Evidence map›Paper›PMID 30497519›Full record

ArticleBiological research2018

The deubiquitinase USP38 affects cellular functions through interacting with LSD1.

Wenbin Liu, Qi Zhang, Yuanyuan Fang, Yanan Wang

Open access · goldAbstract read
In one paragraph

Article in Biological research, 2018. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 15 papers.

0numbers the graph read from it
0cells of the map it votes in
15citing papers in PubMed
0.6field-weighted citation impact, top 33% 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

15 citing papers in PubMed, 25 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Review
  5. Strategies that regulate LSD1 for novel therapeutics.Acta pharmaceutica Sinica. B · 2024
    Review
  6. Review
  7. Article
  8. Article
  9. Ubiquitin-specific protease 38 promotes inflammatory atrial fibrillation induced by pressure overload.Europace : European pacing, arrhythmias, and cardiac electrophysiology : journal of the working groups on cardiac pacing, arrhythmias, and cardiac cellular electrophysiology of the European Society of Cardiology · 2023
    Article
  10. Article
  11. Review
  12. Article
  13. Article
  14. Article
  15. Article
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 2 institutions in 1 country.

Wenbin LiuHubei Key Laboratory of Animal Nutrition and Feed Science, Wuhan Polytechnic University, Wuhan, Hubei, China. liuwenbin_1@yeah.net.
Qi ZhangCollege of Life Sciences, Wuhan University, Wuhan, Hubei, China.
Yuanyuan FangCollege of Health Sciences and Nursing, Wuhan Polytechnic University, No. 68 Southern Xuefu Road, Wuhan, 430023, Hubei, China.
Yanan WangCollege of Health Sciences and Nursing, Wuhan Polytechnic University, No. 68 Southern Xuefu Road, Wuhan, 430023, Hubei, China.
Wuhan Polytechnic University · CNWuhan University · CN

Funding

Hubei Key Laboratory of Animal Nutrition and Feed Science 201810
6 · The paper itself

Abstract

backgroundDeubiquitination is a posttranslational protein modification prevalent in mammalian cells. Deubiquitinases regulate the functions of the target protein by removing its ubiquitin chain. In this study, the effects of the deubiquitinase USP38's functions on the LSD1 protein and on cell physiology were investigated. MATERIALS AND

methodsWestern blotting, real-time quantitative PCR, immunoprecipitation, denaturing immunoprecipitation and luciferase reporter assays were used to analyze the protein stability, protein interactions and changes in the ubiquitin chain. Cell proliferation assays, colony formation assays, drug treatments and western blotting were used to explore the functions of USP38 in cells.

resultsThe deubiquitinase USP38 stabilizes protein LSD1 in cells by binding LSD1 and cleaving its ubiquitin chain to prevent the degradation of LSD1 by the intracellular proteasome. USP38 enhances the ability of LSD1 to activate signaling pathways and hence promotes cellular abilities of proliferation and colony formation through interacting with LSD1. Furthermore, USP38 enhances the drug tolerance of human colon cancer cells.

conclusionsUSP38 is an LSD1-specific deubiquitinase that affects cellular physiology through interacting with LSD1.

Indexed as

ApoptosisBlotting, WesternCell ProliferationCells, CulturedColony-Forming Units AssayHistone DemethylasesHumansImmunoprecipitationReal-Time Polymerase Chain ReactionSignal TransductionUbiquitin-Specific ProteasesHistone DemethylasesKDM1A protein, humanUbiquitin-Specific ProteasesUSP38 protein, humanDeubiquitinaseLSD1ProliferationUSP38

Identifiers

PMID30497519
PMCPMC6263071
OpenAlexW2902766220

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.