Evidence map›Paper›PMID 38651282›Full record

ReviewCancer science2024

USP3: Key deubiquitylation enzyme in human diseases.

Hongyan Zhang, Wenjing Liu, Yingying Wu, Ceshi Chen

Open access · goldAbstract readReview
In one paragraph

Review in Cancer science, 2024. 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
2.8field-weighted citation impact, top 9% 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, 12 citations in OpenAlex.

  1. Article
  2. Review
  3. Review
  4. Article
  5. Research progress of DUB enzyme in breast cancer.Clinical and experimental medicine · 2025
    Review
  6. Review
  7. Article
  8. Characterization of Isolated Human Astrocytes from Aging Brain.International journal of molecular sciences · 2025
    Article
  9. Review
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.

Hongyan ZhangFaculty of Life Science and Technology, Kunming University of Science and Technology, Kunming, China.
Wenjing LiuThe Third Affiliated Hospital, Kunming Medical University, Kunming, China.ORCID https://orcid.org/0000-0001-5081-9047
Yingying WuThe First Affiliated Hospital, Kunming Medical University, Kunming, China.
Ceshi ChenThe Third Affiliated Hospital, Kunming Medical University, Kunming, China.ORCID https://orcid.org/0000-0001-6398-3516
Kunming Medical University · CNKunming University of Science and Technology · CN

Funding

Biomedical Projects of Yunnan Key Science and Technology Program 202302AA310046China Postdoctoral Science Foundation 2023M731448National Natural Science Foundation of China 82060548National Natural Science Foundation of China U2102203the National Key R&D Program of China 2020YFA0112300Yunnan Fundamental Research Projects 202101AS070050Yunnan (Kunming) Science and Technology Department of Yunnan Province 202101AY070001-083
6 · The paper itself

Abstract

Ubiquitination and deubiquitylation are pivotal posttranslational modifications essential for regulating cellular protein homeostasis and are implicated in the development of human diseases. Ubiquitin-specific protease 3 (USP3), a member of the ubiquitin-specific protease family, serves as a key deubiquitylation enzyme, playing a critical role in diverse cellular processes including the DNA damage response, cell cycle regulation, carcinogenesis, tumor cell proliferation, migration, and invasion. Despite notable research efforts, our current understanding of the intricate and context-dependent regulatory networks governing USP3 remains incomplete. This review aims to comprehensively synthesize existing published works on USP3, elucidating its multifaceted roles, functions, and regulatory mechanisms, while offering insights for future investigations. By delving into the complexities of USP3, this review strives to provide a foundation for a more nuanced understanding of its specific roles in various cellular processes. Furthermore, the exploration of USP3's regulatory networks may uncover novel therapeutic strategies targeting this enzyme in diverse human diseases, thereby holding promising clinical implications. Overall, an in-depth comprehension of USP3's functions and regulatory pathways is crucial for advancing our knowledge and developing targeted therapeutic approaches for human diseases.

Indexed as

NeoplasmsUbiquitinationUbiquitin-Specific ProteasesAnimalsCarcinogenesisCell ProliferationDNA DamageHumansProtein Processing, Post-TranslationalUbiquitin-Specific ProteasesUSP3 protein, humancancerdeubiquitylationDNA damageposttranslation modificationUSP3

Identifiers

PMID38651282
PMCPMC11247611
OpenAlexW4395042990

What OpenQuestion holds

Textmetadata
LicenceCC BY-NC
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.