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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:

Loss of SIRT2 leads to axonal degeneration and locomotor disability associated with redox and energy imbalance
Stéphane Fourcade, Laia Morató, Janani Parameswaran, et al.
Aging Cell (2017) Vol. 16, Iss. 6, pp. 1404-1413
Open Access | Times Cited: 43

Showing 1-25 of 43 citing articles:

SIRT2: Controversy and multiple roles in disease and physiology
Yan Wang, Jingqi Yang, Tingting Hong, et al.
Ageing Research Reviews (2019) Vol. 55, pp. 100961-100961
Closed Access | Times Cited: 221
Oligodendrocytes enhance axonal energy metabolism by deacetylation of mitochondrial proteins through transcellular delivery of SIRT2
Kelly A. Chamberlain, Ning Huang, Yuxiang Xie, et al.
Neuron (2021) Vol. 109, Iss. 21, pp. 3456-3472.e8
Open Access | Times Cited: 117
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: 115
New Insights for Cellular and Molecular Mechanisms of Aging and Aging-Related Diseases: Herbal Medicine as Potential Therapeutic Approach
Yanfei Liu, Weiliang Weng, Rui Gao, et al.
Oxidative Medicine and Cellular Longevity (2019) Vol. 2019, pp. 1-25
Open Access | Times Cited: 89
Mechanisms of axonal support by oligodendrocyte-derived extracellular vesicles
Eva‐Maria Krämer‐Albers, Hauke Werner
Nature reviews. Neuroscience (2023) Vol. 24, Iss. 8, pp. 474-486
Closed Access | Times Cited: 27
Sirtuins at the Crossroads between Mitochondrial Quality Control and Neurodegenerative Diseases: Structure, Regulation, Modifications, and Modulators
Hui Xu, Yiyang Liu, Lin-Seng Li, et al.
Aging and Disease (2023) Vol. 14, Iss. 3, pp. 794-794
Open Access | Times Cited: 26
Emerging Role of Sirtuin 2 in Parkinson’s Disease
Yumei Liu, Yingying Zhang, Konghua Zhu, et al.
Frontiers in Aging Neuroscience (2020) Vol. 11
Open Access | Times Cited: 64
Sirtuin 2 (SIRT2): Confusing Roles in the Pathophysiology of Neurological Disorders
Xiuqi Chen, Wenmei Lu, Danhong Wu
Frontiers in Neuroscience (2021) Vol. 15
Open Access | Times Cited: 43
Reductive Stress-Induced Mitochondrial Dysfunction and Cardiomyopathy
WEI-XING MA, Chunyan Li, Ran Tao, et al.
Oxidative Medicine and Cellular Longevity (2020) Vol. 2020, pp. 1-11
Open Access | Times Cited: 46
SIRT2 functions in aging, autophagy, and apoptosis in post-maturation bovine oocytes
Dejun Xu, Xiaohan Jiang, Huanshan He, et al.
Life Sciences (2019) Vol. 232, pp. 116639-116639
Closed Access | Times Cited: 41
Proteomic analysis of the effects of caffeine in a neonatal rat model of hypoxic‐ischemic white matter damage
Liu Yang, Xuefei Yu, Yajun Zhang, et al.
CNS Neuroscience & Therapeutics (2022) Vol. 28, Iss. 7, pp. 1019-1032
Open Access | Times Cited: 20
The pathogenesis of amyotrophic lateral sclerosis: Mitochondrial dysfunction, protein misfolding and epigenetics
Wenzhi Chen, Ling Guo, Manna Li, et al.
Brain Research (2022) Vol. 1786, pp. 147904-147904
Closed Access | Times Cited: 19
SIRT2 as a potential new therapeutic target for Alzheimer’s disease
Noemí Sola-Sevilla, Elena Puerta
Neural Regeneration Research (2023) Vol. 19, Iss. 1, pp. 124-131
Open Access | Times Cited: 12
Swimming Exercise Pretreatment Attenuates Postoperative Delirium‐Like Behavior in Type 2 Diabetic Rats by Enhancing Mitochondrial Biogenesis Through Activation of SIRT2 Deacetylation
Kaixi Liu, Lei Chen, Xinning Mi, et al.
MedComm (2025) Vol. 6, Iss. 4
Open Access
NAD+, Axonal Maintenance, and Neurological Disease
Athanasios S. Alexandris, Vassilis E. Koliatsos
Antioxidants and Redox Signaling (2023) Vol. 39, Iss. 16-18, pp. 1167-1184
Open Access | Times Cited: 9
SIRT6 in Regulation of Mitochondrial Damage and Associated Cardiac Dysfunctions: A Possible Therapeutic Target for CVDs
K Divya, Navjot Kanwar, P.V. Anuranjana, et al.
Cardiovascular Toxicology (2024) Vol. 24, Iss. 6, pp. 598-621
Closed Access | Times Cited: 3
SIRT1 activation with neuroheal is neuroprotective but SIRT2 inhibition with AK7 is detrimental for disconnected motoneurons
David Romeo-Guitart, Tatiana Leiva-Rodríguez, Maria Espinosa‐Alcantud, et al.
Cell Death and Disease (2018) Vol. 9, Iss. 5
Open Access | Times Cited: 31
Proteomics of the corpus callosum to identify novel factors involved in hypomyelinated Niemann-Pick Type C disease mice
Fan Yang, Yudong Guan, Xiao Feng, et al.
Molecular Brain (2019) Vol. 12, Iss. 1
Open Access | Times Cited: 29
Opportunities for histone deacetylase inhibition in amyotrophic lateral sclerosis
Yvonne E. Klingl, Donya Pakravan, Ludo Van Den Bosch
British Journal of Pharmacology (2020) Vol. 178, Iss. 6, pp. 1353-1372
Open Access | Times Cited: 26
Sirtuins Modulation: A Promising Strategy for HIV-Associated Neurocognitive Impairments
Izchel Figarola-Centurión, Martha Escoto-Delgadillo, Gracia Viviana González-Enríquez, et al.
International Journal of Molecular Sciences (2022) Vol. 23, Iss. 2, pp. 643-643
Open Access | Times Cited: 14
Non-catalytic allostery in α-TAT1 by a phospho-switch drives dynamic microtubule acetylation
Abhijit Deb Roy, Evan G. Gross, Gayatri S. Pillai, et al.
The Journal of Cell Biology (2022) Vol. 221, Iss. 11
Open Access | Times Cited: 14
Quantitative proteomic analysis of the lysine acetylome reveals diverse SIRT2 substrates
Hui Zhang, Eric B. Dammer, Duc M. Duong, et al.
Scientific Reports (2022) Vol. 12, Iss. 1
Open Access | Times Cited: 13
Improvement of oocyte quality through the SIRT signaling pathway
Kim Vo, Yorino Sato, Kazuhiro Kawamura
Reproductive Medicine and Biology (2023) Vol. 22, Iss. 1
Open Access | Times Cited: 7
Understanding the Potential Role of Sirtuin 2 on Aging: Consequences of SIRT2.3 Overexpression in Senescence
Noemí Sola-Sevilla, Ana Ricobaraza, Rubén Hernández-Alcoceba, et al.
International Journal of Molecular Sciences (2021) Vol. 22, Iss. 6, pp. 3107-3107
Open Access | Times Cited: 16
Supplementation with low molecular weight peptides from fish protein hydrolysate reduces acute mild stress-induced corticosterone secretion and modulates stress responsive gene expression in mice
Anne‐Laure Dinel, Céline Lucas, Julie Le Faouder, et al.
Journal of Functional Foods (2020) Vol. 76, pp. 104292-104292
Open Access | Times Cited: 13
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