Evidence map›Paper›PMID 36988770›Full record

ReviewCellular and molecular neurobiology2023

Tripartite Motif Protein Family in Central Nervous System Diseases.

Mengtian Pan, Xiang Li, Guangchen Xu, Xinjuan Tian, Yunman Li, Weirong Fang

Open access · greenAbstract readReview
In one paragraph

Review in Cellular and molecular neurobiology, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.

0numbers the graph read from it
0cells of the map it votes in
7citing papers in PubMed
2.6field-weighted citation impact, top 10% 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

7 citing papers in PubMed, 16 citations in OpenAlex.

  1. The Roles of E3 Ubiquitin Ligases in Cerebral Ischemia-Reperfusion Injury.International journal of molecular sciences · 2025
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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

6 authors at 1 institution in 1 country.

Mengtian PanState Key Laboratory of Natural Medicines, School of Basic Medical Sciences and Clinical Pharmacy, China Pharmaceutical University, Tongjiaxiang 24, Nanjing, Jiangsu, 210009, People's Republic of China.ORCID https://orcid.org/0000-0001-5560-0300
Xiang LiState Key Laboratory of Natural Medicines, School of Basic Medical Sciences and Clinical Pharmacy, China Pharmaceutical University, Tongjiaxiang 24, Nanjing, Jiangsu, 210009, People's Republic of China.ORCID https://orcid.org/0000-0002-4855-0701
Guangchen XuState Key Laboratory of Natural Medicines, School of Basic Medical Sciences and Clinical Pharmacy, China Pharmaceutical University, Tongjiaxiang 24, Nanjing, Jiangsu, 210009, People's Republic of China.ORCID https://orcid.org/0000-0003-0325-974X
Xinjuan TianState Key Laboratory of Natural Medicines, School of Basic Medical Sciences and Clinical Pharmacy, China Pharmaceutical University, Tongjiaxiang 24, Nanjing, Jiangsu, 210009, People's Republic of China.ORCID https://orcid.org/0000-0002-9049-0415
Yunman LiState Key Laboratory of Natural Medicines, School of Basic Medical Sciences and Clinical Pharmacy, China Pharmaceutical University, Tongjiaxiang 24, Nanjing, Jiangsu, 210009, People's Republic of China. liyunman@cpu.edu.cn.ORCID https://orcid.org/0000-0001-5565-3322
Weirong FangState Key Laboratory of Natural Medicines, School of Basic Medical Sciences and Clinical Pharmacy, China Pharmaceutical University, Tongjiaxiang 24, Nanjing, Jiangsu, 210009, People's Republic of China. weirongfang@cpu.edu.cn.ORCID https://orcid.org/0000-0002-0169-576X
China Pharmaceutical University · CN

Funding

National Natural Science Foundation of China 82073845National Natural Science Foundation of China, China 82174051Natural Science Foundation of Jiangsu Province of China BK202013 28
6 · The paper itself

Abstract

Tripartite motif (TRIM) protein superfamily is a group of E3 ubiquitin ligases characterized by the conserved RING domain, the B-box domain, and the coiled-coil domain (RBCC). It is widely involved in various physiological and pathological processes, such as intracellular signal transduction, cell cycle regulation, oncogenesis, and innate immune response. Central nervous system (CNS) diseases are composed of encephalopathy and spinal cord diseases, which have a high disability and mortality rate. Patients are often unable to take care of themselves and their life quality can be seriously declined. Initially, the function research of TRIM proteins mainly focused on cancer. However, in recent years, accumulating attention is paid to the roles they play in CNS diseases. In this review, we integrate the reported roles of TRIM proteins in the pathological process of CNS diseases and related signaling pathways, hoping to provide theoretical bases for further research in treating CNS diseases targeting TRIM proteins. TRIM proteins participated in CNS diseases. TRIM protein family is characterized by a highly conserved RBCC domain, referring to the RING domain, the B-box domain, and the coiled-coil domain. Recent research has discovered the relations between TRIM proteins and various CNS diseases, especially Alzheimer's disease, Parkinson's disease, and ischemic stroke.

Indexed as

Central Nervous System DiseasesUbiquitin-Protein LigasesHumansProtein DomainsTripartite Motif ProteinsTripartite Motif ProteinsUbiquitin-Protein LigasesCNS diseasesE3 ubiquitin ligasesSignaling pathwayTRIM proteins

Identifiers

PMID36988770
PMCPMC11410135
OpenAlexW4361301824

What Socratic holds

Textmetadata
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 Socratic graph.