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Articles Published Processes
10/13/2023 1:41:42 PM | Browse: 189 | Download: 451
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Received |
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2023-07-19 19:38 |
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Peer-Review Started |
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2023-07-19 19:40 |
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To Make the First Decision |
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Return for Revision |
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2023-08-31 07:10 |
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Revised |
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2023-09-08 19:34 |
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Second Decision |
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2023-09-26 02:52 |
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Accepted by Journal Editor-in-Chief |
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Accepted by Executive Editor-in-Chief |
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2023-09-26 08:48 |
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Articles in Press |
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2023-09-26 08:48 |
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Publication Fee Transferred |
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Edit the Manuscript by Language Editor |
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Typeset the Manuscript |
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2023-10-11 01:40 |
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Publish the Manuscript Online |
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2023-10-13 13:41 |
| ISSN |
1949-8454 (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) 2023. 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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| Permissions |
For details, please visit: http://www.wjgnet.com/bpg/gerinfo/207
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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 |
Biochemistry & Molecular Biology |
| Manuscript Type |
Basic Study |
| Article Title |
Protein arginine methyltransferase 6 is a novel substrate of protein arginine methyltransferase 1
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| Manuscript Source |
Unsolicited Manuscript |
| All Author List |
Meng-Tong Cao Cao, You Feng and Y George Zheng |
| ORCID |
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| Funding Agency and Grant Number |
| Funding Agency |
Grant Number |
| National Institutes of Health (NIH) |
1R35GM149230 |
| National Institutes of Health (NIH) |
1R01GM126154 |
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| Corresponding Author |
Y George Zheng, PhD, Professor, Department of Pharmaceutical and Biomedical Sciences, University of Georgia, No. 250 W. Green St., Athens, GA 30602, United States. yzheng@uga.edu |
| Key Words |
Posttranslational modification; Arginine methylation; Protein arginine methyltransferase 1; Protein arginine methyltransferase 6; Cross-talk; Protein-protein interaction |
| Core Tip |
We reported the interplay between protein arginine methyltransferase (PRMT) 1 and PRMT6, and PRMT6 is a substrate of PRMT1. The major methylation site in PRMT6 is R106 for PRMT1 catalysis and the methylation by PRMT1 regulates the enzymatic activity of PRMT6. This study is important for understanding the cross-talking relationship between PRMTs. |
| Publish Date |
2023-10-13 13:41 |
| Citation |
Cao MT, Feng Y, Zheng YG. Protein arginine methyltransferase 6 is a novel substrate of protein arginine methyltransferase 1. World J Biol Chem 2023; 14(5): 84-98 |
| URL |
https://www.wjgnet.com/1949-8454 /full/v14/i5/84.htm |
| DOI |
https://dx.doi.org/10.4331/wjbc.v14.i5.84 |
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