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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:

The human O-GlcNAcome database and meta-analysis
Eugenia Wulff‐Fuentes, Rex Berendt, Logan Massman, et al.
Scientific Data (2021) Vol. 8, Iss. 1
Open Access | Times Cited: 202

Showing 1-25 of 202 citing articles:

Dual-specificity RNA aptamers enable manipulation of target-specific O-GlcNAcylation and unveil functions of O-GlcNAc on β-catenin
Yi Zhu, Gerald W. Hart
Cell (2023) Vol. 186, Iss. 2, pp. 428-445.e27
Open Access | Times Cited: 62
Expanding the horizons of targeted protein degradation: A non-small molecule perspective
Xiaowei Huang, Fengbo Wu, Jing Ye, et al.
Acta Pharmaceutica Sinica B (2024) Vol. 14, Iss. 6, pp. 2402-2427
Open Access | Times Cited: 16
FBXO31-mediated ubiquitination of OGT maintains O-GlcNAcylation homeostasis to restrain endometrial malignancy
Na Zhang, Yang Meng, Song Mao, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access | Times Cited: 2
O-GlcNAcylation in health and neurodegenerative diseases
Byeong Eun Lee, Pann‐Ghill Suh, Jae‐Ick Kim
Experimental & Molecular Medicine (2021) Vol. 53, Iss. 11, pp. 1674-1682
Open Access | Times Cited: 89
Advances in chemical probing of protein O-GlcNAc glycosylation: structural role and molecular mechanisms
Abhijit Saha, Davide Bello, Alberto Fernández‐Tejada
Chemical Society Reviews (2021) Vol. 50, Iss. 18, pp. 10451-10485
Open Access | Times Cited: 79
Cofilin and Actin Dynamics: Multiple Modes of Regulation and Their Impacts in Neuronal Development and Degeneration
James R. Bamburg, Laurie S. Minamide, O’Neil Wiggan, et al.
Cells (2021) Vol. 10, Iss. 10, pp. 2726-2726
Open Access | Times Cited: 79
Demystifying the O-GlcNAc Code: A Systems View
Junfeng Ma, Chunyan Hou, Ci Wu
Chemical Reviews (2022) Vol. 122, Iss. 20, pp. 15822-15864
Closed Access | Times Cited: 58
OGT controls mammalian cell viability by regulating the proteasome/mTOR/ mitochondrial axis
Xiang Li, Xiaojing Yue, Hugo Sepúlveda, et al.
Proceedings of the National Academy of Sciences (2023) Vol. 120, Iss. 3
Open Access | Times Cited: 27
The functions and mechanisms of post-translational modification in protein regulators of RNA methylation: Current status and future perspectives
Youming Chen, Zuli Jiang, Ying Yang, et al.
International Journal of Biological Macromolecules (2023) Vol. 253, pp. 126773-126773
Closed Access | Times Cited: 23
Targeted Protein O-GlcNAcylation Using Bifunctional Small Molecules
Bowen Ma, Khadija Shahed Khan, Tongyang Xu, et al.
Journal of the American Chemical Society (2024) Vol. 146, Iss. 14, pp. 9779-9789
Open Access | Times Cited: 13
Emerging roles of O-GlcNAcylation in protein trafficking and secretion
Jianchao Zhang, Yanzhuang Wang
Journal of Biological Chemistry (2024) Vol. 300, Iss. 3, pp. 105677-105677
Open Access | Times Cited: 12
OGT and OGA: Sweet guardians of the genome
Chen Wu, Jiaheng Li, Lingzi Lu, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 4, pp. 107141-107141
Open Access | Times Cited: 9
The multifaceted role of intracellular glycosylation in cytoprotection and heart disease
Priya Umapathi, Akanksha Aggarwal, Fiddia Zahra, et al.
Journal of Biological Chemistry (2024) Vol. 300, Iss. 6, pp. 107296-107296
Open Access | Times Cited: 8
Genetic gradual reduction of OGT activity unveils the essential role of O-GlcNAc in the mouse embryo
Sara Formichetti, Agnieszka Sadowska, Michela Ascolani, et al.
PLoS Genetics (2025) Vol. 21, Iss. 1, pp. e1011507-e1011507
Open Access | Times Cited: 1
Novel antibodies detect nucleocytoplasmic O-fucose in protist pathogens, cellular slime molds, and plants
Megna Tiwari, Elisabet Gas‐Pascual, Manish Goyal, et al.
mSphere (2025)
Open Access | Times Cited: 1
Comorbidity-associated glutamine deficiency is a predisposition to severe COVID-19
T. Matsuyama, Steven K. Yoshinaga, Kimitaka Shibue, et al.
Cell Death and Differentiation (2021) Vol. 28, Iss. 12, pp. 3199-3213
Open Access | Times Cited: 48
Tools, tactics and objectives to interrogate cellular roles of O-GlcNAc in disease
Charlie Fehl, John A. Hanover
Nature Chemical Biology (2021) Vol. 18, Iss. 1, pp. 8-17
Open Access | Times Cited: 44
Mechanistic roles for altered O-GlcNAcylation in neurodegenerative disorders
Aaron T. Balana, Matthew R. Pratt
Biochemical Journal (2021) Vol. 478, Iss. 14, pp. 2733-2758
Open Access | Times Cited: 42
The Beginner’s Guide to O-GlcNAc: From Nutrient Sensitive Pathway Regulation to Its Impact on the Immune System
Michael P. Mannino, Gerald W. Hart
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 36
O-GlcNAcylation: an important post-translational modification and a potential therapeutic target for cancer therapy
Qingsong Lu, Xiaozhen Zhang, Tingbo Liang, et al.
Molecular Medicine (2022) Vol. 28, Iss. 1
Open Access | Times Cited: 36
Integration of O-GlcNAc into Stress Response Pathways
Kamau Fahie, Kyriakos N. Papanicolaou, Natasha E. Zachara
Cells (2022) Vol. 11, Iss. 21, pp. 3509-3509
Open Access | Times Cited: 35
Thermal Proteome Profiling Reveals the O-GlcNAc-Dependent Meltome
Dustin T. King, Jesús E. Serrano-Negrón, Yanping Zhu, et al.
Journal of the American Chemical Society (2022) Vol. 144, Iss. 9, pp. 3833-3842
Open Access | Times Cited: 34
O-GlcNAcylation promotes cerebellum development and medulloblastoma oncogenesis via SHH signaling
Liping Chen, Ying Li, Zhihong Song, et al.
Proceedings of the National Academy of Sciences (2022) Vol. 119, Iss. 34
Open Access | Times Cited: 31
Emerging roles of O-glycosylation in regulating protein aggregation, phase separation, and functions
Xiang Li, Pinou Lv, Yifei Du, et al.
Current Opinion in Chemical Biology (2023) Vol. 75, pp. 102314-102314
Closed Access | Times Cited: 22
O-glycosylation of the transcription factor SPATULA promotes style development in Arabidopsis
Yuxiang Jiang, Seamus Curran-French, Samuel W.H. Koh, et al.
Nature Plants (2024) Vol. 10, Iss. 2, pp. 283-299
Open Access | Times Cited: 7
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