Evidence map›Paper›PMID 37679322›Full record

ReviewCell death discovery2023

USP32 deubiquitinase: cellular functions, regulatory mechanisms, and potential as a cancer therapy target.

Shuang Li, Yang Song, Kexin Wang, Guoxiang Liu, Xiaolei Dong, Fanghao Yang, Guang Chen, Can Cao, Huhu Zhang, Mengjun Wang and 4 more

Open access · goldAbstract readReview
In one paragraph

Review in Cell death discovery, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 27 papers.

0numbers the graph read from it
0cells of the map it votes in
27citing papers in PubMed
4.2field-weighted citation impact, top 5% 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

27 citing papers in PubMed, 27 citations in OpenAlex.

  1. Deubiquitination of Vangl by USP6 and USP32 Regulates Planar Cell Polarity Signaling.Advanced science (Weinheim, Baden-Wurttemberg, Germany) · 2026
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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 1 institution in 1 country.

Shuang LiDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Yang SongDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Kexin WangDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Guoxiang LiuDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Xiaolei DongDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Fanghao YangDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Guang ChenDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Can CaoDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Huhu ZhangDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Mengjun WangDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Ya LiDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Teng ZengDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China.
Chunyan LiuDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China. Liuchy@qdu.edu.cn.ORCID http://orcid.org/0000-0002-5893-8507
Bing LiDepartment of Genetics and Cell Biology, School of Basic Medicine, Qingdao University, Qingdao, China. libing_516619@163.com.ORCID http://orcid.org/0000-0002-8243-8705
Qingdao University · CN

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

An essential protein regulatory system in cells is the ubiquitin-proteasome pathway. The substrate is modified by the ubiquitin ligase system (E1-E2-E3) in this pathway, which is a dynamic protein bidirectional modification regulation system. Deubiquitinating enzymes (DUBs) are tasked with specifically hydrolyzing ubiquitin molecules from ubiquitin-linked proteins or precursor proteins and inversely regulating protein degradation, which in turn affects protein function. The ubiquitin-specific peptidase 32 (USP32) protein level is associated with cell cycle progression, proliferation, migration, invasion, and other cellular biological processes. It is an important member of the ubiquitin-specific protease family. It is thought that USP32, a unique enzyme that controls the ubiquitin process, is closely linked to the onset and progression of many cancers, including small cell lung cancer, gastric cancer, breast cancer, epithelial ovarian cancer, glioblastoma, gastrointestinal stromal tumor, acute myeloid leukemia, and pancreatic adenocarcinoma. In this review, we focus on the multiple mechanisms of USP32 in various tumor types and show that USP32 controls the stability of many distinct proteins. Therefore, USP32 is a key and promising therapeutic target for tumor therapy, which could provide important new insights and avenues for antitumor drug development. The therapeutic importance of USP32 in cancer treatment remains to be further proven. In conclusion, there are many options for the future direction of USP32 research.

Identifiers

PMID37679322
PMCPMC10485055
OpenAlexW4386498186

What OpenQuestion holds

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LicenceCC BY
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Registered trials

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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.