Evidence map›Paper›PMID 41799925›Full record

ReviewTransboundary and emerging diseases2025

Selective Autophagy Mediated by Protein Ubiquitination in Major Prevalent Zoonoses.

Chi Meng, Fengyuan Jiao, Gengxu Zhou, Lingjie Wang, Shengping Wu, Cailiang Fan, Jixiang Li, Liting Cao, Zuoyong Zhou, Yuefeng Chu and 1 more

Abstract readReview
In one paragraph

Review in Transboundary and emerging diseases, 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. Review
  2. 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

11 authors.

Chi MengThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.ORCID https://orcid.org/0009-0005-8629-6926
Fengyuan JiaoThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.
Gengxu ZhouThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.ORCID https://orcid.org/0009-0009-4367-5423
Lingjie WangThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.
Shengping WuThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.
Cailiang FanThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.
Jixiang LiThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.
Liting CaoThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.
Zuoyong ZhouThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.ORCID https://orcid.org/0000-0002-5098-1367
Yuefeng ChuState Key Laboratory for Animal Disease Control and Prevention, College of Veterinary Medicine, Lanzhou University, Lanzhou Veterinary Research Institute, Chinese Academy of Agricultural Sciences, Lanzhou, Gansu, 730000, China, caas.cn.
Hanwei JiaoThe College of Veterinary Medicine, Southwest University, Chongqing, 402460, China, southwest.edu.ORCID https://orcid.org/0009-0007-0561-6276

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Zoonotic diseases not only cause great harm to animal health but also involve the development of animal husbandry, which in turn endangers human life and health and public health safety. Protein ubiquitination and autophagy are important ways for the body to degrade invading pathogens, which correspond to the ubiquitin (Ub)-proteasome system (UPS) and autophagic lysosomal pathway (ALP), respectively, and play an important role in the occurrence and development of diseases. For UPS, the substrate is delivered to the 26S proteasome system via a ubiquitination cascade and subsequently degraded and removed. For ALP, the substrate is encapsulated to form autophagosomes, which subsequently fuse with lysosomes to form autophagolysosomes, which are eventually degraded and cleared. However, a variety of zoonotic pathogens can interfere with the protein ubiquitination pathway and autophagy process to promote self-replication and survival, and resist host immune defense. This article reviews the mechanisms by which multiple pathogens interfere with protein degradation pathways, providing a new perspective for the treatment and prevention of zoonotic diseases.

Indexed as

AutophagyUbiquitinationZoonosesAnimalsHumansUbiquitinUbiquitinregulatory mechanismsselective autophagyubiquitination modificationzoonotic diseases

Identifiers

PMID41799925
PMCPMC12961972

What Socratic 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 Socratic graph.