L
L Zhou
Researcher at Fudan University
Publications - 11
Citations - 1064
L Zhou is an academic researcher from Fudan University. The author has contributed to research in topics: Acetylation & Glycolysis. The author has an hindex of 6, co-authored 9 publications receiving 769 citations. Previous affiliations of L Zhou include Fudan University Shanghai Medical College.
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Journal ArticleDOI
Acetylation Regulates Gluconeogenesis by Promoting PEPCK1 Degradation via Recruiting the UBR5 Ubiquitin Ligase
Wenqing Jiang,Shiwen Wang,Mengtao Xiao,Yan Lin,L Zhou,Qun-Ying Lei,Yue Xiong,Yue Xiong,Kun-Liang Guan,Kun-Liang Guan,Shimin Zhao +10 more
TL;DR: It is shown that acetylation regulates the stability of the gluconeogenic rate-limiting enzyme PEPCK1, thereby modulating cellular response to glucose and identifying potential therapeutic targets for diabetes.
Journal ArticleDOI
SIRT5 Desuccinylates and Activates Pyruvate Kinase M2 to Block Macrophage IL-1β Production and to Prevent DSS-Induced Colitis in Mice
Fang Wang,Ke Wang,Wei Xu,Shimin Zhao,Dan Ye,Yi Wang,Ying Xu,L Zhou,Yiwei Chu,Cuiping Zhang,Xue Qin,Pengyuan Yang,Hongxiu Yu +12 more
TL;DR: The findings reveal a mechanism by which SIRT5 suppresses the pro-inflammatory response in macrophages at least in part by regulating PKM2 succinylation, activity, and function.
Journal ArticleDOI
SIRT5 promotes IDH2 desuccinylation and G6PD deglutarylation to enhance cellular antioxidant defense
L Zhou,Fang Wang,Renqiang Sun,Xiufei Chen,Mengli Zhang,Qi Xu,Yi Wang,Shiwen Wang,Yue Xiong,Yue Xiong,Kun-Liang Guan,Kun-Liang Guan,Pengyuan Yang,Hongxiu Yu,Dan Ye +14 more
TL;DR: A SIRT5‐dependent mechanism that regulates cellular NADPH homeostasis and redox potential by promoting IDH2 desuccinylation and G6PD deglutarylation is uncovered.
Journal ArticleDOI
Acetylation of PGK1 promotes liver cancer cell proliferation and tumorigenesis
Hongli Hu,Wenwei Zhu,Jun Qin,Min Chen,Liyan Gong,Long Li,Xiangyuan Liu,Yongzhen Tao,Huiyong Yin,Hu Zhou,L Zhou,Dan Ye,Qing-Hai Ye,Daming Gao +13 more
TL;DR: A novel regulation of PGK1 is demonstrated as an important regulatory mechanism for promoting its enzymatic activity and cancer cell metabolism and its important role in liver cancer progression.
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SIRT3‐dependent GOT2 acetylation status affects the malate–aspartate NADH shuttle activity and pancreatic tumor growth
Hui Yang,L Zhou,L Zhou,Qian Shi,Qian Shi,Yuzheng Zhao,Huaipeng Lin,Huaipeng Lin,Mengli Zhang,Mengli Zhang,Shimin Zhao,Shimin Zhao,Yi Yang,Zhi Qiang Ling,Kun-Liang Guan,Yue Xiong,Dan Ye +16 more
TL;DR: This study uncovers a previously unknown mechanism by which GOT2 acetylation stimulates the malate–aspartate NADH shuttle activity and oxidative protection.