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3/27/2024 1:51:18 PM | Browse: 102 | Download: 112
Publication Name World Journal of Hepatology
Manuscript ID 90653
Country China
2023-12-11 08:10
Peer-Review Started
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2023-12-29 00:50
2024-01-08 09:18
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2024-03-01 02:56
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2024-03-01 07:22
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2024-03-01 07:22
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2024-03-01 01:11
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2024-03-27 13:28
ISSN 1948-5182 (online)
Open Access This article is an open-access article that was selected by an in-house editor and fully peer-reviewed by external reviewers. It is distributed in accordance with the Creative Commons Attribution NonCommercial (CC BY-NC 4.0) license, which permits others to distribute, remix, adapt, build upon this work non-commercially, and license their derivative works on different terms, provided the original work is properly cited and the use is non-commercial. See: https://creativecommons.org/Licenses/by-nc/4.0/
Copyright © The Author(s) 2024. Published by Baishideng Publishing Group Inc. All rights reserved.
Article Reprints For details, please visit: http://www.wjgnet.com/bpg/gerinfo/247
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Publisher Baishideng Publishing Group Inc, 7041 Koll Center Parkway, Suite 160, Pleasanton, CA 94566, USA
Website http://www.wjgnet.com
Category Cell Biology
Manuscript Type Minireviews
Article Title Protein succinylation, hepatic metabolism, and liver diseases
Manuscript Source Invited Manuscript
All Author List Shuang Liu, Rui Li, Ya-Wen Sun, Hai Lin and Hai-Fang Li
Funding Agency and Grant Number
Corresponding Author Hai-Fang Li, Doctor, Associate Professor, College of Life Sciences, Shandong Agricultural University, No. 61 Daizong Street, Tai’an 271018, Shandong Province, China. haifangli@sdau.edu.cn
Key Words Protein succinylation; Hepatic metabolism; Fatty liver; Hepatitis; Hepatocellular carcinoma
Core Tip Succinylation is the process of transferring succinyl groups through enzymatic and non-enzymatic means using succinyl CoA as a direct substrate. The succinylation degree could be promoted by succinyltransferases, such as lysine acetyltransferase 2A, histone acetyltransferase 1, α-ketoglutarate dehydrogenase complex, and carnitine palmitoyltransferase 1A. Meanwhile, desuccinylases including CobB, sirtuin 5, and sirtuin 7 negatively regulate the extent of protein succinylation. Several proteins and enzymes in glucose, amino acid, and lipid metabolisms are succinylated in the liver. Succinylation is also associated with the progression of several liver diseases. Thus, proteins with varied levels of succinylation may be potential targets for the treatment of fatty liver, hepatitis, and hepatocellular carcinoma.
Publish Date 2024-03-27 13:28
Citation Liu S, Li R, Sun YW, Lin H, Li HF. Protein succinylation, hepatic metabolism, and liver diseases. World J Hepatol 2024; 16 (3): 344-352
URL https://www.wjgnet.com/1948-5182/full/v16/i3/344.htm
DOI https://dx.doi.org/10.4254/wjh.v16.i3.344
Full Article (PDF) WJH-16-344-with-cover.pdf
Manuscript File 90653_Auto_Edited-XLQ-FilipodiaCL-YJP.docx
Answering Reviewers 90653-Answering reviewers.pdf
Audio Core Tip 90653-Audio core tip.m4a
Conflict-of-Interest Disclosure Form 90653-Conflict-of-interest statement.pdf
Copyright License Agreement 90653-Copyright license agreement.pdf
Non-Native Speakers of English Editing Certificate 90653-Language certificate.pdf
Peer-review Report 90653-Peer-review(s).pdf
Scientific Misconduct Check 90653-Bing-Qu XL-2.jpg
Scientific Editor Work List 90653-Scientific editor work list.pdf