Evidence map›Paper›PMID 37415097›Full record

ReviewMolecular medicine (Cambridge, Mass.)2023

Roles of protein post-translational modifications in glucose and lipid metabolism: mechanisms and perspectives.

Yu-Hang Yang, Ri Wen, Ni Yang, Tie-Ning Zhang, Chun-Feng Liu

Open access · goldAbstract readReview
In one paragraph

Review in Molecular medicine (Cambridge, Mass.), 2023. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 57 papers, 2 of them syntheses that pooled it.

0numbers the graph read from it
0cells of the map it votes in
57citing papers in PubMed, 2 pooled it
13.4field-weighted citation impact, top 1% 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

57 citing papers in PubMed, 2 syntheses or guidelines pooled it, 87 citations in OpenAlex.

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  8. PKCβ II antagonizes O-GlcNAcylated FOXO4 and inhibits lipid synthesis.Apoptosis : an international journal on programmed cell death · 2026
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  19. Expanding the understanding of insulin resistance in brain and periphery.Trends in endocrinology and metabolism: TEM · 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

5 authors at 1 institution in 1 country.

Yu-Hang Yang *Department of Pediatrics, Shengjing Hospital of China Medical University, No.36, SanHao Street, Liaoning Province, Shenyang City, 110004, China.
Ri Wen *Department of Pediatrics, Shengjing Hospital of China Medical University, No.36, SanHao Street, Liaoning Province, Shenyang City, 110004, China.
Ni YangDepartment of Pediatrics, Shengjing Hospital of China Medical University, No.36, SanHao Street, Liaoning Province, Shenyang City, 110004, China.
Tie-Ning ZhangDepartment of Pediatrics, Shengjing Hospital of China Medical University, No.36, SanHao Street, Liaoning Province, Shenyang City, 110004, China. cmuztn@vip.qq.com.
Chun-Feng LiuDepartment of Pediatrics, Shengjing Hospital of China Medical University, No.36, SanHao Street, Liaoning Province, Shenyang City, 110004, China. liucf@sj-hospital.org.ORCID 0000-0001-5360-616X
China Medical University · CN

Funding

345 Talent Project of Shengjing Hospital of China Medical University M0691Major Scientific and Technological Special Project of Liaoning Province No. 2020JH1/10300001National Natural Science Foundation of China 81971810National Natural Science Foundation of China 82102254Natural Science Foundation of Liaoning Province 2017225003Natural Science Foundation of Liaoning Province 2018108001Shenyang's Science and Technology Program 20-205-4-002
6 · The paper itself

Abstract

The metabolism of glucose and lipids is essential for energy production in the body, and dysregulation of the metabolic pathways of these molecules is implicated in various acute and chronic diseases, such as type 2 diabetes, Alzheimer's disease, atherosclerosis (AS), obesity, tumor, and sepsis. Post-translational modifications (PTMs) of proteins, which involve the addition or removal of covalent functional groups, play a crucial role in regulating protein structure, localization function, and activity. Common PTMs include phosphorylation, acetylation, ubiquitination, methylation, and glycosylation. Emerging evidence indicates that PTMs are significant in modulating glucose and lipid metabolism by modifying key enzymes or proteins. In this review, we summarize the current understanding of the role and regulatory mechanisms of PTMs in glucose and lipid metabolism, with a focus on their involvement in disease progression associated with aberrant metabolism. Furthermore, we discuss the future prospects of PTMs, highlighting their potential for gaining deeper insights into glucose and lipid metabolism and related diseases.

Indexed as

Diabetes Mellitus, Type 2GlucoseHumansLipid MetabolismPhosphorylationProtein Processing, Post-TranslationalProteinsGlucoseProteinsGlucose metabolismLipid metabolismMetabolic diseasePost-translational modification

Identifiers

PMID37415097
PMCPMC10327358
OpenAlexW4383374218

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.