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:

Discovery and mechanistic analysis of a novel source protein glutaminase PG5 and its potential application
Weijun Leng, Ying Li, Xin Liang, et al.
Food Chemistry (2024) Vol. 457, pp. 140121-140121
Closed Access | Times Cited: 5

Showing 5 citing articles:

Thermo-reversible gelation and enhanced umami perception of myofibrillar proteins induced by protein-glutaminase-mediated deamidation
Weijun Leng, Ying Li, Xin Liang, et al.
Food Chemistry (2025) Vol. 471, pp. 142802-142802
Closed Access

Engineering of protein glutaminase for highly efficient modification of fish myofibrillar protein through structure-based and computational-aided strategy
Weijun Leng, Ying Li, Xin Liang, et al.
Food Chemistry (2024) Vol. 461, pp. 140845-140845
Closed Access | Times Cited: 3

Enzyme Engineering: Performance Optimization, Novel Sources, and Applications in the Food Industry
Shucan Mao, Jun Jiang, Ke Xiong, et al.
Foods (2024) Vol. 13, Iss. 23, pp. 3846-3846
Open Access | Times Cited: 1

Functional and Mechanistic Dissection of Protein Glutaminase PG3 and Its Rational Engineering for Enhanced Modification of Myofibrillar Proteins
Weijun Leng, Ying Li, Li Yuan, et al.
Journal of Agricultural and Food Chemistry (2024)
Closed Access

In vitro activation of recombinant pro-protein-glutaminases from Bacteroides helcogenes and Flavobacterium sp.
Gudrun Horstmann, Anja Luz, Julius Plomer, et al.
Molecular Catalysis (2024) Vol. 572, pp. 114718-114718
Open Access

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