChromatinCo-Repressor ProteinsDNAHistone DemethylasesHistonesKDM1A protein, humanNerve Tissue ProteinsNucleosomesPeptidesRCOR1 protein, humanchromatin biologyepigeneticsgene regulationhistone demethylationhistone modificationsnucleosome bindingX-ray crystallography

Identifiers

PMID32396821
PMCPMC7275924
OpenAlexW3022526195

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.