Evidence map›Paper›PMID 37752518›Full record

ReviewJournal of translational medicine2023

Spotlights on ubiquitin-specific protease 12 (USP12) in diseases: from multifaceted roles to pathophysiological mechanisms.

Kaiyi Niu, Yanlong Shi, Qingpeng Lv, Yizhu Wang, Jiping Chen, Wenning Zhang, Kung Feng, Yewei Zhang

Open access · goldAbstract readReview
In one paragraph

Review in Journal of translational medicine, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.

0numbers the graph read from it
0cells of the map it votes in
9citing papers in PubMed
2.2field-weighted citation impact, top 12% 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

9 citing papers in PubMed, 14 citations in OpenAlex.

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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

8 authors at 1 institution in 1 country.

Kaiyi Niu *Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.
Yanlong Shi *Hepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.
Qingpeng LvHepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.
Yizhu WangHepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.
Jiping ChenHepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.
Wenning ZhangHepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.
Kung FengHepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China.
Yewei ZhangHepato-Pancreato-Biliary Center, The Second Affiliated Hospital of Nanjing Medical University, Nanjing, 210003, Jiangsu Province, China. zhangyewei@njmu.edu.cn.ORCID 0000-0002-8966-3833
Second Affiliated Hospital of Nanjing Medical University · CN

Funding

Foreword Leading Technology Fundamental Research Project of Jiangsu BK20212012Jiangsu Province Social Development Project BE2022812Major Program of the National Natural Science Foundation of China 62227803National Natural Science Foundation of China 62141109
6 · The paper itself

Abstract

Ubiquitination is one of the most significant post-translational modifications that regulate almost all physiological processes like cell proliferation, autophagy, apoptosis, and cell cycle progression. Contrary to ubiquitination, deubiquitination removes ubiquitin from targeted protein to maintain its stability and thus regulate cellular homeostasis. Ubiquitin-Specific Protease 12 (USP12) belongs to the biggest family of deubiquitinases named ubiquitin-specific proteases and has been reported to be correlated with various pathophysiological processes. In this review, we initially introduce the structure and biological functions of USP12 briefly and summarize multiple substrates of USP12 as well as the underlying mechanisms. Moreover, we discuss the influence of USP12 on tumorigenesis, tumor immune microenvironment (TME), disease, and related signaling pathways. This study also provides updated information on the roles and functions of USP12 in different types of cancers and other diseases, including prostate cancer, breast cancer, lung cancer, liver cancer, cardiac hypertrophy, multiple myeloma, and Huntington's disease. Generally, this review sums up the research advances of USP12 and discusses its potential clinical application value which deserves more exploration in the future.

Indexed as

Prostatic NeoplasmsApoptosisAutophagyCarcinogenesisHumansMaleTumor MicroenvironmentUbiquitin-Specific ProteasesUbiquitin ThiolesteraseUbiquitin-Specific ProteasesUbiquitin ThiolesteraseUSP12 protein, humanCancerDeubiquitinationImmune responseTumorigenesisUSP12

Identifiers

PMID37752518
PMCPMC10521459
OpenAlexW4387059008

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.