Evidence map›Paper›PMID 33318631›Full record

ReviewExperimental & molecular medicine2020

LSD1: more than demethylation of histone lysine residues.

Bruno Perillo, Alfonso Tramontano, Antonio Pezone, Antimo Migliaccio

Open access · goldAbstract readReview
In one paragraph

Review in Experimental & molecular medicine, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 107 papers, 1 of them a synthesis that pooled it.

0numbers the graph read from it
0cells of the map it votes in
107citing papers in PubMed, 1 pooled it
9.3field-weighted citation impact, top 1% 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

107 citing papers in PubMed, 1 synthesis or guideline pooled it, 202 citations in OpenAlex.

  1. Pooled it
  2. Review
  3. Review
  4. Article
  5. Review
  6. Targeting MYC-Driven Cancers: From Oncogenic Addiction to Therapeutic Vulnerability.BioDrugs : clinical immunotherapeutics, biopharmaceuticals and gene therapy · 2026
    Review
  7. Review
  8. Article
  9. Review
  10. Epigenetic treatment of synaptic and behavioral deficits in Dyrk1a-mutant mice.Neuropsychopharmacology : official publication of the American College of Neuropsychopharmacology · 2026
    Article
  11. Article
  12. Review
  13. Review
  14. Review
  15. Article
  16. Article
  17. Review
  18. Review
  19. Review
  20. Article

47 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

4 authors at 3 institutions in 1 country.

Bruno Perillo *Istituto per l'Endocrinologia e l'Oncologia Sperimentale "G. Salvatore" C.N.R, 80131, Naples, Italy. bruno.perillo@cnr.it.
Alfonso Tramontano *Dipartimento di Medicina di Precisione Università della Campania "L. Vanvitelli", 80138, Naples, Italy.
Antonio PezoneDipartimento di Medicina Molecolare e Biotecnologie Mediche Università Federico II, 80131, Naples, Italy. antoniopezone@gmail.com.
Antimo MigliaccioDipartimento di Medicina di Precisione Università della Campania "L. Vanvitelli", 80138, Naples, Italy.ORCID http://orcid.org/0000-0002-4197-2055
University of Campania "Luigi Vanvitelli" · ITCeinge Biotecnologie Avanzate (Italy) · ITInstitute for Experimental Endocrinology and Oncology · IT

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Lysine-specific histone demethylase 1 (LSD1) represents the first example of an identified nuclear protein with histone demethylase activity. In particular, it plays a special role in the epigenetic regulation of gene expression, as it removes methyl groups from mono- and dimethylated lysine 4 and/or lysine 9 on histone H3 (H3K4me1/2 and H3K9me1/2), behaving as a repressor or activator of gene expression, respectively. Moreover, it has been recently found to demethylate monomethylated and dimethylated lysine 20 in histone H4 and to contribute to the balance of several other methylated lysine residues in histone H3 (i.e., H3K27, H3K36, and H3K79). Furthermore, in recent years, a plethora of nonhistone proteins have been detected as targets of LSD1 activity, suggesting that this demethylase is a fundamental player in the regulation of multiple pathways triggered in several cellular processes, including cancer progression. In this review, we analyze the molecular mechanism by which LSD1 displays its dual effect on gene expression (related to the specific lysine target), placing final emphasis on the use of pharmacological inhibitors of its activity in future clinical studies to fight cancer.

Indexed as

Epigenesis, GeneticGene Expression RegulationAlternative SplicingAnimalsBiomarkers, TumorDemethylationHistone DemethylasesHistonesHumansLysineMolecular Targeted TherapyProtein BindingProtein Processing, Post-TranslationalProtein StabilityReceptors, Cytoplasmic and NuclearStructure-Activity RelationshipBiomarkers, TumorHistone DemethylasesHistonesKDM1A protein, humanLysineReceptors, Cytoplasmic and Nuclear

Identifiers

PMID33318631
PMCPMC8080763
OpenAlexW3111400820

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.