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:

Functions of the sirtuin deacylase SIRT5 in normal physiology and pathobiology
Surinder Kumar, David B. Lombard
Critical Reviews in Biochemistry and Molecular Biology (2018) Vol. 53, Iss. 3, pp. 311-334
Open Access | Times Cited: 219

Showing 26-50 of 219 citing articles:

The Emerging Role of HDACs: Pathology and Therapeutic Targets in Diabetes Mellitus
Saikat Dewanjee, V. Jayalakshmi, Rajkumar Singh Kalra, et al.
Cells (2021) Vol. 10, Iss. 6, pp. 1340-1340
Open Access | Times Cited: 48

Therapeutic Potential and Activity Modulation of the Protein Lysine Deacylase Sirtuin 5
Francesco Fiorentino, Carola Castiello, Antonello Mai, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 14, pp. 9580-9606
Open Access | Times Cited: 35

Aryl Fluorosulfate Based Inhibitors That Covalently Target the SIRT5 Lysine Deacylase**
Julie E. Bolding, Pablo Martín‐Gago, Nima Rajabi, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 47
Open Access | Times Cited: 33

Sirtuin 5 aggravates microglia-induced neuroinflammation following ischaemic stroke by modulating the desuccinylation of Annexin-A1
Qian Xia, Shuai Gao, Tangrui Han, et al.
Journal of Neuroinflammation (2022) Vol. 19, Iss. 1
Open Access | Times Cited: 30

Mechanism of histone deacetylases in cardiac hypertrophy and its therapeutic inhibitors
Yu Han, Jiali Nie, Dao Wen Wang, et al.
Frontiers in Cardiovascular Medicine (2022) Vol. 9
Open Access | Times Cited: 28

Research progress on post-translational modification of proteins and cardiovascular diseases
Xueli Cheng, Kai Wang, Yan Zhao, et al.
Cell Death Discovery (2023) Vol. 9, Iss. 1
Open Access | Times Cited: 17

Revisiting Histone Deacetylases in Human Tumorigenesis: The Paradigm of Urothelial Bladder Cancer
Aikaterini F. Giannopoulou, Athanassios D. Velentzas, Eumorphia G. Konstantakou, et al.
International Journal of Molecular Sciences (2019) Vol. 20, Iss. 6, pp. 1291-1291
Open Access | Times Cited: 53

The Role of Sirtuins in Kidney Diseases
Yu Ah Hong, Ji Eun Kim, Min-Jee Jo, et al.
International Journal of Molecular Sciences (2020) Vol. 21, Iss. 18, pp. 6686-6686
Open Access | Times Cited: 49

Mito-Nuclear Communication by Mitochondrial Metabolites and Its Regulation by B-Vitamins
Joëlle J. E. Janssen, Sander Grefte, Jaap Keijer, et al.
Frontiers in Physiology (2019) Vol. 10
Open Access | Times Cited: 47

Sirtuins and Renal Oxidative Stress
Yoshio Ogura, Munehiro Kitada, Daisuke Koya
Antioxidants (2021) Vol. 10, Iss. 8, pp. 1198-1198
Open Access | Times Cited: 39

The deacylase SIRT5 supports melanoma viability by influencing chromatin dynamics
William Giblin, Lauren Bringman-Rodenbarger, Angela H. Guo, et al.
Journal of Clinical Investigation (2021) Vol. 131, Iss. 12
Open Access | Times Cited: 36

Sirtuins: To Be or Not To Be in Diabetic Cardiomyopathy
Xavier Palomer, David Aguilar-Recarte, Raquel García, et al.
Trends in Molecular Medicine (2021) Vol. 27, Iss. 6, pp. 554-571
Closed Access | Times Cited: 33

Sirtuins as molecular targets, mediators, and protective agents in metal-induced toxicity
Alexey A. Tinkov, Thuy Nguyen, Abel Santamarı́a, et al.
Archives of Toxicology (2021) Vol. 95, Iss. 7, pp. 2263-2278
Closed Access | Times Cited: 33

Hesperetin derivative-16 attenuates CCl4-induced inflammation and liver fibrosis by activating AMPK/SIRT3 pathway
Juanjuan Li, He-Chun Jiang, Ao Wang, et al.
European Journal of Pharmacology (2021) Vol. 915, pp. 174530-174530
Closed Access | Times Cited: 33

Roles of sirtuin family members in chronic obstructive pulmonary disease
Xi-Yue Zhang, Wei Li, Jinrong Zhang, et al.
Respiratory Research (2022) Vol. 23, Iss. 1
Open Access | Times Cited: 27

Lysine Malonylation and Its Links to Metabolism and Diseases
Lu Zou, Yanyan Yang, Zhibin Wang, et al.
Aging and Disease (2022) Vol. 14, Iss. 1, pp. 84-84
Open Access | Times Cited: 27

Overexpression of SLC25A51 promotes hepatocellular carcinoma progression by driving aerobic glycolysis through activation of SIRT5
Lu Bai, Zhao-Xu Yang, Pengfei Ma, et al.
Free Radical Biology and Medicine (2022) Vol. 182, pp. 11-22
Closed Access | Times Cited: 25

Investigation of Carboxylic Acid Isosteres and Prodrugs for Inhibition of the Human SIRT5 Lysine Deacylase Enzyme**
Nima Rajabi, Tobias Hansen, Alexander L. Nielsen, et al.
Angewandte Chemie International Edition (2022) Vol. 61, Iss. 22
Open Access | Times Cited: 25

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

Molecular and cellular regulatory roles of sirtuin protein
Shubhra Pande, Sheikh Raisuddin
Critical Reviews in Food Science and Nutrition (2022) Vol. 63, Iss. 29, pp. 9895-9913
Closed Access | Times Cited: 24

Redox Homeostasis in Cardiovascular Disease: The Role of Mitochondrial Sirtuins
Alberto Zullo, Rosa Guida, Rosaria Sciarrillo, et al.
Frontiers in Endocrinology (2022) Vol. 13
Open Access | Times Cited: 23

Histone deacetylase (HDACs) inhibitors: Clinical applications
Kumar D. Shanmukha, Harikrishnareddy Paluvai, Santosh K. Lomada, et al.
Progress in molecular biology and translational science (2023), pp. 119-152
Closed Access | Times Cited: 14

Sirtuins: Promising Therapeutic Targets to Treat Ischemic Stroke
Yue Liu, Liuding Wang, Guang Yang, et al.
Biomolecules (2023) Vol. 13, Iss. 8, pp. 1210-1210
Open Access | Times Cited: 14

Set7/9 aggravates ischemic brain injury via enhancing glutamine metabolism in a blocking Sirt5 manner
Jinghuan Wang, Subei Tan, Yuyu Zhang, et al.
Cell Death and Differentiation (2024) Vol. 31, Iss. 4, pp. 511-523
Closed Access | Times Cited: 5

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