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:

Insights into the modulation of bacterial NADase activity by phage proteins
Hang Yin, Xuzichao Li, Xiaoshen Wang, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 13

Showing 13 citing articles:

Mechanism of phage sensing and restriction by toxin-antitoxin-chaperone systems
Toomas Mets, Tatsuaki Kurata, Karin Ernits, et al.
Cell Host & Microbe (2024) Vol. 32, Iss. 7, pp. 1059-1073.e8
Open Access | Times Cited: 13

Recent advancements in bacterial anti-phage strategies and the underlying mechanisms altering susceptibility to antibiotics
Hao Zou, Xiaoyi Huang, W. Xiao, et al.
Microbiological Research (2025) Vol. 295, pp. 128107-128107
Closed Access

Activation of the bacterial defense-associated sirtuin system
Kaixiang Zhu, Kun Shang, Linyue Wang, et al.
Communications Biology (2025) Vol. 8, Iss. 1
Open Access

Filamentation activates bacterial Avs5 antiviral protein
Yiqun Wang, Yuqing Tian, Xu Yang, et al.
Nature Communications (2025) Vol. 16, Iss. 1
Open Access

Structural insights into autoinhibition and activation of defense-associated sirtuin protein
Yang Xu, Yiqun Wang, Jianting Zheng
International Journal of Biological Macromolecules (2024) Vol. 277, pp. 134145-134145
Closed Access | Times Cited: 3

Tetramerization-dependent activation of the Sir2-associated short prokaryotic Argonaute immune system
Ning Cui, Juntao Zhang, Zhuolin Li, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access | Times Cited: 2

Targeting SIRT2 in Aging-Associated Fibrosis Pathophysiology
Yongjiao Huang, Wei He, Yingting Zhang, et al.
Aging and Disease (2024)
Open Access | Times Cited: 1

Structural basis for the concerted antiphage activity in the SIR2–HerA system
Fumeng Liao, Guimei Yu, Chendi Zhang, et al.
Nucleic Acids Research (2024)
Open Access | Times Cited: 1

Adaptations in gut Bacteroidales facilitate stable co-existence with their lytic bacteriophages
Adrián Cortés‐Martín, Colin Buttimer, Jessie L. Maier, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access | Times Cited: 1

Cryo-EM Structure of an Active Bacterial SIR2-STAND Filament
Yiqun Wang, Yuqing Tian, Yang Xu, et al.
bioRxiv (Cold Spring Harbor Laboratory) (2024)
Open Access

Filamentation activates bacterial NLR-like antiviral protein
Jianting Zheng, Yiqun Wang, Yuqing Tian, et al.
Research Square (Research Square) (2024)
Open Access

Mechanistic basis for the allosteric activation of NADase activity in the Sir2-HerA antiphage defense system
Xiangkai Zhen, Biao Zhou, Zihe Liu, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access

The structural basis of the activation and inhibition of DSR2 NADase by phage proteins
Ruiwen Wang, Qi Xu, Zhuoxi Wu, et al.
Nature Communications (2024) Vol. 15, Iss. 1
Open Access

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