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-related desuccinylation modification of AIFM1 protects against compression-induced intervertebral disc degeneration by regulating mitochondrial homeostasis
Jianxin Mao, Di Wang, Dong Wang, et al.
Experimental & Molecular Medicine (2023) Vol. 55, Iss. 1, pp. 253-268
Open Access | Times Cited: 32

Showing 1-25 of 32 citing articles:

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

SUCLG2 Regulates Mitochondrial Dysfunction through Succinylation in Lung Adenocarcinoma
Qifan Hu, Jing Xu, Lei Wang, et al.
Advanced Science (2023) Vol. 10, Iss. 35
Open Access | Times Cited: 23

Glutamine suppresses senescence and promotes autophagy through glycolysis inhibition-mediated AMPKα lactylation in intervertebral disc degeneration
Yangyang Zhang, Zhengqi Huang, Weitao Han, et al.
Communications Biology (2024) Vol. 7, Iss. 1
Open Access | Times Cited: 9

Altered Metabolism and Inflammation Driven by Post-translational Modifications in Intervertebral Disc Degeneration
Dingchao Zhu, Huaizhen Liang, Cheng‐Feng Du, et al.
Research (2024) Vol. 7
Open Access | Times Cited: 5

Sirtuins in intervertebral disc degeneration: current understanding
Jianlin Shen, Yujian Lan, Ziyu Ji, et al.
Molecular Medicine (2024) Vol. 30, Iss. 1
Open Access | Times Cited: 5

Role of succinylation modification in central nervous system diseases
Chao Wang, Weigang Cui, Bing Yu, et al.
Ageing Research Reviews (2024) Vol. 95, pp. 102242-102242
Closed Access | Times Cited: 4

Emerging roles of mitochondrial sirtuin SIRT5 in succinylation modification and cancer development
Z. J. Ke, Kaikai Shen, Li Wang, et al.
Frontiers in Immunology (2025) Vol. 16
Open Access

SIRT5 -mediated desuccinylation of UQCRC2 attenuates osteogenic differentiation of aged BM-MSCs through impairing mitochondrial homeostasis
Xin Yin, Xiao Yuan Wang, Shi Chang Liu, et al.
Cellular Signalling (2025), pp. 111636-111636
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

Protein succinylation mechanisms and potential targeted therapies in urinary disease
Y.C. Lou, Caitao Dong, Qinhong Jiang, et al.
Cellular Signalling (2025), pp. 111744-111744
Closed Access

Transcription factor EP300 targets SIRT5 to promote autophagy of nucleus pulposus cells and attenuate intervertebral disc degeneration
Xiaowei Liu, Shanshan Huang, Pei Xu, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Cell Research (2025), pp. 119933-119933
Closed Access

SIRT5 Alleviates Apoptosis of Vascular Endothelial Cells Under Simulated Microgravity via Desuccinylation of ERO1A
Yikai Pan, Qian Zhang, Chengfei Li, et al.
International Journal of Molecular Sciences (2025) Vol. 26, Iss. 7, pp. 2908-2908
Open Access

SIRT5 promote malignant advancement of chordoma by regulating the desuccinylation of c-myc
Minghui Jiang, Zheng Huang, Li Chen, et al.
BMC Cancer (2024) Vol. 24, Iss. 1
Open Access | Times Cited: 2

SIRTUIN 5 ALLEVIATES EXCESSIVE MITOCHONDRIAL FISSION VIA DESUCCINYLATION OF ATPASE INHIBITORY FACTOR 1 IN SEPSIS-INDUCED ACUTE KIDNEY INJURY
Jiaxin Li, Yi Yao, Xiaobao Lei, et al.
Shock (2024) Vol. 62, Iss. 2, pp. 235-244
Closed Access | Times Cited: 2

SIRT5 suppresses the trophoblast cell proliferation, invasion, and migration to promote preeclampsia via desuccinylating HOXB3
Jingyan Ruan, Jiacui Zheng, Xue Zhang, et al.
Journal of Assisted Reproduction and Genetics (2024) Vol. 41, Iss. 10, pp. 2759-2770
Closed Access | Times Cited: 2

Sirtuin 5 (SIRT5) Suppresses Tumor Growth by Regulating Mitochondrial Metabolism and Synaptic Remodeling in Gliomas
Wanjun Tang, Bo Chen, Gkk Leung, et al.
International Journal of Molecular Sciences (2024) Vol. 25, Iss. 16, pp. 9125-9125
Open Access | Times Cited: 2

Proteogenomics offers a novel avenue in neoantigen identification for cancer immunotherapy
Yuqing Ren, Yi Yue, Xinyang Li, et al.
International Immunopharmacology (2024) Vol. 142, pp. 113147-113147
Closed Access | Times Cited: 2

Up-regulated succinylation modifications induce a senescence phenotype in microglia by altering mitochondrial energy metabolism
Xinnan Zhao, Xiaohan Yang, Cong Du, et al.
Journal of Neuroinflammation (2024) Vol. 21, Iss. 1
Open Access | Times Cited: 2

Nanotechnology-Enhanced Pharmacotherapy for Intervertebral Disc Degeneration Treatment
Shaoyan Shi, Xuehai Ou, Chao Liu, et al.
International Journal of Nanomedicine (2024) Vol. Volume 19, pp. 14043-14058
Open Access | Times Cited: 2

SIRT5 induces autophagy and alleviates myocardial infarction via desuccinylation of TOM1
Zengliang Li, Zihe Zheng, Xiao-Fu Dai
BMC Cardiovascular Disorders (2024) Vol. 24, Iss. 1
Open Access | Times Cited: 1

Sirtuin 5 Attenuates the Sepsis Induced Lung Injury via Modulation the Succinylation of Serine-Arginine Protein Kinase 1
Wei Guo, Zhansheng Hu, Lili Ji
Journal of Surgical Research (2024) Vol. 305, pp. 304-312
Closed Access | Times Cited: 1

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