OpenAlex Citation Counts

OpenAlex Citations Logo

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:

LDHA Desuccinylase Sirtuin 5 as a Novel Cancer Metastatic Stimulator in Aggressive Prostate Cancer
Oh Kwang Kwon, In Hyuk Bang, So Young Choi, et al.
Genomics Proteomics & Bioinformatics (2022) Vol. 21, Iss. 1, pp. 177-189
Open Access | Times Cited: 40

Showing 1-25 of 40 citing articles:

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: 53

Revisiting the Warburg Effect with Focus on Lactate
Eva Kociánová, Viktoria Piatrikova, Tereza Golias
Cancers (2022) Vol. 14, Iss. 24, pp. 6028-6028
Open Access | Times Cited: 51

Emerging Roles of SIRT5 in Metabolism, Cancer, and SARS-CoV-2 Infection
Emanuele Fabbrizi, Francesco Fiorentino, Vincenzo Carafa, et al.
Cells (2023) Vol. 12, Iss. 6, pp. 852-852
Open Access | Times Cited: 35

LncRNA GLTC targets LDHA for succinylation and enzymatic activity to promote progression and radioiodine resistance in papillary thyroid cancer
Liang Shi, Rui Duan, Zhenhua Sun, et al.
Cell Death and Differentiation (2023) Vol. 30, Iss. 6, pp. 1517-1532
Open Access | Times Cited: 32

LDHA as a regulator of T cell fate and its mechanisms in disease
Maosha Dai, Li Wang, Juexi Yang, et al.
Biomedicine & Pharmacotherapy (2023) Vol. 158, pp. 114164-114164
Open Access | Times Cited: 28

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: 10

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

Activation and inhibition of sirtuins: From bench to bedside
Francesco Fiorentino, Emanuele Fabbrizi, Antonello Mai, et al.
Medicinal Research Reviews (2024)
Open Access | Times Cited: 6

The Mechanistic Roles of Sirtuins in Breast and Prostate Cancer
Cosmos Ifeanyi Onyiba, Christopher J. Scarlett, Judith Weidenhofer
Cancers (2022) Vol. 14, Iss. 20, pp. 5118-5118
Open Access | Times Cited: 23

Targeting succinylation-mediated metabolic reprogramming as a potential approach for cancer therapy
Zhenya Liu, Runxian Wang, Yunshan Wang, et al.
Biomedicine & Pharmacotherapy (2023) Vol. 168, pp. 115713-115713
Open Access | Times Cited: 13

The crosstalking of lactate‐Histone lactylation and tumor
Yao Rong, Fengyuan Dong, Guiqian Zhang, et al.
PROTEOMICS - CLINICAL APPLICATIONS (2023) Vol. 17, Iss. 5
Closed Access | Times Cited: 12

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

The Sirtuin 5 Inhibitor MC3482 Ameliorates Microglia‑induced Neuroinflammation Following Ischaemic Stroke by Upregulating the Succinylation Level of Annexin-A1
Qian Xia, Yongbo Yu, Gaofeng Zhan, et al.
Journal of Neuroimmune Pharmacology (2024) Vol. 19, Iss. 1
Closed Access | Times Cited: 4

Emerging roles of mitochondrial sirtuin SIRT5 in succinylation modification and cancer development
Z. J. Ke, Kaikai Shen, Li Wang, et al.
Frontiers in Immunology (2025) Vol. 16
Open Access

Intranuclear TCA and mitochondrial overload: the nascent sprout of tumors metabolism
Weixi Yuan, Guozhong Lu, Yin Zhao, et al.
Cancer Letters (2025), pp. 217527-217527
Closed Access

SIRT5: a potential target for discovering bioactive natural products
Yuwei Xie, Ning Cai, Xiaohua Liu, et al.
Journal of Natural Medicines (2025)
Open Access

Protein succinylation mechanisms and potential targeted therapies in urinary disease
Y.C. Lou, Caitao Dong, Qinhong Jiang, et al.
Cellular Signalling (2025), pp. 111744-111744
Closed Access

SDH defective cancers: molecular mechanisms and treatment strategies
Jia'er Wang, Tao Yuan, Bo Yang, et al.
Cell Biology and Toxicology (2025) Vol. 41, Iss. 1
Open Access

HDAC8-mediated CAPZB desuccinylation enhances cytoskeleton remodeling to promote idiopathic pulmonary fibrosis
Bo Liu, Di Kang, Jinjin Zhang, et al.
Research Square (Research Square) (2025)
Closed Access

The involvement of high succinylation modification in the development of prostate cancer
Zhenyang Zhang, Yanru Chen, Lingyu Fang, et al.
Frontiers in Oncology (2022) Vol. 12
Open Access | Times Cited: 15

Targeting mRNA-coding genes in prostate cancer using CRISPR/Cas9 technology with a special focus on androgen receptor signaling
Mobina Tabibian, Fahimeh Salasar Moghaddam, Elahe Motevaseli, et al.
Cell Communication and Signaling (2024) Vol. 22, Iss. 1
Open Access | Times Cited: 2

Page 1 - Next Page

Scroll to top