Evidence map›Paper›PMID 38939997›Full record

ReviewCurrent medicinal chemistry2025

The Magic and Mystery of TRIM65 in Diseases.

Qinyi Zhou, Yuan Li, Zhixiang Zhou, Yiren Zhou, Yizhou Liu, Wang Liu, Xiaofeng Ma

Abstract readReview
PubMed Publisher
In one paragraph

Review in Current medicinal chemistry, 2025. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 2 papers.

0numbers the graph read from it
0cells of the map it votes in
2citing papers in PubMed
–field-weighted citation impact
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

2 citing papers in PubMed.

  1. Ubiquitin E3 Ligases and p53 in Doxorubicin-Induced Cardiotoxicity.International journal of molecular sciences · 2025
    Review
  2. 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

7 authors.

Qinyi ZhouDepartment of Cardiology, The Affiliated Nanhua Hospital, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.
Yuan LiHealth School of Nuclear Industry, The Affiliated Nanhua Hospital, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.
Zhixiang ZhouKey Laboratory for Arteriosclerology of Hunan Province, Institute of Cardiovascular Disease, Hunan International Scientific and Technological Cooperation Base of Arteriosclerotic Disease, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.
Yiren ZhouDepartment of Cardiology, The Affiliated Nanhua Hospital, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.
Yizhou LiuDepartment of Cardiology, The Affiliated Nanhua Hospital, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.
Wang LiuDepartment of Gastrointestinal Surgery, The Affiliated Nanhua Hospital, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.
Xiaofeng MaDepartment of Cardiology, The Affiliated Nanhua Hospital, Hengyang Medical School, University of South China, Hengyang, 421001, Hunan, China.

Funding

Clinical Medical Research Center of Hunan 2020SK4007Hunan Provincial Health Commission General Guidance project D202303016868Key Guidance Program of the Health Commission of Hunan Province 20201905Major Scientific Research Project of Health High-Level Talents in Hunan Province R2023068
6 · The paper itself

Abstract

Tripartite-motif protein family member 65 (TRIM65) belongs to the tripartite motif (TRIM) protein family. Its typical structure consists of the RING, B-Box motif, and coiled-coil domains, which are highly conserved at the N-terminus and the variable SPRY domain at the C-terminus. TRIM65 is an E3 ubiquitin ligase that participates in physiological and pathological processes through the ubiquitination pathway, including intracellular signal transduction, protein degradation, cell proliferation, apoptosis, carcinogenesis, autophagy, and phenotypic transformation. Evidence shows that TRIM65 plays a remarkable and obscure role in diseases, including multisystem tumours, neurodegenerative diseases, immune system diseases, and inflammatory diseases. This review is devoted to elaborating on the relationship between TRIM65 and diseases and its pathogenic mechanism, providing a theoretical basis for TRIM65 as a possible pathogenic target of diseases and exploring the possible future research direction of TRIM65 and the challenges it may face.

Indexed as

NeoplasmsNeurodegenerative DiseasesTripartite Motif ProteinsUbiquitin-Protein LigasesAnimalsHumansImmune System DiseasesInflammationTRIM65 protein, humanTripartite Motif ProteinsUbiquitin-Protein LigasesatherosclerosisE3 ubiquitin ligaseTRIM65tumourubiquitinationubiquitin-proteasome system.

Identifiers

PMID38939997

What OpenQuestion holds

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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.