Evidence map›Paper›PMID 37779139›Full record

ReviewExperimental & molecular medicine2023

Targeting E3 ubiquitin ligases and their adaptors as a therapeutic strategy for metabolic diseases.

Yelin Jeong, Ah-Reum Oh, Young Hoon Jung, HyunJoon Gi, Young Un Kim, KyeongJin Kim

Open access · goldAbstract readReview
In one paragraph

Review in Experimental & molecular medicine, 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 32 papers.

0numbers the graph read from it
0cells of the map it votes in
32citing papers in PubMed
4.8field-weighted citation impact, top 4% 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

32 citing papers in PubMed, 31 citations in OpenAlex.

  1. Article
  2. E3 Ubiquitin Ligases in MASH-Associated Liver Fibrosis: Mechanisms and Therapeutic Opportunities.Liver international : official journal of the International Association for the Study of the Liver · 2026
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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.

Yelin Jeong *Department of Biomedical Sciences, College of Medicine, Inha University, Incheon, Republic of Korea.
Ah-Reum Oh *Department of Biomedical Sciences, College of Medicine, Inha University, Incheon, Republic of Korea.
Young Hoon Jung *Department of Biomedical Sciences, College of Medicine, Inha University, Incheon, Republic of Korea.
HyunJoon GiDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon, Republic of Korea.
Young Un KimDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon, Republic of Korea.
KyeongJin KimDepartment of Biomedical Sciences, College of Medicine, Inha University, Incheon, Republic of Korea. kimkj@inha.ac.kr.ORCID http://orcid.org/0000-0001-6865-9141
Inha University · KR

Funding

No grant is acknowledged in the PubMed record.

6 · The paper itself

Abstract

Posttranslational modification of proteins via ubiquitination determines their activation, translocation, dysregulation, or degradation. This process targets a large number of cellular proteins, affecting all biological pathways involved in the cell cycle, development, growth, and differentiation. Thus, aberrant regulation of ubiquitination is likely associated with several diseases, including various types of metabolic diseases. Among the ubiquitin enzymes, E3 ubiquitin ligases are regarded as the most influential ubiquitin enzymes due to their ability to selectively bind and recruit target substrates for ubiquitination. Continued research on the regulatory mechanisms of E3 ligases and their adaptors in metabolic diseases will further stimulate the discovery of new targets and accelerate the development of therapeutic options for metabolic diseases. In this review, based on recent discoveries, we summarize new insights into the roles of E3 ubiquitin ligases and their adaptors in the pathogenesis of metabolic diseases by highlighting recent evidence obtained in both human and animal model studies.

Indexed as

Metabolic DiseasesNeoplasmsAnimalsHumansUbiquitinUbiquitinationUbiquitin-Protein LigasesUbiquitinUbiquitin-Protein Ligases

Identifiers

PMID37779139
PMCPMC10618535
OpenAlexW4387229935

What OpenQuestion 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 OpenQuestion graph.