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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:

USP10 deubiquitinates Tau, mediating its aggregation
Zhen Wei, Kuan Zeng, Jichang Hu, et al.
Cell Death and Disease (2022) Vol. 13, Iss. 8
Open Access | Times Cited: 21

Showing 21 citing articles:

Stress, epigenetics, and aging: Unraveling the intricate crosstalk
Zeming Wu, Jing Qu, Weiqi Zhang, et al.
Molecular Cell (2023) Vol. 84, Iss. 1, pp. 34-54
Open Access | Times Cited: 54
Cellular and pathological functions of tau
C Bravo, Sarah Naguib, Li Gan
Nature Reviews Molecular Cell Biology (2024) Vol. 25, Iss. 11, pp. 845-864
Closed Access | Times Cited: 36
Abnormal protein post-translational modifications induces aggregation and abnormal deposition of protein, mediating neurodegenerative diseases
Wei Li, Honglian Li, Jian‐Zhi Wang, et al.
Cell & Bioscience (2024) Vol. 14, Iss. 1
Open Access | Times Cited: 10
Tau degradation in Alzheimer's disease: Mechanisms and therapeutic opportunities
Lisha Wang, Sooram Banesh, Rajnish Kumar, et al.
Alzheimer s & Dementia (2025) Vol. 21, Iss. 3
Open Access | Times Cited: 1
Targeting tau in Alzheimer's disease: from mechanisms to clinical therapy
Jinwang Ye, Hua-Li Wan, Sihua Chen, et al.
Neural Regeneration Research (2023) Vol. 19, Iss. 7, pp. 1489-1498
Open Access | Times Cited: 22
E3 ligases and DUBs target ferroptosis: A potential therapeutic strategy for neurodegenerative diseases
Linxia Lu, Cili Jifu, Jun Xia, et al.
Biomedicine & Pharmacotherapy (2024) Vol. 175, pp. 116753-116753
Open Access | Times Cited: 6
The autophagy adaptor TRIAD3A promotes tau fibrillation by nested phase separation
Jiechao Zhou, Yang ‘an Chuang, Javier Redding‐Ochoa, et al.
Nature Cell Biology (2024) Vol. 26, Iss. 8, pp. 1274-1286
Closed Access | Times Cited: 5
Ubiquitin-specific peptidase 10 promotes renal interstitial fibrosis progression through deubiquitinating and stabilizing P53 protein
Suwen Liu, Yunwen Yang, Qian Li, et al.
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease (2025) Vol. 1871, Iss. 3, pp. 167660-167660
Closed Access
Roles of Ubiquitin Ligases and Deubiquitylases in Alzheimer’s Disease
Fengju Jia, Lin Fu
Molecular Neurobiology (2025)
Closed Access
Tau proteins and senescent Cells: Targeting aging pathways in Alzheimer’s disease
Mahaveer Singh, Haider Ali, S. Renuka Jyothi, et al.
Brain Research (2024) Vol. 1844, pp. 149165-149165
Closed Access | Times Cited: 3
Investigation of the mechanism of Buyang Huanwu decoction in improving learning and memory impairment in Alzheimer's disease mice based on lipidomics
Jing Jiang, Kai Duo, Shuangli Zhu, et al.
Journal of Natural Medicines (2025)
Open Access
Involvement of heterologous ubiquitination including linear ubiquitination in Alzheimer’s disease and amyotrophic lateral sclerosis
Yusuke Sato, Seigo Terawaki, Daisuke Oikawa, et al.
Frontiers in Molecular Biosciences (2023) Vol. 10
Open Access | Times Cited: 9
Complicated Role of Post-translational Modification and Protease-Cleaved Fragments of Tau in Alzheimer’s Disease and Other Tauopathies
Jie Yang, Naiting Shen, Jianying Shen, et al.
Molecular Neurobiology (2023) Vol. 61, Iss. 7, pp. 4712-4731
Open Access | Times Cited: 9
Proteomic analysis of anti-aging effects of Dendrobium nobile Lindl. alkaloids in aging-accelerated SAMP8 mice
Bo Liu, Ling-Li Lv, Ping Liu, et al.
Experimental Gerontology (2023) Vol. 177, pp. 112198-112198
Open Access | Times Cited: 7
Erasing marks: Functions of plant deubiquitylating enzymes in modulating the ubiquitin code
Karin Vogel, Erika Isono
The Plant Cell (2024) Vol. 36, Iss. 9, pp. 3057-3073
Closed Access | Times Cited: 2
Untangling the complexity and impact of tau protein ubiquitination
Daniele Trivellato, Francesca Munari, Michael Assfalg, et al.
ChemBioChem (2024) Vol. 25, Iss. 22
Open Access | Times Cited: 2
DUBs in Alzheimer’s disease: mechanisms and therapeutic implications
Biying Qin, Xiaohong Chen, Feng Wang, et al.
Cell Death Discovery (2024) Vol. 10, Iss. 1
Open Access | Times Cited: 2
Targeting USP11 regulation by a novel lithium-organic coordination compound improves neuropathologies and cognitive functions in Alzheimer transgenic mice
Yi Guo, Cai Chuan-bin, Bingjie Zhang, et al.
EMBO Molecular Medicine (2024) Vol. 16, Iss. 11, pp. 2856-2881
Closed Access | Times Cited: 1
Excess Ub-K48 Induces Neuronal Apoptosis in Alzheimer’s Disease
Wenming Zhang, Yiyuan Yuan, Shi Huang, et al.
Journal of Integrative Neuroscience (2024) Vol. 23, Iss. 12
Open Access | Times Cited: 1
Elovanoids are neural resiliency epigenomic regulators targeting histone modifications, DNA methylation, tau phosphorylation, telomere integrity, senescence programming, and dendrite integrity
Nicolás G. Bazán, Surjyadipta Bhattacharjee, Sayantani Kala-Bhattacharjee, et al.
Research Square (Research Square) (2023)
Open Access | Times Cited: 1
YOD1 regulates microglial homeostasis by deubiquitinating MYH9 to promote the pathogenesis of Alzheimer’s disease
Jinfeng Sun, Fan Chen, Lingyu She, et al.
Acta Pharmaceutica Sinica B (2024) Vol. 15, Iss. 1, pp. 331-348
Open Access
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