Publication Name	World Journal of Hepatology
Manuscript ID	90653
Country	China

Received	2023-12-11 08:10
Peer-Review Started	2023-12-11 08:10
To Make the First Decision
Return for Revision	2023-12-29 00:50
Revised	2024-01-08 09:18
Second Decision	2024-03-01 02:56
Accepted by Journal Editor-in-Chief
Accepted by Executive Editor-in-Chief	2024-03-01 07:22
Articles in Press	2024-03-01 07:22
Publication Fee Transferred
Edit the Manuscript by Language Editor	2024-03-01 01:11
Typeset the Manuscript	2024-03-11 02:29
Publish the Manuscript Online	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/
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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
CrossCheck Report	90653-CrossCheck report.pdf