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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:

O-GlcNAcylation promotes pancreatic tumor growth by regulating malate dehydrogenase 1
Qiang Zhu, Hong Zhou, Liming Wu, et al.
Nature Chemical Biology (2022) Vol. 18, Iss. 10, pp. 1087-1095
Closed Access | Times Cited: 63

Showing 26-50 of 63 citing articles:

O-GlcNAc transferase promotes synaptic assembly independent of catalytic activity in C. elegans
Mengting Wu, Huihui Jiang, Qian Li, et al.
Journal of Biosciences (2025) Vol. 50, Iss. 2
Closed Access
ID3 enhances PD-L1 expression by restructuring MYC to promote colorectal cancer immune evasion
Chuanzhong Huang, Ling Wang, Changhua Zhuo, et al.
Proceedings of the National Academy of Sciences (2025) Vol. 122, Iss. 15
Open Access
The Deinococcus protease PprI senses DNA damage by directly interacting with single-stranded DNA
Huizhi Lu, Zijing Chen, Teng Xie, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 4
Pancreatic ductal adenocarcinoma cells reshape the immune microenvironment: Molecular mechanisms and therapeutic targets
Yutong Zhao, C.M. Qin, Lin Chen, et al.
Biochimica et Biophysica Acta (BBA) - Reviews on Cancer (2024) Vol. 1879, Iss. 6, pp. 189183-189183
Closed Access | Times Cited: 4
Role of malate dehydrogenase 1 and isocitrate dehydrogenase 1 and their posttranslational modifications in diseases
Chunxia Shi, Yukun Wang, Jin Guo, et al.
Biochemical and Biophysical Research Communications (2025) Vol. 754, pp. 151535-151535
Closed Access
Knocking down GALNT6 promotes pyroptosis of pancreatic ductal adenocarcinoma cells through NF-κB/NLRP3/GSDMD and GSDME signaling pathway
Mengyang Ding, Jingyu Liu, Honghui Lv, et al.
Frontiers in Oncology (2023) Vol. 13
Open Access | Times Cited: 10
Physiology of malate dehydrogenase and how dysregulation leads to disease
Amy D. Parente, Danielle E. Bolland, Kathryn L. Huisinga, et al.
Essays in Biochemistry (2024) Vol. 68, Iss. 2, pp. 121-134
Closed Access | Times Cited: 3
O-GlcNAcylation of enolase 1 serves as a dual regulator of aerobic glycolysis and immune evasion in colorectal cancer
Qiang Zhu, Jingchao Li, Haofan Sun, et al.
Proceedings of the National Academy of Sciences (2024) Vol. 121, Iss. 44
Closed Access | Times Cited: 3
Extracellular arginine availability modulates eIF2α O-GlcNAcylation and heme oxygenase 1 translation for cellular homeostasis
Yu‐Wen Hung, Ching Ouyang, Xiaoli Ping, et al.
Journal of Biomedical Science (2023) Vol. 30, Iss. 1
Open Access | Times Cited: 7
Glycan Metabolic Fluorine Labeling for In Vivo Visualization of Tumor Cells and In Situ Assessment of Glycosylation Variations
Dongxia Chen, Yaying Lin, Yifan Fan, et al.
Angewandte Chemie International Edition (2023) Vol. 62, Iss. 50
Closed Access | Times Cited: 7
RAD18 O-GlcNAcylation promotes translesion DNA synthesis and homologous recombination repair
Xiaolu Ma, Hui Fu, Chenyi Sun, et al.
Cell Death and Disease (2024) Vol. 15, Iss. 5
Open Access | Times Cited: 2
Sugar symphony: glycosylation in cancer metabolism and stemness
Venkatesh Varadharaj, W. E. Petersen, Surinder K. Batra, et al.
Trends in Cell Biology (2024)
Closed Access | Times Cited: 2
E3 ubiquitin ligase UBR5 promotes gemcitabine resistance in pancreatic cancer by inducing O-GlcNAcylation-mediated EMT via destabilization of OGA
Yunyan Du, Zhangjian Yang, Hao Shi, et al.
Cell Death and Disease (2024) Vol. 15, Iss. 5
Open Access | Times Cited: 1
Exploring the uncharted territory of the potential protein–protein interactions of cytosolic malate dehydrogenase
Joseph Provost, Amy D. Parente, Kristin M. Slade, et al.
Essays in Biochemistry (2024)
Closed Access | Times Cited: 1
O-GlcNAcylation of the intellectual disability protein DDX3X exerts proteostatic cell cycle control
Conor W. Mitchell, Huijie Yuan, Marie Sønderstrup-Jensen, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1
O-GlcNAcylation Facilitates the Interaction between Keratin 18 and Isocitrate Dehydrogenases and Potentially Influencing Cholangiocarcinoma Progression
Xiangfeng Meng, Yue Zhou, Lei Xu, et al.
ACS Central Science (2024) Vol. 10, Iss. 5, pp. 1065-1083
Open Access | Times Cited: 1
Inhibition of DEF‐p65 Interactions as a Potential Avenue to Suppress Tumor Growth in Pancreatic Cancer
Sicong Huang, Jiaqi Yang, Teng Xie, et al.
Advanced Science (2024) Vol. 11, Iss. 28
Open Access | Times Cited: 1
Opportunities for Therapeutic Modulation of O-GlcNAc
Steven S. Cheng, Alison Mody, Christina M. Woo
Chemical Reviews (2024) Vol. 124, Iss. 22, pp. 12918-13019
Closed Access | Times Cited: 1
DNA damage-induced YTHDC1 O-GlcNAcylation promotes homologous recombination by enhancing m6A binding
Mengyao Li, Jie Li, Yibo Wang, et al.
Fundamental Research (2023)
Open Access | Times Cited: 3
A sialyltransferases-related gene signature serves as a potential predictor of prognosis and therapeutic response for bladder cancer
Penglong Cao, Mingying Chen, Tianya Zhang, et al.
European journal of medical research (2023) Vol. 28, Iss. 1
Open Access | Times Cited: 3
Role of O-GlcNAcylation in cancer biology
Yuxuan Li, Shu-Han Qu, Hai Jin, et al.
Pathology - Research and Practice (2023) Vol. 253, pp. 155001-155001
Closed Access | Times Cited: 3
Exploiting O-GlcNAc transferase promiscuity to dissect site-specific O-GlcNAcylation
Conor W. Mitchell, Sergio G. Bartual, Andrew T. Ferenbach, et al.
Glycobiology (2023) Vol. 33, Iss. 12, pp. 1172-1181
Open Access | Times Cited: 2
FoxO3a Drives the Metabolic Reprogramming in Tamoxifen-Resistant Breast Cancer Cells Restoring Tamoxifen Sensitivity
Marco Fiorillo, Elena Ricci, Mariarosa Fava, et al.
Cells (2023) Vol. 12, Iss. 24, pp. 2777-2777
Open Access | Times Cited: 2
The diverging role of O-GlcNAc Transferase in corticotroph and somatotroph adenomas
Roel Gonzalez, Logan Massman, Sophia Ho, et al.
Research Square (Research Square) (2024)
Open Access
O-GlcNAc signaling: Implications for stress-induced adaptive response pathway in the tumor microenvironment
Yu Zhao, Renlong Li, Weizhen Wang, et al.
Cancer Letters (2024) Vol. 598, pp. 217101-217101
Closed Access

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