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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:

Mitochondrial Sirtuin Network Reveals Dynamic SIRT3-Dependent Deacetylation in Response to Membrane Depolarization
Wen Yang, Koji Nagasawa, Christian Münch, et al.
Cell (2016) Vol. 167, Iss. 4, pp. 985-1000.e21
Open Access | Times Cited: 293

Showing 26-50 of 293 citing articles:

SIRT3 Activation a Promise in Drug Development? New Insights into SIRT3 Biology and Its Implications on the Drug Discovery Process
Chiara Lambona, Clemens Zwergel, Sérgio Valente, et al.
Journal of Medicinal Chemistry (2024) Vol. 67, Iss. 3, pp. 1662-1689
Open Access | Times Cited: 20
Role of Argininosuccinate Synthase 1 ‐Dependent L‐Arginine Biosynthesis in the Protective Effect of Endothelial Sirtuin 3 Against Atherosclerosis
Xiaoyun Cao, Vivian Wei Yan Wu, Yumeng Han, et al.
Advanced Science (2024) Vol. 11, Iss. 12
Open Access | Times Cited: 16
Context-dependent role of SIRT3 in cancer
Jin Zhang, Jing Ye, Shiou Zhu, et al.
Trends in Pharmacological Sciences (2024) Vol. 45, Iss. 2, pp. 173-190
Closed Access | Times Cited: 16
SIRT3: A New Regulator of Cardiovascular Diseases
Wei Sun, Caixia Liu, Qiuhui Chen, et al.
Oxidative Medicine and Cellular Longevity (2018) Vol. 2018, Iss. 1
Open Access | Times Cited: 151
Acetylation of Mitochondrial Proteins in the Heart: The Role of SIRT3
Rebecca Parodi‐Rullán, Xavier R. Chapa‐Dubocq, Sabzali Javadov
Frontiers in Physiology (2018) Vol. 9
Open Access | Times Cited: 140
SIRT3 promotes antimycobacterial defenses by coordinating mitochondrial and autophagic functions
Tae Sung Kim, Yeung Bae Jin, Yi Sak Kim, et al.
Autophagy (2019) Vol. 15, Iss. 8, pp. 1356-1375
Open Access | Times Cited: 139
The mitochondrion: a central architect of copper homeostasis
Zakery N. Baker, Paul A. Cobine, Scot C. Leary
Metallomics (2017) Vol. 9, Iss. 11, pp. 1501-1512
Open Access | Times Cited: 136
The different axes of the mammalian mitochondrial unfolded protein response
Christian Münch
BMC Biology (2018) Vol. 16, Iss. 1
Open Access | Times Cited: 130
SIRT4 interacts with OPA1 and regulates mitochondrial quality control and mitophagy
Alexander Lang, Ruchika Anand, Simone Altinoluk-Hambüchen, et al.
Aging (2017) Vol. 9, Iss. 10, pp. 2163-2189
Open Access | Times Cited: 129
SIRT3-Dependent Mitochondrial Dynamics Remodeling Contributes to Oxidative Stress-Induced Melanocyte Degeneration in Vitiligo
Xiuli Yi, Weinan Guo, Qiong Shi, et al.
Theranostics (2019) Vol. 9, Iss. 6, pp. 1614-1633
Open Access | Times Cited: 129
Mechanisms and disease implications of sirtuin-mediated autophagic regulation
In Hye Lee
Experimental & Molecular Medicine (2019) Vol. 51, Iss. 9, pp. 1-11
Open Access | Times Cited: 122
The unique histidine in OSCP subunit of F‐ATP synthase mediates inhibition of the permeability transition pore by acidic pH
Manuela Antoniel, Kristen L. Jones, Salvatore Antonucci, et al.
EMBO Reports (2017) Vol. 19, Iss. 2, pp. 257-268
Open Access | Times Cited: 107
Non-oncogene Addiction to SIRT3 Plays a Critical Role in Lymphomagenesis
Meng Li, Ying‐Ling Chiang, Costas A. Lyssiotis, et al.
Cancer Cell (2019) Vol. 35, Iss. 6, pp. 916-931.e9
Open Access | Times Cited: 104
LRPPRC: A Multifunctional Protein Involved in Energy Metabolism and Human Disease
Jie Cui, Li Wang, Xiaoyue Ren, et al.
Frontiers in Physiology (2019) Vol. 10
Open Access | Times Cited: 101
Interplay between TRAP1 and Sirtuin-3 Modulates Mitochondrial Respiration and Oxidative Stress to Maintain Stemness of Glioma Stem Cells
Hye-Kyung Park, Jun-Hee Hong, Young Taek Oh, et al.
Cancer Research (2019) Vol. 79, Iss. 7, pp. 1369-1382
Open Access | Times Cited: 100
SIRT3 and mitochondrial metabolism in neurodegenerative diseases
Illari Salvatori, Cristiana Valle, Alberto Ferri, et al.
Neurochemistry International (2017) Vol. 109, pp. 184-192
Closed Access | Times Cited: 99
Mitochondrial Membrane Potential Regulates Nuclear Gene Expression in Macrophages Exposed to Prostaglandin E2
David E. Sanin, Mai Matsushita, Ramon I. Klein Geltink, et al.
Immunity (2018) Vol. 49, Iss. 6, pp. 1021-1033.e6
Open Access | Times Cited: 94
Glucose limitation activates AMPK coupled SENP1-Sirt3 signalling in mitochondria for T cell memory development
Jianli He, Xun Shangguan, Wei Zhou, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 92
Post-translational Modifications of Key Machinery in the Control of Mitophagy
Liming Wang, Hao Qi, Yancheng Tang, et al.
Trends in Biochemical Sciences (2019) Vol. 45, Iss. 1, pp. 58-75
Closed Access | Times Cited: 87
SIRT3 Haploinsufficiency Aggravates Loss of GABAergic Interneurons and Neuronal Network Hyperexcitability in an Alzheimer's Disease Model
Aiwu Cheng, Jing Wang, Nathaniel Ghena, et al.
Journal of Neuroscience (2019) Vol. 40, Iss. 3, pp. 694-709
Open Access | Times Cited: 76
Neuroprotective Effects of Trilobatin, a Novel Naturally Occurring Sirt3 Agonist from Lithocarpus polystachyus Rehd., Mitigate Cerebral Ischemia/Reperfusion Injury: Involvement of TLR4/NF-κB and Nrf2/Keap-1 Signaling
Jianmei Gao, Nana Chen, Na Li, et al.
Antioxidants and Redox Signaling (2020) Vol. 33, Iss. 2, pp. 117-143
Closed Access | Times Cited: 76
The role of SIRT3-mediated mitochondrial homeostasis in osteoarthritis
Yuzhe He, Zhipeng Wu, Langhai Xu, et al.
Cellular and Molecular Life Sciences (2020) Vol. 77, Iss. 19, pp. 3729-3743
Closed Access | Times Cited: 75
Defining the molecular mechanisms of the mitochondrial permeability transition through genetic manipulation of F-ATP synthase
Andrea Carrer, Ludovica Tommasin, Justina Šileikytė, et al.
Nature Communications (2021) Vol. 12, Iss. 1
Open Access | Times Cited: 73
ALS motor neurons exhibit hallmark metabolic defects that are rescued by SIRT3 activation
Jin‐Hui Hor, Munirah Mohamad Santosa, Valerie Jing Wen Lim, et al.
Cell Death and Differentiation (2020) Vol. 28, Iss. 4, pp. 1379-1397
Open Access | Times Cited: 72
Mitochondrial Sirt3 contributes to the bone loss caused by aging or estrogen deficiency
Wen Ling, Kimberly J. Krager, Kimberly Richardson, et al.
JCI Insight (2021) Vol. 6, Iss. 10
Open Access | Times Cited: 71

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