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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:

SIRT5-mediated SDHA desuccinylation promotes clear cell renal cell carcinoma tumorigenesis
Yuanzhen Ma, Yijun Qi, Lei Wang, et al.
Free Radical Biology and Medicine (2019) Vol. 134, pp. 458-467
Closed Access | Times Cited: 81

Showing 1-25 of 81 citing articles:

NAD+ metabolism: pathophysiologic mechanisms and therapeutic potential
Na Xie, Lu Zhang, Wei Gao, et al.
Signal Transduction and Targeted Therapy (2020) Vol. 5, Iss. 1
Open Access | Times Cited: 637
Insights into the post-translational modification and its emerging role in shaping the tumor microenvironment
Wen Li, Feifei Li, Xia Zhang, et al.
Signal Transduction and Targeted Therapy (2021) Vol. 6, Iss. 1
Open Access | Times Cited: 122
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: 112
An Epigenetic Role of Mitochondria in Cancer
Yue Liu, Chao Chen, Xinye Wang, et al.
Cells (2022) Vol. 11, Iss. 16, pp. 2518-2518
Open Access | Times Cited: 85
Circulating tumor cells: from new biological insights to clinical practice
Xuyu Gu, Shiyou Wei, Xin Lv
Signal Transduction and Targeted Therapy (2024) Vol. 9, Iss. 1
Open Access | Times Cited: 18
Epigenetic regulation in cancer
Minzhi Gu, Bo Ren, Yuan Fang, et al.
MedComm (2024) Vol. 5, Iss. 2
Open Access | Times Cited: 17
The Roles of Sirtuin Family Proteins in Cancer Progression
Erhu Zhao, Jianbing Hou, Xiaoxue Ke, et al.
Cancers (2019) Vol. 11, Iss. 12, pp. 1949-1949
Open Access | Times Cited: 103
Resveratrol’s Anti-Cancer Effects through the Modulation of Tumor Glucose Metabolism
Aranka Brockmueller, Saba Sameri, Alena Líšková, et al.
Cancers (2021) Vol. 13, Iss. 2, pp. 188-188
Open Access | Times Cited: 60
Oncometabolites drive tumorigenesis by enhancing protein acylation: from chromosomal remodelling to nonhistone modification
Yidian Fu, Jie Yu, Fang Li, et al.
Journal of Experimental & Clinical Cancer Research (2022) Vol. 41, Iss. 1
Open Access | Times Cited: 52
The emerging roles of HDACs and their therapeutic implications in cancer
Rihan Hai, Deyi Yang, Feifei Zheng, et al.
European Journal of Pharmacology (2022) Vol. 931, pp. 175216-175216
Closed Access | Times Cited: 48
Sirtuin5 protects colorectal cancer from DNA damage by keeping nucleotide availability
Hao-Lian Wang, Yan Chen, Yun-Qian Wang, et al.
Nature Communications (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 43
Assembly of mitochondrial succinate dehydrogenase in human health and disease
Ke Cao, Jie Xu, Wenli Cao, et al.
Free Radical Biology and Medicine (2023) Vol. 207, pp. 247-259
Closed Access | Times Cited: 27
Metabolic alterations in hereditary and sporadic renal cell carcinoma
Nathan J. Coffey, M. Celeste Simon
Nature Reviews Nephrology (2024) Vol. 20, Iss. 4, pp. 233-250
Open Access | Times Cited: 11
A glimpse into novel acylations and their emerging role in regulating cancer metastasis
Huifang Shi, Weigang Cui, Qin Yan, et al.
Cellular and Molecular Life Sciences (2024) Vol. 81, Iss. 1
Open Access | Times Cited: 8
Tricarboxylic acid cycle metabolites: new players in macrophage
Ying Yang, Bingbing Cui, Jian Li, et al.
Inflammation Research (2024) Vol. 73, Iss. 4, pp. 531-539
Closed Access | Times Cited: 8
Estrogen inhibits autophagy and promotes growth of endometrial cancer by promoting glutamine metabolism
Wen‐Jie Zhou, Jie Zhang, Hui‐Li Yang, et al.
Cell Communication and Signaling (2019) Vol. 17, Iss. 1
Open Access | Times Cited: 73
Comprehensive characterization of extracellular matrix-related genes in PAAD identified a novel prognostic panel related to clinical outcomes and immune microenvironment: A silico analysis with in vivo and vitro validation
Xu Chen, Qihang Yuan, Jifeng Liu, et al.
Frontiers in Immunology (2022) Vol. 13
Open Access | Times Cited: 36
Therapeutic Potential and Activity Modulation of the Protein Lysine Deacylase Sirtuin 5
Francesco Fiorentino, Carola Castiello, Antonello Mai, et al.
Journal of Medicinal Chemistry (2022) Vol. 65, Iss. 14, pp. 9580-9606
Open Access | Times Cited: 35
Shedding light on structure, function and regulation of human sirtuins: a comprehensive review
Abhishek Sharma, Pragati Mahur, Jayaraman Muthukumaran, et al.
3 Biotech (2022) Vol. 13, Iss. 1
Open Access | Times Cited: 35
Overview of SIRT5 as a potential therapeutic target: Structure, function and inhibitors
Yingying Wang, Hui Chen, Xiaoming Zha
European Journal of Medicinal Chemistry (2022) Vol. 236, pp. 114363-114363
Closed Access | Times Cited: 33
Anti-silencing function 1B histone chaperone promotes cell proliferation and migration via activation of the AKT pathway in clear cell renal cell carcinoma
Jiangqiao Zhou, Tao Qiu, Zhongbao Chen, et al.
Biochemical and Biophysical Research Communications (2019) Vol. 511, Iss. 1, pp. 165-172
Closed Access | Times Cited: 48
Repression of p53 function by SIRT5-mediated desuccinylation at Lysine 120 in response to DNA damage
Xing Liu, Fangjing Rong, Jinhua Tang, et al.
Cell Death and Differentiation (2021) Vol. 29, Iss. 4, pp. 722-736
Open Access | Times Cited: 40
Mitochondrial SENP2 regulates the assembly of SDH complex under metabolic stress
Ying Liu, Kejia Liu, Rick F. Thorne, et al.
Cell Reports (2023) Vol. 42, Iss. 2, pp. 112041-112041
Open Access | Times Cited: 13
Role of succinylation modification in central nervous system diseases
Chao Wang, Weigang Cui, Bing Yu, et al.
Ageing Research Reviews (2024) Vol. 95, pp. 102242-102242
Closed Access | Times Cited: 4
PDZK1 suppresses TNBC development and sensitizes TNBC cells to erlotinib via the EGFR pathway
Yuanzhen Ma, Zhiyu Fang, Hongning Zhang, et al.
Cell Death and Disease (2024) Vol. 15, Iss. 3
Open Access | Times Cited: 4
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