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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:

Improvement of the fibrinolytic activity, acid resistance and thermostability of nattokinase by surface charge engineering
Yuan Li, Xiyu Tang, Liangqi Chen, et al.
International Journal of Biological Macromolecules (2023) Vol. 253, pp. 127373-127373
Closed Access | Times Cited: 11

Showing 11 citing articles:

Enhanced Thermostability of Nattokinase by Computation-Based Rational Redesign of Flexible Regions
Liangqi Chen, Kongfang Yu, Aixia Ma, et al.
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 25, pp. 14241-14254
Closed Access | Times Cited: 5
Mining and Modification of Key Functional Regions of the Nattokinase Propeptide
Aixia Ma, Hong Wang, Huiyang Jia, et al.
Journal of Agricultural and Food Chemistry (2025)
Closed Access
Overview of various protein engineering strategies to improve the catalytic activity, thermostability, and acid/base stability of β-glucanase
Xun Yu, Yang Hu, Qiaoling Li, et al.
International Journal of Biological Macromolecules (2025), pp. 142685-142685
Closed Access
Advances in recombinant protease production: current state and perspectives
Xiufang Liu, Mulin Lian, Mouming Zhao, et al.
World Journal of Microbiology and Biotechnology (2024) Vol. 40, Iss. 5
Closed Access | Times Cited: 4
Enhanced thermostability of nattokinase by rational design of disulfide bond
Kongfang Yu, Liangqi Chen, Yaolei Tang, et al.
Microbial Cell Factories (2025) Vol. 24, Iss. 1
Open Access
Mechanism of influence of nattokinase terminal sequence on catalytic performance and molecular modification
Yuan Li, Hong Wang, Kongfang Yu, et al.
International Journal of Biological Macromolecules (2025), pp. 141872-141872
Closed Access
Shifting the pH profiles of Staphylococcus epidermidis lipase (SEL) and Staphylococcus hyicus lipase (SHL) through generating chimeric lipases by DNA shuffling strategy
Wan Atiqah Najiah Binti Wan Hasan, Nima Ghahremani Nezhad, Mohd Adilin Yaacob, et al.
World Journal of Microbiology and Biotechnology (2024) Vol. 40, Iss. 4
Closed Access | Times Cited: 3
Modification of the active centre of nattokinase to enhance its thermostability using a strategy based on molecular dynamics simulation, steered dynamics simulation, and conservative prediction
Yuan Li, Wenhui Zhu, Liangqi Chen, et al.
Frontiers in Nutrition (2024) Vol. 11
Open Access | Times Cited: 2
Precise redesign for improving enzyme robustness based on coevolutionary analysis and multidimensional virtual screening
Jie Luo, Chenshuo Song, Wenjing Cui, et al.
Chemical Science (2024) Vol. 15, Iss. 38, pp. 15698-15712
Open Access | Times Cited: 1
Comprehensive Understanding of Laboratory Evolution for Food Enzymes: From Design to Screening Innovations
Junhao Wu, Zhaojun Wang, Maomao Zeng, et al.
Journal of Agricultural and Food Chemistry (2024) Vol. 72, Iss. 45, pp. 24928-24943
Closed Access | Times Cited: 1
Maggot Kinase and Natural Thrombolytic Proteins
Can Liu, Kaixin Zhang, Shihao Zhang, et al.
ACS Omega (2024)
Open Access
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