Evidence map›Paper›PMID 32193608›Full record

ReviewCellular and molecular life sciences : CMLS2020

Biological roles of LSD1 beyond its demethylase activity.

Feiying Gu, Yuxin Lin, Zhun Wang, Xiaoxin Wu, Zhenyue Ye, Yuezhen Wang, Huiyin Lan

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular life sciences : CMLS, 2020. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 69 papers.

0numbers the graph read from it
0cells of the map it votes in
69citing papers in PubMed
7.8field-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

69 citing papers in PubMed, 126 citations in OpenAlex.

  1. Review
  2. Article
  3. Article
  4. Review
  5. Article
  6. Article
  7. Article
  8. Article
  9. Review
  10. Synaptic Deficits in Adnp-Mutant Mice Are Ameliorated by Histone Demethylase LSD1 Inhibition.Autism research : official journal of the International Society for Autism Research · 2025
    Article
  11. Article
  12. Review
  13. Phase separation of RXRγ drives tumor chemoresistance and represents a therapeutic target for small-cell lung cancer.Proceedings of the National Academy of Sciences of the United States of America · 2025
    Article
  14. Article
  15. Article
  16. Role of lysine-specific demethylase 1 in immunotherapy of gastric cancer: An update.Chinese journal of cancer research = Chung-kuo yen cheng yen chiu · 2024
    Article
  17. Article
  18. Article
  19. Article
  20. Review

9 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

7 authors at 3 institutions in 1 country.

Feiying GuInstitute of Cancer and Basic Medicine (ICBM), Chinese Academy of Sciences, Hangzhou, China.
Yuxin LinDepartment of Oncology, Hospital of Chinese Medicine of Changxing County, Huzhou, 313100, China.
Zhun WangInstitute of Cancer and Basic Medicine (ICBM), Chinese Academy of Sciences, Hangzhou, China.
Xiaoxin WuState Key Laboratory for Diagnosis and Treatment of Infectious Diseases, National Clinical Research Center for Infectious Diseases, The First Affiliated Hospital, School of Medicine, Zhejiang University, Hangzhou, China.
Zhenyue YeDepartment of Respiratory Diseases, Hwa Mei Hospital, University of Chinese Academy Sciences, Ningbo, China.
Yuezhen WangInstitute of Cancer and Basic Medicine (ICBM), Chinese Academy of Sciences, Hangzhou, China. wangyz@zjcc.org.cn.
Huiyin LanInstitute of Cancer and Basic Medicine (ICBM), Chinese Academy of Sciences, Hangzhou, China. lanhuiyin@zju.edu.cn.ORCID http://orcid.org/0000-0002-7925-0066
Chinese Academy of Sciences · CNState Key Laboratory of Diagnosis and Treatment of Infectious DiseasesZhejiang Cancer Hospital · CN

Funding

Natural Science Foundation of Zhejiang Province 20160171
6 · The paper itself

Abstract

It is well-established that Lysine-specific demethylase 1 (LSD1, also known as KDM1A) roles as a lysine demethylase canonically acting on H3K4me1/2 and H3K9me1/2 for regulating gene expression. Though the discovery of non-histone substrates methylated by LSD1 has largely expanded the functions of LSD1 as a typical demethylase, recent groundbreaking studies unveiled its non-catalytic functions as a second life for this demethylase. We and others found that LSD1 is implicated in the interaction with a line of proteins to exhibit additional non-canonical functions in a demethylase-independent manner. Here, we present an integrated overview of these recent literatures charging LSD1 with unforeseen functions to re-evaluate and summarize its non-catalytic biological roles beyond the current understanding of its demethylase activity. Given LSD1 is reported to be ubiquitously overexpressed in a variety of tumors, it has been generally considered as an innovative target for cancer therapy. We anticipate that these non-canonical functions of LSD1 will arouse the consideration that extending the LSD1-based drug discovery to targeting LSD1 protein interactions non-catalytically, not only its demethylase activity, may be a novel strategy for cancer prevention.

Indexed as

AutophagyDemethylationF-Box-WD Repeat-Containing Protein 7Histone DemethylasesHistonesHumansNeoplasmsProteasome Endopeptidase ComplexSequestosome-1 ProteinUbiquitinationF-Box-WD Repeat-Containing Protein 7Histone DemethylasesHistonesKDM1A protein, humanProteasome Endopeptidase ComplexSequestosome-1 ProteinSQSTM1 protein, humanDemethylaseFBXW7LSD1Non-catalyticUbiquitylation

Identifiers

PMID32193608
PMCPMC11105033
OpenAlexW3011810360

What OpenQuestion holds

Textmetadata
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.