Evidence map›Paper›PMID 42064091›Full record

ReviewFrontiers in immunology2026

The role of HECT-type E3 ubiquitin ligases in inflammation.

Ziyi Wang, Peirui Wang, Huawang Xie, Zhibo You, Xiping Liu, Fang Cao, Shengtao Yao

Abstract readReview
In one paragraph

Review in Frontiers in immunology, 2026. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Not yet cited in PubMed.

0numbers the graph read from it
0cells of the map it votes in
0citing 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

0 citing papers in PubMed.

No citing paper in PubMed yet.

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.

Ziyi WangDepartment of Neurosurgery, The Affiliated Hospital of Zunyi Medical University, Zunyi, Guizhou, China.
Peirui WangDepartment of Neurosurgery, The Affiliated Hospital of Zunyi Medical University, Zunyi, Guizhou, China.
Huawang XieDepartment of Neurosurgery, The Affiliated Hospital of Zunyi Medical University, Zunyi, Guizhou, China.
Zhibo YouDepartment of Neurosurgery, The Affiliated Hospital of Zunyi Medical University, Zunyi, Guizhou, China.
Xiping LiuDepartment of Biochemistry, Zunyi Medical University, Zunyi, Guizhou, China.
Fang CaoDepartment of Neurosurgery, The Affiliated Hospital of Zunyi Medical University, Zunyi, Guizhou, China.
Shengtao YaoDepartment of Neurosurgery, The Affiliated Hospital of Zunyi Medical University, Zunyi, Guizhou, China.

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Homologous to the E6-AP Carboxyl Terminus (HECT)-type E3 ubiquitin ligases are key components of the ubiquitin-proteasome system (UPS) and play an important role in the regulation of inflammatory responses. Inflammation serves as a core defense mechanism of the host against infection and tissue damage, while its dysregulated and unresolved activation drives the pathogenesis of diverse chronic inflammatory diseases. In recent years, the functions of HECT-type E3 ubiquitin ligases in inflammatory signaling pathways have gradually been revealed, particularly the differential roles of members of the HECT and RCC1-Like Domain Containing E3 Ubiquitin Protein Ligase (HERC) and Neural Precursor Cell Expressed Developmentally Downregulated 4 (NEDD4) subfamilies in immune cell activation, cytokine expression, and ubiquitination modifications. Although some molecular mechanisms of certain HECT-type E3 ubiquitin ligases have been reported, the complex regulatory networks and mechanisms of action of these ligases remain largely unelucidated, with conflicting research conclusions, unclarified cell type-specific functional heterogeneity, and notable limitations in current research systems remaining unresolved. This article systematically reviews the research progress of HECT-type E3 ubiquitin ligases in inflammation, focusing on the functional characteristics of different subfamilies and their molecular mechanisms in regulating inflammatory processes, and further conducts a critical analysis of conflicting findings in existing studies, the limitations of current research, and the context-dependent functions of specific ligases in different cell types. It aims to provide theoretical support and research directions for a deeper understanding of the biological functions of HECT-type E3 ubiquitin ligases and their application as potential therapeutic targets in inflammation-related diseases.

Indexed as

InflammationUbiquitin-Protein LigasesAnimalsHumansSignal TransductionUbiquitinUbiquitinationUbiquitinUbiquitin-Protein LigasesHECT-type E3 ubiquitin ligasesHERC subfamilyinflammationNEDD4subfamilyother HECTssignaling pathwaysubiquitination

Identifiers

PMID42064091
PMCPMC13124474

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.