OpenAlex Citation Counts

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OpenAlex is a bibliographic catalogue of scientific papers, authors and institutions accessible in open access mode, named after the Library of Alexandria. It's citation coverage is excellent and I hope you will find utility in this listing of citing articles!

If you click the article title, you'll navigate to the article, as listed in CrossRef. If you click the Open Access links, you'll navigate to the "best Open Access location". Clicking the citation count will open this listing for that article. Lastly at the bottom of the page, you'll find basic pagination options.

Requested Article:

SIRT5 impairs aggregation and activation of the signaling adaptor MAVS through catalyzing lysine desuccinylation
Xing Liu, Chunchun Zhu, Huangyuan Zha, et al.
The EMBO Journal (2020) Vol. 39, Iss. 11
Open Access | Times Cited: 53

Showing 1-25 of 53 citing articles:

Mitochondrial Sirtuin 3: New emerging biological function and therapeutic target
Jin Zhang, Honggang Xiang, Jie Liu, et al.
Theranostics (2020) Vol. 10, Iss. 18, pp. 8315-8342
Open Access | Times Cited: 312

Understanding the Function of Mammalian Sirtuins and Protein Lysine Acylation
Miao Wang, Hening Lin
Annual Review of Biochemistry (2021) Vol. 90, Iss. 1, pp. 245-285
Open Access | Times Cited: 112

The global succinylation of SARS-CoV-2–infected host cells reveals drug targets
Quan Liu, Heming Wang, Libin Chen, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 30
Open Access | Times Cited: 38

Emerging Roles of SIRT5 in Metabolism, Cancer, and SARS-CoV-2 Infection
Emanuele Fabbrizi, Francesco Fiorentino, Vincenzo Carafa, et al.
Cells (2023) Vol. 12, Iss. 6, pp. 852-852
Open Access | Times Cited: 34

Dual modifying of MAVS at lysine 7 by SIRT3-catalyzed deacetylation and SIRT5-catalyzed desuccinylation orchestrates antiviral innate immunity
Xing Liu, Chunchun Zhu, Shuke Jia, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 17
Closed Access | Times Cited: 8

Arginine monomethylation by PRMT7 controls MAVS-mediated antiviral innate immunity
Junji Zhu, Xiong Li, Xiaolian Cai, et al.
Molecular Cell (2021) Vol. 81, Iss. 15, pp. 3171-3186.e8
Open Access | Times Cited: 49

Genome editing of FTR42 improves zebrafish survival against virus infection by enhancing IFN immunity
Zi-Ling Qu, Xiu-Ying Gong, Lili An, et al.
iScience (2024) Vol. 27, Iss. 4, pp. 109497-109497
Open Access | Times Cited: 7

Grass carp (Ctenopharyngodon idella) SIRT3 enhances MAVS-mediated antiviral innate immunity in response to GCRV infection
Chunchun Zhu, Wen Liu, Shuke Jia, et al.
Aquaculture (2024) Vol. 587, pp. 740871-740871
Closed Access | Times Cited: 7

Repression of p53 function by SIRT5-mediated desuccinylation at Lysine 120 in response to DNA damage
Xing Liu, Fangjing Rong, Jinhua Tang, et al.
Cell Death and Differentiation (2021) Vol. 29, Iss. 4, pp. 722-736
Open Access | Times Cited: 40

MAVS: A Two-Sided CARD Mediating Antiviral Innate Immune Signaling and Regulating Immune Homeostasis
Yunqiang Chen, Yuheng Shi, Jing Wu, et al.
Frontiers in Microbiology (2021) Vol. 12
Open Access | Times Cited: 34

SIRT5 is a proviral factor that interacts with SARS-CoV-2 Nsp14 protein
Marius Walter, Irene P. Chen, Albert Vallejo-Gracia, et al.
PLoS Pathogens (2022) Vol. 18, Iss. 9, pp. e1010811-e1010811
Open Access | Times Cited: 25

Ctenopharyngodon idella (grass carp) pVHL suppresses antiviral innate immunity by targeting MAVS for degradation upon GCRV infection
Wen Liu, Xueyi Sun, Chunchun Zhu, et al.
Aquaculture (2025), pp. 742274-742274
Closed Access

SIRT5: a potential target for discovering bioactive natural products
Yuwei Xie, Ning Cai, Xiaohua Liu, et al.
Journal of Natural Medicines (2025)
Open Access

SIRT5 modulates mitochondria function via mitophagy and antioxidant mechanisms to facilitate oocyte maturation in mice
Jingjing Yan, Yanyu Wang, Zhanjun Shi, et al.
International Journal of Biological Macromolecules (2025), pp. 141488-141488
Closed Access

Deubiquitination enzyme USP35 negatively regulates MAVS signaling to inhibit anti-tumor immunity
Heping Zhang, Jiali Zhu, Rong He, et al.
Cell Death and Disease (2025) Vol. 16, Iss. 1
Open Access

Protein post-translational modification by lysine succinylation: Biochemistry, biological implications, and therapeutic opportunities
Zhao Guo, Junfeng Zhen, Xinyuan Liu, et al.
Genes & Diseases (2022) Vol. 10, Iss. 4, pp. 1242-1262
Open Access | Times Cited: 19

USP13 Cooperates with MARCH8 to Inhibit Antiviral Signaling by Targeting MAVS for Autophagic Degradation in Teleost
Pengfei Wang, Yuena Sun, Tianjun Xu
The Journal of Immunology (2024) Vol. 212, Iss. 5, pp. 801-812
Closed Access | Times Cited: 4

Virus subtype-specific suppression of MAVS aggregation and activation by PB1-F2 protein of influenza A (H7N9) virus
Pak‐Hin Hinson Cheung, Tak-Wang Terence Lee, Chun Kew, et al.
PLoS Pathogens (2020) Vol. 16, Iss. 6, pp. e1008611-e1008611
Open Access | Times Cited: 29

Propionate induces intestinal oxidative stress via Sod2 propionylation in zebrafish
Qianwen Ding, Zhen Zhang, Yu Li, et al.
iScience (2021) Vol. 24, Iss. 6, pp. 102515-102515
Open Access | Times Cited: 25

Role of novel protein acylation modifications in immunity and its related diseases
Xiaoqian Li, Tao Yu, Xiaolu Li, et al.
Immunology (2024) Vol. 173, Iss. 1, pp. 53-75
Open Access | Times Cited: 3

Roles of lipid metabolism and its regulatory mechanism in idiopathic pulmonary fibrosis: A review
Yunchuan Tian, Chunyan Duan, Jia-Yue Feng, et al.
The International Journal of Biochemistry & Cell Biology (2022) Vol. 155, pp. 106361-106361
Closed Access | Times Cited: 15

Ischemic accumulation of succinate induces Cdc42 succinylation and inhibits neural stem cell proliferation after cerebral ischemia/reperfusion
Suhua Qi, Linyan Huang, Juyun Ma, et al.
Neural Regeneration Research (2022) Vol. 18, Iss. 5, pp. 1040-1040
Open Access | Times Cited: 13

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